Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O43897
|
TLL1_HUMAN
|
MGLGTLSPRMLVWLVASGIVFYGELWVCAGLDYDYTFDGNEEDKTETIDYKDPCKAAVFWGDIALDDEDLNIFQIDRTIDLTQNPFGNLGHTTGGLGDHAMSKKRGALYQLIDRIRRIGFGLEQNNTVKGKVPLQFSGQNEKNRVPRAATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCPACGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKLPEVLTSTDSRMWIEFRSSSNWVGKGFAAVYEAICGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDKPEDIRSTSNTLWMKFVSDGTVNKAGFAANFFKEEDECAKPDRGGCEQRCLNTLGSYQCACEPGYELGPDRRSCEAACGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEVPEVITSQFNNMRIEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNKHDCKEAECEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKIPDPLVATGNKMFVRFVSDASVQRKGFQATHSTECGGRLKAESKPRDLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFCGSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRYKSIRYPDTTHTKK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01211}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01211};
|
cell differentiation [GO:0030154]; collagen fibril organization [GO:0030199]; dorsal/ventral pattern formation [GO:0009953]; protein processing [GO:0016485]; skeletal system development [GO:0001501]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270]
|
PF01400;PF00431;PF14670;
|
3.40.390.10;2.10.25.10;2.60.120.290;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis.
|
Homo sapiens (Human)
|
O43900
|
PRIC3_HUMAN
|
MFARGSRRRRSGRAPPEAEDPDRGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVHAVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRGIVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHVGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMDHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCGRALLGRPFLPRRGLIFCSRACSLGSEPTAPGPSRRSWSAGPVTAPLAASTASFSAVKGASETTTKGTSTELAPATGPEEPSRFLRGAPHRHSMPELGLRSVPEPPPESPGQPNLRPDDSAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRAPSRRRHHHHNHHHHHNRHPSRRRHYQCDAGSGSDSESCSSSPSSSSSESSEDDGFFLGERIPLPPHLCRPMPAQDTAMETFNSPSLSLPRDSRAGMPRQARDKNCIVA
| null | null |
cell projection organization [GO:0030030]
|
mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
zinc ion binding [GO:0008270]
|
PF00412;PF06297;
|
2.10.110.10;
|
Prickle / espinas / testin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69, ECO:0000269|PubMed:32516135}. Cell membrane {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side {ECO:0000250|UniProtKB:A8WH69}. Mitochondrion {ECO:0000269|PubMed:32516135}. Note=Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity). WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}.
| null | null | null | null | null |
FUNCTION: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (PubMed:32516135). {ECO:0000250|UniProtKB:A8WH69, ECO:0000269|PubMed:32516135}.
|
Homo sapiens (Human)
|
O43903
|
GAS2_HUMAN
|
MCTALSPKVRSGPGLSDMHQYSQWLASRHEANLLPMKEDLALWLTNLLGKEITAETFMEKLDNGALLCQLAETMQEKFKESMDANKPTKNLPLKKIPCKTSAPSGSFFARDNTANFLSWCRDLGVDETCLFESEGLVLHKQPREVCLCLLELGRIAARYGVEPPGLIKLEKEIEQEETLSAPSPSPSPSSKSSGKKSTGNLLDDAVKRISEDPPCKCPNKFCVERLSQGRYRVGEKILFIRMLHNKHVMVRVGGGWETFAGYLLKHDPCRMLQISRVDGKTSPIQSKSPTLKDMNPDNYLVVSASYKAKKEIK
| null | null |
actin crosslink formation [GO:0051764]; antral ovarian follicle growth [GO:0001547]; apoptotic process [GO:0006915]; basement membrane organization [GO:0071711]; cell cycle [GO:0007049]; initiation of primordial ovarian follicle growth [GO:0001544]; ovulation [GO:0030728]; regulation of cell cycle [GO:0051726]; regulation of cell shape [GO:0008360]; regulation of Notch signaling pathway [GO:0008593]
|
actin filament [GO:0005884]; cytosol [GO:0005829]; membrane [GO:0016020]; stress fiber [GO:0001725]
|
actin filament binding [GO:0051015]; cytoskeletal anchor activity [GO:0008093]; microtubule binding [GO:0008017]
|
PF00307;PF02187;
|
1.10.418.10;3.30.920.20;
|
GAS2 family
|
PTM: Cleaved, during apoptosis, on a specific aspartic residue by caspases.; PTM: Phosphorylated on serine residues during the G0-G1 transition phase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:24706950}. Membrane {ECO:0000250|UniProtKB:P11862}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11862}. Note=Component of the microfilament system. Colocalizes with actin fibers at the cell border and along the stress fibers in growth-arrested fibroblasts. Mainly membrane-associated. When hyperphosphorylated, accumulates at membrane ruffles. {ECO:0000250|UniProtKB:P11862}.
| null | null | null | null | null |
FUNCTION: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May be involved in the membrane ruffling process (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43909
|
EXTL3_HUMAN
|
MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEAGKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLHNCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVILVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQSTFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEARSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGEREDRLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNEAALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQIPAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDFYRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPREQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVDSVLFKTRLPHDKTKCFKFI
|
2.4.1.223
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9ES89};
|
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of inflammatory response [GO:0050728]; negative regulation of inflammatory response to wounding [GO:0106015]; negative regulation of keratinocyte differentiation [GO:0045617]; positive regulation of cell growth [GO:0030307]; positive regulation of detection of glucose [GO:2000972]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein glycosylation [GO:0006486]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0001888]; glycosyltransferase activity [GO:0016757]; magnesium ion binding [GO:0000287]; protein-hormone receptor activity [GO:0016500]
|
PF03016;PF09258;
| null |
Glycosyltransferase 47 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000269|PubMed:10639137}. Golgi apparatus {ECO:0000269|PubMed:28132690}. Cell membrane {ECO:0000269|PubMed:19158046}. Nucleus {ECO:0000269|PubMed:19158046}. Note=Interaction with REG3A induces its translocation to the nucleus. {ECO:0000269|PubMed:19158046}.
|
CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16221, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12574, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132093, ChEBI:CHEBI:132104; EC=2.4.1.223; Evidence={ECO:0000269|PubMed:11390981, ECO:0000269|PubMed:35676258, ECO:0000305|PubMed:28132690, ECO:0000305|PubMed:28148688};
| null |
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
| null | null |
FUNCTION: Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS) (PubMed:28132690, PubMed:28148688). Initiates HS synthesis by transferring the first N-acetyl-alpha-D-glucosamine (alpha-GlcNAc) residue (GlcNAcT-I activity) to the tetrasaccharide linker (GlcA-Gal-Gal-Xyl-)Ser core linker (PubMed:11390981, PubMed:35676258). May also transfer alpha-GlcNAc residues during HS elongation (GlcNAcT-II activity) (PubMed:11390981, PubMed:35676258). Lacks glucuronyl transferase II (GlcAT-II) activity (PubMed:11390981, PubMed:35676258). Important for both skeletal development and hematopoiesis, through the formation of HS proteoglycans (HSPGs) (PubMed:11390981, PubMed:22727489, PubMed:28132690, PubMed:28148688, PubMed:35676258). Through the synthesis of HS, regulates postnatal pancreatic islet maturation and insulin secretion (By similarity). {ECO:0000250|UniProtKB:Q9WVL6, ECO:0000269|PubMed:11390981, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688, ECO:0000269|PubMed:35676258}.; FUNCTION: Receptor for REG3A, REG3B and REG3G, induces the activation of downstream signaling pathways such as PI3K-AKT or RAS-RAF-MEK-ERK signaling pathway (PubMed:22727489, PubMed:27830702, PubMed:34099862). Required for the function of REG3A in regulating keratinocyte proliferation and differentiation (PubMed:22727489). Required for the inhibition of skin inflammation mediated by REGA through the activation of PI3K-AKT-STAT3 pathway (PubMed:27830702). Required for the function of REGA and REG3G in glucose tolerance in pancreas (PubMed:19158046). Expressed in microglia, is activated by nociceptor-derived REG3G in response to endotoxins, leading to the inhibition of kynurenine pathway to prevent endotoxic death (By similarity). {ECO:0000250|UniProtKB:Q9WVL6, ECO:0000269|PubMed:19158046, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:27830702, ECO:0000269|PubMed:34099862}.
|
Homo sapiens (Human)
|
O43913
|
ORC5_HUMAN
|
MPHLENVVLCRESQVSILQSLFGERHHFSFPSIFIYGHTASGKTYVTQTLLKTLELPHVFVNCVECFTLRLLLEQILNKLNHLSSSEDGCSTEITCETFNDFVRLFKQVTTAENLKDQTVYIVLDKAEYLRDMEANLLPGFLRLQELADRNVTVLFLSEIVWEKFRPNTGCFEPFVLYFPDYSIGNLQKILSHDHPPEYSADFYAAYINILLGVFYTVCRDLKELRHLAVLNFPKYCEPVVKGEASERDTRKLWRNIEPHLKKAMQTVYLREISSSQWEKLQKDDTDPGQLKGLSAHTHVELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHEKTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTLVGHDDQLDGPKYKCTVSLDFIRAIARTVNFDIIKYLYDFL
| null | null |
DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; regulation of DNA replication [GO:0006275]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nuclear origin of replication recognition complex [GO:0005664]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; origin recognition complex [GO:0000808]
|
ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; nucleotide binding [GO:0000166]
|
PF13191;PF14630;PF21639;
|
3.40.50.300;
|
ORC5 family
|
PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for efficient DNA replication origin site activation. Ubiquitination levels are low in mitotic and early G1-phAse cells and are induced in late G1-/early S-phase, peaking in S-phase and decrease toward the end of the cell cycle. {ECO:0000269|PubMed:31160578}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31160578}. Chromosome {ECO:0000269|PubMed:31160578}.
| null | null | null | null | null |
FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. {ECO:0000269|PubMed:31160578}.
|
Homo sapiens (Human)
|
O43914
|
TYOBP_HUMAN
|
MGGLEPCSRLLLLPLLLAVSGLRPVQAQAQSDCSCSTVSPGVLAGIVMGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK
| null | null |
actin cytoskeleton organization [GO:0030036]; apoptotic cell clearance [GO:0043277]; cellular defense response [GO:0006968]; forebrain development [GO:0030900]; intracellular signal transduction [GO:0035556]; microglial cell activation involved in immune response [GO:0002282]; myeloid leukocyte activation [GO:0002274]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of transforming growth factor beta1 production [GO:0032911]; negative regulation of type I interferon production [GO:0032480]; neutrophil activation involved in immune response [GO:0002283]; osteoclast differentiation [GO:0030316]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage fusion [GO:0034241]; positive regulation of microglial cell mediated cytotoxicity [GO:1904151]; positive regulation of natural killer cell activation [GO:0032816]; positive regulation of osteoclast development [GO:2001206]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of tumor necrosis factor production [GO:0032760]; protein stabilization [GO:0050821]; response to axon injury [GO:0048678]; signal transduction [GO:0007165]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stimulatory killer cell immunoglobulin-like receptor signaling pathway [GO:0002222]
|
cell surface [GO:0009986]; membrane [GO:0016020]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
| null |
1.10.287.770;
|
TYROBP family
|
PTM: Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation. {ECO:0000269|PubMed:9490415}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9655483}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (PubMed:10604985, PubMed:9490415, PubMed:9655483). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (PubMed:9490415). Also has an inhibitory role in some cells (PubMed:21727189). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (PubMed:15557162, PubMed:16920917, PubMed:17928527, PubMed:26221034). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (PubMed:10449773). Associates with natural killer (NK) cell receptors such as KIR2DS2 and the KLRD1/KLRC2 heterodimer to mediate NK cell activation (PubMed:23715743, PubMed:9490415, PubMed:9655483). Also enhances trafficking and cell surface expression of NK cell receptors KIR2DS1, KIR2DS2 and KIR2DS4 and ensures their stability at the cell surface (PubMed:23715743). Associates with SIRPB1 to mediate activation of myeloid cells such as monocytes and dendritic cells (PubMed:10604985). Associates with TREM1 to mediate activation of neutrophils and monocytes (PubMed:10799849). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (PubMed:11602640). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (PubMed:18957693). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (PubMed:25957402). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability (By similarity). Negatively regulates B cell proliferation (PubMed:21727189). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity). {ECO:0000250|UniProtKB:O54885, ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:10604985, ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:11602640, ECO:0000269|PubMed:15557162, ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527, ECO:0000269|PubMed:18957693, ECO:0000269|PubMed:21727189, ECO:0000269|PubMed:23715743, ECO:0000269|PubMed:25957402, ECO:0000269|PubMed:26221034, ECO:0000269|PubMed:9490415, ECO:0000269|PubMed:9655483}.
|
Homo sapiens (Human)
|
O43915
|
VEGFD_HUMAN
|
MYREWVVVNVFMMLYVQLVQGSSNEHGPVKRSSQSTLERSEQQIRAASSLEELLRITHSEDWKLWRCRLRLKSFTSMDSRSASHRSTRFAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRRSIQIPEEDRCSHSKKLCPIDMLWDSNKCKCVLQEENPLAGTEDHSHLQEPALCGPHMMFDEDRCECVCKTPCPKDLIQHPKNCSCFECKESLETCCQKHKLFHPDTCSCEDRCPFHTRPCASGKTACAKHCRFPKEKRAAQGPHSRKNP
| null | null |
dopaminergic neuron differentiation [GO:0071542]; fibroblast proliferation [GO:0048144]; induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of protein phosphorylation [GO:0001934]; response to bacterium [GO:0009617]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor signaling pathway [GO:0038084]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; platelet alpha granule lumen [GO:0031093]
|
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; platelet-derived growth factor receptor binding [GO:0005161]; vascular endothelial growth factor receptor 3 binding [GO:0043185]; vascular endothelial growth factor receptor binding [GO:0005172]
|
PF03128;PF00341;
|
2.10.90.10;
|
PDGF/VEGF growth factor family
|
PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer linked by disulfide bonds before secretion. The fully processed VEGF-D is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions. {ECO:0000269|PubMed:10542248}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors. {ECO:0000269|PubMed:21148085}.
|
Homo sapiens (Human)
|
O43916
|
CHST1_HUMAN
|
MQCSWKAVLLLALASIAIQYTAIRTFTAKSFHTCPGLAEAGLAERLCEESPTFAYNLSRKTHILILATTRSGSSFVGQLFNQHLDVFYLFEPLYHVQNTLIPRFTQGKSPADRRVMLGASRDLLRSLYDCDLYFLENYIKPPPVNHTTDRIFRRGASRVLCSRPVCDPPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLRALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNLDVTQLTTVCEDFSNSVSTGLMRPPWLKGKYMLVRYEDLARNPMKKTEEIYGFLGIPLDSHVARWIQNNTRGDPTLGKHKYGTVRNSAATAEKWRFRLSYDIVAFAQNACQQVLAQLGYKIAASEEELKNPSVSLVEERDFRPFS
|
2.8.2.21
| null |
galactose metabolic process [GO:0006012]; inflammatory response [GO:0006954]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; N-acetylglucosamine metabolic process [GO:0006044]; polysaccharide metabolic process [GO:0005976]; sulfur compound metabolic process [GO:0006790]
|
Golgi membrane [GO:0000139]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]
|
keratan sulfotransferase activity [GO:0045130]; N-acetylglucosamine 6-O-sulfotransferase activity [GO:0001517]; sulfotransferase activity [GO:0008146]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family, Gal/GlcNAc/GalNAc subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21; Evidence={ECO:0000269|PubMed:17690104, ECO:0000269|PubMed:9405439};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.4 mM for Galbeta1->4(6-sulfo)GlcNAcbeta1->3(6-sulfo)Galbeta1->4(6-sulfo)GlcNAc (L2L4) {ECO:0000269|PubMed:10642612}; KM=0.65 mM for NeuAcalpha2->3Galbeta1->4(6-sulfo)GlcNAcbeta1->3(6-sulfo)Galbeta1->4(6-sulfo)GlcNAc (SL2L4) {ECO:0000269|PubMed:10642612}; KM=0.38 mM for keratan sulfate {ECO:0000269|PubMed:10642612}; Vmax=85 pmol/min/mg enzyme toward Galbeta1->4(6-sulfo)GlcNAcbeta1->3(6-sulfo)Galbeta1->4(6-sulfo)GlcNAc (L2L4) {ECO:0000269|PubMed:10642612}; Vmax=20 pmol/min/mg enzyme toward NeuAcalpha2->3Galbeta1->4(6-sulfo)GlcNAcbeta1->3(6-sulfo)Galbeta1->4(6-sulfo)GlcNAc (SL2L4) {ECO:0000269|PubMed:10642612}; Vmax=6.1 pmol/min/mg enzyme toward keratan sulfate {ECO:0000269|PubMed:10642612};
|
PATHWAY: Glycan metabolism. {ECO:0000269|PubMed:17690104}.
| null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of internal galactose (Gal) residues of keratan. Cooperates with B4GALT4 and B3GNT7 glycosyltransferases and CHST6 sulfotransferase to construct and elongate disulfated disaccharide unit [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer (PubMed:10642612, PubMed:17690104, PubMed:9405439). Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer (PubMed:9405439). Involved in biosynthesis of phosphacan, a major keratan sulfate proteoglycan in the developing brain (By similarity). Involved in biosynthesis of 6-sulfoGalbeta-containing O-linked glycans in high endothelial venules of lymph nodes. May act in a synergistic manner with CHST4 to generate sialyl 6',6-disulfo Lewis X motif, a recognition determinant for immune cell receptors implicated in leukocyte trafficking (PubMed:10330415). Catalyzes sulfation of N-acetyllactosamine (LacNAc) oligosaccharides with highest efficiency for sialylated LacNAc structures (PubMed:10642612). {ECO:0000250|UniProtKB:Q9EQC0, ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:10642612, ECO:0000269|PubMed:17690104, ECO:0000269|PubMed:9405439}.
