entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A8R7E6
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CERK1_ARATH
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Chitin elicitor receptor kinase 1 (AtCERK1) (EC 2.7.11.1) (LysM domain receptor-like kinase 1) (LysM RLK1) (LysM-containing receptor-like kinase 1)
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MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATDNFNLSFKIGQGGFGAVYYAELRGEKAAIKKMDMEASKQFLAELKVLTRVHHVNLVRLIGYCVEGSLFLVYEYVENGNLGQHLHGSGREPLPWTKRVQIALDSARGLEYIHEHTVPVYVHRDIKSANILIDQKFRAKVADFGLTKLTEVGGSATRGAMGTFGYMAPETVYGEVSAKVDVYAFGVVLYELISAKGAVVKMTEAVGEFRGLVGVFEESFKETDKEEALRKIIDPRLGDSYPFDSVYKMAELGKACTQENAQLRPSMRYIVVALSTLFSSTGNWDVGNFQNEDLVSLMSGR
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Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI). Mediates chitin-induced phosphorylation of PBL27.
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A8R7K9
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VP35C_ARATH
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Vacuolar protein sorting-associated protein 35C (Vesicle protein sorting 35C)
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MIADDDEKWLAAAIAAVKQNAFYMQRAIDSNNLKDALKFSAQMLSELRTSKLSPHKYYELYMRVFNELGTLEIFFKEETGRGCSIAELYELVQHAGNILPRLYLLCTIGSVYIKSKDVTATDILKDLVEMCRAVQHPLRGLFLRSYLAQVTRDKLPSIGSDLEGDGDAHMNALEFVLQNFTEMNKLWVRMQHQGPSREKEKREKERNELRDLVGKNLHVLSQLEGVDLGIYRDTVLPRILEQVVNCKDELAQCYLMDCIIQVFPDDFHLQTLDVLLGACPQLQPSVDIKTVLSGLMERLSNYAASSVEALPNFLQVEAFSKLNYAIGKVVEAQADLPAAASVTLYLFLLKFTLHVYSDRLDYVDQVLGSCVTQLSATGKLCDDKAAKQIVAFLSAPLEKYNNVVTILKLTNYPLVMEYLDRETNKAMAIILVQSVFKNNTHIATADEVDALFELAKGLMKDFDGTIDDEIDEEDFQEEQNLVARLVNKLYIDDPEEMSKIIFTVRKHIVAGGPKRLPLTIPPLVFSALKLIRRLRGGDENPFGDDASATPKRILQLLSETVEVLSDVSAPDLALRLYLQCAQAANNCELETVAYEFFTKAYLLYEEEISDSKAQVTALRLIIGTLQRMRVFNVENRDTLTHKATGYSARLLRKPDQCRAVYECAHLFWADECENLKDGERVVLCLKRAQRIADAVQQMANASRGTSSTGSVSLYVELLNKYLYFLEKGNQQVTGDTIKSLAELIKSETKKVESGAEPFINSTLRYIEFQRQQEDGGMNEKYEKIKMEWFE
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Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. Also involved in the efficient sorting of seed storage proteins (By similarity). The VPS29-VPS26-VPS35 subcomplex may be involved in recycling of specific cargos from endosome to the plasma membrane.
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A8T644
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PCSK9_PANTR
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSIHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPMLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTAGSTSEEAVAAVAICCRSRHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T650
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PCSK9_GORGO
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGEHMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYGIDNTCVVRSRDVSTTGRTSEEALAAVAICCRSRHLVQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T655
|
PCSK9_PANPA
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAAHRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVRPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRNRDVSTAGSTSEEAVAAVAICCRSRHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T658
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PCSK9_PONPY
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHDLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLMPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSVEPELTLAELRQRLIHFSAKDVINEVWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVCAIARCCLLPQANCSVHTAPPAGSGMGTRVLCHQQVHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDISTTGSTSEEAMAAVAICCRRRHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T662
|
PCSK9_MACNE
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVARCAQDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEEAVAAVAICCRSRHLVQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T666
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PCSK9_MACMU
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVARCAQDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCSPLPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSKEAVAAVAICCRSRHLVQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T672
|
PCSK9_COLGU
|
Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
|
MGTVSSRRSWWPLPLPLLLLLLLGLAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVVRCAPDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCNALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEEAMAAVAICCRSRHLVQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T677
|
PCSK9_PLEMO
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRLWWPLPLLLLLLLGPPGARAQEDDDGDYEELVLALRSEEDGPADALQHGATATFHRCAKDPWRLPGTYVVVLKDSDAHRSQPERTARRLQAQAARRGYLIKLLHVFHHLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSSHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLHVLNCQGKGTVSSALIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACRRLAGAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPLTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVATLPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGRRVCLAPNAFGGEGVYAVARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHVLTGCSSHWEMKDLGTHKPPVLKPRGQPDQCMGHSGASTHASCCYAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGSTSEEAVAAVAICCRSRHLA
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T682
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PCSK9_SAGLB
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRLWWPLPLLLLLLLGPAGTRAQEDDDDDYEELVLALRSEEEGLADALQNGATATFHRCAKDPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYQADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPKEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLHSLRVLNCQGKGTVSSTLIGLEFICKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARARVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGEGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHILTGCSSHWEVEDLGTHKPPVLRPEGQHNQCMGHRGASTHASCCHAPGLECKVKEHGLPAPQEQVTVTCEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGSTSEETVAAIAICCRSQHLAQAS
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T688
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PCSK9_CALJA
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRLWWPLPLLLLLLLGPTGTRAQEEDDDDYEELVLALRSEEDGLVDALQHGATATFHRCAKDSWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAKPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGRRRGERIEAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHILTGCSSHWEVEDLGTHKPPVLRPGGQHDQCMGHRGASTHASCCHAPGLECKVKEHGLPAPQEQVTVTCEEGWTLTGCSALPGTSHILGAYAVDDTCVVRSRDVSTTSSTSEETVATVAICCRSQHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T695
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PCSK9_SAIBB
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVSSRRLWWPLPLLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLADALQHGATATFHRCAKEPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAVMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSSSGKRRGERIEAQGGRRVCLAHNAFGGKGVYAIARCCLLPQANCSIHTAPPAGASMGTRAHCHQQGHVLTGCSAHWEVEELGTHKPPVLRPGGQPSQCMGHSGASTHATCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHILGAYAVDDTCVVRSQDVSTTGSTSEEAVAAVAICCRSRHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T6A1
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PCSK9_ATEGE
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVRSRRLWWPLPLLLLLLRGPAGARAQEDDDGDYEELVLALRSEEDGLAEAPQHGATATFHRCAKDPWRLPGTYVVVLKEETQRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLAKAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIKAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRVHCHHQGHVLTGCSSHWEVEDLGTHKPSVLRPRVQPDQCMGHSGASTHASCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGNTSEQAVAAVAICCRSRHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8T6A6
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PCSK9_LAGLA
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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)
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MGTVRSRRLWWPLPLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLAEALQHGATATFHRCAKDPWRLPGTYVVVLKEETQRLQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGTGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRVQPDQCMGHSGASTHASCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVGTTGNISEEAVTAVAICCRSWHLAQASQELQ
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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
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A8TX70
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CO6A5_HUMAN
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Collagen alpha-5(VI) chain (Collagen alpha-1(XXIX) chain) (von Willebrand factor A domain-containing protein 4)
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MKILLIIFVLIIWTETLADQSPGPGPVYADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQIGKALQEAHRTYFSAPINGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFNLRTIRDLSTFSQNMTQIIKDVTKYKEGAVDADMQVHFPISCQKDSLADLVFLVDESLGTGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSNTGAAIDQMRRDGFSESYGSRRAQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQTISTLKSYADLETYSTKFLKKLQNEIWSQISTYAEQRNLDKTGCVDTKEADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTYTGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGKEERVSFGQNFDALKSIKNEVVREICAEKGCEDMKADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTLTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSSLVFHVENFDHLKALERKLIFRVCALHDCKRITLLDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTYTAKALKHANALFTEEHGSRIKQNVKQMLIVITDGESHDHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNTIYVDNFDKLKDVFTLVQERMCTEAPEVCHLQEADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPRIDFALKKVSNMFNLHAGGRRNAGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITGNSEKIITFQDFDKLKNVDVKKRIIREICQSCGKTNCFMDIVVGFDISTHVQGQPLFQGHPQLESYLPGILEDISSIKGVSCGAGTEAQVSLAFKVNSDQGFPAKFQIYQKAVFDSLLQVNVSGPTHLNAQFLRSLWDTFKDKSASRGQVLLIFSDGLQSESNIMLENQSDRLREAGLDALLVVSLNTTAHHEFSSFEFGKRFDYRTHLTIGMRELGKKLSQYLGNIAERTCCCTFCKCPGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPKGGHGDDGIDGLDGEEGCHGFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQNNNIKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQTGQRGRQGDSGIPGYGQMGRKGVKGPRGFPGDAGQKGDIGNPGIPGGPGPKGFRGLALTVGLKGEEGSRGLPGPPGQRGIKGMAGQPVYSQCDLIRFLREHSPCWKEKCPAYPTELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENNCPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDTTEPRDVGNAMRFVTRNVFKRTYAGANVRRVAVFFSNGQTASRSSIITATMEFSALDISPTVFAFDERVFLEAFGFDNTGTFQVIPVPPNGENQTLERLRRCALCYDKCFPNACIREAFLPEDSYMDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDPLISDSGDRIALLSYSPWESSRRKMGTVKTEFDFITYDNQLLMKNHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRKHKVIFVVSAGENYERKEFVKMMALRAKCQGYVIFVISLGSTRKDDMEELASYPLDQHLIQLGRIHKPDLNYIAKFLKPFLYSVRRGFNQYPPPMLEDACRLINLGGENIQNDGFQFVTELQEDFLGGNGFIGQELNSGRESPFVKTEDNGSDYLVYLPSQMFEPQKLMINYEKDQKSAEIASLTSGHENYGRKEEPDHTYEPGDVSLQEYYMDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTPLTSTLGDRVAVLSYSPPGYMPNTEECPVYLEFDLVTYNSIHQMKHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRKNKVIFVISAGETNSLDKDVLRNVSLRAKCQGYSIFVFSFGPKHNDKELEELASHPLDHHLVQLGRTHKPDWNYIIKFVKPFVHLIRRAINKYPTEDMKATCVNMTSPNPENGGTENTVLLLPGIYEIKTENGDLFDEFDSQAQHLLVLGNNHSSGSETATDLMQKLYLLFSTEKLAMKDKEKAHLEEISALVVDKQQEKEDKEMEATDI
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Collagen VI acts as a cell-binding protein.
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A8VU90
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ANKL1_MOUSE
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Ankyrin repeat and LEM domain-containing protein 1 (EC 3.1.-.-) (Ankyrin repeat domain-containing protein 41) (LEM-domain containing protein 3)
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MADTACLALRLLAALREEEARAVEELLRLGADPNLVLDDGAAAVHLAARASHPRALHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQPDETREPTETFHVAQGSFETETCQGPALAESSGVSQDSELHVHRAELEVEAVEVAVHPQSSEATENSDYSSDASFVTAVEDSLQPGRPGGALELVAGLWVTRGAVSAGKGAPNCQPQVLTLTARDTDKPVLPGDGDLGALHPHSSVPPMSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQASRADVGHSQELAEALRTGTIPDCQVDEEALAQCFQRLDPLKKWREGITKSSFTYLLLDPRLTKDLPARASSLTLAECLQCFVRAIFYVGKGTRARPDAHLWEAFGYHDQPRKQVCPKVRRILDIWASGRGIISLHCFQHVVAMEAYTREACLLDALGLQTLTNQKQGHYYGVVAHWPPSRRRRLGVHLLQRALLVFLAEGERELRPQDIQARG
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Endonuclease that probably plays a role in the DNA damage response and DNA repair.
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A8WCF8
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TPRGL_RAT
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Tumor protein p63-regulated gene 1-like protein (Mossy fiber terminal-associated vertebrate-specific presynaptic protein)
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MLQLRDTVDSAGTSPTAVLAAGEDAGAGRQGAGTPLRQTLWPLNVHDPTRRARVKEYFVFRPGTIEQAVEEIRAVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTDQSLLICKYDFISLQCQQVVRVALSAVDTISCGEFQFPPKSLNKREGFGVRIQWDKQSRPSFINRWNPWSTNMPYATFIEHPMAGMDEKTASLCHLESFKALLIQAVKKAQKESPLPGQANNVLVLDRPLLIETYVGLMSFINNEAKLGYSMTRGKIGF
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Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release.
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A8WFJ9
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ETS4_CAEEL
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Transcription factor ets-4
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MNGTGSVGHRWNSLSPEPHSGTESTASTPFVKSEFPFDDDLFGIDQVNNVKPHPMDMPCNLPIQPIEYNRRFSKDADHSTFVKNEIEENILNFNVNPEIAQDNGLDTQQIDIYRDLILRHLIQDISTTCAKLGLPNDFYLWSSEHGARWINEMCMQFNLQPPRNCSITGIDLLGMSQKDFEMILPAGGDTLHAQLQVWKTGTSDYVKAFENYHPPVTVQSSGMTAAENNMQSKTNWLASTNNQTNNMAAAENPNHPFFNGNGGYPNMSMSSFFQQGTVLPSPSNSDTSSNGSSQDMNDDDIDLHMNNSNCGFSNFFHNQGYMNSPIDAMCNGSEGDDDERAYTRHQGTVHLWQFIRELLDQPKQYSACVRWVDRDEGTFKIESSLLLARYWGQRKNRSQMNYDKLSRSLRQYYKKGIIQKPEKKQRLVYKFLPPYNL
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Transcription factor which binds to 5'-GGAA/T-3' DNA consensus sequences. Both positively and negatively regulates the expression of target genes. Plays a role in the regulation of adult lifespan, which may in part be through modulation of daf-16 activity. Regulates the expression of genes such as svh-2 in response to axon injury and in addition, may function downstream of the cAMP signaling pathway to promote axon regeneration. Regulates the expression of lipid metabolism genes and may also control the expression of the RNA-binding protein rege-1 which too has been implicated in the control of fat accumulation.
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A8WFU8
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KIF22_DANRE
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Kinesin-like protein KIF22
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MAQRVAVNDGAAGSKRTSRVRVAVRLRPYMDKQDEKSEGSCVRGLGPQKLEIINWRNATETLQYQFDVFHGEETTQQEVFLTSVKPILPHILNGQNASVFAYGPTGAGKTHTMLGSQEQPGVIPRAVKEVFNLVGAQKKEQDGWEYSIGMSYLEIYNEKVLDLLSPGSQDLPIREDKDRNILIPGLTHTPLSSFADFDTHFIPASLNRTTASTKLNQRSSRSHAILLIKVVKSQRGPPHRQQTGKLYLVDLAGSEDNRRTGNQGIRLKESGAINLSLFTLSKVVDALNTGAGGRVPYRDSKLTRLLQDSLGGSAHSVMITNIAPEYKYYFDTFSALNFAAKSKQIVNRPFVRETVLAPTIAPGKRTREEQEAGGSGEPQNKRSKEGKKAEHSPSPPLHPQSSPDSSVLDRLLALEKMMMGSAERERLNLLKTVAQSRKEIQMLKEKQKELEDKANMFNKQKETTEKESKDALLFKTDLPPLHRKQSTAAKPRKQQAVVTPLQVSQVQPLQQCAVVCKPSQTLVKKKRVQTEVCDGKENIGVDLPPVEDVNWESRLDPALLEQSRKKILQTLNSGSLKELKSLQQIGDKKAKLIMGWREINGDFTQVEDLKKIEGVTVKRFSSFIKANILSSMGK
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Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA.
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A8WGA0
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C27C1_DANRE
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Cytochrome P450 27C1 (EC 1.14.19.53) (All-trans retinol 3,4-desaturase)
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MALQSTILHMARKNLLQESCRQLLIQTHGLHKSVASGSLEIAAHSQADLKEESAVSPAEEVQKAARVKSLKEMPGPSTVANLLEFFYRDGFSRIHEIQMEHAKKYGKIFKSRFGPQFVVSIADRDMVAQVLRSESATPQRGNMESWKEYRDLRGRSTGLISAEGDEWLKMRSVLRQLIMRPRDVAVFSSDVNDVVADLVKRVKTLRSQQDDSQTVLNINDLFFKYAMEGVATILYETRLGCLENEIPKMSQEYITALHLMFSSFKTTMYAGAIPKWLRPIIPKPWEEFCSSWDGLFKFSQIHVDKRLSEIKKQMEKSEEIKGGLLTHMLVTREMNLEEIYANMTEMLLAGVDTTSFTLSWSTYLLARHPTIQQQIFEEVDRVLGGRVPTGEDVPYLPLIRGLVKETLRLFPVLPGNGRVTHDDLIVGGYLIPKGTQLALCHYSTSMDEENFPRPEEFRPDRWIRKDASDRVDNFGSIPFGYGIRSCIGRRIAELEMHLALTQLLQNFHIEVSPQTTEVHAKTHGLLCPGASINLRFTDRK
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Efficiently catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). Also acts on all-trans retinal and all-trans retinoic acid. The replacement of 11-cis retinal chromophore in photopigments with 11-cis 3,4-didehydroretinal enhances sensitivity to long-wavelength light. This may improve vision in fresh water which is often turbid.
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A8WGB1
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CCBE1_DANRE
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Collagen and calcium-binding EGF domain-containing protein 1 (Full of fluid protein)
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MIYPGRGASLSVAVALVLFSSGAPWTFREEKEDVDREVCSESKIATTKYPCVKSTGEVTTCYRKKCCEGFKFVLGQCIPEDYDVCAGAPCEQQCTDHFGRVVCTCYDGYRYDRERHRNREKPYCLDIDECANNNETVCSQMCVNTPGSYRCDCHSGFYLEDDGKTCTKGERAPLFEKSDNVMKEGTCSATCEDFHQMKMTVLQLKQKMSLLSSNTEINKQMTNEKMMMTTNSFLPGPPGPPGPAGTPGAKGSSGSPGQMGPPGLPGPRGDMGPIGPSPDLSHIKQGRRGPVGPPGAPGRDGMKGERGFPGPSGPPGPPGSFDFLLLMMADIRNDIAELQSKVFSRPLHSSFEDFPSAPDSWRDTPENLDFGSGEDYKSQSPPKSSRKRKLPRNLKNPDWPV
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Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. Necessary for lymphangiogenesis, but is probably not part of either the vegfc-vegfr3 signaling or sox18-prox1 transcriptional pathways.
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A8WGP3
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PP4CA_DANRE
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Serine/threonine-protein phosphatase 4 catalytic subunit A (PP4C-A) (EC 3.1.3.16)
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MCVIMGDFTDLDRQIEQLRRCELIKENEVKALCAKAREILVEESNVQSVDSPVTVCGDIHGQFYDLKELFRVGGEVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFFDECHRKYGSATVWRYCTEIFDYLSLSAIVDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDISMICRAHQLVMEGYKWHFNDTVLTVWSAPNYCYRCGNVAAILELDEHLQKEFIIFEAAPQETRGLPSKKPVADYFL
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Protein phosphatase that regulates many processes such as microtubule organization at centrosomes.
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A8WIP6
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CDK20_DANRE
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Cyclin-dependent kinase 20 (EC 2.7.11.22) (Cell cycle-related kinase) (Cell division protein kinase 20)
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MDQYSILGRIGEGAHGIVFKAKHIETGETVALKKVALRRLEDGIPNQALREIKALQEIEDNQYVVKLKDVFPHGTGFVLVFEYMLSDLSEVIRNSQRPLTASQVKSYMMMLLKGVAFCHENSIMHRDLKPANLLISSTGHLKIADFGLARLFSNEGDRLYSHQVATRWYRAPELLYGARKYDEGVDLWAVGCIFGELLNNSPLFPGENDIEQLCCVLRVLGTPNQKVWPEITELPDYNKITFKENPPIPLEEIVPDTSPQAVDLLKKFLVYPSKQRISARQALLHPYFFTDPLPAHHSELPIPQRGGKHSRQRMQPPHEFTVDRPLHESVVDPSLIQKHAMSCS
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Involved in cell growth. Activates cdk2, a kinase involved in the control of the cell cycle, by phosphorylating residue 'Thr-160' (By similarity). Required for high-level Shh responses in the developing neural tube. Together with tbc1d32, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing gli2 to be properly activated in response to SHH signaling. {ECO:0000250, ECO:0000269|PubMed:20159594}.
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A8WJR8
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MBK2_CAEBR
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Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2 (EC 2.7.12.1) (Dual specificity Yak1-related kinase mbk-2) (Minibrain Kinase 2)
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MAALASFTRNSRSYGQQPIDVTQQGQRDRSVMSLDAQGRSKMSNINYTRPAALSTSDSTIGVFRRAPSSFSGASSSSSNHHHPVYHSHNSLPPTLIGGSPHSASSNSLAQGHRNPALGSGNTLTRSYHQPSSTNSSTSNLHGPLGTYSRDLKQAIRDISPPVINSSANPHLVNYIHTSSFDNGSYEFPSGQAQQQRRLGGSQQHLAPLQQTSSSLYSNPQSSSSQLLGQQAVRSNYAYQQSLPRQQHINSHQTQAFFGTIRAPGNSTNIVTPLRASKTMIDVLAPVRDSVAAQATTGALPSVGTSSSNGSSNSSSGVGSGGSGSLMTQSIGGPNKHLSASHSTLNTASTHDSMMHTKIPKSPSNESLSRSHTSSSGGSQGGHNSNSGSNSGFRPEDAVQTFGAKLVPYEKNEIYNYTRVFFVGSHAKKQPGVIGGANNGGYDDENGSYQLVVHDHIAYRYEVLKVIGKGSFGQVIKAFDHKYQQYVALKLVRNEKRFHRQADEEIRILDHLRRQDSDGTHNIIHMLDYFNFRNHKCITFELLSINLYELIKRNKFQGFSLMLVRKFAYSMLLCLDLLQKNRLIHCDLKPENVLLKQQGRSGIKVIDFGSSCFDDQRIYTYIQSRFYRAPEVILGTKYGMPIDMWSLGCILAELLTGYPLLPGEDENDQLALIIELLGMPPPKSLETAKRARTFITSKGYPRYCTATSMPDGSVVLAGARSKRGKMRGPPESRSWSTALKNMGDELFVDFLKRCLDWDPETRMTPAQALKHKWLRRRLPNPPRDGMDSMGGLADHDKKADLPNIDSNANILMRKKF
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Required for oocyte-to-zygote transition in which it phosphorylates oocyte proteins, including mei-1, oma-1, oma-2, mex-5, and mex-6, modifying their activity and/or stability following meiosis. Through phosphorylation of P granule components including meg-1, promotes the disassembly of zygotic P granules in the anterior cytoplasm during zygote polarization, and thus plays a role in P granule distribution and segregation in early stage embryos following meiosis (By similarity). Functions in both spindle positioning and in the posterior localization of cytoplasmic determinants, including pie-1, pos-1, and pgl-1, in early embryos. Involved in the asymmetric distribution of plk-1 at the 2-cell embryonic stage.
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A8WUG4
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KPC3_CAEBR
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Protein kinase C-like 3 (EC 2.7.11.13) (Atypical protein kinase C-3) (aPKC3)
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MSSPTSVEEDGDIKLKTRFHGQVVVLYARPPLILDDFFALLRDACKQHAKQDITVKWIDEDGDPISIDSQMELDEAVRCLNVSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQGKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQTPQGPNVPVAPSSGVGSLRGGRLDTSSSTTRSGGGIDNGAFHEHEIESPGSAKDMSRSTNGNGASKWAVSLNDFRLLTVIGRGSYAKVVQAEHIATRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRRLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENINAGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASNILKGFLNKDPSQRLGCKLDINDGLNDMKEHDFFRGFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDEPPQLSPDNSAVIARIDQSEFDGFEYVNPLQMSREDSV
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Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphorylates serine residues of num-1. Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury.
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A8WVD0
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STX1A_CAEBR
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Syntaxin-1A (Uncoordinated protein 64)
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MTKDRLAALKAAQSEDEQDDDMHMETGNAQYMEEFFEQVEEIRGSVDIIANNVEEVKKKHSAILSNPVNDQKTKEELDELMAVIKRAANKVRGKLKLIENAIEHDENQQGAGNADLRIRKTQHSTLSRRFVEVMTDYNKTQTDYRERCKGRIQRQLDIAGKQVGDEDLEEMIESGNPGVFTQGIITDTQQAKQTLADIEARHNDIMKLESSIRELHDMFMDMAMLVESQGEMVDRIEYNVEHAKEFVDRAVADTKKAVQYQSKARRKKIIILIVVTVIIVILSLWLIQYIPGI
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Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation (By similarity). Plays a role in synaptic vesicle docking and tethering through its association with unc-18 (By similarity). Through binding to unc-18 mediates the release of the neurotransmitter acetylcholine from cholinergic motor neurons, and thereby promotes locomotory behaviors (By similarity). Essential for embryonic viability and development (By similarity). Has a role in dauer formation and adult life span. Required for locomotion (By similarity). Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt (By similarity).
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A8WVU9
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ROCK_CAEBR
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Rho-associated protein kinase let-502 (EC 2.7.11.1) (Lethal protein 502) (Rho-binding kinase let-502)
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MEQDELLHQLVDPKSPINIESLLDTITALVNDCKIPVLMRMKSVDNFISRYERIVESVAALRMKATDFRQLKVIGRGAFGEVHLVRHTRTNTVYAMKMLNKDDMIKRADSAFFWEERDIMAHANSEWIVRLQYAFQDPRHLYMVMEYMPGGDLVNLMTSYEVSEKWTRFYTAEIVEALAALHNMGYIHRDVKPDNMLISRSGHIKLADFGTCVKMNSNGVVRCSTAVGTPDYISPEVLRNQGKDSEFGKEVDWWSVGVFIYEMLVGETPFYAEALVSTYANIMNHQTSLRFPDEPLISTQAKDIIKKFLSAAPERLGKNNVDEIRNHKFFKNDEWTFETLKDATPPIVPSLKSDDDTTHFEEIETRDRDNASDFQLPKTFNGNQLPFIGFTYSNEYSPVKKLLNGASSNGVQNGVENKPVVVQQPLTNGHSTGIPEEQYEEVVIELDSKKRELESLKDSISRTEIRAKLIETEKNSLSSKINDLERELKDNKERLRLGADSDTKVNELSVELRMSKEYNGEMENELSKFRDKCEQLKEDLRKKSGELAQEKNETQRVLQQKKNAEEAFAEIKRDHEMLQTREAEKSLQLKKALDERKENGAYQQSVAKATDAEWERKMQYYEKQLEQATDDRKREEQKRTAAEFDQSRVARKLAGIEANYELLQNDYTNMKEARKDLERDLQDVIAEKRRLEIRVEQLMDSRNTDERVLNLCQEELLESQEEAKYKEDGLRGKIDGIRNELENEKMKSQTLEENLIVADKERGMLKMEVQELMQRHKWEMANKEQNLKHIENQLEELKEHSRIESTEQESNDKKTIADLNKKLELEKAHKKAVINKLEEEMAKRQPLKKGDKGITKSALIKKEREIVGFKKCRTGRILMSLQQENQHLQQKMTEMYMDSEKQGEHFSYQMQEMSQLIETLRDELKEYKDEYPQRHSVNRYEDKRSLDSREGIPTSISHQNIQIDGWLSLRDMTKKSRKPKVVFKKKSDHQLTLFFQWTNYFVILNEYAFTIYTDEKHLNSVVLTIEAGAMAHVRHVTSADLRNVDDNQLPKIFHIMYDDTSSNSSRHASNSDLSICEPREEGWKRHDFQELSYHTRTYCDDCGKKLSDFIRPTPAFECKNCHYKTHKEHIAQGTITMCRYTGLSRELVLMGTHKEVCNQWVSQLRRFIEASRPANVSVSRVSSRRHVGGPGSSA
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Negatively regulates mel-11 to relieve the inhibition of mlc-4, allowing contraction of the circumferentially oriented microfilaments in epidermal cells and thereby regulating myosin II contractility during spermathecal contraction, cleavage furrow contraction in early embryos, and embryonic elongation and morphogenesis. Required for P-cell migration. May also play a role in oocyte cellularization (By similarity).
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A8WWH5
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POP1_CAEBR
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Protein pop-1 (Posterior pharynx defect protein 1)
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MMADEELGDEVKVFRRDEDADDDPMISGETSEQQLADDKKDAVMEAELDGAGRVPLIGGLKAEIKAEPSPSFPMPSMLPCGPYSPFSGLPIMFPMVVPQYLSPNPNINMMNMMTMRAAMAGAPLSPAFPAMFSPNPLFPFPGVVAKQHLENTMPMHMRAGPLSSLNHMKMPPYMPHQMMPQHNERRGHGGGKVKKEDHIKKPLNAFMWYMKENRPKLLEEVGNDQKQSAELNKELGKRWHDLPKEEQQKYFEMAKKDRESHKEKYPQWSARENYAVNKKKPKRKRDKSVVSGSENNDQKKCRARFGVTNTSMWCKPCQRKKKCIYATDRSGSELNDGHDGRGTSGGCSSSSESSSPNNNQPMPMNAPQTVAAMHAMLMGMQIGQSAHLASSHSTGSSGTSPPVANPSDSESDVDEDEDIDPTITQQTQEYIMQESVCTL
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Part of the Wnt signaling pathway essential for the specification of the mesodermal cell fate in early embryos (By similarity). Required for asymmetrical division of somatic gonadal precursor descendants which initiate axis formation required to control organ shape (By similarity). Similarly, involved in asymmetrical division of seam cells, a stem cell-like lineage (By similarity). Represses expression of target genes via its interaction with hda-1 histone deacetylase (By similarity). Required for specification of the M lineage-derived coelomocyte and sex myoblast fate (By similarity). Regulates coelomocyte fate by positively regulating proliferation and ceh-34 and possibly eya-1 expression in M.dlpa and M.drpa precursors (By similarity).
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A8X181
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FICD_CAEBR
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Protein adenylyltransferase fic-1 (EC 2.7.7.108) (De-AMPylase fic-1) (EC 3.1.4.-)
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MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIPGQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDGNLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHDLRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHHEISIDDILEMHRRVLGNADPVEAGKIRTTQVYVGKFTPVAPEYVLEQLADMVDWLNDESTMAMDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSGNVINGEEPNLTAEESKVSEKIETECRAGS
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Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-273 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2. Can AMPylate core histone H3 in vitro (By similarity). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (By similarity).