|
Homo sapiens (Human)
|
O43918
|
AIRE_HUMAN
|
MATDAALRRLLRLHRTEIAVAVDSAFPLLHALADHDVVPEDKFQETLHLKEKEGCPQAFHALLSWLLTQDSTAILDFWRVLFKDYNLERYGRLQPILDSFPKDVDLSQPRKGRKPPAVPKALVPPPRLPTKRKASEEARAAAPAALTPRGTASPGSQLKAKPPKKPESSAEQQRLPLGNGIQTMSASVQRAVAMSSGDVPGARGAVEGILIQQVFESGGSKKCIQVGGEFYTPSKFEDSGSGKNKARSSSGPKPLVRAKGAQGAAPGGGEARLGQQGSVPAPLALPSDPQLHQKNEDECAVCRDGGELICCDGCPRAFHLACLSPPLREIPSGTWRCSSCLQATVQEVQPRAEEPRPQEPPVETPLPPGLRSAGEEVRGPPGEPLAGMDTTLVYKHLPAPPSAAPLPGLDSSALHPLLCVGPEGQQNLAPGARCGVCGDGTDVLRCTHCAAAFHWRCHFPAGTSRPGTGLRCRSCSGDVTPAPVEGVLAPSPARLAPGPAKDDTASHEPALHRDDLESLLSEHTFDGILQWAIQSMARPAAPFPS
| null | null |
central tolerance induction to self antigen [GO:0002509]; humoral immune response [GO:0006959]; immune response [GO:0006955]; negative thymic T cell selection [GO:0045060]; peripheral T cell tolerance induction [GO:0002458]; positive regulation of chemokine production [GO:0032722]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of thymocyte migration [GO:2000410]; thymus epithelium morphogenesis [GO:0097536]; transcription by RNA polymerase II [GO:0006366]
|
cytoplasm [GO:0005737]; female germ cell nucleus [GO:0001674]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; translation regulator activity [GO:0045182]; zinc ion binding [GO:0008270]
|
PF03172;PF00628;PF01342;
|
3.10.390.10;3.30.40.10;
| null |
PTM: Phosphorylated. Phosphorylation could trigger oligomerization. {ECO:0000269|PubMed:11533054}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14974083, ECO:0000269|PubMed:26084028}. Cytoplasm {ECO:0000269|PubMed:11274163, ECO:0000269|PubMed:14974083}. Note=Predominantly nuclear but also cytoplasmic (PubMed:11274163, PubMed:14974083). Found in nuclear body-like structures (dots) and in a filamentous vimentin-like pattern (PubMed:11274163, PubMed:14974083, PubMed:26084028). Associated with tubular structures (PubMed:11274163, PubMed:14974083). {ECO:0000269|PubMed:11274163, ECO:0000269|PubMed:14974083, ECO:0000269|PubMed:26084028}.
| null | null | null | null | null |
FUNCTION: Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) (PubMed:26084028). Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla (PubMed:26084028). Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program. Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression. Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes. In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection. In secondary lymphoid organs, induces functional inactivation of CD4(+) T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli (By similarity). {ECO:0000250|UniProtKB:Q9Z0E3, ECO:0000269|PubMed:11274163, ECO:0000269|PubMed:18292755, ECO:0000269|PubMed:26084028, ECO:0000305|PubMed:19302042, ECO:0000305|PubMed:26972725}.
|
Homo sapiens (Human)
|
O43920
|
NDUS5_HUMAN
|
MPFLDIQKRFGLNIDRWLTIQSGEQPYKMAGRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFVECLLRQKTMRRAGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF10200;
| null |
Complex I NDUFS5 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}. Mitochondrion intermembrane space {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
|
Homo sapiens (Human)
|
O43921
|
EFNA2_HUMAN
|
MAPAQRPLLPLLLLLLPLPPPPFARAEDAARANSDRYAVYWNRSNPRFHAGAGDDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMEHYVLYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNAVDRPCLRLKVYVRPTNETLYEAPEPIFTSNNSCSSPGGCRLFLSTIPVLWTLLGS
| null | null |
axon guidance [GO:0007411]; bone remodeling [GO:0046849]; cell-cell signaling [GO:0007267]; ephrin receptor signaling pathway [GO:0048013]; olfactory bulb development [GO:0021772]; osteoclast differentiation [GO:0030316]
|
neuromuscular junction [GO:0031594]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
ephrin receptor binding [GO:0046875]
|
PF00812;
|
2.60.40.420;
|
Ephrin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43924
|
PDE6D_HUMAN
|
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV
| null | null |
response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]
|
GTPase inhibitor activity [GO:0005095]; small GTPase binding [GO:0031267]
|
PF05351;
|
2.70.50.40;
|
PDE6D/unc-119 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:9712853}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9712853}; Peripheral membrane protein {ECO:0000269|PubMed:9712853}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24166846}.
| null | null | null | null | null |
FUNCTION: Promotes the release of prenylated target proteins from cellular membranes (PubMed:9712853). Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (PubMed:22002721, PubMed:23698361). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (PubMed:24166846). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity). {ECO:0000250|UniProtKB:O55057, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23559067, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24166846, ECO:0000269|PubMed:9712853}.
|
Homo sapiens (Human)
|
O43927
|
CXL13_HUMAN
|
MKFISTSLLLMLLVSSLSPVQGVLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNGCPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKRSSSTLPVPVFKRKIP
| null | null |
activation of GTPase activity [GO:0090630]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; B cell chemotaxis [GO:0035754]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; chronic inflammatory response [GO:0002544]; defense response to bacterium [GO:0042742]; endothelial cell chemotaxis to fibroblast growth factor [GO:0035768]; germinal center formation [GO:0002467]; immune response [GO:0006955]; inflammatory response [GO:0006954]; lymphocyte chemotaxis across high endothelial venule [GO:0002518]; negative regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000545]; neutrophil chemotaxis [GO:0030593]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of integrin activation [GO:0033625]; positive regulation of T cell chemotaxis [GO:0010820]; regulation of angiogenesis [GO:0045765]; regulation of humoral immune response [GO:0002920]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
CCR10 chemokine receptor binding [GO:0031735]; chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; CXCR5 chemokine receptor binding [GO:0031724]; fibroblast growth factor binding [GO:0017134]; heparin binding [GO:0008201]; receptor ligand activity [GO:0048018]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. Does not induce calcium release in B-lymphocytes. Binds to BLR1/CXCR5.
|
Homo sapiens (Human)
|
O43929
|
ORC4_HUMAN
|
MSSRKSKSNSLIHTECLSQVQRILRERFCRQSPHSNLFGVQVQYKHLSELLKRTALHGESNSVLIIGPRGSGKTMLINHALKELMEIEEVSENVLQVHLNGLLQINDKIALKEITRQLNLENVVGDKVFGSFAENLSFLLEALKKGDRTSSCPVIFILDEFDLFAHHKNQTLLYNLFDISQSAQTPIAVIGLTCRLDILELLEKRVKSRFSHRQIHLMNSFGFPQYVKIFKEQLSLPAEFPDKVFAEKWNENVQYLSEDRSVQEVLQKHFNISKNLRSLHMLLMLALNRVTASHPFMTAVDLMEASQLCSMDSKANIVHGLSVLEICLIIAMKHLNDIYEEEPFNFQMVYNEFQKFVQRKAHSVYNFEKPVVMKAFEHLQQLELIKPMERTSGNSQREYQLMKLLLDNTQIMNALQKYPNCPTDVRQWATSSLSWL
| null | null |
DNA replication initiation [GO:0006270]; polar body extrusion after meiotic divisions [GO:0040038]; protein polymerization [GO:0051258]
|
chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nuclear origin of replication recognition complex [GO:0005664]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; origin recognition complex [GO:0000808]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA replication origin binding [GO:0003688]; nucleotide binding [GO:0000166]
|
PF13191;PF14629;
|
3.40.50.300;
|
ORC4 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}.
|
Homo sapiens (Human)
|
O43933
|
PEX1_HUMAN
|
MWGSDRLAGAGGGGAAVTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSHQPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPCSHVVSCQQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAASYGRLETDTKLLIQPKTRRAKENTFSKADAEYKKLHSYGRDQKGMMKELQTKQLQSNTVGITESNENESEIPVDSSSVASLWTMIGSIFSFQSEKKQETSWGLTEINAFKNMQSKVVPLDNIFRVCKSQPPSIYNASATSVFHKHCAIHVFPWDQEYFDVEPSFTVTYGKLVKLLSPKQQQSKTKQNVLSPEKEKQMSEPLDQKKIRSDHNEEDEKACVLQVVWNGLEELNNAIKYTKNVEVLHLGKVWIPDDLRKRLNIEMHAVVRITPVEVTPKIPRSLKLQPRENLPKDISEEDIKTVFYSWLQQSTTTMLPLVISEEEFIKLETKDGLKEFSLSIVHSWEKEKDKNIFLLSPNLLQKTTIQVLLDPMVKEENSEEIDFILPFLKLSSLGGVNSLGVSSLEHITHSLLGRPLSRQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAVPEHEHSPDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVSAQGVHIFQCVQHIQPPNQEQRCEILCNVIKNKLDCDINKFTDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLSSGLQDGSSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGTSSDLSSQCLSAPSSMTQDLPGVPGKDQLFSQPPVLRTASQEGCQELTQEQRDQLRADISIIKGRYRSQSGEDESMNQPGPIKTRLAISQSHLMTALGHTRPSISEDDWKNFAELYESFQNPKRRKNQSGTMFRPGQKVTLA
|
3.6.4.-
| null |
microtubule-based peroxisome localization [GO:0060152]; peroxisome organization [GO:0007031]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein targeting to peroxisome [GO:0006625]; protein unfolding [GO:0043335]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; protein transporter activity [GO:0140318]; protein-containing complex binding [GO:0044877]; ubiquitin-dependent protein binding [GO:0140036]
|
PF00004;PF17862;PF09262;PF09263;
|
1.10.8.60;2.40.40.20;3.10.330.10;3.40.50.300;
|
AAA ATPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16854980}. Peroxisome membrane {ECO:0000269|PubMed:11439091, ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980, ECO:0000269|PubMed:21362118}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16854980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000269|PubMed:16854980};
| null | null | null | null |
FUNCTION: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:11439091, PubMed:16314507, PubMed:16854980, PubMed:21362118, PubMed:29884772). Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (PubMed:29884772). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (PubMed:29884772). {ECO:0000269|PubMed:11439091, ECO:0000269|PubMed:16314507, ECO:0000269|PubMed:16854980, ECO:0000269|PubMed:21362118, ECO:0000269|PubMed:29884772}.
|
Homo sapiens (Human)
|
O43948
|
PK4_PLAFA
|
MKKRIRSSYKVGSSNKYHKKNYTDNEKDKKKYRSYKEKHINEKMFDKKEFLNFLTNFNKKFMKKNSLVDHLMKMNDKAEDNYDGYNSSGSRYNNINDDGVELCGTKRYTNNKNNSDYDNYNNNNNMKNKRYSNKKHNNDNIIINNNNNKYTDERKYRNKSIKEDVDYTNDYYNIQLNNNKINNNQTKNKIDTIRNISHEKLGNNKSSSARNLSLIQTSHIPYDAPLADFLENGRFLRTFENISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVSSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMHLMPKEIQNLVKKNKDTFKKRLTKNKKYSNNCISDSSNNNNSSCYSASSYNSSINSNYRNMKLWIKKKEQSPDMKRYKEVLRKNNAPNLVFYSDNDGLTSKNKENPEKNHNPFLSDKNFSDSIYKKKKSHDYNSSSHKLKKRKNKKKKSKKKRKSKSKIKTNAQGIYEESENDEGRDHFQYKKGKEQFSKFIGKLILWVLHKVSKNMILLIMVILSEEDRDLIVFADNEESNGNDQQMIRHDNMNNENVIIKHRNEDDKNGLDGDKNGLDGDKNGLDGDKNGLDGDKNELDDNKNELDDLLMKQKINSLTRNDIVNIENENPAPHATNNIKNKKVDLNGELTYYDYVGKNEVIPNSRTETNVESINTNGMFNNKFSVMKDEGGEYKKKENMTWGDTKRDGLYENGKHEKDGLGVNKCITNKYIENDDDDDDDDDDNNNNNNIDERKKDLKKKQKNAITKGNEDLLATNGTNNKEKRKKDDDINKNMEKIKSYKKKTPVPEFSIVLLLQMELCKGYTLRKWLDRSTRSDKPLHFTYSDKKMNHPLEFDLFKQLIKGLKDIHATCFIHRDLKPENIFVDNDTYTLKIGDLGLVRFIEEKKREKDFNNIDCYKDNIYTDINQNRITSQISIKGQIIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFTTIMERYKRLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADVYSKIKVLLDPHLTDFAFSFNDIHNEHMNKPPQGTNNFERITDNKDKFVIQSVVDMKNKVENEEIPIEKGLNSNVENIKNENNGADK
|
2.7.11.1
| null |
negative regulation of translation [GO:0017148]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily
|
PTM: Auto-phosphorylated. {ECO:0000269|PubMed:9371731}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A509AMC3}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9371731}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:9371731}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A509AMC3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:A0A509AMC3};
| null | null | null | null |
FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:9371731). Plays a role in trophozoite differentiation into schizonts (By similarity). {ECO:0000250|UniProtKB:C6KTB8, ECO:0000269|PubMed:9371731}.
|
Plasmodium falciparum
|
O44074
|
SDHB_ASCSU
|
MLRGSTSVCRSLELVTQAARYASAATAAAPTGKRIKTFEIYRFNPEEPGAKPKLQKFDVDLDKCGTMVLDALIKIKNEVDPTLTFRRSCREGICGSCAMNIAGENTLACICNIDQNTSKTTKIYPLPHMFVIKDLVPDMNLFYAQYASIQPWLQKKTKINLGEKQQYQSIKEQEKLDGLYECILCACCSASCPSYWWNADKYLGPAVLMQAYRWIIDSRDDSAAERLARMQDGFSAFKCHTIMNCTKTCPKHLNPARAIGEIKMLLTKMKTKPAPLPTPANF
|
1.3.5.1
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|RuleBase:RU361237}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|RuleBase:RU361237, ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000255|RuleBase:RU361237}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000255|RuleBase:RU361237, ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|RuleBase:RU361237}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|RuleBase:RU361237, ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225};
|
respiratory electron transport chain [GO:0022904]; tricarboxylic acid cycle [GO:0006099]
|
mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; plasma membrane [GO:0005886]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177]
|
PF13085;PF13534;
|
3.10.20.30;1.10.1060.10;
|
Succinate dehydrogenase/fumarate reductase iron-sulfur protein family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|RuleBase:RU361237, ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0000269|PubMed:2843227, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436}; Peripheral membrane protein {ECO:0000255|RuleBase:RU361237}; Matrix side {ECO:0000255|RuleBase:RU361237}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + succinate = a ubiquinol + fumarate; Xref=Rhea:RHEA:13713, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; EC=1.3.5.1; Evidence={ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:26198225, ECO:0000269|PubMed:2843227, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13714; Evidence={ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:26198225, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436}; CATALYTIC ACTIVITY: Reaction=a rhodoquinone + succinate = a rhodoquinol + fumarate; Xref=Rhea:RHEA:75711, Rhea:RHEA-COMP:18569, Rhea:RHEA-COMP:18570, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:194432, ChEBI:CHEBI:194433; EC=1.3.5.1; Evidence={ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:2843227, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75713; Evidence={ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:2843227, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.09 mM for fumarate (adult complex II, at 25 degrees Celsius and in anaerobic conditions) {ECO:0000269|PubMed:2843227}; KM=190 uM for succinate (free larvae complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:8435436}; KM=740 uM for succinate (adult complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:8435436}; KM=31 uM for fumarate (adult complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:8435436}; KM=150 uM for fumarate (free larvae complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:8435436}; KM=608 uM for succinate (adult complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:7822332}; KM=3 uM for ubquinone-1 (adult and larval complex II, succinate as cosubstrate and at 25 degrees Celsius) {ECO:0000269|PubMed:7822332}; KM=143 uM for fumarate (adult complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:7822332}; KM=153 uM for succinate (free larvae complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:7822332}; KM=455 uM for fumarate (free larvae complex II, at 25 degrees Celsius) {ECO:0000269|PubMed:7822332}; KM=28.5 uM for fumarate (free larvae complex II, n-decyl-rhodoquinol as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=47.3 uM for n-decyl-rhodoquinol (free larvae complex II, fumarate as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=385 uM for succinate (free larvae complex II, n-decyl-ubiquinone as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=12 uM for n-decyl-ubiquinone (free larvae complex II, succinate as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=16.6 uM for fumarate (adult complex II, n-decyl-rhodoquinol as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=40.6 uM for n-decyl-rhodoquinol (free larvae complex II, fumarate as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=625 uM for succinate (adult complex II, n-decyl-ubiquinone as cosubstrate) {ECO:0000269|PubMed:12742584}; KM=11.4 uM for n-decyl-ubiquinone (adult complex II, succinate as cosubstrate) {ECO:0000269|PubMed:12742584}; Vmax=49 umol/min/mg enzyme toward fumarate (adult complex II, at 25 degrees Celsius and in anaerobic conditions) {ECO:0000269|PubMed:2843227}; Vmax=2.99 umol/min/mg enzyme toward fumarate (free larvae complex II, n-decyl-rhodoquinol as cosubstrate) {ECO:0000269|PubMed:12742584}; Vmax=7.53 umol/min/mg enzyme toward succinate (free larvae complex II, n-decyl-ubiquinone as cosubstrate) {ECO:0000269|PubMed:12742584}; Vmax=0.89 umol/min/mg enzyme toward fumarate (adult complex II, n-decyl-rhodoquinol as cosubstrate) {ECO:0000269|PubMed:12742584}; Vmax=1.39 umol/min/mg enzyme toward succinate (adult complex II, n-decyl-ubiquinone as cosubstrate) {ECO:0000269|PubMed:12742584}; Note=kcat is 6000 min(-1) with fumarate as substrate (adult complex II, at 25 degrees Celsius and in anaerobic conditions). {ECO:0000269|PubMed:2843227};
|
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1. {ECO:0000255|RuleBase:RU361237, ECO:0000269|PubMed:7822332}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:2843227};
| null |
FUNCTION: Iron-sulfur protein (Ip) subunit of the mitochondrial electron transport chain complex II which, together with the flavoprotein (Fp) subunit forms the catalytic core of the complex (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the free-living egg-larvae stages, which occur in an aerobic environment, complex II acts as a succinate dehydrogenase by transferring electrons from succinate to ubiquinone (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, complex II acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). {ECO:0000269|PubMed:10743611, ECO:0000269|PubMed:12742584, ECO:0000269|PubMed:17933581, ECO:0000269|PubMed:2843227, ECO:0000269|PubMed:7822332, ECO:0000269|PubMed:8435436}.