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A8X3A7
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PAT2_CAEBR
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Integrin alpha pat-2 (Paralyzed arrest at two-fold protein 2)
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MREGSFPRRTRLLCLLAAVVLISTVTSFNIDTKNVVLHHMANNYFGYSLDFYNEQKGMPVLVVGAPEAETTNPNLSGIRRPGAVYACSVNRPTCREVHVDKMKGNLKKLNGSHLVPIEDKAYQFFGATVKSNDKHDKLLMCAPKYKYFYSKFEVIEPVGTCFYAENGFEKTEEFSSCKQEPARHGRHRLGYGQCGFSGAIPGKKNQDRVFLGAPGVWYWQGAIFSQNTKNQTDRPNTEYGSKEYDHDMMGYATATGDFDGDGIDDIVAGVPRGNDLHGKLVLYTSKLKMMINLTDEVSTQHGQYCGGALAVADVNKDGRDDIIMGCPFYTDYGSVKDAKTQERKPQYDVGKVIVFLQTAPGVFGKQLAVVGDDQWGRFGHSLAAAGDLNLDGYNDVIVGAPYAGKNKQGAVYVIHGSKDGVREKPTQKIEASQIGHGTARAFGFAVAGGVDVDGNGMPDIAVGAWKSGNAAVLLTKPVVTVTGATEPESALINVEEKNCDVDGKLGKQACRHINTCFKYEGKGDTPNDLEFDLRFNLDDHSPEPRAYFLQKDVKSDRSIKVASGSKTRDHPSSIEQRVRLEKGRQKCFRHRFFASSTMKDKLSPIHWSVNYTYVESKSGKLRGDKLEPAIDTTVPLSFQNKINIANNCGKDDLCVPDLKVTAVADREKFLLGTQDNTMLINVTVQNGGEDSYETKLYFDVPQGFEYGGIESVGADGSAPACSPTSDEPDSDGKWTFACDLGNPLPANKVVSSVVRVTASSDKPPLAPISINAHVNSSNDEEAHTIADNKVTFTIPVDFKNQLSLNGRSNPEQVDFSMTNKTRSDVFDDNEIGPVVSHLYQISNRGPSEIDAATLDIFWPSFSTEGGHLLYIITEPVVNPPNKGRCRVKQLQNVNPLNLRITNEHVPTEPPVAKTPNEYSREEDDESYEDETTTQSQTHHQTRTEHTQHHQGPVHVYERDEDKIRQNTGNWQYVEDKKKKGDYEYIPDDQEYDGDDFEDDDEDFDRAGSKRVKRAPVPKKKKKEGSRSGEPRSDKARFSDLREAVKLSKEAGGVVDYKGPLSRASVDCNGLRCTHIECDIYDLKEDEFVLVEIFSRLYTNTLVDERNPGGDISSLALARVTSTKYNWPHKPTLITAVSTNMNAIASEEGRDLPWWLYLLAILIGLAILILLILLLWRCGFFKRNRPPTEHAELRAEKQPAAHYADTQSRYAPQDQYSQGRHGQML
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Required for muscle development probably through the regulation of the actin-myosin cytoskeleton. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably through lamins such as epi-1, lam-2 and unc-52. Required for distal tip cell migration and dorsal pathfinding. Required for egg-laying. May play a role in cell motility and cell-cell interactions.
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A8X811
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WRM1_CAEBR
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Armadillo repeat-containing protein wrm-1 (Worm armadillo protein 1)
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MEERGPDIEKYGSQPCTPLSFDPMLPSTSRVATPVRPSSTLSARQAPASPFRAQPQNMEPSISRVHELREGAAVKRSYTNDWMQGNYIPPNPQQQQYQRPPSMIGSTISNMSNLSHMTKFSALSVNTQCGQFDNWIYQSQPALSKVSHSSVENQDPMKRRERMSIPEIVQSLASYEMSDQVAAIRELEPLAKAEALESTYCQADLGKIINALFEVLVPRPQENENVIRKVFEILHRAAVPKHVRMTEKIFHSLNLELMNTNSSKHSFQVPRPYSIYELVIERASRLDTAYDQAAMLLLAQICCKPFFMKYVFSEKEQSAGHRRLHEVVMQFAIKNLQQQETKRKSKGFCVSIIKNLSRRNRSIWSIVYELHVIPIFHDIIKDEYSDEDLLWPTMQALTTFCSIERVGEDFVKLGGAQDLCNLLYHGSTRLLHELLACMQRLSLLQEIGNQDMEESIRRVIQVVGSDDATIAERATGVLRNIGQPNKQNKVIMVRNGVTAHAIAVLRTSMRFQSQLREQQNARTPKNQIDAAKNQILSIYENCLSILNNVTKMGKDDILDSAIQACRMISANPDAAIVLLHFLNAGAPKCRKLAVNVMKRVIENVPAFAEPFVDLPGTTQETLPILLLKRAYESLDEWKKAVVEVMRSEPNTQQFRDAIEKRQDHEDIVWKSVSLLSNLCRNGNPRFFERVKVEMLYTRPTNPFTSLFPEMSDVILYEWLDFILAICGTEWSLQNCLMYHFLKQANITHEYLLHYRRPNPQICDKIKNIIDTGMRQQQQHNQLEQMAMMHAQQQHQQLPM
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Antagonistic role in the Wnt signaling pathway that operates in embryogenesis (By similarity). When located at the cortex it has been shown to inhibit Wnt signaling during asymmetric cell division but when relocated to the nucleus it shows positive regulation (By similarity). Has a role in blastomere signaling during endoderm specification (By similarity). Component of the beta-catenin-lit-1 complex which promotes phosphorylation, down-regulation and subcellular relocation of pop-1 (By similarity). Within the complex, activates lit-1-dependent kinase activity (By similarity). Can substitute for bar-1 indicating functional redundancy (By similarity). Appears to have a role in centrosome positioning (By similarity). Involved in the development of distal tip cells (DTC) by regulating the asymmetric distribution of cye-1 and cki-1 between the daughters of Z1.a and Z4.p cells (By similarity).
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A8Y987
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VP2_POVSM
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Minor capsid protein VP2 (Minor structural protein VP2)
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MGALLAVLAEVVELASVTGLSVESFISGEAFATAELLEAHIANLVTVGGLTEAEALAATEVPAEAYAALTSLSSTFPQAFTAVAATELATTGTLTVGATVAAALYPYYYDYSTPVANLNRGLNPEMALQLWFPEIDYEFPGLMPFVRFINYIDPTQWATNLFETIGRYSWESAQRYGQNLIAHEVRSASRELATRTAQGFSEAVARYFENARWAVSTLPRSLYSGLQSYYEQLPSLNPMQVRDLHRRLGQPIPNRIALEEQAIKSAEYVQKVDPPGGANQRIAPDWLLPLILGLYGDISPSWESTLEDIEEEEDAPQKKKRKRTKKNTPRSA
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[Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity).
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A8YPR6
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SVMI_ECHOC
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Snake venom metalloprotease inhibitor 02D01 (02E11) (10F07) (Svmpi-Eoc7) [Cleaved into: Tripeptide pEKW 1; Tripeptide pEKW 2; Tripeptide pEKW 3; Tripeptide pEKW 4; Tripeptide pEKW 5; Tripeptide pEKW 6; Tripeptide pEKW 7; Tripeptide pEKW 8; Tripeptide pEKW 9; Tripeptide pEKW 10; Tripeptide pEKW 11; Poly-His-poly-Gly peptide 4 (pHpG-4); Poly-His-poly-Gly peptide 3 (pHpG-3); Poly-His-poly-Gly peptide 2 (pHpG-2); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (CNP)]
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MFVSRLAASGLLLLSLLALSLDGKPLPQRQPHHIQPMEQKWLAPDAPPLEQKWLAPDAPPLEQKWLAPAAPPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAAPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWQPQIPSLMEQRQLSSGGTTALRQELSPRAEAASGPAVVGGGGGGGGGSKAALALPKPPKAKGAAAATSRLMRDLRPDGKQASQKWGRLVDHDHDHHHHHHPGSSVGGGGGGGGGGARRLKGLAKKGVAKGCFGLKLDRIGSMSGLGC
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pEKW and poly-His-poly-Gly peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the prey.
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A8YPR9
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SVMI1_CERCE
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Snake venom metalloprotease inhibitor 02A10 (01F09) [Cleaved into: Tripeptide pEKW 1; Tripeptide pEKW 2; Tripeptide pEKW 3; Tripeptide pEKW 4; Tripeptide pEKW 5; Tripeptide pEKW 6; Tripeptide pEKW 7; Tripeptide pEKW 8; Tripeptide pEKW 9; Tripeptide pEKW 10; Tripeptide pEKW 11; Tripeptide pEKW 12; Tripeptide pEKW 13; Tripeptide pEKW 14; Tripeptide pEKW 15; Tripeptide pEKW 16; Tripeptide pEKW 17; C-type natriuretic peptide (CNP)]
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MSVSRLAASGLLLVSLLALALDGKPVEKWSPWLWPPRPRPPIPPLQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWQRPLQPEVPSLMELHQERQKQGRMMHHDEDPGDAAEGPRRQKKEPGKPEGNGCFGKKIDRINAGFGCPKLPPSGGH
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pEKW peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the victim.
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A8YZP8
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HCHA_STAAT
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A9BHI9
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GPGS_PETMO
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Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266)
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MKDNILKRSFHHSKFENIKELVKLKEKQDVKISLAFPSLNEEKTIGKEIIIMKSELMEKYPLLDEIAVIDSGSEDETVSIAKEYGAKVFYSSDILPEYGFYKGKGENLWKSLYALDGDIIVWVDSDIENIHPKFVYGLVGALLNYPEIGYVKAFYDRPIVGKSAMQPTGGGRVTELVARPLFSLFYPELSTIIQPLSGEYAGRREILEKLPFFVGYGVEIAHLIDIAEKFGSEIIAQVDLELRIHDNQPLHSLSKMAFELTKVVLKRLEKYGKLDLNTELTDKHIMIQKKENEKVLVPTEILSVERPPMITIPEYKEKFSKEEKV
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Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). UDP-glucose is the preferred substrate, but it can be partially replaced by ADP-glucose.
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A9C3R8
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RP65C_DANRE
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Retinal Mueller cells isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl ester 13-cis isomerohydrolase C) (EC 3.1.1.90) (All-trans-retinylester 11-cis isomerohydrolase C) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein homolog C) (RPE56c)
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MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGEIPAWLSGSLLRMGPGLFEVGDEPFYHLFDGQALLHKFDLKDGRVTYHRRFIRTDAYVRAMTEKRVVITEFGTTAYPDPCKNIFSRFFTYFQGIEVTDNCLVNIYPIGEDFYACTETNFITKVDPDTLETVKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEDKSDQFEKSKILVQFPSSERFKPSYVHSFGITENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDKMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMRSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPVTLHGIYKP
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Catalyzes both 11-cis retinol and 13-cis retinol, 2 stereoisomeric forms of retinoic acid from all-trans-retinyl ester. Acts as an alternative isomerohydrolase in retinal Mueller cells by catalyzing formation of 11-cis retinol, to meet the high demand for the chromophore by cones. Capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity).
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A9C3R9
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RP65B_DANRE
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All-trans-retinyl ester 13-cis isomerohydrolase (13cIMH) (EC 3.1.1.90) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein homolog B) (RPE56b)
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MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGKIPAWLSGSLLRMGPGLFEIGDEPFNHLFDGQALIHKFDLKDGRVTYHRKFIRTDAYVRAMTEKRVVITELGTAAYPDPCKNIFSRFFTYFQGTEVTDNCSVNIYPIGEDFYACTETNFITKVNPDTLETIKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEEKSDPLAMSKVLVQFPSSERFKPSYVHSFGMTENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDRMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMCSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPLTLHGIYKP
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Specifically generates 13-cis retinol, a stereoisomeric form of retinoic acid. Capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity).
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A9CB27
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ZPR1_PAPAN
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Zinc finger protein ZPR1 (Zinc finger protein 259)
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MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPAEKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLASQR
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Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death (By similarity).
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A9CH28
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DPES_AGRFC
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D-psicose 3-epimerase (DPEase) (EC 5.1.3.30)
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MKHGIYYSYWEHEWSAKFGPYIEKVAKLGFDIIEVAAHHINEYSDAELATIRKSAKDNGIILTAGIGPSKTKNLSSEDAAVRAAGKAFFERTLSNVAKLDIHTIGGALHSYWPIDYSQPVDKAGDYARGVEGINGIADFANDLGINLCIEVLNRFENHVLNTAAEGVAFVKDVGKNNVKVMLDTFHMNIEEDSFGDAIRTAGPLLGHFHTGESNRRVPGKGRMPWHEIGLALRDINYTGAVIMEPFVKTGGTIGSDIKVWRDLSGGADIAKMDEDARNALAFSRFVLGG
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Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose. The substrate specificity decreases in the following order: D-fructose, D-tagatose, D-ribulose, D-xylulose, and D-sorbose. It shows a higher level of activity for cis ketoses than for trans-ketoses.
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A9CH39
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PHRB_AGRFC
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(6-4) photolyase (EC 4.1.99.13) ((6-4)DNA photolyase) (DNA photolyase PhrB) (Photoreactivating enzyme PhrB)
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MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWLAGPDYVDSNFFENDRSLPVFYWTGKTHMNCMAKVITETIENAYAHHIQRLMITGNFALLAGIDPKAVHRWYLEVYADAYEWVELPNVIGMSQFADGGFLGTKPYAASGNYINRMSDYCDTCRYDPKERLGDNACPFNALYWDFLARNREKLKSNHRLAQPYATWARMSEDVRHDLRAKAAAFLRKLD
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Photolyase involved in the repair of UV-induced (6-4) lesions in DNA. Catalyzes the photoreactivation of (6-4) pyrimidine-pyrimidone photoproducts by using blue-light energy. Can repair (6-4) photoproducts in ssDNA as well as in dsDNA.
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A9CK16
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TADA_AGRFC
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tRNA-specific adenosine deaminase (EC 3.5.4.33)
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MAERTHFMELALVEARSAGERDEVPIGAVLVLDGRVIARSGNRTRELNDVTAHAEIAVIRMACEALGQERLPGADLYVTLEPCTMCAAAISFARIRRLYYGAQDPKGGAVESGVRFFSQPTCHHAPDVYSGLAESESAEILRQFFREKRLDD
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Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2). {ECO:0000255|HAMAP-Rule:MF_00972, ECO:0000269|PubMed:16142903}.
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A9CMA6
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TM163_RAT
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Transmembrane protein 163 (Synaptic vesicle membrane protein of 31 kDa)
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MERAPGSERRSPPGPGVPRPPPRGHAPSTAAPAPNPAPLSSSMQPDEERQPRISESGQFSDGFEDRGLLESSTRLKPHEAQNYRKKALWVSWLSIIVTLALAVAAFTVSVMRYSASAFGFAFDAILDVLSSAIVLWRYSNAAAVHSAHREYIACVILGVIFLLSSICIVVKAIHDLSTRLLPEVDDFLFSVSILSGILCSVLAVLKFMLGKVLTSRALITDGFNSLVGGVMGFSILLSAEVFKHNAAVWYLDGSIGVLIGLTIFAYGVKLLIDMVPRVRQTRHYEMFE
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Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By similarity). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (By similarity).
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A9JRL3
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CBPC1_XENTR
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Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein 1) (Protein deglutamylase CCP1)
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MSKAKATADKCLSNNSRIQSLLSQLEKVNAEPLLFDSDNTRYVTAKILHLAQTQEKTRKEIAAKGSTGMEVILCTLENTRDLQTILNILNILNELASTAGGRRINALISKGGSRILLQLLLSASKESSSNEELMMVLHSLLAKVGPKDKKFGIKARVSGALNISLNLVKQNLQNPRLILPCLQVLRVCCMNSVNSVYLGKNGAVEILFKLIGPFTRRNTGLIKVSLDTFAALLKSKTNARKAVDRGYVQALLSIYTDWHRHDTRHRHMLIRKGILQCLKSITNIKIGRKAFIDANGMKTLYNTSQECQAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSAFQFQLPIMPTSGPVALLYSMPPEVDDVVDESDDNDDTEAETEAEAENEESDQLCKNDDIETDITKLIPGQELGRTLEDLKMYERFFPELTEDFQEFDLVSNEPKPGAKLGPIIVPTAGEEQPEVPNNFMKDLEKRSCNISLEDECNKRPTFLDMPKNVTNKGNDGLGQQVHGDIDRSCYYFSSDIVKDLEKLSLRKPSGNHPCRNGCVSAKDKPIFLPHPCNKSTSNSGSCSNNLFEKHSMHLSPLCCSGITPDDDESSPLDELAMREITDFDNLLPLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHVPPFFKERLLERPYGVQRSKIFQDIERMIHPNDIIDRVVYDLDNSSCSAQDESEVLKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRTGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALASRPWWYRVGMDICYYKNHFSRSSIATGGQKGKSYYTITFTVTFPHRDDVCYFAYHYPYTYSTLKMHLKKLESLHNPQQVYFRQEVLCETLGGNGCPVITITAMPESNYYEHVYQFRNRPYIFLSSRVHPGETNASWVMKGTLEFLMGSSTSAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQNPNVDLHPTIYHTKGLLQYLAAIRRTPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNANAASCDMVEDSGYRTLPKVLNQLAPAFSMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKDLQIGTKELEEMGAKFCVGLLRLKRLTSPMELTLPPSLIDIENELIESSCKVASPTTYVLEDDEPRFLEEVDYSAESNDDADPDLPDTIGDFENTALEEEGFSDSEITRTHTSGQST
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Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins.
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A9KU91
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FADB_SHEB9
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLASLDAALDSIKQDSNIKALVLTSSKDTFIVGADITEFLGLFAQDDAVLLSWVEQANAVFNKLEDLPFPTASAIKGFALGGGCETILATDFRVADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRAEDALKVGAVDAVVAPQALEAAAIQMLKDAVAEKLDWQARRNRKLSALTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVIEQASTKGRAEALQIEHQAFIKLAKTDVAKALIGIFLNDQFVKGKAKKAGKLAKEVNNAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLNEAAKLLSAQVARGRSTPEKMAKVLNNITPSLDYAAIKHSDVVVEAVVEHPKIKAQVLAEVEGYVSEDAIIASNTSTISINLLAKSMKKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLAEGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGTDAIDVMFENKRLGQKNGKGFYVYSVDSRGKPKKDVDPTSYGLLKDAFGELKAFEADDIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRTLAANNGSYYQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A9LLI7
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RP6L2_ARATH
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Protein RRP6-like 2 (AtRRP6L2)
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MSDGNMDVDESPVSWKVKSLEKLIDGSSFSSTLSRLSSSSRLIPTSRDFHFYYNFDEFKRPIDEITGTSQSTLATIGDSEQVWGKSMKFPGDVDDVYAEDWLCNVNDELIERFDVSVDEFQRIRKKEKEIGRSVVADDGDDGFQMVYGKKKKPVGNVVTGSAAVNGGGSVIDVKMAERDKNSSGKAKVPFHVPTIKKPQEEYNILVNNANLPFEHVWLERSEDDLRAMHPLEKFSVLDFVDKDVNEMEPVKPLPLEQTPFKFVQEVKDLKELVAKLRSVEEFAVDLEHNQYRSFQGLTCLMQISTRTEDYIVDTFKLRIHIGPYLREIFKDPKKKKVMHGADRDIIWLQRDFGIYVCNLFDTGQASRVLNLERNSLEFLLQHFCGVTANKEYQNADWRIRPLPEEMTRYAREDTHYLLYIYDLIKLELQRMAKDDAHTDSPLLEVYKRSYDVCTQLYEKELLTENSYLHVYGLQAAGFNAAQLAIVAGLCEWRDFIARAEDESTGYVLPNKVLLEIAKEMPDSVGKLRRMLKSKHPYIERNVDSVVSVIRQSMQHYAAFESAALSLKDVSPGNVMDKNIEPISEKKDLHTGDVASPSLKENSSQLESTRDLIMGAANTNEGRGLGSGLFGSAKVSAAVRISKKPSSGLGALLGNAASKKKSRTDEKVKEDVKLEQIRSSVNLSFHSFTEKVPDSKSTSETSPKVYGKPEEMSSTMPASVSKEDGVKELKDDSEEASEIVGTSGRVSESKVSSSEMGDIILLENGDEKKVDAEDEPMSLSELSTNFQKCFKSMNKSKKAQKQTEFLNIEPFDYEAARKEVKFGEGHKGRQGKREAAAGQKKGSTQEQSEFGQGKRRQAFPASGNRSMSFKN
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Acts as an important epigenetic regulator through multiple silencing mechanisms. Involved in association with RRP6L1 in the silencing of the solo LTR locus. Controls levels of non-coding RNAs (ncRNAs) from the solo LTR locus. Seems to function independently of the RNA-mediated gene silencing (RdDM) pathway. Functions redundantly with RRP6L1 in the regulation of FLC locus. Participates in the maintenance of trimethylated 'Lys-27' (H3K27me3) at FLC locus via the regulation of antisense long non-coding RNAs (lncRNAs) and the regulation of diverse antisense RNAs derived from the FLC locus. Seems not involved in the exosomal RNA degradation. May be involved in poly(A)-mediated RNA degradation.
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A9LNK9
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CPSF_ARATH
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30-kDa cleavage and polyadenylation specificity factor 30 (EC 3.1.21.-) (Protein OXIDATIVE STRESS TOLERANT 6) (Zinc finger CCCH domain-containing protein 11) (AtC3H11)
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MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYGRNFSVKWLKLCELSFHKTRNLRNPYNENLPVKISRDCQELEPSVGEQLASLLYLEPDSELMAISIAAEAKREEEKAKGVNPESRAENPDIVPFEDNEEEEEEEDESEEEEESMAGGPQGRGRGRGIMWPPQMPLGRGIRPMPGMGGFPLGVMGPGDAFPYGPGGYNGMPDPFGMGPRPFGPYGPRFGGDFRGPVPGMMFPGRPPQQFPHGGYGMMGGGRGPHMGGMGNAPRGGRPMYYPPATSSARPGPSNRKTPERSDERGVSGDQQNQDASHDMEQFEVGNSLRNEESESEDEDEAPRRSRHGEGKKRR
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Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection. Binds RNA in a calcium-dependent manner. Exhibits endonuclease activity with an ability to nick and degrade linear as well as circular single-stranded RNA that leaves RNA 3' ends with hydroxyl groups, thus mediating processing of the pre-mRNA as a prelude to the polyadenylation. Involved in the post-transcriptional control, probably via poly(A) addition, of the responses of plants to stress, especially genes mediating tolerance to oxidative stress. Plays a role in the regulation of salicylic acid (SA) production via the control of messenger RNA 3' end processing, thus being a key component of programmed cell death and plant immune responses required for resistance to virulent Pseudomonas syringae pv tomato DC3000 (Pst).
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A9MYB0
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FADB_SALPB
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALEVLEKQHDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRMLGADSALEIIAAGKDVGAEHALKIGLVDGVVKQEKLIEGAIAVLRQAITGDLDWRAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMTAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDIETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLNLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPETVLASNTSTIPIGELASALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKEYRDAIDALFDASRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLASVSQPKRDFSDDEIIARMMIPMINEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTQGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGSLKTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A9NJG2
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13S_FAGTA
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13S globulin seed storage protein (13S globulin) (Legumin-like protein) (Major allergen Fag t 1) (TBt) (allergen Fag t 1) [Cleaved into: 13S globulin seed storage protein acidic chain (13S globulin TBb chain) (34 kDa allergenic protein) (Allergen b) (N-terminal subunit TBb) (TBb); 13S globulin seed storage protein basic chain (13S globulin TBa chain) (Allergen a) (C-terminal subunit TBa) (FTAP) (Major 24 kDa allergenic protein) (TBa)]
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MSTKLILSFSLCLMVLSCSAQAAQLWPWRKGQDSRPHHGHQQFQQQCDIQRLTASEPSRRVRSEAGVTEIWDHNTPEFRCTGFVAVRYVIQPGGLLLPSYSNAPYITFVEQGRGVQGVVIPGCPETFQSDSEYPQSQRGQHSRESESQESSRGDQHQKIFRVREGDVIPSPAGVVQWTHNDGDQDLISVTLLDANSFHNQLDENVRSFFLAGQSQQGREERRSQQQTREEGGDRQSRESDDVEALIGANILSGFQDEILHELFRDVDRETISKLRGENDQRGFIVQAQDLKLRVPEDSEEGYERQRGDRKRDERGSGRSNGLEQAFCNLKFRQNVNRPSHADVFNPRAGRINTVNSNNLPILEFLQLSAQHVVLYKNAIIGPRWNLNAHSALYVTRGEGRVQVVGDEGKSVFDDNVQRGQILVVPQGFAVVVKAGRQGLEWVELKNNDNAITSPIAGRTSVLRAIPVEVLANSYDISTEEAYKLKNGRQEVEVFRPFQSRYEKEEEKERERFSIV
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Seed storage protein.
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A9Q751
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PCDP1_MOUSE
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Cilia- and flagella-associated protein 221 (Primary ciliary dyskinesia protein 1)
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MEVVKSPMQELQQAKEPFDTMSPLLLKSLVEEPKKRTEVPNHLLESRVYAKLLNNKVIQARPGIVHFGGYEIESKHQQILNIANISDEDTHLHILPPQTKYFQINFEKKEHRLIPGLSLTVTITFSPDEWRYYYDCIRIHCKGDDTLLVPIHAYPVLNNLDFPTFINLSDVFLGESKSYVIPLQCSCPVDFEFHITLLRSHQAFTIEPKSGIIPANGKAKVTVKFTPIQYGMAQIKIQLWISQFNSQPYECVFTGTCYPNMALPLEEFKRLNTRSKKVNVPLEKTTYVQFYPAPAKAKPQKLKEIDYQDLRFPADLSNPFAVATVLNQEPGKLKIKELKQVLDQGDEISKTRQMKEAIFEQKVRQDILTEIENHLKWQVHLGKEHTTYRFKRELTEEWKKARAKYKQNRGDPVEGEELQRLQTEQSQKRIVRDLKGKRQEFHPNFDPLVNNVWLTRHRAQRRFQQAARKIMLERRLLSMLGAIRGMDKESILRKIIQVNGKLIQGENPSRGRRAHLKQEDNIWRYSLESEEVLHFAFPTDSESYNELALDGLGLVPIKSPEIQIKHSYPYFTLKVPQLYKIKGYHPFSVNKSSTNYRLQKLARPLKHGAEDEVTTIITIPKKDTTPLSAKPSILSMKPPEGLAMSVEYDPLYIFNPSPGLFAVKHPLTYAETLIDYHLCSHPKYKYTQESHMGSSIPLTQRQFLHHTDIIPGIMNWKKFQPLVFSSMSDPSMVEATQRSDWYSSVMLPIDVPAPLEDLPEEDRLETTERDLCDQGIEVMLTPEMVQVEFPMLIHRDSKKEKDFKDSTQLPEKVGERVQEEMKNLRSKALNTYLILD
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May play a role in cilium morphogenesis.
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A9QA56
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ABC3H_FELCA
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DNA dC->dU-editing enzyme APOBEC-3H (APOBEC3H) (EC 3.5.4.38) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H) (A3H) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3Z3) (A3Z3)
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MNPLQEVIFCRQFGNQHRVPKPYYRRKTYLCYQLKLPEGTLIHKDCLRNKKKRHAEMCFIDKIKALTRDTSQRFEIICYITWSPCPFCAEELVAFVKDNPHLSLRIFASRLYVHWRWKYQQGLRHLHASGIPVAVMSLPEFEDCWRNFVDHQDRSFQPWPNLDQYSKSIKRRLGKILTPLNDLRNDFRNLKLE
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DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). Exhibits single-stranded DNA deaminase activity (in vitro). Incorporates into the released virions of the virion infectivity factor (vif)-deficient feline immunodeficiency virus (FIV) and suppresses FIV infectivity, probably in a deaminase-dependent manner (in vitro). Induces G-to-A hypermutations in vif-deficient FIV (in vitro). The APOBEC3H/APOBEC3Z3 haplotype 5 exhibits antiviral activity against vif-proficient FIV, strains Petaluma, C36 and Shizuoka (in vitro). Does not exhibit inhibitory activity against feline leukemia virus (FeLV), feline endogenous retrovirus (RD-114 virus) or a long interspersed nuclear element-1 (LINE-1) retrotransposon (in vitro).
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A9QM73
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SMG7_ARATH
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Nonsense-mediated mRNA decay factor SMG7 (Protein SMG7) (SMG7 homolog)
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MMTLQMDKTTASSSWERAKSIYDEIAELANKRQKAGNPPDPNLLQLLREKYEAIILESHTFSEQHNIEIPLWQLHYKRIEYFRLHINRVLASSTSTAAQNVKGPSKAEQIAQLKLQFRTFLSEATGFYHDMILKIRSKYGLPLGSFSEDQQSQNLSDKDGKELAEVQKALKSCHRCLIYLGDLARYKGMYAEGDSRSRQYASASSYYLQAASLWPASGNPHHQLAIVASYSRDEFVTTYRYFRSLAVEYPFPTARDNLIVAFDKNRQSYEKLFVPSKDSSKRLTGKGRGKGADISLKDATLVAGPEKDKVTIANEMLKAFSIRFVHLNGILFTRTSLETFFDVLASTSSSLREVISLGSAKELTLGIDTSDSALFIVRVVTMLIFSVHNSKKETEGQSYAEIVQRVEPARNSLTASFELLGLVIEKCVQLGDPSSSYFLPGVLVFVEWLACCPDIALGSDPDDRQTAVRNSFWNQFVVFFNQVLSLGPTFIDDVEDETCFSNMSLYDERETENRLALWEDYELRGFLPLLPAQTILNFSRKHSFGTEGPKEKKARIKRIFAAGKALTSVIKVDQNHVYFDSKKKKFLVGVKPADDFLDSHSSPPKACNALQDNQVMIDHNSPIMQLDQQIYMGEEDDDDEVIVFKPLVTEKRKEASDQIYVPSGGFRKSDQVTTMGDFKALSGSDVAFHENQILQARGNASIQVPASVGANLLGPLQPSTQSQAMHMQQVQTQVQVPASVGANLLGLLLTSTQSQAMHMQQVQTQAVNPQPAQSLAASRLQPIQSQVAQPLPSRVVHFQQTQAQVSHVSPAHSQSTSFGGGSKWSPEEAASLASSLSGFAQLGNGHVMRNEMQGNHGVSYYPAHSLPVHQSYNGNGMGGMPYSQSRTPEAVFPPKIDPVLSSGVVADGLGVQSSLAKKNPISRAFRHLGPPPGFNSVPAKLQKEPAPGSELSGNNHLPVDDYSWLDGYQAQSSRGVGLNSSLNYATSGKPEHLGSTGNGLNGPANFPFPGKQVPTSQVQADFPYFQNPQKDNFVDKNHQSTQLPEQYQGQSTWSSRHFV
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Plays multiple roles in growth and development. Involved in nonsense-mediated mRNA decay (NMD). May provide a link to the mRNA degradation machinery to initiate NMD and serve as an adapter for UPF proteins function. Required for meiotic progression through anaphase II of pollen mother cells. May counteract cyclin-dependent kinase (CDK) activity at the end of meiosis. May play a role in plant defense through its involvement in NMD. Together with EXA1, helps to restrict cell death induction during pathogen infection in a salicylic acid- (SA) and reactive oxygen species- (ROS) independent manner.