|
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
|
O44081
|
DKC1_DROME
|
MADVEVRKEKKKKKIKEEPLDGDDIGTLQKQGNFQIKPSSKIAELDTSQWPLLLKNFDKLNIRSNHYTPLAHGSSPLNRDIKEYMKTGFINLDKPSNPSSHEVVAWIKKILKVEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQSAGKEYVAIFKLHGAVESVAKVRQGLEKLRGALFQRPPLISAVKRQLRVRTVYDSKLLDYDETRNMGVFWVSCEAGSYIRTMCVHLGLVLGVGGQMLELRRVRSGIQSERDGMVTMHDVLDAMWLYENHKDESMLRRVIKPLEGLLVNHKRIIMKDSSVNAVCYGAKITLPGVLRYEDGIEIDQEIVICTTKGEAICLAIALMTTATMASCDHGVVAKIKRVIMERDTYPRKWGLGPKASAKKALIAAGKLDKFGRPNENTPKEWLTGYVDYNAKKPAAQEVSPTNGSSEPSKRKLSTSSVEETAAAAVSEETPSKDKKKKKKKHKGDEEAPEAAEEEAEPVEKEKKKKKKKDKDRDRDEAQE
|
5.4.99.-
| null |
box H/ACA RNA 3'-end processing [GO:0000495]; germ cell development [GO:0007281]; mRNA pseudouridine synthesis [GO:1990481]; pseudouridine synthesis [GO:0001522]; ribosome biogenesis [GO:0042254]; rRNA processing [GO:0006364]; rRNA pseudouridine synthesis [GO:0031118]; snRNA pseudouridine synthesis [GO:0031120]; wing disc development [GO:0035220]
|
box H/ACA snoRNP complex [GO:0031429]; nucleolus [GO:0005730]
|
pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]
|
PF08068;PF01472;PF16198;PF01509;
|
3.30.2350.10;2.30.130.10;
|
Pseudouridine synthase TruB family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10087258, ECO:0000269|PubMed:9829824}.
|
CATALYTIC ACTIVITY: Reaction=a uridine in RNA = a pseudouridine in RNA; Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
| null | null | null | null |
FUNCTION: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for maintenance of the germline stem cell lineage during spermatogenesis. {ECO:0000269|PubMed:10087258, ECO:0000269|PubMed:12645924, ECO:0000269|PubMed:9829824}.
|
Drosophila melanogaster (Fruit fly)
|
O44126
|
LEG1_HAECO
|
MVSQFLHWYEYNKPVPYRSLLQEKIEPGQTLIVKGSTIDESQRFTINLHSKSADFSGNDVPLHISVRFDEGKVVMNTFANGEWGKEERKSLPIKKGDSFDIRIRAHDDRFQIVIDQKEFKDYEHRLPLTSITHLSIDGDLYLNHVHWGGKYYPVPYESGIASGFPIDKTLLIFGTVEKKAKRFNINLLRRNGDIALHFNPRFDEKAVIRNALAANEWGNEEREGKMPFEKGVGFDLAIKNEAYAFQIFVNGERFTSFAHRQDPNDISGLQIQGDIELTGIQIQ
| null | null |
negative regulation of mononuclear cell proliferation [GO:0032945]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic process [GO:0042981]; regulation of cytokine production [GO:0001817]; regulation of mononuclear cell proliferation [GO:0032944]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of phagocytosis [GO:0050764]
|
membrane raft [GO:0045121]
|
carbohydrate binding [GO:0030246]; galactoside binding [GO:0016936]
|
PF00337;
|
2.60.120.200;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10599080}.
| null | null | null | null | null |
FUNCTION: Binds galactose. Exerts immunomodulatory effects on host peripheral blood mononuclear cells to down-regulate host immune response (PubMed:25879191, PubMed:27337943, PubMed:28870237). Hemagglutinates human, dog, rabbit, chicken and mouse erythrocytes but does not hemagglutinate the erythrocytes of goat, its natural host (PubMed:17125929). {ECO:0000269|PubMed:17125929, ECO:0000269|PubMed:25879191, ECO:0000269|PubMed:27337943, ECO:0000269|PubMed:28870237}.
|
Haemonchus contortus (Barber pole worm)
|
O44185
|
FLP13_CAEEL
|
MMTSLLTISMFVVAIQAFDSSEIRMLDEQYDTKNPFFQFLENSKRSDRPTRAMDSPLIRFGKRAADGAPLIRFGRAPEASPFIRFGKRAADGAPLIRFGRAPEASPFIRFGKRASPSAPLIRFGRSPSAVPLIRFGRSAAAPLIRFGRASSAPLIRFGRK
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of cellular response to heat [GO:1900034]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]
|
extracellular region [GO:0005576]
|
neuropeptide receptor binding [GO:0071855]
|
PF01581;
| null |
FARP (FMRFamide related peptide) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Probable FMRFamide-like neuropeptides (PubMed:16377032, PubMed:28094002). Binds to neuronal receptors such as dmsr-1 to promote sleep in response to cellular stress also known as stress-induced sleep (SIS) (PubMed:28094002). Plays a role in behaviors associated with SIS, acting in concert with the FMRFamide related peptide, flp-24 and neuropeptide-like protein nlp-8 (PubMed:27546573). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:27546573, ECO:0000269|PubMed:28094002, ECO:0000305}.; FUNCTION: AADGAPLIRF-amide: Inhibits muscle tension in somatic muscle (PubMed:11527423). Acts as a ligand for the npr-22 receptor in vitro (PubMed:16377032). Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:11527423, ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.; FUNCTION: APEASPFIRF-amide: Inhibits muscle tension in somatic muscle (PubMed:9070852). Potent inhibitor of the activity of the dissected pharyngeal myogenic muscle system (PubMed:16187307). Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:16187307, ECO:0000269|PubMed:28094002, ECO:0000269|PubMed:9070852}.; FUNCTION: [ASPSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.; FUNCTION: [SPSAVPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.; FUNCTION: [SAAAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.; FUNCTION: [ASSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro (PubMed:28094002). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.; FUNCTION: [AMDSPLIRF-amide]: Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro. {ECO:0000269|PubMed:28094002}.
|
Caenorhabditis elegans
|
O44249
|
PRP1_MANSE
|
MTDAKNNLLYFFDRPNEPCFMQKGEDKVVFEIPDHYYPDKYKSLSNTLSNRFGNEATKRIPIRNITLPNLEVPMQLPYNDQFSLFVPKHRTMAAKLIDIFMGMRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAETFPDKFMDSKVFLRAREVSNVVISGSRMPVNVPINYTANTTEPEQRVAYFREDIGINLHHWHWHLVYPFDSADRSIVNKDRRGELFYYMHQQIIGRYNVERMCNGLPQVKPFSDFSAPIEEGYFPKLDSQVASRTWPPRFAGSVFRNLDRTVDQVKIDVRKLFTWRDQFLEAIQKMAIKMPNGRELPLDEVTGIDMLGNLMESSIISPNRGYYGDLHNMGHVFAAYTHDPDHRHLEQFGVMGDSATAMRDPFFYRWHRFVDDVFNIYKEKLTPYTNERLDFPGVRVSSVGIEGARPNTLRTLWQQSTVELGRGLDFTPRGSVLARFTHLQHDEFQYVIEVNNTTGGNLMGTVRIFMAPKVDDNGQPMSFNKQRRLMIELDKFSQALRPGTNTIRRRSVDSSVTIPYERTFRNQSERPGDPGTAGAAEFDFCGCGWPHHMLIPKGTAQGYPVVLFVMISNWNNDRIEQDLVGSCNDAASYCGIRDRKYPDKQAMGYPFDRKMANDAATLSDFLRPNMAVRDCSIQFSDTTVERGQQG
|
1.14.18.1
|
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:19805072}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:19805072};
|
defense response [GO:0006952]; melanin biosynthetic process from tyrosine [GO:0006583]; positive regulation of melanization defense response [GO:0035008]
|
extracellular region [GO:0005576]
|
chloride ion binding [GO:0031404]; copper ion binding [GO:0005507]; tyrosinase activity [GO:0004503]
|
PF03723;PF00372;PF03722;
|
1.10.1280.10;2.60.40.1520;1.20.1370.10;
|
Tyrosinase family
|
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9474780}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9474780}.
|
CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1;
| null | null | null | null |
FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization. {ECO:0000269|PubMed:16291091, ECO:0000305}.
|
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
|
O44326
|
HMP2_CAEEL
|
MLLHSTNSYSIFTDHEVETRTSRIRSAMFPDWIPPTSAAEATNSTTSIVEMMQMPTQQLKQSVMDLLTYEGSNDMSGLSLPDLVKLMCDHDESVVARAVHRAYMLSREDPNFFNAPGFDHRSFVEALMAASKSSNVNVRRNAIGALSHMSEQRGGPLLIFRSGGLAEIIRMLYDSLESVVHYAVTTLRNLLMHVSDSRAQARALNAVEALTPHLHKTNPKLLAQVADGLYFLLIDDAPSKITFLSLLGPQILVSILREYSDHRKLIYTVVRCIRSLSVCPSNKPALISLGCLPALYVELCTAKDERSQTAILVAMRNLSDSATNEENLTQLIIKLLEIIRVANDGMTACACGTLSNLTCNNTRNKQTVCSHGGIDALVTAIRRLPEVEEVTEPALCALRHCTARHSLAEEAQSELRFCQAFPVILDQLETLRTPVIKAALGVIRNSALLQTNLIELTQEQTANGHTAVSLTMDILRRAITAIEENPDIAVDGVPMWGVIEGAVSALHQLANHPAVAAACCDDIGQVGNPECPPFLDLLHRLLAHPRLGSMDDEVLEREILGLLYQLSKRPDGARAVESTGVSALLMESRGSQYKSVVTYANGVLSNLKRGDSAAIMNMSNSYDYEMSGSAADWQRDGLERELFAEMYPTNDGGHSESINMALNNSQMRPNHNWYDTDL
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell migration [GO:0016477]; cell migration involved in gastrulation [GO:0042074]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cortical actin cytoskeleton organization [GO:0030866]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; establishment of mitotic spindle orientation [GO:0000132]; left/right axis specification [GO:0070986]; negative regulation of cell division [GO:0051782]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization [GO:0032880]
|
adherens junction [GO:0005912]; catenin complex [GO:0016342]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; DNA-binding transcription factor binding [GO:0140297]; molecular function inhibitor activity [GO:0140678]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; transcription coactivator activity [GO:0003713]
|
PF00514;
|
1.25.10.10;
|
Beta-catenin family
| null |
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:9531567}.
| null | null | null | null | null |
FUNCTION: Required for cell migration during body enclosure and cell shape changes during body elongation (PubMed:9531567). Plays a role in recruitment of the cadherin protein hmr-1 to adherens junctions (PubMed:26412237). {ECO:0000269|PubMed:26412237, ECO:0000269|PubMed:9531567}.
|
Caenorhabditis elegans
|
O44342
|
WBL_DROME
|
MMHILVTLLLVAIHSIPTTWAVTCTGCVDLDELSFEKTVERFPYSVVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRDGCIKEFNEVLKNYANIPDAEQLKLIEKLQAKQEQLTDPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKVTEAKKEELLRKLNILEVFRVHKVTKTAPEKEEL
| null | null |
dorsal/ventral axis specification [GO:0009950]; embryo development ending in birth or egg hatching [GO:0009792]; maternal specification of dorsal/ventral axis, oocyte, soma encoded [GO:0007313]; protein folding in endoplasmic reticulum [GO:0034975]; protein secretion [GO:0009306]; regulation of multicellular organism growth [GO:0040014]
|
endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]
|
protein homodimerization activity [GO:0042803]
|
PF07749;PF07912;
|
1.20.1150.12;3.40.30.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
| null | null | null | null | null |
FUNCTION: Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi. {ECO:0000269|PubMed:11076773, ECO:0000269|PubMed:9568717}.
|
Drosophila melanogaster (Fruit fly)
|
O44386
|
ITA3_DROME
|
MNAESTMFPHIFLALLALISHIEAFNFMPRPSRVINSPKHLKFHINQTRSSYFGYTLVIRQTSIIVGAPRAQSTLESQRTINETGAIYRCSLTNGVCSPYVLDSRGNVDAPYSEYTFDSERKDFQWLGGSMDGGTKDTDKLLVCAPRFYAPSSRDNHLHGVCYWVNNTVASTPQHVTRISPLRLKSEQVKEEDNGNKASFFYIMGELGLSAHVADDNTKFLIGAPGINTWRGSVILYRQVDPVDNPTASRRDTSKALRRTYRDVDSNDYTPEHYAPEIPTPGLWGQEEDSYFGYAVSSGFFDSSNPTKLLYVATAPQANKQSGEAYIFDVRGKSIHKYHVFRGEQFGEYFGYSVLAEDLNGDGKTDVIVSAPQHALEDSHDNGAIYVFINKGFFNFERQILRSPVETMARFGTALSRLGDINHDGYNDVAVGAPFAGNGTVFIYLGSENGLRDQPSQRLDAPSQQPSKYGSHMFGHGLSRGSDIDGNGFNDFAIGAPNAEAVYLYRAYPVVKVHATVKSESREIKPEQEKVKITACYRLSTTSTDKLVQEQELAIRIAMDKQLKRVKFTQTQTNEISFKVNANFGEQCRDFETQVRYSEKDIFTPIDLEMHYELTKKVPDSEEFCETCAIVDPTEPKVSTQNIIFSTGCATDVCTADLQLRSKDVSPTYILGSADTLRLNYEITNIGETAYLPQFNVTSTSRLAFAQVPGNCKVVDAVMVCDLNRGRPLAKGDTDSVTISFDVSQLSGQSLIIHAEVFSTGYEQNPTDNRQTNVIGLKEFTEIDASGGQTNSQIDLEHYSNSAEIVNNYEIKSNGPSVIEQLTVSFYIPIAYKVAGSTAIIPIINVTSLKMQASYDSQLLSIDLYDQNNTMLVVDPVEVTTTLSGGLERTVITQNRQSYDIHTSGHVHQTMEVLDTSMVATASMSRKRRDLKALTANREQYARISNVKAHDLLSDDFKGKLPVNRTIVFNCRDPEMTICVRAEMRVHFRPEKSINLNMRYSVDLNEVNAILVDPWEYFVILTDLKLQKKGDPTSTSFSINRRIEPNIISKHQETGLPIWIIIVSVIGGLLLLSAISYLLYKFGFFNRTKKDELDRLVQQNPVEPEAENLNSGGNN
| null | null |
apoptotic cell clearance [GO:0043277]; axon guidance [GO:0007411]; behavioral response to ethanol [GO:0048149]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; dorsal closure [GO:0007391]; dorsal trunk growth, open tracheal system [GO:0035001]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; integrin-mediated signaling pathway [GO:0007229]; larval heart development [GO:0007508]; memory [GO:0007613]; midgut development [GO:0007494]; negative regulation of cell migration [GO:0030336]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; oocyte growth [GO:0001555]; pericardium morphogenesis [GO:0003344]; phagocytosis [GO:0006909]; salivary gland development [GO:0007431]; short-term memory [GO:0007614]; wound healing [GO:0042060]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]
|
integrin binding [GO:0005178]; protein heterodimerization activity [GO:0046982]
|
PF01839;PF08441;PF20805;
|
1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;
|
Integrin alpha chain family
| null |
SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type I membrane protein. Lateral cell membrane; Single-pass type I membrane protein. Cytoplasm. Note=Apical membrane localization in primordial dorsal-appendage cells at oogenesis stages 10B and 11. Later, weakly expressed in lateral membrane of cells surrounding the outgrowing dorsal appendages.
| null | null | null | null | null |
FUNCTION: Integrin alpha-PS3/beta-PS is a receptor for laminin. Also binds to wb. Important during embryogenesis for the development of the trachea, dorsal vessel and salivary gland, as well as for dorsal closure. Required for short-term memory processes. Minor involvement in the establishment of the oocyte anterior-posterior length. Plays a role in timely border cell migration during oogenesis, probably mediated by JNK signaling. Integrin alpha-PS3/Itgbn is required for effective phagocytosis of apoptotic cells during embryonic development and for the phagocytic elimination of S.aureus by mediating the binding of S.aureus peptidoglycan to larval hemocytes, which probably activates a signaling pathway involving Rac1 and Rac2. Integrin alpha-PS3/Itgbn also regulates Fak activity during neuromuscular junction (NMJ) growth and is required for its activation in presynapsis of NMJs. Seems to be dispensable for major morphogenetic processes. {ECO:0000269|PubMed:18925939, ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:9409675, ECO:0000269|PubMed:9461212}.
|
Drosophila melanogaster (Fruit fly)
|
O44406
|
ERI1_CAEEL
|
MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGLDDATNIAAIAIQMMKLKIELRINQKCSYKENQRSAARKDEERELEDAANVDLTSVDISRRDFQLWMRRLPLKLSSVTRREFINEEYLDCDSCDDLTDDKNDEAAFQEKMAIREYLENKQTEDFAKIAAERGIFKIGEIKSYQTARPIIEDDDVDVESEEEDYGTEFEMLEVVERMPPVSSTLHTEVDLDAVWERDGGSDSERENLSNAPSLHEFPSSSTSSPHATSEHVTSSSPLHIDDDVDRVLNAPPKNSLASSSNRSSF
|
3.1.-.-
| null |
exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; germ cell development [GO:0007281]; meiotic chromosome segregation [GO:0045132]; multicellular organismal reproductive process [GO:0048609]; negative regulation of post-transcriptional gene silencing by regulatory ncRNA [GO:1900369]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; RNA catabolic process [GO:0006401]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]
|
3'-5'-RNA exonuclease activity [GO:0000175]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]
|
PF00929;
|
3.30.420.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14961122}.
| null | null | null | null | null |
FUNCTION: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) (PubMed:14961122). Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) (PubMed:14961122). Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA-mediated gene-silencing or RNA interference (RNAi) (Probable). {ECO:0000269|PubMed:14961122, ECO:0000305|PubMed:33378643}.
|
Caenorhabditis elegans
|
O44408
|
KGB1_CAEEL
|
MEVDLPVHNEYDASRFHQVTIRDPIAGADSTFTIPTRYVNLSFLNAGAQGTVVMADDLVTTQRVAIKKMQQPFVMTMSAKRAYREFILLTTIKHPNIIRLLNAFTPDTSLSTFREVYLVMELMTHNLHEVIHRLRLDHKTLSFFVYQSLCAIKHLHNSGVIHRDLKPSNIVVNDRCVLKVLDFGLARKKNVDTSMRMSDYVVTRYYRAPEVILGLPYSEKVDIWSVGCIFAEMINHTVLFPGKDRIDQWTKIYSVLGTPDDHFISQLGQSAAMYVRSLPRHQARAFSEIVPDTNFLPETENPRVHLTPHVARDLLFNMLKINPEERYSVEDALNHPYVKLWFKDDEVNAPASENRYDQEIDFADKTLIEWKELIFNEVQRYQADHDIFTG
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8WQG9};
|
cellular response to arsenite ion [GO:1903843]; cellular response to toxic substance [GO:0097237]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; JNK cascade [GO:0007254]; male meiotic nuclear division [GO:0007140]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of gene expression [GO:0010629]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of protein-containing complex assembly [GO:0031333]; oocyte development [GO:0048599]; phosphorylation [GO:0016310]; positive regulation of gene expression [GO:0010628]; positive regulation of RNA splicing [GO:0033120]; regulation of protein localization to nucleus [GO:1900180]; reproduction [GO:0000003]; response to cadmium ion [GO:0046686]; response to copper ion [GO:0046688]; response to endoplasmic reticulum stress [GO:0034976]; response to nematicide [GO:0093002]; response to starvation [GO:0042594]; response to unfolded protein [GO:0006986]; spermatogenesis [GO:0007283]; stress response to copper ion [GO:1990169]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DEAD/H-box RNA helicase binding [GO:0017151]; JUN kinase activity [GO:0004705]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: May be phosphorylated by mek-1 on Ser-198 and/or Tyr-200 (PubMed:15116070). Phosphorylation is induced upon Cu(2+) and arsenite-mediated cell stimulation and by fasting (PubMed:15116070, PubMed:23352664). {ECO:0000269|PubMed:23352664, ECO:0000305|PubMed:15116070}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17699606}. Note=Uniformly cytoplasmic in distal germline but resolves into discrete particles in developing oocytes. {ECO:0000269|PubMed:17699606}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15116070}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15116070};
| null | null | null | null |
FUNCTION: Mitogen-activated protein kinase which is an essential component of the JNK pathway composed of mlk-1, mek-1 and kgb-1 (PubMed:15116070, PubMed:22554143, PubMed:23352664). Phosphorylates the transcription factor fos-1 which prevents fos-1 dimerization and promoter binding and results in activation of target genes including F53A9.2/kreg-1 and lys-3/kreg-2 (PubMed:23437011). Phosphorylates jun-1 and activates the AP-1 transcription factor which is a heterodimer of jun-1 and fos-1 (PubMed:23352664). Phosphorylates glh-1 in vitro which may play a role in controlling glh-1 protein levels in the germline by targeting it for degradation by the proteasome (PubMed:17699606). Required for oogenesis and probably also for spermatogenesis (PubMed:12435362). Involved in the response to environmental stress such as heavy metals, infection and protein folding stress in an age-dependent manner (PubMed:15116070, PubMed:22554143). In larvae, has a protective role which becomes detrimental in adults (PubMed:22554143). May control susceptibility to infection, heavy metal stress and premature lethality by regulating daf-16 cellular localization (PubMed:22554143). Involved in the transcriptional response to bacterial pore-forming toxins and to fasting (PubMed:15256590, PubMed:21408619, PubMed:23352664). Required for fasting-induced longevity (PubMed:23352664). Involved in axon regeneration after injury downstream of tyrosine receptor svh-2 (PubMed:21670305, PubMed:22388962). {ECO:0000269|PubMed:12435362, ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21408619, ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:22554143, ECO:0000269|PubMed:23352664, ECO:0000269|PubMed:23437011}.
|
Caenorhabditis elegans
|
O44411
|
NOG1_CAEEL
|
MTSMYNFKRITCVPNAQELKDVVLSKTQRKTPTVVHRQYSIGRIRAFYARKIKFLQQTLHDKLTQIITEFPKMEEIHPFYSDLMNILYDRDHYKIALGQMNTARHLIDGIAREYVRLMKYADSLYRCKMLKRAALGRMVKLLKRQKSSFEYLEQVRQHLSRLPSIDPATRTLILCGFPNVGKSSFINNVTRADVEVQPYAFTTKALYVGHLDYRFLRWQVIDTPGILDQPLEDRNTIEMQAVTALAHLKASVLFMMDVSEQCDRSIEEQLHLFESIRPLFANKPVLIGLNKVDIRHRSDLPPEKAALLDQLEKEGIPIIETSTLTQEGVMGLRDRACDELLAQRVEAKIQAKKITNVEDCVLNRVFVAYPAPRDEKVRAPFVPPGLAAKRAQKKLQEAQELMETDGDEFAAKIPQKPGKIGKEKIAKGGSQSTDLGDLRDENTRRLEREIELEMQDDYILDLKKHYMLKNPDEKYDIVPEIWEGHNLADFVDPEIQSKLENLLREEELLEQAGEYESDLDSDDEETKEKLKLALQIREKEKLLTLDHAVNKRIAGRIGSRIHGSRKRDRSMSRLENELGELGVDVDTKKMKNLQGQCAKPQLGKKMKVGRSRSLSAVRPAPRDELAFPDEEKRAHVDKLRTKAMRGLRREAKKGEADRHVYDLKPKHLFCGKRGNGKTDWR
| null | null |
determination of adult lifespan [GO:0008340]; negative regulation of lipid storage [GO:0010888]; regulation of reproductive process [GO:2000241]; ribosomal large subunit biogenesis [GO:0042273]
|
nucleolus [GO:0005730]; nucleus [GO:0005634]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]
|
PF06858;PF17835;PF08155;
|
1.20.120.1190;3.40.50.300;
|
TRAFAC class OBG-HflX-like GTPase superfamily, OBG GTPase family, NOG subfamily
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24552710}.
| null | null | null | null | null |
FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit (By similarity). Has a role in regulating longevity, growth and brood size (PubMed:24552710). May regulate fat storage via the insulin/IGF pathway (PubMed:24552710). {ECO:0000250|UniProtKB:Q02892, ECO:0000269|PubMed:24552710}.
|
Caenorhabditis elegans
|
O44437
|
SMD3_DROME
|
MSIGVPIKVLHEAEGHIITCETITGEVYRGKLIEAEDNMNCQMTQITVTYRDGRTANLENVYIRGSKIRFLILPDMLKNAPMFKKQTGKGLGGTAGRGKAAILRAQARGRGRGGPPGGGRGTGGPPGAPGGSGGRGAWQGGPTGGRGRGGL
| null | null |
central nervous system development [GO:0007417]; lymph gland development [GO:0048542]; mitotic cell cycle [GO:0000278]; mRNA splicing, via spliceosome [GO:0000398]; muscle organ development [GO:0007517]; neuron differentiation [GO:0030182]; oogenesis [GO:0048477]; peripheral nervous system development [GO:0007422]; pole plasm oskar mRNA localization [GO:0045451]; spliceosomal snRNP assembly [GO:0000387]
|
catalytic step 2 spliceosome [GO:0071013]; commitment complex [GO:0000243]; cytosol [GO:0005829]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; pole plasm [GO:0045495]; precatalytic spliceosome [GO:0071011]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosomal tri-snRNP complex [GO:0097526]; U1 snRNP [GO:0005685]; U12-type spliceosomal complex [GO:0005689]; U2 snRNP [GO:0005686]; U4 snRNP [GO:0005687]; U5 snRNP [GO:0005682]
|
RNA binding [GO:0003723]
|
PF01423;
|
2.30.30.100;
|
SnRNP core protein family
|
PTM: Methylated on arginine residues by Art5 and Art7; methylation is not required for assembly and biogenesis of snRNPs. {ECO:0000269|PubMed:18369183}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62318}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62318}.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). {ECO:0000250|UniProtKB:P62318}.
|
Drosophila melanogaster (Fruit fly)
|
O44476
|
RNZ2_CAEEL
|
MLGAIARKTVENRILVSRHLISSTSCLFKDNNEELLESIKERIARNRRILQKHSSSHLKAREVNASISNLRQSMAAVQKKQKAAHEPPANSIVNIPSQVSIEVLGNGTGLLRACFILRTPLKTYMFNCPENACRFLWQLRIRSSSVVDLFITSANWDNIAGISSILLSKESNALSTRLHGAMNIKHFLECIRPFQDSDYGSCKYPSQVEERPYTMENYEDAGLKVTYIPLSPPLNIGSNNEKSKNVKVNNVDIAFLIEMKEAARRIDTMKLMELKVPKGPLIGKLKSGEAVTLPDGRTIQPDQVFSSDKVEGDKPLLLVTECTTEDHVKALIDSSSLQPFLNGEKQLDYMVHISDDAVINTPTYRHLMEKLNNPSITHLLINGGNPVIPAVESVYKHTRLLRSIAPSLFPALHPIDWSGIITQNEELSQRQDQFIRVAPMQRYWMRRGASFNEEPIVNNLLAAEPELSDKAKELIKEYQKLEKENKMDCEFPKLTFFGTSSAVPSKYRNVTGYLVEASENSAILIDVGEGTYGQMRAVFGEDGCKQLLVNLNCVLITHAHQDHMNGLYTIIARRKEAFESLGAPYRPLVLVCNRNVLKPMKTYSICFENIEHLLEIVDISRYPLTPPGSPGGPPGKRPRLPSPHLPPSRDVLQDMSSSFDKKAWKLDELKAVQVHHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVLPEYLDKENIGVAMDMLRVRFDHLPLVSKLLPIFREVFVAELFELTIKKEQRVLKDKELSEKRGQLKA
|
3.1.26.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
|
germ cell development [GO:0007281]; meiotic cell cycle [GO:0051321]; nematode larval development [GO:0002119]; positive regulation of vulval development [GO:0040026]
|
mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
3'-tRNA processing endoribonuclease activity [GO:0042781]; metal ion binding [GO:0046872]
|
PF12706;
|
3.60.15.10;
|
RNase Z family
| null |
SUBCELLULAR LOCATION: [Isoform a]: Mitochondrion {ECO:0000269|PubMed:35451962}.; SUBCELLULAR LOCATION: [Isoform b]: Nucleus {ECO:0000269|PubMed:35451962}. Note=Accumulates in the nucleus upon mitochondrial stress. {ECO:0000269|PubMed:35451962}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.; EC=3.1.26.11; Evidence={ECO:0000305|PubMed:35451962};
| null | null | null | null |
FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity (PubMed:35451962). Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity). Involved in germline proliferation (PubMed:14729485). May be required for both mitosis and meiosis in germ cells (PubMed:14729485). {ECO:0000250|UniProtKB:Q9BQ52, ECO:0000269|PubMed:14729485, ECO:0000269|PubMed:35451962}.; FUNCTION: [Isoform a]: Does not regulate the mitochondrial unfolded protein response following mitochondrial stress. {ECO:0000269|PubMed:35451962}.; FUNCTION: [Isoform b]: Plays a role in mitochondrial unfolded protein response (PubMed:35451962). Upon mitochondrial stress is exported from the nucleus where its tRNA endonuclease activity is negatively regulated (PubMed:35451962). In response to mitochondrial stress, might be involved in activating a transcriptional response in an ATFS-1- and DVE-1-dependent manner (PubMed:35451962). May play a role in negatively regulating the mitochondrial membrane potential (PubMed:35451962). {ECO:0000269|PubMed:35451962}.
|
Caenorhabditis elegans
|
O44514
|
PMK3_CAEEL
|
MASVPSSSSLPVSHVRRHEDVSTPSAPPTKRSNNQSQPPESYEPNTWLQQQREQEQQKKLAAENIKKQSIEATGNNEMVGEEEEDILSKPCGPHKRRFQFVMIRNITFAIPEGYDVEPNSIEYLGGGSFGNVIKTSAVCRDGLRRYVAIKKMREPFFDPHHARRIFRETKLLQLMRHDNIICALDIYTPDEENDFRDVYVVTEFAGRSLYQILKQQRDYGRRVLTDEHIKFIIYQIIRALKYIHSANIIHRDLKPGNLALTDDSDLMILDFGLARSLEKKDTSLTQYVQTRWYRSPEVIYWKIDSYTNLADMWSLGCIAAELLTGEPLFPGDEPNAQYQRITQLCGSPDEELLTKIENDNSSAIKAVIQSYTTHKRRNFRDVFSAHNPSEDFIDLLEKLLVLDPEKRITVEEAIQHPYLAEFSLPEDEPRADHIFDLDDSQARTRFEWRDAVWKEIMNYKRLSSSPLIPGEADR
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11703092};
|
axon regeneration [GO:0031103]; behavioral response to nicotine [GO:0035095]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension involved in regeneration [GO:0048691]; regulation of 3'-UTR-mediated mRNA stabilization [GO:1905868]; regulation of axon extension involved in axon guidance [GO:0048841]; regulation of synapse organization [GO:0050807]; response to osmotic stress [GO:0006970]
|
axon [GO:0030424]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-285 and Tyr-287, which activates the enzyme. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11703092, ECO:0000269|PubMed:26657059}. Cytoplasm {ECO:0000269|PubMed:26657059}. Cell projection, axon {ECO:0000269|PubMed:26657059}. Cell projection, dendrite {ECO:0000269|PubMed:26657059}. Cell projection, cilium {ECO:0000269|PubMed:26657059}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11703092}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11703092};
| null | null | null | null |
FUNCTION: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets (PubMed:11703092). Involved in axon regeneration after injury, probably downstream of dlk-1 and mkk-4 and upstream of mak-2 (PubMed:19737525, PubMed:21670305). May phosphorylate mak-2 (PubMed:19737525). Plays a role in cilium length regulation, possibly by reducing rab-5 mediated endocytosis (PubMed:26657059). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord (PubMed:27123983). {ECO:0000269|PubMed:11703092, ECO:0000269|PubMed:19737525, ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:26657059, ECO:0000269|PubMed:27123983}.
|
Caenorhabditis elegans
|
O44516
|
EFN4_CAEEL
|
MKQFFEFLITTFLLLGLAAADEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEEGRNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEGTAEKVLRTQQLSGGRREDWKKQKVPPKNVAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLSMKVSASQPHPTRRAPTRRQEDFVTTASAELMGGQEDEDSDNDNAHLLPRDLEGSTNPKFRRPSQLETAGVENQQFMKVVQMAQAGKTGTFENEKEAIAQKSSEKDGWHPVNVQYVADLMNNAYQNADERISYQRDFEIHEENDLAVKSLEYSSSSTSLSTNFAILLAVIYVLY
| null | null |
axon guidance [GO:0007411]; cell migration involved in gastrulation [GO:0042074]; embryo development ending in birth or egg hatching [GO:0009792]; ephrin receptor signaling pathway [GO:0048013]; morphogenesis of embryonic epithelium [GO:0016331]; nematode male tail tip morphogenesis [GO:0045138]; regulation of axon guidance [GO:1902667]; regulation of cell adhesion [GO:0030155]
|
axon [GO:0030424]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
ephrin receptor binding [GO:0046875]
|
PF00812;
|
2.60.40.420;
|
Ephrin family
|
PTM: May undergo proteolysis by metalloprotease sup-17 to give rise to a soluble form. {ECO:0000305|PubMed:26903502}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Regulates the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis (PubMed:12679110). In early embryonic development, involved in ventral closure of the epidermis (PubMed:12403719). During male tail morphogenesis, regulates precursor cell sorting together with mab-20 and allows the formation of distinct sensory rays (PubMed:15030761). Probably acts as a ligand for lad-2 to regulate axon guidance of several neurons including SDQL, SDQR, SMD and PLN neurons during neurogenesis (PubMed:26903502). {ECO:0000269|PubMed:12403719, ECO:0000269|PubMed:12679110, ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:26903502}.
|
Caenorhabditis elegans
|
O44518
|
CYFIP_CAEEL
|
MNANVTVDDAISNVNLLDTLAIPDDLPDIEARALPLLYRSNFDTNFEDRSAFVTGIAKYSEEATRHAQFNDMLSEGLQHAANMYTWRCCSRAVPMAKSNDQPNRTEINEMVVEVLKPEVSKLGSFMRFTLTAIQRFCEEVRRLCHSEKRRDFVSEAYLLTLGRFINMFAVLDELKNMKASIKNDFSTFRRASQFLTAMSDTQAVHDMQNLSMFLATQNKIKDDLKLQMKTIEGYEELLCDVVNICAHMYEHQLYLSPNEKHMFVKVIAFSLFLMDGDAANVAKLDQKKRLSISRLDKIFKTLEVVPLYGDMQIQPFAFVRRSSHYEPSKWPLSDKESDRCHVNIVEKVQSIRSDHESYVTQFAKINNEVAICDRPGNDSENREITSLALSGIQLLCQWSCAVVETISWKLLNPTNPKDNRECPENAEEYERATRYNYSPAEKTALIQIIAMIKGLQSMLGKTESDMSNSTRKCVYVELQAFIHHTINEPLQKAVKHKKDLLASILQSVKDSISDAGNELNRMTDVKGKKKSSAPKGDSANSSSSDIRIPRRTAAPGSTQLYMARTQLESLISDKLCGGKKILRKELDSKTIEKISVFLRKSAHWPALFRLSDSMTEAGELSQLWFREFYLEMTMGQRIQFPIEMSMPWILTDYILSCNEPSLIESALYQLDLYNDAAQYSLFNFNKQFLYDEVEAEVNLCFDQFVYKLSEMVFTHYKQLASCMLLDKRFKAEILRSGTMIRSPSAARFESLLQQRHVQLLGRSVDLNRVVSQRVNMALLKALDAAIWKFESEPLSSIVELDMLIDTNRLCHTLLSDVLHSIAPFDDLFQEANHAVNSPHGRITLHVFWELNYDFVPNFVYNGSTHRFVRARHVFRKTPAREKPPQVGQVYYWGSKSLMAAFMNICNAYSQCIGTQHLKAITRLLHYQGIAVILDELLKMTNRLLNDKIRRHVRNVFNMMPKVCKLPRSDYGSNALLQYYVHHLEAVGKYPELKSEFCQDLRELGNMIVFCQQLEVALGQEEAHDLFLAAAYTGTVPQPPARNAQEQMKQLAKLEDKYSRIHLTEIIDKISPDDGQAAIAKDAELMTKERLCCGLNAFENFLVRIKQMLAADDIWTGGYPTNGVFWIDECVEWYRVYSALQFFLCQPTRDDNEVYAEELFGDSLQWGGLTLITLLGQHRRFEVLDFCYHLHRVNKADGKDEVISGIRLAKMVERIRRFQLLNNQIFIILENQLNENNDDPNERVREFAPPVHPNYANHAARRQ
| null | null |
axon guidance [GO:0007411]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; cell projection assembly [GO:0030031]; embryonic body morphogenesis [GO:0010172]; positive regulation of clathrin-dependent endocytosis [GO:2000370]; positive regulation of egg-laying behavior [GO:1901046]; regulation of actin filament polymerization [GO:0030833]; regulation of translation [GO:0006417]
|
cell junction [GO:0030054]; neuron projection [GO:0043005]; SCAR complex [GO:0031209]; synapse [GO:0045202]
|
RNA 7-methylguanosine cap binding [GO:0000340]; small GTPase binding [GO:0031267]
|
PF07159;PF05994;
| null |
CYFIP family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11877381}. Note=Enriched at cell boundaries. {ECO:0000269|PubMed:11877381}.