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A9QM74
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IMA8_HUMAN
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Importin subunit alpha-8 (Karyopherin subunit alpha-7)
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MPTLDAPEERRRKFKYRGKDVSLRRQQRMAVSLELRKAKKDEQTLKRRNITSFCPDTPSEKTAKGVAVSLTLGEIIKGVNSSDPVLCFQATQTARKMLSQEKNPPLKLVIEAGLIPRMVEFLKSSLYPCLQFEAAWALTNIASGTSEQTRAVVEGGAIQPLIELLSSSNVAVCEQAVWALGNIAGDGPEFRDNVITSNAIPHLLALISPTLPITFLRNITWTLSNLCRNKNPYPCDTAVKQILPALLHLLQHQDSEVLSDACWALSYLTDGSNKRIGQVVNTGVLPRLVVLMTSSELNVLTPSLRTVGNIVTGTDEQTQMAIDAGMLNVLPQLLQHNKPSIQKEAAWALSNVAAGPCHHIQQLLAYDVLPPLVALLKNGEFKVQKEAVWMVANFATGATMDQLIQLVHSGVLEPLVNLLTAPDVKIVLIILDVISCILQAAEKRSEKENLCLLIEELGGIDRIEALQLHENRQIGQSALNIIEKHFGEEEDESQTLLSQVIDQDYEFIDYECLAKK
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Functions in nuclear protein import.
|
A9QT41
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NEMO_PIG
|
NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
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MSRTPWKSQPCEMVQPSGGPAGDQDVLGEESSLGKPTMLHLPSEQGAPETFQRCLEENQELRDAIRQSNQMLRERCEELQRFQGSQREEKEFLMQKFCEARRLVERLSLEKLELRRQREQALQEVELLKTCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQALESRVRATSEQVRQLENEREALQQQHSVQVDQLRLQSQSMEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVSSERNRGLQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREQLAERKELLQEQLEQLQREYSRLKTSCQESARIEDMRKRHVEVSQPTLPPAPAHHSFHPALPSQRRSPPEEPPNFCCPKCQYQAPDMDTLQIHVMECIE
|
Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response this function requires 'Lys-27'-linked polyubiquitination.
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A9RA84
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HMGB1_PAPAN
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High mobility group protein B1 (High mobility group protein 1) (HMG-1)
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MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE
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Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.
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A9RVK2
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M3K1B_PHYPA
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Mitogen-activated protein kinase kinase kinase 1b (PpMEKK1b) (EC 2.7.11.25) (MAP kinase kinase kinase 1b)
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MVEERGSSRSSRGGSWGSGEDGGSSHGGKGVPKLSRTVAKKIHKYDVSADHSDYEDDGSVHSTSSSGSRRNPLSKSIIQQQSFRVGANFEEDLKTLYELIGVSKPADLAISASDWQSRGKSIAYSQPLSSPSLSQEHGEASHSNDLKPSIIDFRSEAPAASPRELPVAPVKLDAHERMTYRSDYVNSQPQNHYGRKNSPSQRSPPPESFPAFDSSPSRLGREGYGLHRMQSDPVMPTLGALSPLGTGNAHPESAGSTATRRWSFDLVPGNHEGDYANMSQVVRDNLPSAAVAMPKNGLVRRSPIIRDPNRSNSSVSNPYAQRQYPNLAEEAESSAKPESSAIPDSSAMPELPAKLESTAVPELSAKPESNAKPESEPEQDSSVEARTEHYGSVRKSKIPSALIIDKFEEPSIVSTGRSPGVVSKRPPWDTWFKGDFIGSGTFGSVYEGIDNNGMFFAVKEVSLKDQGKVGQEAIKQLEHEIALLSDIQHPNIVQYLGTERDDEKLYIFLELVSKGSLASLYKKYYFVYDQVRAYTKQILSGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVDKLGLLKSFMGSAHWMAPEVVNPKRQYNFLADIWSLGCTVLEMATGDAPFGELECHSVLWKVGNGEGPLIPDDLEDEMKDFISKCLEVTVGNRPTCDMLLTHPFITGEPMTGPVKLVPMPELSTISEERSIDVSESPSIATSSQSGSSPSVAGDAVSPASVAVRPRSMRTLRSEFSMSSPESIAS
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The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a.
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A9S9Q8
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MPK4B_PHYPA
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Mitogen-activated protein kinase 4b (EC 2.7.11.24) (MAP kinase 4b) (PpMPK4b)
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MDVAGAGGGGAADGNIQGVPTHNGEYTQYNIFGNLFEVSRKYVPPIRPIGRGAYGIVCSAVNSETGEEVAIKKIGNAFDNRIDAKRTLREIKLLRHMDHENIVAIRDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQPLTEDHCQYFLYQLLRGLKYIHSAKVLHRDLKPSNLLLNANCDLKICDFGLARTTSETDFMTEYVVTRWYRAPELLLNCSEYTAAIDVWSVGCIFMELLNREPLFPGRDYVQQLRLITELIGSPEDHDLGFLRSDNARRYIRQLPRFARQPLDRKFPNMGPAAIDLVEHMLRFDPARRITVEEALAHPYLATLHDINDEPICHSPFEFDFEQPSFTEEHIKELIMMEAIAFNPGNVGDMMS
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The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein may act redundantly with MPK4a in innate immunity triggered by pathogen-associated molecular patterns (PAMPs). May also be involved in resistance to necrotrophic fungi B.cinerea.
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A9SIZ6
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D5FAD_PHYPA
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Acyl-lipid (8-3)-desaturase (EC 1.14.19.30) (AN Delta(5)-fatty-acid desaturase) (Acyl-lipid 5-desaturase) (Delta-5 desaturase) (PPDES5)
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MAPHSADTAGLVPSDELRLRTSNSKGPEQEQTLKKYTLEDVSRHNTPADCWLVIWGKVYDVTSWIPNHPGGSLIHVKAGQDSTQLFDSYHPLYVRKMLAKYCIGELVPSAGDDKFKKATLEYADAENEDFYLVVKQRVESYFKSNKINPQIHPHMILKSLFILGGYFASYYLAFFWSSSVLVSLFFALWMGFFAAEVGVSIQHDGNHGSYTKWRGFGYIMGASLDLVGASSFMWRQQHVVGHHSFTNVDNYDPDIRVKDPDVRRVATTQPRQWYHAYQHIYLAVLYGTLALKSIFLDDFLAYFTGSIGPVKVAKMTPLEFNIFFQGKLLYAFYMFVLPSVYGVHSGGTFLALYVASQLITGWMLAFLFQVAHVVDDVAFPTPEGGKVKGGWAAMQVATTTDFSPRSWFWGHVSGGLNNQIEHHLFPGVCHVHYPAIQPIVEKTCKEFDVPYVAYPTFWTALRAHFAHLKKVGLTEFRLDG
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Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond.
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A9SR33
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M2K1B_PHYPA
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Mitogen-activated protein kinase kinase 1b (EC 2.7.12.2) (MAP kinase kinase 1b) (PpMKK1b)
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MSRRHRTGGLRVAVPKQENSIHRFLTANGVFHDDDIQLDHMGLRVVSSESTAYANPPDAQLSLADLEAVRVLGKGAGGSVQLVRHKWTNDIYALKGIQMNINETVRKQIVQELKINQLTLHQCPYIVKCYHSFYHNGIISIVLEYMDRGSLADIIKQTKQIPEPYLAVISNQVLKGLNYLHQVRHIIHRDIKPSNLLINQKGEVKISDFGVSAVLISSMAQRDTFVGTYTYMSPERLGGQSYAYDSDIWSLGLTILECALGYFPYRPPGQEEGWNNFFMLMELVINQPPVAAPPDKFSPEFCSFIAACIQKRPGDRLSTADLLKHPFLQKYSEEEYHLSNLR
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The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin.
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A9SY39
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M3K1A_PHYPA
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Mitogen-activated protein kinase kinase kinase 1a (PpMEKK1a) (EC 2.7.11.25) (MAP kinase kinase kinase 1a)
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MIEERGSSRGSREDRGSSRGSSRGSFEDKGSSHDWKGMGGSTPRPRLTRLVAKKDRNYDAKVDSDFDDDSSVHSTSSPRLSPASSDNLSKITIGQQSFRVGGDVDNLKALYEALGATSPAALGIEASDWESRRKSAVYSRPTSPPRVSHDTGQSSYSHDFQFPASRVDSSLESPPLSPRGLAPMSPVRPIEVEWRKHRNNYAKPTISNRPGRENNPLKPSQPPPTMFPQSSGLRTPDPLPPIDTSTSRLGRESLELQNRHTTLGAYSPPGLRKVHSELTGLVSARSDGAGWASDIESAKRNEDLAVASPVFRDNLPSAAVAMPNGSLVRASFTPRDSNRMNSVRSNSHGLRWNSCHAQEAEAIAKTALEETSNGLRIEDPERIRDLEKPSPLIIEKVDEPLSEVSSSVSTESSPSVIPKRPPWDTWAKGEFLGSGTFGSVYEGVARNGTFFAVKEVNLADEGKLGRQAVKQLEREIALLSDIQHPNIVQYLGTERTEDKLYIFLELLNKGSLANLYRKYGLFYEQIKAYTEQILTGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVEKFGFAKSFVGSAHWMAPEVVDPKQQYNFAADIWSLGCTVLEMATEGPPFGELEFIAVFWKIGRGEAPLIPDDLEDELKDFIAQCLQVDASKRPTCDMLLAHPFITGEEMTGPVTQMGTPGLSTISEERSVDMSVTSSIAVSSNSGTSPRVIENLVNHLSIERRPKSMRTLRSELSMSSAESIAS
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The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1b.
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A9T142
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MPK4A_PHYPA
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Mitogen-activated protein kinase 4a (EC 2.7.11.24) (MAP kinase 4a) (PpMPK4a)
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METSSGTPELKVISTPTYGGHYVKYVVAGTDFEVTARYKPPLRPIGRGAYGIVCSLFDTVTGEEVAVKKIGNAFDNRIDAKRTLREIKLLRHMDHENVVAITDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQALTEDHCQYFLYQILRGLKYIHSANVLHRDLKPTNLLVNANCDLKIADFGLARTLSETDFMTEYVVTRWYRAPELLLNCSAYTAAIDIWSVGCIFMELLNRSALFPGRDYVHQLRLITELIGTPEDRDLGFLRSDNARRYIKHLPRQSPIPLTQKFRGINRSALDLVEKMLVFDPAKRITVEAALAHPYLASLHDINDEPASVSPFEFDFEEPSISEEHIKDLIWREALDCSLGPDDMVQ
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The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for innate immunity triggered by pathogen-associated molecular patterns (PAMPs). Involved in resistance to necrotrophic fungi B.cinerea and A.brassicicola. Involved in the transduction of signals from chitosan perception to the activation of defense genes.
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A9TXT1
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CERK1_PHYPA
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Chitin elicitor receptor kinase 1 (PpCERK1) (EC 2.7.11.1) (Chitin receptor CERK1) (LysM domain receptor-like kinase 1) (LysM-containing receptor-like kinase 1)
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MKFQMKMKSELCRTYKYWLILLVLWLSGVTQRETGVLIVDADCIPPNGCKALAYYRLKQGDDLEKLQGRFQTNNSEVLAYNPQLVDANSIQAGTNIYLPFDCLCLNGELVHRFSYTVTTNDTAEKVVDVTYQKLTTVGAVRSASNSGDLSSIYSGQSLTIPVRCYCGDPNVDPKYGLFSTYVVQADDQLTSLSTNFSVDADVISKFNSDTRNLSPDSIIFIPSKAANGSFPPFSGYVLGTVHWRSNVGIIVGVVVGGIVLAVLLLFALIFGFKHFRRRKLAKEPTMQQSGLLSSSSMAGSKPSRSGSTMLPVPKSVEFTYEELAAATDNFSLAKKIGQGGFASVYYGVIRDQKLAIKKMTLQCTKEFLAELQVLTNVHHTNLVQLIGYCTTNSLFLVYEYIENGTLDHHLRRRKSDDKPPLSWLQRVQICLDSARGLEYIHEHTKPTYIHRDIKSANILLDDNFRAKVADFGLAKLAEEGTGTGIVGTFGYMPPEYALYGEVSPKLDVYAFGVVLFEIISGRVAISSALPSENDQQSPAQNRESRTLTSFFEPVLNDPDGKTLLPKCIDPALNGEYSLDAVWKMAQLARRCTHQSPDMRPTMRFAVVQLMTLASVTQEWDVGYFSRASSQSQPPSGNDQL
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Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses (By similarity). The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for response to chitin. Is able to complement the A.thaliana cerk1 mutant.
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A9UHW6
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MI4GD_HUMAN
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MIF4G domain-containing protein (SLBP-interacting protein 1) (hSLIP1)
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MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQAREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD
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Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation.
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A9ULC7
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OSTA_XENTR
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Organic solute transporter subunit alpha (OST-alpha) (Solute carrier family 51 subunit alpha)
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MDPEQNDTKPPFNPICATRQAPYSHEILENLDITGILLFAILTFMTLVSLLVFLEEAYYMYRKIPNPKNSIIIWINAGAMMIATTSCFGMWIPRSTMFTDFTASVFLAVLIHKFQLMLVNECGGRREFLSTFGDTKLKISTGPFCCCCLCLPHKDINRKTLFILKLGTFQFAFLRPVLMFLAVVLWTNGTYMIGNSSAEKATIWINIGVGITTITALWAVGIMFNLVKDNLKEKNIIGKFAVYQFTVILSQLQTSIINILGTTGVISCVPPLPGPSRASYMNQQLLIMEMFLVTVICRVLYRRRYDDKNLLENQETNDNLRNSMMHLNGKALEDGPQSV
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Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2).
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A9ULR9
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BACD1_DANRE
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BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 (BTB/POZ domain-containing protein KCTD13)
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MSAEASGSSGGHAVTVSGSSPSSSSHVGEEKPGRSLVSSKYVKLNVGGTLHYTTVQTLSKEDSLLRSICDGSTEVSIDSEGWVVLDRCGRHFSLVLNFLRDGTVPLPDSTRELEEVLKEAQYYRLQGLVQHCLSTLQKRRDVCRGCHIPMITSAKEEQRMIATCRKPVVKLQNNRGNNKYSYTSNSDDNLLKNIELFDKLGLRFNGRVLFIKDVLGDEICCWSFYGEGRKIAEVCCTSIVYATEKKQTKVEFPEARIFEETLNILIYENGRGSGGMALLESGGVSSSGAGQSEEEGAGAGGGDRRVRRIHVRRHIMHDERGHGQQTVYKD
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (By similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission.
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A9WGE2
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CCL_CHLAA
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(R)-citramalyl-CoA lyase (EC 4.1.3.46)
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MEAVTIVDVAPRDGLQNEPDVLEPATRVELIERLLAAGVPRIEIGSFVNPRQVPQMAGIDQIARMLIERGHNLAARTTNDLFRFTALVPNQRGYELAAAAGLRHVRLVLAASDGLNRANFKRTTAESLIEFSRFALNIRRDGLTFGVAIGAAFGCPFDGYVSPERVRAIAEHAVDIGAGEIILADTTGMAVPTQVAALCRTILDRIPDVTVTLHLHNTRNTGYANAFAAWQVGIRSFDAALGGIGGCPFAPRAVGNIASEDLVHLFNGLGVPTGIDLSALIAASDWLSATLGRPLPALVGKAGPVYPQVVSMAPYLS
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Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the cleavage of (R)-citramalyl-CoA to yield acetyl-CoA and pyruvate.
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A9X1A0
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PI4KB_PAPAN
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Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67)
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MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLRGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
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Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development.