| null | null | null | null | null |
FUNCTION: Required for initial steps of body morphogenesis (PubMed:11877381). May play a role in egg laying and yolk protein clatherin-mediated endocytosis by oocytes during oogenesis (PubMed:19798448). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord (PubMed:27123983). {ECO:0000269|PubMed:11877381, ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:27123983}.
|
Caenorhabditis elegans
|
O44548
|
KNL2_CAEEL
|
MGDTEIVPLRVQNVLDSEIIRLNLWSMKFNATSFKLEGFVRNEEGTMMQKVCSEFICRRFTSTLLFDVSGRFFDLVGQIDREYQQKMGMPSRIIDEFSNGIPENWADLIYSCMSANQRSALRPIQQAPKEPIRTRTEPIVTLADETELTGGCQKNSENEKERNRREREEQQTKERERRLEEEKQRRDAEAEAERRRKEEEELEEANYTLRAPKSQNGEPITPIRFTRGHDNGGAKKVFIFEQTPVRKQGPIASSTPQQKQRLADGANNQIPPTQKSQDSVQAVQPPPPRPAARNAQFASDADLFAVPKAPPSKSVRNLAASNVDIFADVDSVLDTFHFESTPGRVRKPGRRNVSSPSPEPRHRSSSRDGYEQSRYSQRYEHDNSRWSRHNATYRRHEDESRMSRKRSIVRDDFEYSRRHDDGARRRDYYDADIQGDSKRYRGRDASSSSGRSVRFEEEHRRHGDEYRDPRGPRDYNDYGRRRNHANSRSGEDEEKLNAIVRREKELRNRLQKSQKASSSSYRHRSNSSDAEESLNEWDIENQELLDNSMMFGDGIPKRSNARKDKFVKKQATRSKPANSTKSPAQARKKKRASLEDNRDLNDSIACNRPRRSCVTPVAKKITWRKQDLDRLKRVIALKKPSASDADWTEVLRLLAKEGVVEPEVVRQIAITRLKWVEPEQNEEVLKQVEEVEQKRRRGAVARVKENVKMHEELREGGNHRAEDLQSGVESMEDYQPEDVAADQSLLALRTPIVTKKRGGTRASIMPKPVEDSPMSRGNNSTFNSPRLEQTKAKDIETNFKYVQHLSMMQARPSSRLKKSSSMNNSTYRGNKNTSISLEKGTQKALKIINRGTTIHEDDENEDNDDDDDMREEDTSIY
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiotic cell cycle [GO:0051321]
|
chromosome, centromeric region [GO:0000775]; kinetochore [GO:0000776]; nucleus [GO:0005634]
| null |
PF21506;PF09133;
|
1.10.10.1900;
|
KNL2 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17339379}. Chromosome, centromere {ECO:0000269|PubMed:17339379}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17339379}. Note=Requires hcp-3 for chromatin localization. {ECO:0000269|PubMed:17339379}.
| null | null | null | null | null |
FUNCTION: Required for the recruitment of hcp-3, hcp-4, knl-1, bub-1 and lin-53 to kinetochores, kinetochore assembly, chromosome condensation and chromosome segregation in meiosis and mitosis. {ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}.
|
Caenorhabditis elegans
|
O44712
|
AHR_CAEEL
|
MYASKRRQRNFKRVRDPPKQLTNTNPSKRHRERLNGELETVAMLLPYDSSTISRLDKLSVLRLAVSFLQCKAHFQACLHNSQFLSAGFPMSTHSYSYQPHPPIPFSNKVPTIFDLRIGTPMLDPEESNFEEISLKSLGGFILVLNDNGEIYYASENVENYLGFHQSDVLHQPVYDLIHSEDRDDIRQQLDSNFHIPTSSASNQFDVFAPQNSKYLERNVNARFRCLLDNTCGFLRIDMRGKLMSLHGLPSSYVMGRTASGPVLGMICVCTPFVPPSTSDLASEDMILKTKHQLDGALVSMDQKVYEMLEIDETDLPMPLYNLVHVEDAVCMAEAHKEAIKNGSSGLLVYRLVSTKTRRTYFVQSSCRMFYKNSKPESIGLTHRLLNEVEGTMLLEKRSTLKAKLLSFDDSFLQSPRNLQSTAALPLPSVLKDDQDCLEPSTSNSLFPSVPVPTPTTTKANRRRKENSHEIVPTIPSIPIPTHFDMQMFDPSWNHGVHPPAWPHDVYHLTQYPPTYPHPPGTVGYPDVQIAPVDYPGWHPNDIHMTQLPHGFTPDAQKLVPPHPQMSHFTEYPTPSTHHDLHHHPLKQDNFHLISEVTNLLGT
| null | null |
behavior [GO:0007610]; intracellular receptor signaling pathway [GO:0030522]; negative regulation of locomotion [GO:0040013]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to xenobiotic stimulus [GO:0009410]; xenobiotic metabolic process [GO:0006805]
|
aryl hydrocarbon receptor complex [GO:0034751]; nuclear aryl hydrocarbon receptor complex [GO:0034753]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; nuclear receptor activity [GO:0004879]; protein heterodimerization activity [GO:0046982]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF00989;PF08447;
|
4.10.280.10;3.30.450.20;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Probable ligand-activated transcriptional activator. Acts as a transcriptional regulator in GABAergic motor neuron cell fate specification and development. Promotes cell-type-specific expression of guanylate cyclase genes that have key roles in aggregation behavior and hyperoxia avoidance. Has no role in carbon dioxide avoidance. {ECO:0000269|PubMed:14757639, ECO:0000269|PubMed:15136141, ECO:0000269|PubMed:16919260, ECO:0000269|PubMed:18524955, ECO:0000269|PubMed:9501178}.
|
Caenorhabditis elegans
|
O44740
|
MEI2_CAEEL
|
MSGLDDRKKLTHAKNRKPLNDIPKSAENRPNTRSTSSRRGAEKDVPITFIGSSRTVKADLPEFTNTRSRRPLHSESKKELSRNPVSRGEEHSSSLPKSSPESSVSVMSSNASLWSACTEEVNKIGVCAKRESRNLRVYKMKSFTSNMEQILSNDNQLAPTVIRILNSRNSWCLNSCHACLTFIMENITSDNYGKRSACLKALASITNSLLDTIIGFASTKTRRIGVDVVAEERAAKATECIHNFRKIVKNRDKIYKQIDQETIYKLDAILERLKKVSSHK
| null | null |
cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic spindle disassembly [GO:0051229]; meiotic spindle organization [GO:0000212]; microtubule depolymerization [GO:0007019]
|
condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; katanin complex [GO:0008352]; male pronucleus [GO:0001940]; microtubule [GO:0005874]; spindle pole [GO:0000922]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10809666}. Note=Localized to the spindle poles and condensed chromatin during female meiosis. Also localized to the polar body. Correct localization requires mei-1.
| null | null | null | null | null |
FUNCTION: Forms a heterodimeric complex in conjunction with mei-1 which severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays. May act to target mei-1 within the cell. Required specifically for meiotic spindle formation in the female germline. {ECO:0000269|PubMed:10809666}.
|
Caenorhabditis elegans
|
O44743
|
LE607_CAEEL
|
MDQDFDLDEGAGQFNLKTTLMMFTSNDSQNDDGIWSPGSPYQALEDPSFLDKHFVSDPDRYTADELYSALEKMDGKSDLIGMDDMDNDNCYSLSPPDSGSLPISPASTSPSSYHSSGGEDLMDCYPSIDILQQASEELLYSKDDDYEICSSGPLLAYTNANSVATSAVHQNQQQQQRRLNQAGFPHQNSNGLVRFKSSQPRVLNPASISLNAPSSSFNPQSTSSTPATSSSSSSSTNGGFVKSSTGERRKYPPLRLDEEEIKLCKKEGICLPDFFPLTKAEERDLKRIRRKIRNKRSAQTSRKRKQDYIEQLEDRVSESTKENQALKQQIERLSSENQSVISQLKKLQAQLGQNAKRTTQAGRCLAVFMLSACLLVSPQLSPLGNQDNQKVLECIEEACQPSATSMNSANSAQRAIAGVTAPSVVIPSGGPVMVSTNANRQMNRNAVLNHHNNSKYPASGNQNHHPIALEDLNHPPPTLQPKQSYQQQHQPSMYRRSDETIAMAMAKIGARKGSSTSSSSASSVASSTSTSSATSPIYRTSRTLGAFEDQCDASSDDSNCANMPSLVPMKMSAQPPKRKIVTMNGQPRVTYRAVPASSVNVEQAQYYKVPQQKVQYVTMDRPIKYEVLQLNDYIKMEEESTIRLPNSWSTAGPRLHPQVNASSRTVRPLTVATPVHYNGPSAKKIKTQMF
| null | null |
negative regulation of protein kinase C signaling [GO:0090038]; regulation of cell size [GO:0008361]; regulation of distal tip cell migration [GO:1903354]; regulation of establishment of cell polarity [GO:2000114]; regulation of multicellular organism growth [GO:0040014]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00170;
|
1.20.5.170;
|
BZIP family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor, required during migration of the gonadal distal tip cells (DTC) (PubMed:24811939). Probably regulates cell adhesion of DTCs via modulation of expression of genes involved in integrin-mediated adhesion, including tln-1, src-1, and integrin pat-2 (PubMed:24811939). Modulates expression of genes involved in protein trafficking during embryogenesis, including emo-1, sec-61, calu-1, sec-24.1, enpl-1, sar-1 and tfg-1 (PubMed:27510972). {ECO:0000269|PubMed:24811939, ECO:0000269|PubMed:27510972}.
|
Caenorhabditis elegans
|
O44750
|
XPP_CAEEL
|
MTALEKLAKLRSLFHSERVLALTSSKPMVAYLLPSTDAHHSEYLADYDFRVKFLSGFSGSNAYVVVTDREALLWTDGRYFTQAGNQLDSNSWKLMKQGQPDSITVVDWLVRELERGSVIGFDPTLSTFDAGSKTFKRLKAAGLQPVSIPGNLVDEFWTDRPRLAGEPVVVLDVEDTGLTTSKKVENLREKLKQKKCDAAVFTLLDDVMWLLNIRGSDIPYNPLAYSYLFVAMREIHVFIDNEKLDEKSRAHFHKSNVSIHPYGEVYSWISNWLKAKEASKEPHMVYLTPETNYAIGSIIGEENSMVDTSLVQTAKATKNDHEMQGMRNSHLRDSAALVEFLCWLEKELLSGKRYTEIELADKIDHLRSLQDKYVTLSFDTISAVGDHAALPHYKPLGESGNRKAAANQVFLLDSGAHYGDGTTDVTRTVWYTNPPKEFILHNTLVLKGHINLARAKFPDGIYGSRLDTLTRDALWKLGLDFEHGTGHGVGHYLNVHEGPIGIGHRSVPTGGELHASQVLTIEPGFYAKEKYGIRIENCYETVEAVVMSKAQNFLTFKSLTLVPIQTSIVDKSLLIEEEINWLNQYHARVLKEVGEHLQKRGKTDELKWLAEACKPI
|
3.4.11.9
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:25905034}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:25905034};
|
proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]
|
cytoplasm [GO:0005737]
|
metalloaminopeptidase activity [GO:0070006]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]
|
PF01321;PF16189;PF00557;PF16188;
|
3.90.230.10;3.40.350.10;
|
Peptidase M24B family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11606206}.
|
CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:11606206};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45 uM for bradykinin {ECO:0000269|PubMed:11606206};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:11606206};
| null |
FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:11606206, PubMed:25905034). Has activity towards the flp-9 neuropeptide KPSFVRF-amide (PubMed:11606206). {ECO:0000269|PubMed:11606206, ECO:0000269|PubMed:25905034}.
|
Caenorhabditis elegans
|
O44757
|
LIN59_CAEEL
|
MHGAGEQQQRYRYNARSDEQHHHPSTSSHQYQQQGARQMHQMHPIQATLMCTPTTTSAAASTSSSGGSNSSGGSGGHRQQGNILRIGNSIKIGDNILEPAGTLVFSQADGTPWTGQRIVVNGSTHAVVKANLFPIGTTPPVLNMQSNQNWYMNQPSGTVPMSSNAPATTSSATPDSGIQSVPTSPPSPSYAMMNDVDIGDHDDEEDDDGPADFTDMPLLKPVDEDDDCYDVPCTSEGPPPNNSNPAITTIPSSCSTPAPPKESLPTGMNVEEWGSFLIASNMDREEIVRRLMAHDPEMAKAIAMRIRELSAEESKKKKDMEAEVSSTTPTTPRARGTRTRNKCATRSTNSPDVTTSNLPEEPSTSTMGLVKENEDVEKVEGKRRGRKPKKRRGFHKESFEDLESDAKKSKAEQHEDHLPEASCSSRPESVIPPPVDPIQFRLKVREMMERKLEQLTQKMSEDMTELRLSHLTSSKMVNGERGKRRESFLRQLNEQSKKLRKGGMLGRKRLRMFMTESDILEENKDNIKKEVKEESTPPPTKLRGRLPSRRTREPSEIVNPEPVEKKFNGEYFEITKSVPSSDDIIPLWMAPSLTCGCTKGACTSDMDCLNRALRVQCSSDCSVPYCSNRRFWKEDCGNKLCVSNGPRSKRVLKTKIARRAGEFLCEYAGEVITREQAQEKFAQDRDPRIIAIAAHLFVDATKRSNIARFIKHSCKPNSRLEVWSVNGFYRAGVFALSDLNPNAEITVDKSDLLPFDMACNCGATECKRVIRGVRWRCADPNEKIVTRRFVIRNRRKTIERSSHSGLPAILQTPMDENSSIRLKMKQVLAAFAFRVRKIDGSMSRTMLPHYTLIIKFLKTKGNNPNPVEFVSLFRKWLEAIDDDDLERAFVAIESHYMSSSILSSSLQSKKAKDNAPRARALSTSCPSPVPSKRGDADLSYLESLYPIGSYDPDDAWESYSTNKKGNAVRCICGALDEEGTMVQCDTCHFWLHVDCCQYVVRSNEKAQKSKNPPSDDGEYICDFCTNKQNGLRPSADVKLTEQPDVRFENCDYYRSLINRRGIQVVLNETVYVNRVLPEDHKAMLRNLREEKKGSKQKDTNKYRFPKAATSPLPIEKVDRKNARIFRVERLFVCPGNNRFVFGSFYAWPHETYADAGRVFSKKEVFATPYYETLPLDEVIGRCLVLDTATWCKGRPKVPKFKEDDVFLCEMQIGKTQRVFEKVPPKNRYPINTNSYVFTEFTHPKKVVRDFRPYDPSNPSPKPPKTSSIPSTSSIDPPQSSSDGLPEVDTKKLSKRHIQRVLKRLVKNGSRRS
|
2.1.1.-
| null |
ectodermal cell fate specification [GO:0001715]; egg-laying behavior [GO:0018991]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract development [GO:0048566]; locomotion [GO:0040011]; methylation [GO:0032259]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of multicellular organism growth [GO:0040014]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K4 methyltransferase activity [GO:0042800]; metal ion binding [GO:0046872]
|
PF01426;PF00628;PF00856;
|
2.30.30.490;2.170.270.10;3.30.40.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
| null | null | null | null |
FUNCTION: Probable histone methyltransferase (By similarity). Essential protein required to maintain expression of homeotic genes egl-5 and mab-5. May play an analogous role to the trithorax Group (trxG) proteins. TrxG proteins form multiprotein complexes that are required to maintain the transcriptionally active state of homeotic genes throughout development. May act via a modification of chromatin. {ECO:0000250, ECO:0000269|PubMed:10648230}.
|
Caenorhabditis elegans
|
O44783
|
SPY_DROME
|
MDRRNGGDPLAPPRPPKLLPRVHRPRAPEPTLSGVDHNAGATASALASGASSAAPVAIHNNNSQQQLSISAAASNNNTISIIPASPDFDDYQIHHLTFLPQRPSSLSRNSSTASSTTATGISVSGSGSVSGSSSSFTRRRPPAPVPLNNSISNNNNNSINNNFLSHFQSAEPASNALGQPPASPVTLAQPRPESERLTNEYVDTPLQHATRSQHPAGQQDNGQTTTHHLLLLPQRNQHLHLQQHQQHLQQQQQQQQQQQQQQHLQHQQNQQHARLATTTQATSVGSDHTDGLLHSHLQNSTTKPPASKQPAPPRLGMGLGLGLGLGLNQPIITKQPTPATQKERMHALEELLQPGGAGGNGGPLVMAGDPSLLNPIVCPRCGRCRCEQCQSPRPLPQTWVCNKTCLCSAESVIDYASCLCCAKALFYHCARDNDLDCDDGNGTPCVDNPCSCGPYKRTQRWGWLGALSIFLPCLWFYWPMRGCMKLCEKCYGRFAGRGCRCQGIGGGGAGSGGGVGSIGSTSSMLPIVPLGVNGSGLGGGVSLSGGVTDGGLNQANGKAMDHGCSAARSILRKGDLTPEKRLLDSSPDY
| null | null |
animal organ development [GO:0048513]; branching involved in open tracheal system development [GO:0060446]; compound eye morphogenesis [GO:0001745]; dorsal/ventral axis specification, ovarian follicular epithelium [GO:0008069]; glial cell development [GO:0021782]; lamellocyte differentiation [GO:0035171]; muscle cell development [GO:0055001]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of imaginal disc-derived wing vein specification [GO:0110109]; negative regulation of photoreceptor cell differentiation [GO:0046533]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of torso signaling pathway [GO:0120177]; ommatidial rotation [GO:0016318]; open tracheal system development [GO:0007424]; regulation of compound eye photoreceptor development [GO:0045314]; response to hypoxia [GO:0001666]
|
apical part of cell [GO:0045177]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
| null |
PF05210;
| null |
Sprouty family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10089881, ECO:0000269|PubMed:9458049}; Peripheral membrane protein {ECO:0000269|PubMed:10089881, ECO:0000269|PubMed:9458049}; Cytoplasmic side {ECO:0000269|PubMed:10089881, ECO:0000269|PubMed:9458049}.
| null | null | null | null | null |
FUNCTION: Inhibitor of tracheal branching that restricts branch budding by antagonizing the BNL-FGF pathway (BNL: branchless, an fgf inducer of branching). Acts as an antagonist of EGFR-mediated signaling in the eye (where it is important for cell determination) midline glia, chordotonal organs, wing and ovarian follicle cells. {ECO:0000269|PubMed:10089881, ECO:0000269|PubMed:10226010, ECO:0000269|PubMed:10457022, ECO:0000269|PubMed:9458049}.
|
Drosophila melanogaster (Fruit fly)
|
O44836
|
MMPB_CAEEL
|
MTKWSPNGNPLSTIYLILSLFTLAHTAPTTQHSRTTTQLRLEDEDGGGGVDEDSIHFVKGQMEKYGYLKGIDHSSPQEFRQALMFFQEVLEVEQTGNVDEMTVEAASKPRCTQTDVRQEQTKRTKRFTLSKRAKWAHASGQSVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSYIKNEKKVTLTFQEASSKDEADINILWAEGNHGDEHDFDGANGKIEGNKKENVLAHTFFPGYARPLNGDIHFDDAEDWEIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPINEIQLDIDDKCGVIWNYGGASDFCLYVWLMSQIVEAHNSSAQNNHGVGSITSSRTNKKSFKSEGFFLFQLKFPHSTLTHTDDVVMREKDKRSYRGDSKIPKCSSNNSSQRTLAEKKLTLGLHLSEADAKRYTEMVCNFLAGLHMWRTNPNHHASESLEKEYKGVSQEMGTFSGKSIAVRRLIRHAEHQKERSEKGPLDPDYFDDDFFENFFMEYSK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P03956};
|
collagen catabolic process [GO:0030574]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; ecdysis, collagen and cuticulin-based cuticle [GO:0042395]; extracellular matrix organization [GO:0030198]; heat acclimation [GO:0010286]; larval development [GO:0002164]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein oxidation [GO:1904807]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; positive regulation of cellular response to heat [GO:1900036]; positive regulation of cholesterol import [GO:1904109]; positive regulation of eating behavior [GO:1904000]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion [GO:0040017]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]
|
PF00413;
|
3.40.390.10;
|
Peptidase M10A family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:24957743}.
| null | null | null | null | null |
FUNCTION: Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:24957743). Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol (PubMed:20600277, PubMed:24957743). {ECO:0000269|PubMed:20600277, ECO:0000269|PubMed:24957743}.
|
Caenorhabditis elegans
|
O44857
|
NEPL2_CAEEL
|
MRPDEEDGTTKSPGSRWTRIWAIIALILLILFLLVLGAAIYFYINYKDSSDVCLSPGCIKTASVILSSMNSSVDPCDDFYEFACGQWIKGHPIPDDAPSVSNFENLGQDLEFALKELLDENDEPYDYETSAVGKAKYFYNLCLNESEILDNWRTTFDEVVKSFGGWPSLGHQMKPDASIEMLYADMVAKFKADSLFKATVQPDDKNSQRHVLLIDQPQLNLFARDFYVAAENEERMAYLQLIRDVLILLDADRTRATLDAKEIIDFETALANITMADEHRHDIAELYTKITLGEMRRSLPHFNWPLFFNRMFKDLHEKNGKRITFDDNTEVVVYGYEFLRRLDVLIPQYDNRLIVNYLEWCWFFKTMLRDLPDPFALTIFKFYKTLNIMNVQKVRWHGCVTRINSLMPMATSAIYVKNHFDHEAKQQVEEMISLIMESFVDLLLSEDWLTKETKQTAKQKVNEMKRKIGYPDYLNDPAAVNNEYKTFKVYPGHYYQTKFSFYEQYQRDVLERITEAVDRERWVAGAALVNAFYSPNTNEIIFPAGILQPVFYSKDFPSSMNFGGIGVVIGHEITHGFDDRGRLYDNLGNIRQWWDNATISKFEHKAQCIEKQYSSYVLDQINMQINGKSTKGENIADNGGLKQAYRAYKKYEKRHSRPPRLPGVNLTHDQLFFLNYAQIWCGTMNDKEAIRKLRTSEHSPGPIRVKGPLSNSYDFAKAYNCEPGSQMNPREKCRVW
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08473}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};
|
olfactory learning [GO:0008355]; protein processing [GO:0016485]; regulation of chemotaxis [GO:0050920]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]
|
PF01431;PF05649;
|
3.40.390.10;1.10.1380.10;
|
Peptidase M13 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Required for olfactory plasticity, which is the change from positive chemotaxis to dispersal after prolonged exposure to an odorant. Thought to antagonise snet-1 by degrading excess snet-1 peptides and thus enabling olfactory plasticity. {ECO:0000269|PubMed:20929849, ECO:0000303|PubMed:20929849}.
|
Caenorhabditis elegans
|
O44952
|
LONM_CAEEL
|
MYRAGAVLLRGATRTRLLAAASAHQSFATFSQRNQSILMMKSMELAGNSGERRFYSTHDDPIAVDDSLELYKDLGGMSPIQVPADMPNVPMLAINRYPLFPGFIKKVDIVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEETITSLSEVYPTGSFVQIIEVRDQGSVLELVLSAHRRIRALEPIDEITPKNETPLNGRRARGKRAASATSPLTPPPSPPPLAPSVASVAPEISATEEKEEKTTPPSATGEKQKKGIIMVRTENVVAEPVPKNNETKATMMAIVQTIRDVVQFNQLFGQQINLLLHPSQNVIDNPVYLCDLVATLVQSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGIEKDEKTTIIEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMKDVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQCMKKVKTENPLVLIDEVDKIGGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRMEMIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEQQNEDEEPAEKATTAITENSEAEPITSTSSADCLKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALYIETVLKRPVDLTNDKDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDELYEHLFQ
|
3.4.21.53
| null |
cellular response to oxidative stress [GO:0034599]; chaperone-mediated protein complex assembly [GO:0051131]; mitochondrion organization [GO:0007005]; oxidation-dependent protein catabolic process [GO:0070407]; protein catabolic process [GO:0030163]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
|
mitochondrial matrix [GO:0005759]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252]; single-stranded DNA binding [GO:0003697]
|
PF00004;PF05362;PF02190;
|
1.10.8.60;1.20.5.5270;1.20.58.1480;3.30.230.10;2.30.130.40;3.40.50.300;
|
Peptidase S16 family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
| null | null | null | null |
FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner. Involved in the degradation of transcription factor atfs-1 in the mitochondrion (PubMed:22700657). {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:22700657}.
|
Caenorhabditis elegans
|
O44959
|
RIOK1_CAEEL
|
MEKVEHLNLNIQNILEDVDIDTASSSSDDEPEQAVVKQEKLEAGEQIEEQYDTDSDYDDDIVEFAEATGDFTKKLNAARLNTIGPNAARNRLTVDVERHADTSEDRKRKRVKDRADRATVEQVLDPRTRLVLFRLLQRGTLLNIDGCISTGKEANVYHATGTDNDLAIKIYKTSILTFKDRERYVTGEFRYRHGYCKSNPRKMVAVWAEKEMRNLARMHEVGLPVPKPHLLKGHVLVMDFLGKDGWPAPLLKNANLSQEDAEPMYVGLVRDMRRLYRECKLVHADLSEFNMLVHDGKLWIIDVSQSVEQDHPHALEFLRMDCNNVNKFFRELGVPVLSVRRLFEVIVDPLMSSKEMETIIEEERVLVNSEDDSLFMNAFIPHKLEHVLHFERDGKLAKEGVEANNPFQNIVSKIDLKGDGFGEEHDDSDDNDDEENGKKSRKKRAEPTEEEIQEKERKIAMHTRNREETAEERKERKAAVKEEKREQRKEKIPKHLKKRAHRQHMK
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
|
germ cell development [GO:0007281]; germ cell proliferation [GO:0036093]; gonad development [GO:0008406]; maturation of SSU-rRNA [GO:0030490]; meiotic cell cycle [GO:0051321]; negative regulation of MAPK cascade [GO:0043409]; nematode larval development [GO:0002119]; oogenesis [GO:0048477]; phosphorylation [GO:0016310]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of vulval development [GO:0040026]
|
cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF01163;
|
1.10.510.10;
|
Protein kinase superfamily, RIO-type Ser/Thr kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PIRNR:PIRNR038147}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PIRNR:PIRNR038147};
| null | null | null | null |
FUNCTION: Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit (By similarity). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). The catalytic activity regulates its dynamic association with the 40S subunit (By similarity). Plays a role in oogenesis by regulating germ cell proliferation, progression through diplotene and diakinesis stages and oocyte maturation (PubMed:24929033, PubMed:25688864). Regulates germline development probably by regulating the phosphorylation of mpk-1 (PubMed:25688864). Involved in larval development (PubMed:24929033, PubMed:25688864). {ECO:0000250|UniProtKB:G0S3J5, ECO:0000250|UniProtKB:Q12196, ECO:0000250|UniProtKB:Q9BRS2, ECO:0000269|PubMed:24929033, ECO:0000269|PubMed:25688864}.
|
Caenorhabditis elegans
|
O44997
|
DAPK_CAEEL
|
MSDDVNSSATSTSSSTVHFDDTPFEDVYEIETELGSGQFAVVRRVRDRKTGEKYAAKFIKKRRYATSRRGVTRQNIEREVRVLQKIRGNSNVVELHAVYETASDVIIVLELVSGGELFDHVCAKECLDEVEAAAFIKQILLAVRHLHSLHIVHLDIKPENVMLKQRGDSQIKIIDFGLSREIEPGAVVKDMVGTPEFVAPEVVNYEALSPATDMWAVGVVTYILLSGGSPFLGDNRDETFSNITRVRYHFSDRYFKNTSKHAKDFIYRLFVRDVDQRATVEECLQHPWIRGPEGNAIDIRKASCITISHIQSFKTRQRWKRCVELVMVLLKASKSSRRIGDGRFDEEDMVASCTLICAEEGNLRALHKLSALHKLLPNATRKSLKSSFSEPNGATAMHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLKMVKSQEIREEYISQLYPLDTSLRRIKLKLLGHSQSGKTRLVQTLHSSRGISSFLESVTRRISDHYSPSSSMKDDGIHSTNGSFVSESNNNSSFDLAAAAGSKYAPPHSQYTRGIDVQTVNINGCGEFSVWEFGGYEPMHTCYDHFVGNADCIHLILYRTSDPTEVQYKQILYWMNFLKGRVTPFEPIGHCGFSSRRSKVIIVGTHATSSLFPQMNQEGEYVSSDIEAMLNTVRLRFETHFDMDHRLILLDATNPSCIGMKTLKMELAKCRTNILAKLLKPLAILDTVVNHLNLVRKKHANFPVITWPDFIQLVRNEINPLTGDAHCRQIVQQLQLIGELVYLRNDLCDADYVVLNAEWFGTHILGQLLSAEFLSKASPNGSYHTSSLAKIFPEIPEQSDLMTILEVLQLCAPDARTGAHEFPVFIQTEAPDSIWRPYSLKEKERDTVYGGVRILPMRGMERSLHSTFPRIQVALRRSINDYQPAKDTQLHQWSECSKLVSQDREAVIRMVGDAVEIRARGPSESATSMFYFMEDLINLVEHAAAEVGPGISLERHFISPKHLKEHREHPALFPPESMMEMQQRESLSVKGTQDEEELFTDVVCFGSRDVARHLTLGIDVGVADLQMASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDARDALYRTVPLYVFAPLEDQFLLETNDSGVVSSCHSSSEHNPINI
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53355};
|
innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; regulation of response to stimulus [GO:0048583]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00023;PF12796;PF00531;PF00069;
|
1.25.40.20;1.10.533.10;3.40.50.300;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27661253}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27661253}. Note=Exhibits movement along microtubules. {ECO:0000269|PubMed:27661253}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53355}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53355};
| null | null | null | null |
FUNCTION: Negative regulator of epidermal barrier repair and innate immune responses to wounding (PubMed:19164535, PubMed:27661253). The role in epidermal tissue integrity and wound healing is established through the inhibition of epidermal microtubule stability, possibly via the negative regulation of the microtubule minus-end binding protein ptrn-1 (PubMed:27661253). In epidermis, prevents expression of specific unc-44 isoforms probably by promoting nuclear localization of pinn-1, which in turn may affect sydn-1-ssup-72-mediated regulation of alternative polyadenylation of unc-44 mRNA (PubMed:28087624). Appears to act downstream of or in parallel to muscarinic signaling in the regulation of autophagy (PubMed:17785524). {ECO:0000269|PubMed:17785524, ECO:0000269|PubMed:19164535, ECO:0000269|PubMed:27661253, ECO:0000269|PubMed:28087624}.
|
Caenorhabditis elegans
|
O45244
|
DHX16_CAEEL
|
MSVEQFINDQLHSIVGISDRSICQYVHALAKKAKSAPDLVEKLRDAGDFPISPAIQSFADQLMSRMPRQATSARQRGPTTAELAEQELNRLNRAVGVLEDYSASSTKTKNVRKRKESSSEDDEAPIKASKPGKSVKPSKSDDSESDIEAMEAKLDADIAERDALAARINKKEKDKTRNVMEKKRDDNKDKEGSSMDKLREESRRQYLKKRKVDKLEELEAIVHDDQTLFAREKLTKREKADMEYRKKVLEYTKAHGKAGDVMKMKRYHLPDASTKQIPSQYVEDDEEDFRPGGDGAKWEEEQLMASMLHLGAKDAKRKEQEFELLLDEKVDFIQALQMPGTNEEVVETEAEKKKMSIEETRKSLPVYAFRDAFIEAVKEHQVLIIEGETGSGKTTQLPQYLYEAGFCEGGKRIGCTQPRRVAAMSVAARVADEVGCKLGTQVGYSIRFEDCTSEKTVLKYMTDGMLLREFLNEPDLASYSVMMIDEAHERTLHTDILFGLVKDIARFRKDLKLLISSATLDAEKFSSFFDDAPIFRIPGRRFPVDIYYTQAPEADYVDAAIVTIMQIHLTQPLPGDILVFLTGQEEIETVQEALMERSKALGSKIKELIPLPVYANLPSDLQAKIFEPTPKDARKVVLATNIAETSVTIDGINYVIDPGFSKQNSFDARSGVEHLHVVTISKAAANQRAGRAGRTGPGKCFRLYTAWAYKHELEEQPIPEIQRTNLGNVVLMLKSLGIHDLVHFDFLDPPPQETLVIALEQLYALGALNHRGELTKLGRRMAEFPCDPCMSKMIIASEKYECSEEIVTIAAMLSCNAAVFYRPKAQVIHADSARKGFWSPAGDHITLMNVYNKWQESSFSQRWCVENYVQHRTMKRARDVRDQLVGLLERVEIETKSSTDTIKIRKAITAGYFYNVSKLDNTGHYKTVKHKHTTHPHPNSCLFEETPRWVVYFELVFTSKEFMREMSEIESGWLLEVAPHYYKGRELEDATNKKMPKNKGKSGKDLER
|
3.6.4.13
| null |
developmental growth [GO:0048589]; embryonic body morphogenesis [GO:0010172]; feminization of hermaphroditic germ-line [GO:0040022]; germ cell development [GO:0007281]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
catalytic step 2 spliceosome [GO:0071013]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF00270;PF21010;PF04408;PF00271;PF07717;
|
1.20.120.1080;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily, DDX16/PRP8 sub-subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: ATP-binding RNA helicase involved in pre-mRNA splicing (Probable). Operates during embryogenesis. {ECO:0000305}.
|
Caenorhabditis elegans
|
O45293
|
GALT8_CAEEL
|
MRRHVVLSIFVFAGIVFAAEEAEKLPKCEHVDPYENLEGWLDLKPLTERKCNHTLKENLTEAESKKSEWGIKSFAFDALSSEKLGPNRNVGKQAHKLCEEEKYDASYSTSVVVIHHNEALSTILRMINGIIEFTPKSLLKEIVLYEDASEEDHVLTKHLEKFAKIKGLEDKLIIKRSEYRQGLIRAKVHASRLATGEVIVFMDSHCEVAERWLEPLLQPIKEDPKSIVLPVVDLINPVSFDYSPSMVAKSGFDWGFTFKWIYLPWEYFETPENNVKPFNSPAMPGGLLAMRKEYFVELGEYDMGMEIWGSENIELSLKAWLCGGRVVVAPCSRVGHVFRMRRPYTSKPGMDTALYNAVRVAKTWLGEYESKFFAVKPRGAKMVFGDLTEPMQVKDRLKCKDMKWFIENVYPELEPKVHDEL
|
2.4.1.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
protein O-linked glycosylation [GO:0006493]; regulation of Notch signaling pathway [GO:0008593]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
metal ion binding [GO:0046872]; Notch binding [GO:0005112]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;
| null |
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
| null | null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Potential glycopeptide transferase involved in O-linked oligosaccharide biosynthesis (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. {ECO:0000250}.