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A9X1C8
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EXT1_PAPAN
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Exostosin-1 (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostoses protein 1 homolog)
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MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPDALRPFVPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYPQQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSLHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKDHPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKHGKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVMLSNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVEKIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKFTAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVIVIEGESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWDNSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFLVSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHSQMRLDPVLFKDQVSILRKKYRDIERL
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Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
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A9X1D0
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SETD3_PAPAN
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Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3)
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MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERANPNSFWQPYIQTLPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNQDLSVRAKMAIKLRLGEKEILEKAVKSAAVNREFYRQQMEEKAPLPKYEEGNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNIREAISKAQATENGLVNGENSVPNGTRSENENLNQEESKRAVEDAKGSSSDNTAEVKE
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Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin.
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A9XMT3
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CCLOP_LOTJA
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Protein CYCLOPS (LjCYCLOPS) (Protein IPD3 homolog)
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MEGRGFSGLYRNSSEELFLKTVMESPIGMPVPSMEMLGFKNVSQGFRADSEELFKRWLTNGEGYNSSSIGFSSRLSKRISTELVNGSNQLQVGVASDGRNNDKPFIQNNLLANDVSGDFNFPIRDPVDRELQPSNLFLAKAWFLSDQRMTRSRSSELRRRYSEMQNGLATQGIESICMDPQHGAEATKQEVANFNGYNYLSMCELPSQKGSFMSPSNSCSSNFNTPQFGDMDKVSSCVSMLKGTLQRRRLSSQLEKEAAEDDLNGIFYPQEPLFQTGFDQGQENWSNQTPVNVQVDSIGEVKDHGVLQTLEGSTNPVVDGFANQINQIYVGTASGEPSQSESSNAAPVISSGLDTCEGPINSNQTLCESSWKQVGVSKSSENTQNRVKGFREQIMDNLKDDKKRKSLERYGSITSAVSDDKGDTTKKRRVERSRKMAEAKERNSTPSVPSDMQAVLKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEELADEKERLLEEIERILSETEKM
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Involved in symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis, by binding, as a complex comprising CCaMK, CYCLOPS, and DELLA, to RAM1 promoter cis element thus promoting its expression. Acts downstream of CCAMK. Binds to the promoter of ERN1 and strongly transactivates ERN1, a transcriptional regulator required for nodulation.
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A9YTQ3
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AHRR_HUMAN
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Aryl hydrocarbon receptor repressor (AhR repressor) (AhRR) (Class E basic helix-loop-helix protein 77) (bHLHe77)
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MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELHGKPNYSAGRSSRESGVLVLREQTDAGRWAQVPARAPCLCLRGGPDLVLDPKGGSGDREEEQHRMLSRASGVTGRRETPGPTKPLPWTAGKHSEDGARPRLQPSKNDPPSLRPMPRGSCLPCPCVQGTFRNSPISHPPSPSPSAYSSRTSRPMRDVGEDQVHPPLCHFPQRSLQHQLPQPGAQRFATRGYPMEDMKLQGVPMPPGDLCGPTLLLDVSIKMEKDSGCEGAADGCVPSQVWLGASDRSHPATFPTRMHLKTEPDSRQQVYISHLGHGVRGAQPHGRATAGRSRELTPFHPAHCACLEPTDGLPQSEPPHQLCARGRGEQSCTCRAAEAAPVVKREPLDSPQWATHSQGMVPGMLPKSALATLVPPQASGCTFLP
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Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site.
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A9YWR6
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STR2_MEDTR
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ABC transporter G family member STR2 (EC 7.6.2.-) (Protein STUNTED ARBUSCULE 2)
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MKTQGLELETVIDIKHKPVSFTGGLEFESLTYTVTKKKKVDGKWSNEDVDLLHDITGYAPKGCITAVMGPSGAGKSTLLDGLAGRIASGSLKGKVSLDGNSVNASLIKRTSAYIMQEDRLFPMLTVYETLMFAADFRLGPLSAVDKRQRVEKLIEQLGLSSSRNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSALSVIEKLHDIARNGSTVILTIHQPSSRIQLLLDHLIILARGQLMFQGSLKDVGHHLNRMGRKIPKGENPIENLIDVIQEYDQCDFVGVEVLAEFARTGMKPPLLSDMEEIISYTNSIAPSPSPLHRGSKYEEKSQDFSYSSQISRRSLNDEFDHSIRSPYNNTPMSWSASNSAAFLKFTPSRLKNENKVQKPPSHASPGIYTYSSEILPATPTPHSSDYVVDENDYLTPTNSSQEHLGPKFANSYIGETWILMRRNFTNIRRTPELFLSRLMVLTFMGVMMATMFHNPKNTLQGITNRLSFFIFTVCLFFFSSNDAVPAFIQERFIFIRETSHNAYRASCYTIASLITHMPFLALQALAYAAIVWFALELRGPFIYFFLVLFISLLSTNSFVVFVSSIVPNYILGYAAVIAFTALFFLFCGYFLSSEDIPLYWRWMNKVSTMTYPYEGLLMNEYQTNETFGSNDGVSITGFDILKSLHIGTEEIKKRNNVLIMLGWAVLYRILFYIILRFASKNQRS
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Together with STR, required for arbuscule development in arbuscular mycorrhizal symbiosis.
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A9ZLX4
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RIPR2_COTJA
|
Rho family-interacting cell polarization regulator 2 (Myogenesis-related and NCAM-associated protein)
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MSIGSHSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENTSALKKPQAKVKKMHNLGHKNSTTPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMRRNSRLGVLYDLDKQIKAVERYMRRLEFHISKVDELYEAYCIQRRLCDGASKMKQAFAMSPTSKAARESLTEINRSYKEYTENMCTIEAELENLLGEFCIKMKGLAGFARLCPGDQYEIFMRYGRQRWKLKGKIEVNGKQSWDGEEMVFLPLIVGLISIKVTEVKGLATHILVGSVTCETKDLFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDLTPSTGNVSKASALQRRMSMYSQGTPETPTFKDHSFFRWLHPLQDRPRLAILDALQDTFFDKLRRSRSFSDLPSLRLSPKAGLELYSNLPDDVFENGTATTEKRPLSFTFGDLPYEDRVPPANSAEPSSAHVTSSPDIATTATQHRARAQTAAAVTPAEGKACPGVRCEPRGHGDSCQEYPPGFQKPSDTGSDRVFIEANVPVSLLQDTDEGSELKPVELDTYEGNITKQLVKRLTSAEVPGTPERLPCEGSISGESEGYKSYLDGSIEEALQGLLLALEPHKEQYKEFQDLDQEVMHLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDDEDGGGEEVCNGGGGADSVFSDTEVEKNSYRTEHPEARGHLQRSLTEDTGVGTSVAGSPLPLTTGSDSLDITIVKHLQYCTQLIQQIVFSRKTPFVTRDLLDKLSRQTLVMENIAEISTENLGSITSLTDAIPEFHKKLSLLAFWMKCTGPSGVYHTSADKMMKQLDINFAATVNEECPGLAETVFRILVSQILDRTEPVLYSTMSSEIITVFQYYNYFASHSVNDLGSYLLQLAKEASVVQMLQSVKDGKLQQNVSKINSNNLPPQQEVLRALALLLNENKNEVSETVASLLTATAENKHFREKALIYYCEALTQPNLQLQKAACLALRYLKATESIKMLVMLCQSDNEEIRKVASETLLSLGEDGRLAYEQLDNSPGNLSELEVAGELNLPQLSRRTCLSVTATEEGWSCH
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Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation. Maintains naive T lymphocytes in a quiescent state and prevents chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration. Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion. Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear. Plays a role for maintaining the structural organization of the basal domain of stereocilia. Involved in mechanosensory hair cell function. Required for normal hearing (By similarity).
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A9ZPH9
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GMAS_METMY
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Glutamate--methylamine ligase (EC 6.3.4.12) (Gamma-glutamylmethylamide synthetase) (GMAS) (Glutamate--ethylamine ligase) (EC 6.3.1.6) (N(5)-ethyl-L-glutamine synthetase) (Theanine synthetase)
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MKSLEEAQKFLEDHHVKYVLAQFVDIHGVAKVKSVPASHLNDILTTGAGFAGGAIWGTGIAPNGPDYMAIGELSTLSLIPWQPGYARLVCDGHVNGKPYEFDTRVVLKQQIARLAEKGWTLYTGLEPEFSLLKKDEHGAVHPFDDSDTLQKPCYDYKGITRHSPFLEKLTESLVEVGLDIYQIDHEDANGQFEINYTYADCLKSADDYIMFKMAASEIANELGIICSFMPKPFSNRPGNGMHMHMSIGDGKKSLFQDDSDPSGLGLSKLAYHFLGGILAHAPALAAVCAPTVNSYKRLVVGRSLSGATWAPAYIAYGNNNRSTLVRIPYGRLELRLPDGSCNPYLATAAVIAAGLDGVARELDPGTGRDDNLYDYSLEQLAEFGIGILPQNLGEALDALEADQVIMDAMGPGLSKEFVELKRMEWVDYMRHVSDWEINRYVQFY
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Catalyzes the formation of N(5)-methyl-L-glutamine from glutamate and methylamine. In vitro, can also use ethylamine, hydroxylamine and ammonia, with 75%, 40% and 1% activity compared to methylamine, respectively.
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A9ZSZ2
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AGO3_BOMMO
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Piwi-like protein Ago3 (BmAGO3) (EC 3.1.26.-)
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MADPGKGRGRSLALLQALKKSQMMDSPSQSESQSPESTPEQSTAPSTIASATPSTSGVSIGGRGRAAALMLAKMQQKPGSTTPAIFVPPSSTSAPTAGTGRGFKLLQNLQASQKASSQIASSQVTSSAQSDIKDLTEKMSETSVSAQASSVAKNKYFREVKDTPPVVKKGETGVPIEVTCNYIYLNFKENIVFEYEVKFEPDQDYKHLRFKLLNEHIEHFKEKTFDGTTLYVPHELPDAVRNLVSTNPYDQSKVNVSIIFRRTRRLSEMIHIYNVMFKCIMKDLKLIRFGRQHYNEHAAIQIPQHKLEVWPGYVTAVDEYEGGLMLTLDSTHRVLRTQTVLSLIKEVVQTEGANWKRKMTDILIGASVMTTYNKKLFRVDTIDDKMSPRSTFEKTEKGETVQISFIDYYKKNYGIEIMDWDQPLLISRDTKRMPGSDTPTDFMICLIPELCQLTGLTDDQRSNFRLMKDVATYTRITPNQRHAAFKKYIESVMKNETAKSRLAGWGLSIAPETVNLTARTLPPETLYFGDNVRVPGKPNAEWNSEVTKHSVMQAVDIMRWVLLFTQRDKQVAMDFLSTLKRNCRPMGIMVSDAELVPLANDRTDTYVLALKKCITSSVQLVVAICSTKRDDRYAAIKKVCCADNPVPSQVINARTLMNTNKIRSITQKILLQLNCKLGGTLWSISIPFKSAMIVGIDSYHDPSRRNRSVCSFVASYNQSMTLWYSKVIFQEKGQEIVDGLKCCLVDALTHYLRSNGQLPDRIIIYRDGVGDGQLKLLQQYEIPQMKICFTILGSNYQPTLTYVVVQKRINTRIFLKSRDGYDNPNPGTVVDHCITRRDWYDFLIVSQKVTQGTVTPTHYVVVYDDSGITPDQCQRLTYKMCHLYYNWPGTVRVPAPCQYAHKLSYLVGQCVHAQPSDVLVDKLFFL
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Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Strongly prefers a have adenine at position 10 of their guide (g10A preference). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle: antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally cleave complementary transcripts, to couple the amplification of piRNAs with the repression of transposable elements.
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B0BF33
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PKP2_DANRE
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Plakophilin-2
|
MLKPHPEHKEQPQDSFTPSGDSTPDASMAEERDFMRSVLPVYDSFHPEDSSLALPLANKLTLADAHRLNRLQQQVQLTLSRKKRKPKPADSSLAESQSSCQISSSSSLGSLHLKRTFSVNHEATRSLRMVDRSQWPSMEPPLFHRGYGSFRYTPKRAGLCLGSNSLTLPSAPTTSHFQMNKLPLRYAHSEVLRNPRFAGLSAATQIPSSPVYENPHTDDTDDVFLPSTSVERGRMESEKHTLQQTLCKQREGGFVALEQSENVSWQSRVRKPSLEFVAGRRPSQTGSLISMEEQSGSLGRIEKLEVKQHAVTTLTKKGKPGELSAEMTLKEAVNLLTQDNNMETQIAAANFIQNQCFNSPDAKRKILHLQGIPKLLKLMQNDSEELQWAAVSSLRNIVFENNENKMEVKDCEGLPVILRLLKINRDIETRRQLTGLLWNLSSHDLLKEHLSREAVKPLTDSVLVPCSGISEGEDPKLELLADPDIFYNATGCLRNLSSAGPDGRKVMRDCEGLIECVIYYIRGTIADYKPDDKATENCVCILHNLSYRFDCEVPRVDSPVAQKPKQTHTETSNPGCFIIKTPKNSAENLEADEDYPALEENGSPHGVEWLWSAITVRMYLSLIAVSTNQHTKQASIGTLQNLTACSGEISQAIAHFIVQKEGGLSQVKKLLQEAEKEELRISVSLLKNISRYRELHADIVKQVLPELVAILPNSDRNVEQPIEITVTICHILINLSQASASNTCAIINQGALPKIISISSKDNGFGPTRAGQAACVLLHTLWRHSELHSSFKKAGYRKTDFINNRTVKAVNSARE
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Required for development of the heart, potentially via cell-cell adhesion and modulation of expression of cardiac precursor genes. Plays a role in desmosome cell-cell junctions and their intracellular connectivity.
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B0BK71
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MSP1_MYCSO
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Dye-decolorizing peroxidase msp1 (EC 1.11.1.19) (EC 1.11.1.7) (Peroxidase 1) (MsP1)
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MKLFSASVFAAIIASHYASATAHIRAPNVKPRRTNSLLTAPPQQPPLPSAQQAASASSSAGLNLTDIQGDILIGMKKNKELFFFFSITDAATFKAKLGSDILELITSTNQLLAVATQPITAVNVAFSSTGLKALGITDDLKDPVFEAGMLSNAVSDLSDPGTGNWVPGFVGTSVHGVFLLASDTIDNVNTELANIQTILNGSITEIHRLQGEARPGDQQGHEHFGFMDGISNPAVDGFTPPAEIRPGQALIPPGIMLLGEANDTFQNDRPPWAKDGSFLVFRQMQQRAPEFNKFLQDHALNMPNMTSEQGADLLGARIVGRWKSDAPIDLTPLVDDPVLAADNQRNNNFDFSDATNQTRCPFSAHIRKANPRGDLGGINKFPNQHIIRAGIPYGPEVTDAEKASNSSSTDPSLERGLAFVAYQSNIQNGFVFLQKNWVDNTNFFRPGTGVDPLIGTNSRNSGTDAPNTPRVVSGLDPNNATSTIEIGIDFVVSRGGEYFFSPSLSAIRTVLSV
|
Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5. Also degrades beta-carotene.