|
Caenorhabditis elegans
|
O45307
|
OXDD1_CAEEL
|
MTPKIAIIGEGVIGCSTALQVAQAVPDARVTVLSDRPFEQTCSFGPAGLFRIDDIANREFGKSTFDWFAHLHRTEKGDKTGVKLLSGHIQSDSKERLEQQQKAYGDIVYNFRFLEKREILDLFPNPSEHCIHYTAFASEGNKYVPYLKFQCQARGVEFLHRKVRDLEELANEGYDVIVNCAGLSGGTLAGDDDSVYPIRGVVLDVEAHWHKHFNYKDFITFTIPKENSVVIGSVKQENRWDLEITDVDRKDILERYVALHPAMREPKILGEWSGLRPARKTIRIEKVEKKSEKSGKKYTVVHHYGHGGNGFTLGWGTAVEATKLVKSALNSSKL
|
1.4.3.1
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:32376478};
|
D-amino acid catabolic process [GO:0019478]
|
cytoplasm [GO:0005737]; peroxisomal matrix [GO:0005782]
|
D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; D-glutamate oxidase activity [GO:0047821]; FAD binding [GO:0071949]
|
PF01266;
|
3.30.9.10;3.40.50.720;
|
DAMOX/DASOX family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q922Z0}.
|
CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:32376478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12513; Evidence={ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:32376478}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:32376478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:32376478};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.02 mM for D-aspartate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; KM=0.23 mM for D-glutamate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; KM=0.84 mM for N-methyl D-aspartate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; KM=5.54 mM for D-aspartate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; KM=1.06 mM for D-glutamate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; KM=14.6 mM for N-methyl D-aspartate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; Vmax=6.16 umol/min/mg enzyme with D-aspartate as substrate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; Vmax=7.62 umol/min/mg enzyme with D-glutamate as substrate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561}; Vmax=8.8 umol/min/mg enzyme with N-methyl D-aspartate as substrate {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
| null | null | null |
FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:17140416, PubMed:20564561, PubMed:20603179, PubMed:32376478). May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells (PubMed:22393259). {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:22393259, ECO:0000269|PubMed:32376478}.
|
Caenorhabditis elegans
|
O45346
|
OSM11_CAEEL
|
MNFITVAALAIVMVLAQANPARVRRNEEMSERYCIKHLDHYNKYCGDNAGPIDRALFGKVAKFCPAYEKHCAVGKAGLVELPDLGSPLVMPPVLPRGSDFASLDLPIADERKPAHIHSSRTAPQTTRLTAAIVATCTPECTAAHCTDECKCAHTHPKVHQMCNPPSSAAMAETCQRWYSKCTMFTPVQY
| null | null |
cell fate specification [GO:0001708]; Notch signaling pathway [GO:0007219]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of gene expression [GO:0010468]; response to osmotic stress [GO:0006970]; vulval development [GO:0040025]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; extracellular space [GO:0005615]
|
Notch binding [GO:0005112]
| null | null | null | null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:18700817}; Peripheral membrane protein {ECO:0000269|PubMed:18700817}. Note=Concentrated on the apical surface of vulval precursor cells. {ECO:0000269|PubMed:18700817}.
| null | null | null | null | null |
FUNCTION: Probable secreted lin-12/Notch ligand or co-ligand involved in the mediation of Notch signaling (PubMed:18700817, PubMed:21549604). Involved in the lin-12/Notch pathway signaling of cell fate in vulval precursor cells (VPCs), acting redundantly with dsl-1 and lag-2 (PubMed:18700817). Required for normal octanol avoidance response, acting via both lin-12/Notch and glp-1/Notch signaling pathways in neurons, in concert with lag-2 (PubMed:21549604). Involved in regulation of sleep-like quiescence during the larval to adult transition, acting via Notch receptor activation and in parallel with EGF signaling (PubMed:21549604). {ECO:0000269|PubMed:18700817, ECO:0000269|PubMed:21549604}.
|
Caenorhabditis elegans
|
O45405
|
EXL1_CAEEL
|
MPTFSLWLPAGSNNVHPCGDPYAHHLFMRCLYHAKHDPTMKFDVKTTNVNKTSQEFKNTGLRRMPGISAEESGETQTFETEDDILDFLEYLKPERGDDEEAENATCDLFRQFARFVKDVEHRDTAFNTELLRLDKYLSEQETKFLISDDVTHIDCLVLTRLHSIRVAAKMLKNYEIPADLSHVLDYLKAGYATEMFRVSCPSDQEIVLHWTELKDTPRLSAKDRAKLVREEPVFSFSV
| null | null |
chloride transport [GO:0006821]
|
apical plasma membrane [GO:0016324]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; muscle cell projection membrane [GO:0036195]; striated muscle dense body [GO:0055120]
|
chloride channel activity [GO:0005254]
| null |
1.20.1050.10;3.40.30.10;
|
Chloride channel CLIC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14684823}. Membrane {ECO:0000269|PubMed:14684823}. Lysosome membrane {ECO:0000269|PubMed:14684823}. Golgi apparatus membrane {ECO:0000269|PubMed:14684823}. Note=Can be translocated to membranes, possibly as integral membrane proteins, with chloride channel activity (By similarity). Localizes to lysosomal membranes in the intestine, and to Golgi apparatus in neurons and muscle. It also localizes to dense bodies, a transmembrane structure which links the muscle cytoskeleton to the neighboring hypodermis. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable chloride channel. {ECO:0000250}.
|
Caenorhabditis elegans
|
O45495
|
UB2V1_CAEEL
|
MVDVPRNFRLLEELEEGQKGKGDGNISWGLEDDSDMTLTRWTASIIGPPRTPYESRIYNLQIQCGGNYPREPPTVRFTTKVHMVGVNQSNGVIDKRNLTTLRNWSNSYMIKTVLEDIRKNMMMAKENLKLQQPAEGAMF
| null | null |
positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; postreplication repair [GO:0006301]; protein K63-linked ubiquitination [GO:0070534]; regulation of locomotion involved in locomotory behavior [GO:0090325]; regulation of protein localization to cell surface [GO:2000008]
|
cytosol [GO:0005829]; dendrite [GO:0030425]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perikaryon [GO:0043204]; UBC13-UEV1A complex [GO:0035370]
|
ubiquitin conjugating enzyme binding [GO:0031624]
|
PF00179;
|
3.10.110.10;
|
Ubiquitin-conjugating enzyme family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21179194}. Nucleus {ECO:0000269|PubMed:21179194}. Cell projection, dendrite {ECO:0000269|PubMed:21179194}. Perikaryon {ECO:0000269|PubMed:21179194}.
| null | null | null | null | null |
FUNCTION: Involved in protein ubiquitination, but has no ubiquitin ligase activity on its own (PubMed:15530417). The uev-1-ubc-13 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63 (PubMed:15530417, PubMed:24595290). Involved in sorting Lys-63-linked polyubiquitinated maternal membrane proteins for degradation by targeting to multivesicular bodies (PubMed:24595290). Required for glr-1-containing glutamate receptor trafficking in neurons (PubMed:21179194). May have a role in synaptic transmission at motorneurons (PubMed:21179194). May be involved in the ubiquitination and growth of intracellular polyglutamine protein aggregates (PubMed:17663792, PubMed:22494772). {ECO:0000269|PubMed:15530417, ECO:0000269|PubMed:17663792, ECO:0000269|PubMed:21179194, ECO:0000269|PubMed:22494772, ECO:0000269|PubMed:24595290}.
|
Caenorhabditis elegans
|
O45539
|
SRC2_CAEEL
|
MGSCIGKEDPPPGATSPVHTSSTLGRESLPSHPRIPSIGPIAASSSGNTIDKNQNISQSANFVALFQYDARTDDDLSFKKDDILEILNDTQGDWWFARHKATGRTGYIPSNYVAREKSIESQPWYFGKMRRIDAEKCLLHTLNEHGAFLVRDSESRQHDLSLSVRENDSVKHYRIRQLDHGGYFIARRRPFATLHDLIAHYQREADGLCVNLGAPCAKSEAPQTTTFTYDDQWEVDRRSVRLIRQIGAGQFGEVWEGRWNVNVPVAVKKLKAGTADPTDFLAEAQIMKKLRHPKLLSLYAVCTRDEPILIVTELMQENLLTFLQRRGRQCQMPQLVEISAQVAAGMAYLEEMNFIHRDLAARNILINNSLSVKIADFGLARILMKENEYEARTGARFPIKWTAPEAANYNRFTTKSDVWSFGILLTEIVTFGRLPYPGMTNAEVLQQVDAGYRMPCPAGCPVTLYDIMQQCWRSDPDKRPTFETLQWKLEDLFNLDSSEYKEASINF
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:G5EE56}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:G5EE56};
|
cell differentiation [GO:0030154]; innate immune response [GO:0045087]; nematode pharynx development [GO:0160094]; phosphorylation [GO:0016310]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: May be phosphorylated on Tyr-500 by csk-1. {ECO:0000269|PubMed:12527374}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000269|PubMed:12527374};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase which may play a role in larval and pharynx development. Unlike src-1, does not play a role in embryonic development. {ECO:0000269|PubMed:12527374}.
|
Caenorhabditis elegans
|
O45551
|
IF4E1_CAEEL
|
MTETEQTTAPIYPLKRNWTWWYLNDERNKSWEDRLKKVYTFNTVSEFWALYDAIRPPSGLNALCDYNVFRDDIQPMWEVPENSNGGRWLIVIDKGKTPEMVDAIWLEILMALVGEQFGKDMESICGLVCNVRGKGSKISVWTKDCNDDETNMRIGVVLKEKLMAASKDHSKPLFDVIRYEDHESCQKKTSSVVKAKLSLHSSDAPVAEKSAV
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; oocyte maturation [GO:0001556]; spermatid development [GO:0007286]; translational initiation [GO:0006413]
|
cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; P granule [GO:0043186]
|
RNA 7-methylguanosine cap binding [GO:0000340]; RNA trimethylguanosine cap binding [GO:0000341]; translation initiation factor activity [GO:0003743]
|
PF01652;
|
3.30.760.10;
|
Eukaryotic initiation factor 4E family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11641215}. Note=When associated with pgl-1.
| null | null | null | null | null |
FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Required for progression through meiotic divisions during spermatogenesis and for the production of viable sperm. It is not required during oogenesis. {ECO:0000269|PubMed:10744754, ECO:0000269|PubMed:11641215, ECO:0000269|PubMed:9553113}.
|
Caenorhabditis elegans
|
O45657
|
PLX2_CAEEL
|
MLPESVFLLLISHFLRAVTQPPFETEGVKQKLFHFSGHIDDFIVSRDQQTIYVASLNRLTSLSISNFSIQHEVSLGPVQDSPWCSADGKSCLKDNRPFPTDVRTKILQILPTNQILQCGSVKLGSCSTFNSKLSLITESTIAVAANSPDASTVSKIIDNRLIVAASATKESPYRDPFPAVAIRNLPGLNVENAGDLEGEAAVFLRAAYKNAFKFLYTFTHQHFVFVVAMVTPRESRLPMTTRLIRFCRNDTKFESYSEIELQCRGEDNTNYPFLNAIIQSYDKLIASFSTSSTSPKSSICVFSMQKVKLTFWYNVDRCRSGTDSIRLPHIGRDTKCVNKAHIPLDEDSCELGVGGSIELVEMSTKDIMGKVTSLMAVDQKAIFAGTTTSQIVMFKWDEHHSNQLEEYGRKEVGDGRTGSEVSKMVKFGDFVIVQMPYGIILEELSTCSHHSSCTECLVSVDPLCQWCHPTQSCTTSARCTSPVTSQCPIVDGDPIPSIVSVNSSTPISFNIHHLPPPVGFTYRCQFGTSTSSIKANWTTTGVSCPSEIFTSPNTFEILLLTSISNNPISRHNFTVYDCSGYGTCSSCMSSEYNCAWCSGLHKCSNSCGALEKSKACVKIQPMRLPIAIGSQQEIVLEASNLDTLDRRHEHFCKVNEQVSLAKIASDSIRCGKIQLTLSNTTSANMVVPLSLITRDSVIDIANVSLYSCTNLASDCSSCLALSPSLSCGWCNRQCSHECHESKATAVCDPPRIDKFEPTSGPIEGGTIIKIYGNDLGMSVEDVRGKIYVAGSRCNIVEYHVSNMIACQVDKGVSSGPIRISVGRATVAVAESSELYSFVRTSIFSAYPLYGPISGGTRITLYGQNLSSGSQTSVTVGGMPCPIERVNSSTVLTCLTPSGTRIGKSARVVVHVDHSQTQLDQPFEYRSDPSISSIFPMTSFKAGGRIVYVQGNSLNTVQTAKLFLISSPTPPFYIISDLAPCHIINSTLMTCMTPKILETITRRVEYTRQPVGFHMDNVTAVANLGRRIQMGIYPNPTLSPFKGVRYHQGEQSLILEGHNLNLAAEPNDFKIFIGNERCYVTLVDVRQLVCSGPVRQPKATDERGIPINGDNPLVTVIVGSLRMELGLIEYSDHALPSRLSLLILGLLLFIVVTLTVMCLVFKRRRQEREKEYRKIQLQMENLENNVRKECKQAFAELQTNLVLSPKSANSVNLGPELINFPHFVENLLWSDNNLTSAPSLARTLPVTLAQFHALLSFKGFIFTIVEAAESDVSISTSEKSMLASLLISVLLRNFSYCTEVVVDLLRAHIARSVQNKRAELLFRNSDSVVEKMFSKWMSICLYSHLTPQMNSYFYLYKALQYQTDKGPVDAVTGDARYTINEAKLLRESVDTKTLKIRVIPFEKCDESIDLEVHACDAICQVKQKVASAVYRETPYSQRPRITQFELKYKCPKRGDVKLTDVLPIETLSQKKLPVKLFTLADYGISDGCTLEMSPAVYTAESYRNSLADSGQSSWSSLDRCSPIYSSSKYYHLTNPSSGTMTFKKKSSNDSNLLPKSIPEVYLTRLLTSKGTVETYVEDFLESVLYMHDSSYPPILKFFFDILDREASVNGVSENICQQWKANGYVLRVWANFVRNPQLVFDVPHSISMDANLSTVAQTMMDCFSFSEPVLGAHSPSSRLLFAKDVARLRPLSVDLFKRVKNSPPLGMDELRTELVNMANDVSTCKGSSLALSELLSWVRGNGIRISQLLSSNEQFSQQRLPQKLSQVLHVCLETDNHIYSTISDYE
| null | null |
axonal fasciculation [GO:0007413]; embryo development ending in birth or egg hatching [GO:0009792]; motor neuron axon guidance [GO:0008045]; negative regulation of cell adhesion [GO:0007162]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of axonogenesis [GO:0050772]; regulation of axon guidance [GO:1902667]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; sensory neuron axon guidance [GO:0097374]
|
cell leading edge [GO:0031252]; cell surface [GO:0009986]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
|
semaphorin receptor activity [GO:0017154]
|
PF08337;PF20170;PF01437;PF01833;
|
2.60.40.10;2.130.10.10;
|
Plexin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved as a receptor for mab-20/sema-2a in the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis (PubMed:17507686). In early embryonic development, required for proper ventral closure of the epidermis (PubMed:17507686). During male tail morphogenesis, involved in precursor cell sorting and in the formation of distinct sensory rays (PubMed:15030761). Involved in axon guidance of SDQL neurons during neurogenesis (PubMed:26903502). Probably in response to stimulation by mab-20, regulates fln-1-mediated remodeling of the actin cytoskeleton and thus axon guidance and/or fasciculation of DD/VD neurons (PubMed:25358863). {ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:17507686, ECO:0000269|PubMed:25358863, ECO:0000269|PubMed:26903502}.
|
Caenorhabditis elegans
|
O45666
|
NHR49_CAEEL
|
MDYFLDASKHIQLNQIDEESSDDFMDLVDPLAEPCAVCGDKSTGTHYGVISCNGCKGFFRRTVLRDQKFTCRFNKRCVIDKNFRCACRYCRFQKCVQVGMKREAIQFERDPVGSPTSGASLNGTPFKKDRSPGYENGNSNGVGSNGMGQENMRTVPQSSSVIDALMEMEARVNQEMCNRYRRSQIFANGSGGSNGNDTDIQQGSDSGASAFAPPNRPCTTEVDLNEISRTTLLLMVEWAKTINPFMDLSMEDKIILLKNYAPQHLILMPAFRSPDTTRVCLFNNTYMTRDNNTDLNGFAAFKTSNITPRVLDEIVWPMRQLQMREQEFVCLKALAFLHPEAKGLSNSSQIMIRDARNRVLKALYAFILDQMPDDAPTRYGNILLLAPALKALTQLLIENMTLTKFFGLAEVDSLLSEFILDDINDHSTAPVSLQQHLSSPTTLPTNGVSPLNPAGSVGSVSSVSGITPTGMLSATLAAPLAIHPLQSQDSILNSEQNNHML
| null | null |
cell differentiation [GO:0030154]; determination of adult lifespan [GO:0008340]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of fatty acid metabolic process [GO:0019217]; regulation of lipid metabolic process [GO:0019216]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor binding [GO:0140297]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
| null | null | null | null | null |
FUNCTION: Orphan nuclear receptor (PubMed:25981666). Regulates expression of genes involved in fat metabolism and in maintaining homeostasis of fatty acid saturation, such as lipid desaturase fat-7, and acyl-CoA synthetase acs-2 (PubMed:15719061, PubMed:22511885, PubMed:25981666). May form part of a negative feedback loop with fat-7 to limit mitochondrial beta-oxidation, in which it stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation (PubMed:15719061). As part of a lysosome-to-nucleus retrograde lipid signaling pathway, acting in concert with nuclear hormone receptor nhr-80, activates the transcription of genes promoting longevity and mitochondrial beta-oxidation (PubMed:25554789, PubMed:26671266). In concert with nuclear hormone receptor nhr-66, involved in regulating target genes with roles in sphingolipid breakdown and lipid remodeling (PubMed:22511885). Also involved in regulating fatty acid desaturase genes, acting in concert with nuclear hormone receptors nhr-13 and nhr-80 (PubMed:22511885). Plays a role in modulating mitochondrial morphology and function (PubMed:22511885). Plays a role in transgenerational lipid accumulation in response to a high-fat diet (PubMed:35140229). {ECO:0000269|PubMed:15719061, ECO:0000269|PubMed:25981666}.