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B0BK72
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MSP2_MYCSO
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Peroxidase 2 (MsP2) (EC 1.11.1.-)
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MRLTYLPLFAGIAIQSASALPDFFKSSVLKPRRTNSLLINPDAQPDLPTAQQASTAAASVGLNLTDIQGDILIGMKKNKEMFFFFSIADATAFKSHLDSAILPLITSTQQLLTVATQPTTAVNLAFSQTGLNALGLASQGLGDSLFASGQFSGAESLGDPGTSNWVQAFAGTGIHGVFLLASDTIDNVNAELSQIQSILGTSITEAYRLQGEARPDDQQGHEHFGFMDGISNPAIDGFSTALPGQAVLSPGLFLLAEDGDGSSSSRPSWAKDGSLLAFRQLQQRVPEFNKFLADNAALTQGNADLLGARMMGRWKSGAPVDLAPTADDVDLANDPQRNNNFNFTHPDFTETTDQTHCPFSAHIRKTNPRSDFNPLNTANHIIRAGIPYGPEVTDAEASSNTSSTDASLERGLAFVAYQSNIGNGFAFIQQNWVDNANFFFGKTTPPGIDPIIGSNAAQNNFAPNSPRPVSGLDPTDSTTIVTLNTDFVVSRGGEYFFSPSLSAIQNTLSV
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Peroxidase capable of degrading beta-carotene.
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B0BLU1
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RN168_XENTR
|
E3 ubiquitin-protein ligase rnf168 (EC 2.3.2.27) (RING finger protein 168) (RING-type E3 ubiquitin transferase rnf168)
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MAKVQKLPLPWSECICPICQEILLEPVTLPCKHTLCNPCFQMTVEKASLCCPFCRKRVSTWARQHSRTRTLVNKELWEVIQKQYPKQCQRRASGQESDDLSDELTSCPVPVLCKPGEIRQEYEAEVSKIEAERTAQEEAERKASEDYIQKLLAEEEAEENLHAEASQREIEEQLKRDEELARLLSGDMDLSNASCTSVSPVTSKKVVSKSSKIVKSKQRVSGDIERFLSPKPRRALAAFGINESRNSDTSGSCILLDEDEDEIPDLSPQCPSTSLIQERDVELPMPYLPNCYKLESDAASQQDSCSERNDICNGTYSCSDSIDVEVSKTMEQQRATADSQEYRMETNAMSYSTPKRKCEECYLDIEEKAGSCQSVKKKKLSLSEDSPVLSVHAGKFIELEENLYERRKQEEHDRLFALQLQRELDKELKQVNRGKGSPDEYQLRPKRGLKLQECNDSPLPHNEQTPVQDKGGNTQSGYSPDENKKPSRKKSITSSQVRQSRAVTNTERSSEGMNVLKPSNKQPTILDLFQRSAGK
|
E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with ube2n/ubc13 to amplify the rnf8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX, leading to amplify the rnf8-dependent H2A ubiquitination and promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of tp53bp1 and brca1. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066}.
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B0BLW3
|
LGR4_XENTR
|
Leucine-rich repeat-containing G-protein coupled receptor 4
|
MGCPGWPLALFALLLASCSGGPSGVSSPAPCPAPCACDLDGGADCSGKGLVTVPDGLSVFTHSLDLSMNNITKLPEGAFKGFPYLEELRLAGNDLSIIHPMALSGLKELKVLTLQNNQLKTVPSESLKGLVSLQSLRLDANHIVTVPEDSFEGLVQLRHLWLDDNSLTEVPIRPLSNLPSLQALTLALNKISHIPDYAFSNLSSLVVLHLHNNKIRTLGPHCFHGLDNLEALDLNYNNLIDFPDSIRSLPNLKELGFHSNSITIIPDGAFVKNPLLRTIHLYDNPLSFVGNSAFQNLSDLHFLIIRGASNVQWFPNLTGTNNLESLTLTGTKIRSIPIKFCQEQKMLRTLDLSYNEISALVGFEGCSSLEEVYLQNNQIQEVQNETFQGLAALRMLDLSRNRIHTIHKEAFVTLKALTNLDLSFNDLTAFPTAGLHGLNQLKLTGNPNFKETLTAKDLIKLSSVSVPYAYQCCAFSACNSYMTTTVEEDRLRAQRLLLDHDRAAMDPDYMGTEDDKEHVQALIQCNPATGPFKPCEYLLGSWMIRLTVWFIFLLALIFNVIVIVTMFASCSQLTSSKLFIGLIAVSNLFMGVYTGTLTVLDTISWGQFAEFGIWWETGNGCKVAGFLAIFSSESAIFFLMLAAIERSLSAKDIIKKEKHQHLRKFQVASLLAVLLAAAAGCLPLFHIGEFSSSPLCLPFPTGETPSLGFTVTLVLLNSLAFLIMVITYTKLYCTIEKEDLSENAESSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAIYISPEIMKSVTLIFLPLPACLNPVLYVFFNPKFKEDWKLLRWRLTKRSGSVAVATNSQRGCVTQDFYYDFGMYSHLQGGNFAVCDYCESVLLKNPPPCKHLIKSHSCPTLAVVPCQRPDNYWSEFGTQSAHSDCADEEDSFVSDSSDQVQVCGRACFYQSRGLPLVRYAYNIPRMKD
|
Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids (By similarity). Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (By similarity).
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B0BMY1
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LAAT1_RAT
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Lysosomal amino acid transporter 1 homolog (PQ-loop repeat-containing protein 2) (Solute carrier family 66 member 1)
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MVWRTLVASNFSTCPNGSIQWIWDVFGECAQDGWDEASVALGLVSIFCFAASTFPQYIKACKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLLMLTLYFHYKFKKQPSLLSAPINSVLLFILGTVCITPLLSSTDPVAVPREGFRGRTLLSVEPGNKPFTKKEVVGFVIGSASSVLYLLSRLPQIRTNFVRQSTQGISYSLFALVMLGNTLYGLSVLLKNPEVGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRSHDADAASEREPLLPS
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Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes.
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B0BND0
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ENPP6_RAT
|
Glycerophosphocholine cholinephosphodiesterase ENPP6 (GPC-Cpde) (EC 3.1.4.-) (EC 3.1.4.38) (Choline-specific glycerophosphodiester phosphodiesterase) (Ectonucleotide pyrophosphatase/phosphodiesterase family member 6) (E-NPP 6) (NPP-6)
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MAGKLWTFLLLFGFSWVWPASAHRKLLVLLLDGFRSDYISEDALASLPGFREIVNRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPRTNKSFDIGVNRDSLMPLWWNGSEPLWITLMKARRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSLKSGRADLAAIYHERIDVEGHHYGPSSPQRKDALKAVDTVLKYMTQWIQERGLQNDLNVILFSDHGMTDIFWMDKVIELSKYISLDDLQQVKDQGPVVSLWPVPEKHSEIYHKLRTVEHMTVYEKEAIPNRFYYKKGKFVSPLTLVADEGWFIAESREALPFWMNSTGKREGWQHGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNIMCNVVGITPLPNNGSWSRVVCMLKSQTSSSPSIPPNSCALVLILLLYFV
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Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids.
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B0BNF1
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SEPT8_RAT
|
Septin-8
|
MAATDLERISNAEPEPRSLSLGGHVGFDSLPDQLVSKSVTQGFSFNILCVGETGIGKSTLMNTFFNTTFETEEASHHEECVRLRPQTYDLQESNVHLKLTIVDAVGFGDQINKDDSYRPIVDYIDTQFENYLQEELKIRRSLFDYHDTRIHVCLYFITPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMGELVSNGVQIYQFPTDDEAVAEINAVMNAHLPFAVVGSTEEVKVGNKLVRARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFQDSDGDSQPFSLQETYEAKRKEFLSELQRKEEEMRQMFVNKVKETELELKEKERELHEKFEHLKRIHQEEKRKVEEKRRELEEETNAFNCRKAAMEALQSQALHATSQQPLRKDKDKKKVGGWSSIYSVTIP
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Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (By similarity). Seems to participate in the process of SNARE complex formation in synaptic vesicles.
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B0BNF9
|
HAOX1_RAT
|
2-Hydroxyacid oxidase 1 (HAOX1) (EC 1.1.3.15) (Glycolate oxidase) (GOX) (Glyoxylate oxidase) (EC 1.2.3.5)
|
MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI
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Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate. The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones. Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate. Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2.
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B0BNK7
|
LRFN3_RAT
|
Leucine-rich repeat and fibronectin type-III domain-containing protein 3 (Synaptic adhesion-like molecule 4)
|
MAVLPLLLCLLPLAPASSPPQPATSSPCPRRCRCQTQSLPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIAAVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAVGDPEPRVRWVSPQGRLLGNSSRARAFPNGTLELLVTEPEDGGTFTCIAANAAGEATAAVELTVGPPPPPQLANSTSCDPPRDGEPDALTPPSAASASAKVADTVAPTDRGVQVTEHGATAALVQWPDQRPVPGIRMYQIQYNSSADDILVYRMIPADSRSFLLTDLASGRTYDLCVLAVYEDSATGLTATRPVGCARFSTEPALRPCAAPHAPFLGGTMIIALGGVIVASVLVFIFVLLLRYKVHGVQPPGKAKATAPVSSVCSQTNGALGPVPSAPAPEPAAPRAHTVVQLDCEPWGPSHEPAGP
|
Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity).
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B0BNM1
|
NNRE_RAT
|
NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase)
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MSGLRTLLGLGLLVAGSRLPRIASRQSVCRAGPIWWGTQHRSSETMASAAVKYLSQEEAQAVDEELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPAYPDTECVYRLQ
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Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
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B0CM99
|
HMGB1_CALJA
|
High mobility group protein B1 (High mobility group protein 1) (HMG-1)
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MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE
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Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.
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B0D6H2
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ARO1_LACBS
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MANADVLKVSILGKESIHCGFHLIPYIAQTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRISSLPTSSTKPRFLSLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIQTPSADYAGRSKQTRSIAQELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLADPRIASLPAAKLLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEPKATVVPDSIIAKTLSEAAKVIPGVPRHHPVKMATPGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELKGASFAWEDAGETLVVKGGEGSLSVPPKGKELYLGNAGTAARFLTTVCTLVQSSPQDNAEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLKGSQLQLAASVSSQYVSSILLCAPYAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDPVTGKFLDVYEIPKAVYTNPPEYNIESDASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAKEVLEKMGCQVSQTATETTVQGPPIGQLKAIEEVDMEVMTDAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPISDLKRGVSVHCYDDHRVAMAFSVLSTVVEGTIIEEKRCVEKTWPNWWDDLENKIGLTVQGVDLASVASEASASGTINHDSAASIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKSQGHVISLGGGIVETPAARELLKEYAATKGPVVHIVRPIDEVIRYLNSEASRPAYDEAIVDVFRRREPWFGECCSHDFFNRFGDLPYSSPKATSREIARFFNHITGQRPNLAQNLTSGRRSYFLCLTYPDVTQSFPVIHELTQGVDAIELRVDLLRASKDYDSIEYSIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSFPDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSLKGSSHMIASWHDWSGNMIWDGPVVKEKYDAAARFGDIIKIVGKANSIQDNFTLYNFVSKVNSTAGSKPFIAINMGLEGQMSRVLNSTLSPVSHPLLPSKAAPGQLSFKQIQNALHLLGLLPAQRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAVNTIIPRTTGSGRMLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHVLEQLGQWPNGAVPPCVIVSTVPASATTTEEETSGILLPSKLFDYRDGPAVVIDMAYKPAETPLLRLAKTAGDNWATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLGRLTTDHKQFVFEEECES
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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B0EXJ8
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HTOMT_CATRO
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Tabersonine 16-O-methyltransferase (EC 2.1.1.94)
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MDVQSEEFRGAQAQIWSQSCSFITSASLKCAVKLGIPDTIDNHGKPITLSELTNALVPPVHPSKAPFIYRLMRVLAKNGFCSEEQLDGETEPLYSLTPSSRILLKKEPLNLRGIVLTMADPVQLKAWESLSDWYQNEDDSSTAFETAHGKNFWGYSSEHMEHAEFFNEAMASDSQLISKLLIGEYKFLFEGLASLVDIGGGTGTIAKAIAKNFPQLKCTVFDLPHVVANLESKENVEFVAGDMFEKIPSANAIFLKWILHDWNDEDCVKILKSCKKAIPAKGGKVIIIDMVMYSDKKDDHLVKTQTSMDMAMLVNFAAKERCEKEWAFLFKEAGFSDYKIYPKLDFTRSLIEVYP
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16-O-methyltransferase involved in the biosynthesis of vindoline. Highly specific for 16-hydroxytabersonine. No activity with tabersonine, 3-hydroxytyramine, 4-hydroxytyramine, 5-hydroxytryptamine (5HT), 2,3-dihydro-3-hydroxytabersonine, lochnericine, hoerhammericine, 16-hydroxy-2,3-dihydro-3-hydroxytabersonine, 16-hydroxylochnericine, 16-hydroxyhoerhammericine, quercetin, kaempferol and caffeic acid as substrates.
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B0F0H3
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MKRN2_XENLA
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E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2)
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MSPKQVTCRYFLHGVCREGSRCLFSHDLATSKPSTVCRFFLRGQCAYGTRCRYDHVKPCNGTVFIPPQEMSPVLSPPPLFPAQEAAVPPTIPAPQRREKKTLVLRDRDLCGASVDPALQPGCITESQGSEGEAKPHSYLEAICTGLDESQDPASYPGAPQQLCPFAQAGECHCGDSCPYLHGDACEICGLQVLHPHDQEQRRDHEKLCMENFELDMERAFAVQASEGRVCSICMERVYEKQSPAQRRFRILSDCNHTYCLTCIRQWRCARQFDNPVIKSCPECRVISEFVIPSAYWVEDQSKKDELIEAFKQGMGKKLCKYFDQGRGTCPFGGKCLYLHSYPDGTRAQPEKPRKQLGSEGSVRFLNSLRLWDFIEDREQRGVPNAEVGKLGELFMHLSGADEELPAPFN
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E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Inhibits neurogenesis and axis formation during embryonic development by modulating the phosphatidylinositol 3-kinase (PI3K) pathway. Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA expression.
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B0F2B4
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NLGN4_MOUSE
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Neuroligin 4-like (Neuroligin-4) (NL-4)
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MPAPVPALLCLALALASAQPSPPPPPPFPVVATNYGKLRGVRAALPGDVLGPVTQFLGVPYAAPPTGERRFQPPEPPSSWAGVRDATRFAPVCPQHLDERALLRDCLPAWFAANLDAIAAYVQDQSEDCLYLNLYVPGGANGKKMADDVTGNDHGDDQDSRDPGVGGAAAAAARKPVMVYIHGGSYMEGTANIVDGSVLASYGDVIVVTVNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWVEENAGAFGGDPDRVTVFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPARYARALGERVGCATPDPGSPPGSPPGWDSASLVSCLRGKAAGELARARVTPATYHVAFGPTVDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGARFVDGLGGGHDGGYGGYGGGYGGGVEDDEVQDGGPDGAAGGVSAGEFDLAVSGFINDLYGRPEGRGDALRETVKFMYTDWADRDSPEARRKTLVALFTDHQWVAPAVATADLHARYGSPTYFYAFYHRCHGGGGGGGGVDGVAGGVAGGVGGEEARPAWADAAHGDEVPYVFGVHMAGPGDVFGCNFSRNDVMLSAVVMTYWTNFAKTGDPNQPVAQDTRFVHTRPNRFEEVAWAKYDPRGQLYLHIGLRPRVRDHYRAAKVAFWLELVPHLHGLAADPGAYLSAAATRAAPSGDPDRDPGGGGGGRRRPRPATRRPAVMTSSSMASGSGMTSSSGSGMTSSSGSSASAVLIETRRDYSTELSVTIAVGASLLFLNVLAFAALYYKKDKRRHETHRRPPPPRPPQAPPSAAAADRNPRPDPGPAGRRGGECGAVVTAMAAEASAGGLGHDGVGGVGVGGVIGGVAGLRLACPPDYALTLRRSPDDVPRAGAGPGTMTLIPGALGGGGGGAVHGFNTFGSGVGVAGVAGVATSQAGPGLPHGHSTTRV
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Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission.
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B0F481
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BIODA_ARATH
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Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial (Bifunctional BIO3-BIO1 protein) [Includes: Dethiobiotin synthetase (EC 6.3.3.3) (DTB synthetase) (DTBS) (Protein BIOTIN AUXOTROPH 3); 7,8-diamino-pelargonic acid aminotransferase (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (EC 2.6.1.62) (Diaminopelargonic acid synthase) (Protein BIOTIN AUXOTROPH 1)]
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MIPVTATLIRHRLRHLRHRIRFKSTSVSPFHLPLNHPTYLIWSANTSLGKTLVSTGIAASFLLQQPSSSATKLLYLKPIQTGFPSDSDSRFVFSKLDSLSLRRQIPISISNSVLHSSLPAAKSLGLNVEVSESGMCSLNFRDEKTVTGAPELLCKTLYAWEAAISPHLAAERENATVEDSVVLQMIEKCLKEEMECGVKSEKSDLLCLVETAGGVASPGPSGTLQCDLYRPFRLPGILVGDGRLGGISGTIAAYESLKLRGYDIAAVVFEDHGLVNEVPLTSYLRNKVPVLVLPPVPKDPSDDLIEWFVESDGVFKALKETMVLANLERLERLNGMAKLAGEVFWWPFTQHKLVHQETVTVIDSRCGENFSIYKASDNSSLSQQFDACASWWTQGPDPTFQAELAREMGYTAARFGHVMFPENVYEPALKCAELLLDGVGKGWASRVYFSDNGSTAIEIALKMAFRKFCVDHNFCEATEEEKHIVVKVIALRGSYHGDTLGAMEAQAPSPYTGFLQQPWYTGRGLFLDPPTVFLSNGSWNISLPESFSEIAPEYGTFTSRDEIFDKSRDASTLARIYSAYLSKHLQEHSGVRQSAHVGALIIEPVIHGAGGMHMVDPLFQRVLVNECRNRKIPVIFDEVFTGFWRLGVETTTELLGCKPDIACFAKLLTGGMVPLAVTLATDAVFDSFSGDSKLKALLHGHSYSAHAMGCATAAKAIQWFKDPETNHNITSQGKTLRELWDEELVQQISSHSAVQRVVVIGTLFALELKADASNSGYASLYAKSLLIMLREDGIFTRPLGNVIYLMCGPCTSPEICRRLLTKLYKRLGEFNRT
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Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis. Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. {ECO:0000250, ECO:0000269|PubMed:16667573, ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:2909401, ECO:0000269|PubMed:8676868}. Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
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B0F9L4
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GOGC6_ARATH
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Golgin candidate 6 (AtGC6) (Protein MAIGO 4)
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MDLASRYKGVVGMVFGDNQSSNEDSYIQRLLDRISNGTLPDDRRTAIVELQSVVAESNAAQLAFGAAGFPVIVGILKDQRDDLEMVRGALETLLGALTPIDHARAQKTEVQAALMNSDLLSREAENITLLLSLLEEEDFYVRYYTLQILTALLMNSQNRLQEAILTTPRGITRLMDMLMDREVIRNEALLLLTHLTREAEEIQKIVVFEGAFEKIFSIIKEEGGSDGDVVVQDCLELLNNLLRSSSSNQILLRETMGFEPIISILKLRGITYKFTQQKTVNLLSALETINMLIMGRADTEPGKDSNKLANRTVLVQKKLLDYLLMLGVESQWAPVAVRCMTFKCIGDLIDGHPKNRDILASKVLGEDRQVEPALNSILRIILQTSSIQEFVAADYVFKTFCEKNTEGQTMLASTLIPQPHPTSRDHLEDDVHMSFGSMLLRGLCSGEADGDLETCCRAASILSHVVKDNLRCKEKALKIVLESPMPSMGTPEPLFQRIVRYLAVASSMKSKEKSSTLGKSYIQQIILKLLVTWTVDCPTAVQCFLDSRHHLTFLLELVTDPAATVCIRGLASILLGECVIYNKSIENGKDAFSVVDAVGQKMGLTSYFSKFEEMQNSFIFSPSKKPPQGYKPLTRTPTPSEAEINEVDEVDEMVKGNEDHPMLLSLFDASFIGLVKSLEGNIRERIVDVYSRPKSEVAVVPADLEQKSGENEKDYINRLKAFIEKQCSEIQNLLARNAALAEDVASSGRNEQSQGSEQRASTVMDKVQMESIRRELQETSQRLETVKAEKAKIESEASSNKNMAAKLEFDLKSLSDAYNSLEQANYHLEQEVKSLKGGESPMQFPDIEAIKEEVRKEAQKESEDELNDLLVCLGQEESKVEKLSAKLIELGVDVDKLLEDIGDESEAQAESEED
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Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex.
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B0F9W3
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GPER1_MICUN
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G-protein coupled estrogen receptor 1 (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30)
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MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAKLSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV
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Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes.
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B0FPE9
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NLRP3_MACMU
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NACHT, LRR and PYD domains-containing protein 3 (EC 3.6.4.-)
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MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCISLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKKKKDYCKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREHELLAIGKTKTWESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKIMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIRKIVSKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYTFFLSSLLQPRGGSQEHRLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSCLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTCYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHVVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPGSHAACSHRLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPDCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSRSLTRLYVGENALGDAGVAILCEKAKNPQCNLQKLGLVNSGLTSACCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTIVFEPSW
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Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF.
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B0FYY4
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ITB1_SHEEP
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Integrin beta-1 (Fibronectin receptor subunit beta) (Integrin subunit beta-1) (VLA-4 subunit beta) (CD antigen CD29)
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MNLQLIFWIGLISSVCCVFGQADENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDIENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENDMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSGNVIQLIIDAYNSLSSEVILENSKLPEGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKNSETIKIKPLGFTEEVEIILQFICECECQSEGIPGSPKCHDGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTTSCMAVNGQICNGRGVCECGACKCTDPKFQGPTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNITKVENRDKLPQPGQVDPLSHCKEKDVDDCWFYFTYSVNGNNEATVHVVETPECPTGPDIIPIVAGVVAGIVLIGPALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK
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Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (By similarity). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity).
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B0G0Y8
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PDE3_DICDI
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cGMP-specific 3',5'-cGMP phosphodiesterase 3 (EC 3.1.4.35) (Phosphodiesterase 3) (DdPDE3)
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MAPQQNIMKQLQQMQSSPYPSSSPSSTTVSQNNDNLNHNVHSLNNSSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSINEKNKINDNNNRGNSDDGNNNNSNNNSNNNNSNNNNRDDEEEEGDDEDNNNNNNSNNNKIRGYNDNNDINDIFSINFSSWSKSKDNLIENGVLIFEESGLYKELNLSKSSILNFLSIVASSYRNNPFHSFNHAIAVTQTIFLILLKTNLFNILSPIEKLSIIIASICHDLDHPALSNRFQINMKSSIAVLYNNKSVLENHHLSICLGILESKIGNELLSTLTVEEKKQFFRRVKILILATDMENHFTYKKQFDDIISTFSWDNSEHRDLLLIMFLKSADISNELRSFDISNKWANALMEEFFNQSDLEKLNNLPLTPFMEREKVVLHLTQVSFIEKFLLPSYQSLQNLLPSLEDFVQRIIENKEIWSNNGSSSSTTSSSPN
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Phosphodiesterase specific for cGMP, which is not activated by cGMP. Involved in the degradation of intracellular cGMP.
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B0G126
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FYV1_DICDI
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1-phosphatidylinositol 3-phosphate 5-kinase (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (FYVE finger-containing phosphoinositide kinase) (PIKfyve) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (Serine-protein kinase PIKFYVE) (EC 2.7.11.1)
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MAESFQQLGVGSKSNERSFFSKFFGTDDSQKDFGPLPEIEYSDEQRFNPYPAIYEKKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNGNGNRSNSSLNNSNNNNQVRRTHSPSVSNKSDESNTTNTNTNITTNTNITTNTNTNTNTNSTNNDTSSNVTQQQLLTNLGQSKIISALKTKFQRPLPPVDDKKFWMPDHSSAVCYECSEEFTTFKRRHHCRLCGQIFCWKCSQKTLTDGKGERVRVCNFCYRRYMAPDDLDMEGYHYDPITGTVISLITNNDDGTNLNNGNGLIKLDGSTHNMNVSLGNSGDNSSFVQSPNNNFSQSPTFSQQQQQQQQQQQQQQQQQQQQQQQQTTGVMSGLNPFSNSTLLFGRNNNNNNQQQQQPIIEEDKQYYGDINTSYNNSYFNNNGFNNFNNEHYNNTNFNATSLNLNSQLHSNLLANTNGELFYDNSQHSISNYGNLDHHQQQQQSNSHGSLSATPSNTPSGLISPIVGAPSILDPNKMIFYSDQEGNYDNLDDYETSSSDGSDNDNEDNHLKSSHSSANDLGTSNTVSTGESNSESKLSSSSNDISIHHHHYHHHHHHSHGNLLKSNSLTPLNLNNNNIIINNNNINNNNNNDNGNDDNNNNNNDNNNNTTIEVDPRHSMPSKTSNTSFSMASLPSIFKLPTIGRNNNNNNNSGSGNSQYLSANSNASNSISPPNSARGSSSNPNSMTPTPTLSSSFSNLPNAETSPPSLVKAKQQQQQQQQQQQQPQPVLQPTIHHPLKTSLPMFSTQSPPPPTNQLAQSTSMAPPPSIFSPLGKLQALSHPSSSSNNQQQQQPQIVKPIIIAPNSLFFSDPSIVSLKSHPKTTNKTKFLEKYPLPKKYYESTENIIDTFGFKRTPSTEGNLLSQMLATSKQKEFDEKERLKISNNPQMSVYIQHINNLVSEQLEKNNIDLSWRSIIIDLTKKATDNVKIFVRKGDKMSTNEYIKIKKIPGGNKSECNYVDGVVMTKILTHKKMKDKFINPKILLLSCSVEFQRVENKFLYFDQLLQQEKEYLRILVSKIAERKPDLVLVEKTVSRHAQDFLLDAGISLALNVKPKLLERLGRCLGGEVLPTLDIIYNNNSNNNNSNSIQLQQQQNSNSPASLQNSTTTTNNNNNNNNNSTTLGSCGQFKVITYSEIGLKEKEILGKKTLMYFEKCPVELGATIIIRGEDLAVLKIIKKILKLSIFSMHNAYLELKYLNDQSSTSNLLFVNNNGQNLSCSPQIKFPLPKTYPTIPWKYQFTSQHIPVKKALLTSFYKPHSDFGQQQSVIQWTSDDEVLGIGTSDAFKHCDMKFPIENESIYDHQSIVFSHSIFCNSNQCIPFEIHAIDYYTDNDLTLGEFLSKFCFSLHICNIKECNRPLIEHERTFMNSTTRINICVQKTQTIQDRPTNSSPAQQRNQPVQRAGINVINLCKICNKFSPESPMSEEAWEMSFGKFLELCFFGFLPIKTGISPECSHNNAKDHISYFYYQDLAAIFSYEPLPSLELSLPPKNLKATYTEKQRQSVRAKELEIMNQCANQVYSAIHERLYEIGQENQGDRVQELIPSLVQEKQLICSKIESLLLLPESAHKSNDQIINLTKLLYANFMTWNSQLTGLIDSTSYQRSKRNVQQQQQQQQHQQSQQPQPQILIGGDVYSDSHLHTDSVKKINSKQHSHNTILLQSIQSNQEQQLEQQEEFEINVNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTIDNKSENENENKNENKNENENENENKNENKNENENENKKENENQLEIKNENNDSGEEITNNNNNNNNNNNNNNNNNNNNNNNIDNNNNKDENISSTPLLSPSSVLGVSNSGINQAFLNAPNNTYNSVEQDLTLPLNHQSLNFAVGGLVSPGSSSGGLPVGSVPNSSSMPSIHNGGSGNIPSNLVGSASGLSTNYSPNALKDPKKLKIIDTIAGIVSSISQTRILGPTMPYLLLESTDNVALFENEPSTTIAYTLSSSDFKIALNSLLDEEWKRISEIEKQYELQQQQQQDSQDLESSSQQQQQQQQQQQEQQEQPSLPTPSHPLSQSMNFSPSSLLKISSSSLPKDNNNSSENKPNSETNDIVRSRGSVKLSGSPISISPLSNAFEKRKSTSLSSSANNSPISSILEKEKKLKQQSPSLSNSLSGQTIINNNQQQQQQQQPSPIIIDEKDDRNTEKSSIIETDSIIEDLNINQDESNITNEDGGKIGDYESELLYDHHQQGDSENNNNNNNNNNNNNNNNNNNNNNNNNNNTNNNNEQQINNSDTEGDSDSIKSSNSNIYSEKNIKLSKLMVSTQRKEIRSRFKFEKNGYELNIFCSSYYPVQFHALREYMCGDQEFIQSLTRSKIWNAKGGKSGSSWNKTLDDRFILKQVSRIELESFLDFAPLYFEYICKSFLNQIPTALCKILGVFTVRWKDSNGKALKKDLIVMENLFHSKCISKTYDLKGSLRGRLVKNESEVLLDENLLQASFASPICLGEYDKTRVALAVWNDTAFLSSLNVMDYSLLSGIDNQSNQLVVGIIDYMRKFTWDKALEMKVKQSGIMGGGGKVPTVISPKQYKLRFRDAMWLYFTLSPDKFTKVKHLMPYEKKKNNNNNYNYNNFNNNNFNNNNNISNNGNGNINQRQVQQINK
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Dual specificity kinase part of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate.
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B0I1T2
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MYO1G_HUMAN
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Unconventional myosin-Ig [Cleaved into: Minor histocompatibility antigen HA-2 (mHag HA-2)]
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MEDEEGPEYGKPDFVLLDQVTMEDFMRNLQLRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIARYQGRELYERPPHLYAVANAAYKAMKHRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKDVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPIGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDKQLHELHLERNPAVYNFTHQGAGLNMTVHSALDSDEQSHQAVTEAMRVIGFSPEEVESVHRILAAILHLGNIEFVETEEGGLQKEGLAVAEEALVDHVAELTATPRDLVLRSLLARTVASGGRELIEKGHTAAEASYARDACAKAVYQRLFEWVVNRINSVMEPRGRDPRRDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGITWQSVEYFNNATIVDLVERPHRGILAVLDEACSSAGTITDRIFLQTLDMHHRHHLHYTSRQLCPTDKTMEFGRDFRIKHYAGDVTYSVEGFIDKNRDFLFQDFKRLLYNSTDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGKLDENHCRHQVAYLGLLENVRVRRAGFASRQPYSRFLLRYKMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRARLIPIIVLLLQKAWRGTLARWRCRRLRAIYTIMRWFRRHKVRAHLAELQRRFQAARQPPLYGRDLVWPLPPAVLQPFQDTCHALFCRWRARQLVKNIPPSDMPQIKAKVAAMGALQGLRQDWGCRRAWARDYLSSATDNPTASSLFAQRLKTLQDKDGFGAVLFSSHVRKVNRFHKIRNRALLLTDQHLYKLDPDRQYRVMRAVPLEAVTGLSVTSGGDQLVVLHARGQDDLVVCLHRSRPPLDNRVGELVGVLAAHCQGEGRTLEVRVSDCIPLSHRGVRRLISVEPRPEQPEPDFRCARGSFTLLWPSR
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Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication. Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes. Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis. [Minor histocompatibility antigen HA-2]: Constitutes the minor histocompatibility antigen HA-2. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and their expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. HA-2 is restricted to MHC class I HLA-A*0201.
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