|
Caenorhabditis elegans
|
O45679
|
CYSK2_CAEEL
|
MSRELMVETGGELIGNTPLLKLNKIGKDLGASIAVKVEYMNPACSVKDRIAFNMIDTAEKAGLITPGKTVLIEPTSGNMGIALAYCGKLRGYKVILTMPASMSIERRCLLKAYGAEVILTDPATAVKGAVQRAEELRDVIPNAYILNQFGNPANPEAHYKTTGPEIWRQTQGKVDIVCFGVGSGGTCTGVGRFLKEKNPSVQVFPVEPFESSVINGLPHSPHKIQGMGTGMIPDILDLTLFSEALRVHSDDAIAMAKKLADEESILGGISSGANVCAAVQLAKRPENKGKLIVTTVNSFGERYLSTALYAELRDNAANMKQLNLDDSIKIAKEYLGI
|
2.5.1.47; 4.4.1.9
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:24100226};
|
cysteine biosynthetic process from serine [GO:0006535]
|
cytoplasm [GO:0005737]
|
cysteine synthase activity [GO:0004124]; L-3-cyanoalanine synthase activity [GO:0050017]
|
PF00291;
|
3.40.50.1100;
|
Cysteine synthase/cystathionine beta-synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=hydrogen cyanide + L-cysteine = 3-cyano-L-alanine + H(+) + hydrogen sulfide; Xref=Rhea:RHEA:17821, ChEBI:CHEBI:15378, ChEBI:CHEBI:18407, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235, ChEBI:CHEBI:77860; EC=4.4.1.9; Evidence={ECO:0000269|PubMed:24100226}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:24100226};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for O-acetylserine (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:24100226}; KM=0.4 mM for S-sulfocysteine (at 25 degrees Celsius, pH 8.5 and in absence of dithiothreitol) {ECO:0000269|PubMed:24100226}; KM=1.2 mM for cysteine (at 25 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:24100226}; KM=1.4 mM for sulfide (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:24100226}; KM=0.8 mM for cyanide (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:24100226};
| null | null | null |
FUNCTION: Primarily catalyzes the formation of cyanoalanine and hydrogen sulfide from cysteine and hydrogen cyanide. Can also catalyze, although less efficiently, the formation of cyanoalanine and hydrogen sulfide from either S-sulfocysteine or O-acetylserine and hydrogen cyanide and the formation of cysteine from either S-sulfocysteine or O-acetylserine and hydrogen sulfide (PubMed:24100226). By catalyzing the assimilation of cyanide produced by P.aeruginosa, mediates resistance to infection (PubMed:21840852). Involved in fertility, growth and aging (PubMed:24260346). Does not mediate survival in high levels of hydrogen sulfide (PubMed:21840852). {ECO:0000269|PubMed:21840852, ECO:0000269|PubMed:24100226, ECO:0000269|PubMed:24260346}.
|
Caenorhabditis elegans
|
O45717
|
NUD2_CAEEL
|
MDLSEDQIRGLPHHELLGHFLQMREEFNEFQTSSAEIEKMMDSELDDLKTQLKKAETRVQQMTTEQIRNKDRQDDSRVQFAQVEEQLRRENSHLHEQCESQRERIRKLEQRNDVLETSERNKEYLASDLGSKLDHAIEKIAMLESELYERQVAAEEMHRLREEQLRTTERPRLIVEPLRNDPEILPDEPSPGPSKEEFKMSSEDVFMEDVQHHEDVRMEETIAKIDEVRIDDNKNIQEKSQRVSTGTGAGACINRIVKDLMTKVERLDSILSTIRVSNNSSNNNSSHLTTTRA
| null | null |
cell migration [GO:0016477]; centrosome localization [GO:0051642]; chromosome segregation [GO:0007059]; establishment of chromosome localization [GO:0051303]; establishment of mitotic spindle orientation [GO:0000132]; microtubule nucleation [GO:0007020]; mitotic centrosome separation [GO:0007100]; nuclear migration [GO:0007097]; nuclear migration along microfilament [GO:0031022]; synaptic transmission, GABAergic [GO:0051932]; synaptic vesicle transport [GO:0048489]; vesicle transport along microtubule [GO:0047496]
|
centrosome [GO:0005813]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; nuclear envelope [GO:0005635]; synapse [GO:0045202]
|
microtubule binding [GO:0008017]
| null |
6.10.250.1080;
|
NudE family
| null |
SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:20005871}. Note=Recruited to the nuclear envelope by unc-83. {ECO:0000269|PubMed:20005871}.
| null | null | null | null | null |
FUNCTION: Part of a complex with lis-1, which is recruited to the nuclear envelope by unc-83, where, in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871, PubMed:27697906). Plays a role in GABAergic synaptic vesicle localization in the ventral nerve cord (PubMed:16996038). {ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906}.
|
Caenorhabditis elegans
|
O45734
|
CPL1_CAEEL
|
MNRFILLALVAAVVAVNSAKLSRQIESAIEKWDDYKEDFDKEYSESEEQTYMEAFVKNMIHIENHNRDHRLGRKTFEMGLNHIADLPFSQYRKLNGYRRLFGDSRIKNSSSFLAPFNVQVPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKYGNHGCNGGLMDQAFEYIRDNHGVDTEESYPYKGRDMKCHFNKKTVGADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHRSFQLYKKGVYYDEECSSEELDHGVLLVGYGTDPEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHCGVATKASYPLV
|
3.4.22.15
| null |
apoptotic cell clearance [GO:0043277]; immune response [GO:0006955]; lipid droplet disassembly [GO:1905691]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of vitellogenesis [GO:1903188]; proteolysis involved in protein catabolic process [GO:0051603]; regulation of apoptosis involved in tissue homeostasis [GO:0060785]; regulation of protein processing [GO:0070613]
|
cytoplasm [GO:0005737]; endolysosome [GO:0036019]; extracellular space [GO:0005615]; phagolysosome [GO:0032010]; vesicle lumen [GO:0031983]; yolk granule [GO:0042718]
|
cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11707440, ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Lysosome {ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:24829385}. Endosome {ECO:0000269|PubMed:22768338}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:24829385}. Note=The zymogen form localizes to yolk platelets/granules in the developing oocyte and in the pseudocoelom (PubMed:15456850, PubMed:16857685). Following cell corpse phagocytosis, recruited to phagosomes during the late stages of phagolysosome formation (PubMed:24829385). {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24829385}.
|
CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000250|UniProtKB:P06797};
| null | null | null | null |
FUNCTION: Cysteine protease which plays an essential role in the degradation of proteins in lysosomes (PubMed:15456850, PubMed:24829385). During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome-like structure where a slow and controlled degradation of yolk proteins occurs (PubMed:15456850, PubMed:24829385). In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes (PubMed:24829385). In embryos, required for the degradation of endocytic and autophagic cargos (PubMed:24829385). In embryos, may play a role in the degradation of lipid-containing droplets (PubMed:26773047). Required for larval development (PubMed:11707440, PubMed:15456850). {ECO:0000269|PubMed:11707440, ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:24829385, ECO:0000269|PubMed:26773047}.
|
Caenorhabditis elegans
|
O45784
|
TAF9_CAEEL
|
MADTGEKDTETTASGTDGHSKEALAVISMLHECGIQEFDPRVVSMLMDVQYAVTSKILQMSSGLSRHAEKAQIEAEDVQTAADMLGVLTTNAPDREKILQLANDKNQQPLPQIRHNYGLKLPNDRFCQLQQNFVYKADDSYQPMEMQQVTHQPHIIEPPTQVLRPEHVQNMLKRRAPDDDFDS
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of mitotic cell cycle, embryonic [GO:0009794]; RNA polymerase II preinitiation complex assembly [GO:0051123]
|
nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFIID complex [GO:0005669]
|
protein heterodimerization activity [GO:0046982]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; transcription coactivator activity [GO:0003713]
|
PF02291;
|
1.10.20.10;
|
TAF9 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11566890}.
| null | null | null | null | null |
FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-9 (By similarity). Essential for early embryonic development, but not required for transcription of some genes; probably acts via activating transcription initiation by RNA Pol II, as part of the TFIID complex (PubMed:11566890). {ECO:0000250|UniProtKB:Q16594, ECO:0000269|PubMed:11566890}.
|
Caenorhabditis elegans
|
O45797
|
WARTS_CAEEL
|
MRPAAPGTTPNGASSDIRHQRGVAPIPFGSTNSAIDAHHNSEIRVGRHRAKLDEIRESLKAYEHEAGLLSSHVALGSLATPSSSSVSHSDITNDNAEVMNFSSSSSNAAATTTTVSSAAVSNSNSFRTEGGGHKMRITPMPQRHLMMDTGANETVFRSGKEMIRNGNPSTTISSTPSTTTEESIRIHPAGYRYDMPTPAYHMNNNAPQYSPGYSRPPPPAYDSSPVNTRMTPVATDNYRTHLHMKVHPVVKAPPPNPTMLNHNKNMAPPPPPPAKSTISIETMSEERKADNIQRLYHTSMDKKTASSVVSINVASPHTTKVNVGDSPLPSKSFIIGPRYTADVDRKNFVNYKDELRPDPRLIPSTSDANHEDFRPILFKPRNLEITMKSRAQPPPPQYNQPSEPPPKRVSSPIDRTLLEPYIKNTRRVQPCKPNMLRFYMEQHVERLLQQYKEREKRMKQLEKEMVSAQLPDIMRNKMLGLLQQKESKYTRLRRQKMSKSHFTVISHIGVGAFGKVSLVRKNDTRKVYAMKSLEKADVIMKQQAAHVKAERDILAEADSPWIVRLFFSFQDDACLYFIMEYVPGGDMMTLLIQKGIFEEDLARFYIAELACAIEYVHNVGFIHRDLKPDNILIDQHGHIKLTDFGLCTGLRWTHDRRYYGPENDHHRVDSFSLPPEVAAIDKSVKVLNVRQQTRRITAHSLVGTGNYMAPEVIAKTGHNQSCDWWSTGVILYEMVFGRVPFHDDTPGGTQHRIKNWRNFLDFTYCGNLSKECLMMIQQLICDASSRLGSHGKDVAERTAQVKNHPWFRGIDWVNLRKLRADYIYIPRVTHDEDTSNFETFQDNDRADKPNVRGLHNPAFYEFTYRHFFDTDSVGCPSLRPSRRRSLRPLLENGTFNESVSEEDSSSHI
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95835};
|
apical protein localization [GO:0045176]; defecation [GO:0030421]; G1/S transition of mitotic cell cycle [GO:0000082]; hippo signaling [GO:0035329]; negative regulation of protein import into nucleus [GO:0042308]; nematode larval development [GO:0002119]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; post-embryonic digestive tract morphogenesis [GO:0048621]; regulation of organ growth [GO:0046620]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transcription coactivator binding [GO:0001223]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560}. Apical cell membrane {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560}. Note=In epithelial cells, localized near the plasma membrane. In intestinal cells, localized in the subapical membrane region (PubMed:19605499, PubMed:19737560). Membrane localization starts in the late embryo (PubMed:19605499). {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O95835}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O95835};
| null | null | null | null |
FUNCTION: Phosphorylates yap-1 which may negatively regulate yap-1 nuclear localization (PubMed:23396260). Plays an essential role in larval development (PubMed:19605499, PubMed:19737560). Regulates growth, the formation of gut granules, lifespan and cell and body sizes probably in synergy with the TGF-beta sma/mab pathway (PubMed:19737560). Does not appear to regulate apoptosis and proliferation (PubMed:19605499). In addition, may synergize with the TGF-beta daf-7 dauer pathway to regulate entry into the dauer stage (PubMed:19737560). Maintains the cellular integrity of intestinal cells by regulating the localization of apical actin and junctional proteins (PubMed:19605499). {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560, ECO:0000269|PubMed:23396260}.
|
Caenorhabditis elegans
|
O45813
|
SNF12_CAEEL
|
MNGEWKSALRLQIEALAKRNELHRKSSVDEIKKRTVDMDKRIVKLRELVGSSANDAALFYLECVCHADETERLLNRGSSVGKEKKWKKVKRKTSSSVAPPLSRTISSLPGVSSPDVIQTIDVSALEDQTPQRPHWWDQFQLYRRTDLLRFSKQNDRRELWRTQKDFFLSCLGFMVGVGHTMRFPAKVYQHGGGVFFIPYLFSLIFFGLPLVFLHLSLGQYTGQAANTAFQRLMPIGSGVGWALVVIAIPVAVYYNIIVAWAIHYFFQSAKGLLLGDELPWETCRDEWQLDNRCCNLHNLHSCFNSTNSITAPEAFFHSEVLSLSTFGDFALGPLQSHLVLSLAAAWLLVFFGVFKGLGSIAQTMNVTATVPYLLLSILLLRGISLPGANKGLTFLFTVDSTKLWKWQIWKSAAEQVFYELGIDAGPLISMAAFSRYRNNIYRDSVLLVIMDALTSCLSGMVIFSFVGFIASESNSNVNDVLKHDPLYLSFTVYPGVTSFMYWGGLWATLFFGMLVLAAIDAEFAWLEMIASAFMNHFSMKNKAVENRLLAFLCLAGFFLGLPLCAQGGIFVFHAIENLNANWNSFSLALLSVAIVCYVYGIDNYLTDISAMLRVPRIQISKATRLKEKLIYFFGPGGIYIKFSLCFICPVILTVLLVASVLGYQRISFAGRPIPIDYEIVAWIVMIGPLLVVPLVAFMQIRQIRNEGKLLKSLFDTSEWRESQDDSLEPKDLYMRQSGKFESPPNRRRTPTIFTHRENTYMYIDSRGPTVRSRVFPLGASLDPYGWKAGRLRDRQQQIEETASNYSEEDSATTNSFMASTVKHNDDMELTLFGSPPAILGDDEKIMTTRFSESMPVNYKCRNVEVPRIPNKLPQNMERMARKTRKKRSSPSASDPPVPTSPLPPPPKLQHCRSEPPMMNSKESHSPEIITPGDDSPSISNSSDDSSDDCFRRATVIRRKTSDDDAFTHFSTATAESISITPLDFPRQRSLSSVAIYDQEQKNGRSKVLSQLKRPKPIDMPPK
| null | null |
amino acid transport [GO:0006865]; positive regulation of antifungal peptide production [GO:0002804]; sodium ion transmembrane transport [GO:0035725]
|
apical part of cell [GO:0045177]; endocytic vesicle [GO:0030139]; plasma membrane [GO:0005886]
|
STAT family protein binding [GO:0097677]; symporter activity [GO:0015293]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:21575913}. Vesicle {ECO:0000305|PubMed:21575913}. Note=Localized to vesicles, which may be a type of endosome (PubMed:21575913). Localized to an unknown apical membrane compartment (PubMed:31995031). {ECO:0000269|PubMed:21575913, ECO:0000269|PubMed:31995031}.
| null | null | null | null | null |
FUNCTION: Probably mediates sodium-dependent uptake of unknown small molecule(s) (PubMed:21575913). By positively modulating expression, in the epidermis, of antimicrobial peptides such as nlp-29, plays a role in resistance to fungal infection and in the response to physical wounding and phorbol ester PMA treatment (PubMed:21575913). Role in response to wounding of the epidermis may be facilitated by recruitment of snf-12 to the wound site by microtubule-dependent vesicle trafficking (PubMed:31995031). Functions cell autonomously in the epidermis, in concert with STAT transcription factor sta-2, probably acting at vesicular membranes, downstream of a p38 MAPK/pmk-1 pathway (PubMed:21575913). {ECO:0000269|PubMed:21575913, ECO:0000269|PubMed:31995031}.
|
Caenorhabditis elegans
|
O45818
|
DKF2_CAEEL
|
MDANDYPRLYYTSMPSSSTSMVTTTRFSTSFSPSIPCHRQENFRRHSTSALAKRNGSESEKSAEIRENPDEIEVSRVSGRDSSLAFYTTAHETSSMLSRDSRDETLTPNEHIHQASSRRVSANDSVFEDGYVDFVDEPREHGSRRKSFEKFTDRNGEEKEGRVFELSTPQPTREAAPGAHQFQLPTLLVTSTPTTVFDHSDDEVWTPYRPPPNREYSSSSEPMMGDLTFRLQSGIHKKSIAVEGTEIALRDLRNEALQFIKEIYPEKGCSSLEDYILLYKHDLRSINILQLITTSSDVTDGTLVEVVIGSCPQNERIVVHPHTLFVHSYKVPTFCDFCGELLFGLVKQGLKCFGCGLNYHKRCASKIPNNCNGSKQRRPSAIPLSPSNSNILNLNERRHSRRESCLEALDAARPSSTLGGAATPNIFITSDDCGDAVGGNYLQMPRKDRSCSWSGRPLWMEIAEATRVKLQVPHTFQVHSYKLPTVCQHCKKLLKGLIRQGMQCRDCKYNCHKKCSEHVAKDCSGNTKASQFFLGSQADDGASEDRDDDLSLRSGSGAHKKAQNTPSAPLQGSEGSGSPGPVVSFAANALSNMPDDDVISSESANIPLMRVVMSKKQTKRKNNKLLKEGWIVHYTDQQNMRKKHYWRLDTKGITMYQDENTTRYYKEIPLNEILNVSMSPPDKTADYLFEIRTGVCVYFISGSPSDEKGSSLDAQSWTTAIQSALMPVTPQSSVVGGKRIDKLKVPTEGETGHLGAKIQTEHEFSQLYQIFAEEVLGSGQFGTVYGGIHRRNGQHVAVKLIDKLKFPPNKEDLLRAEVQILEKVDHPGVVHFMQMLETTDRIFVVMEKLKGDMLEMILSSEKGRLSERTTQFLVAQILEALRYLHHLNIVHCDLKPENILLNSNSDFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGFNRSLDMWSVGVIVYVSLSGTFPFNEDEDINDQIQNAEFMYPPTPWKEISENAIEFINGLLQVKMSKRYTVTKAQSQIWMQNYTLWSDLRVLEKAVGQRFVTHESDDVRWQAYEKEHNVTPVYV
|
2.7.11.13
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715};
|
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; determination of adult lifespan [GO:0008340]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; phosphorylation [GO:0016310]; protein import into nucleus [GO:0006606]
|
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]; serine/threonine protein kinase complex [GO:1902554]
|
ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00130;PF00169;PF00069;
|
3.30.60.20;2.30.29.30;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PKD subfamily
|
PTM: Phosphorylation on Ser-925 by tpa-1 is the dominant regulator of catalysis, phosphorylation on Ser-929 by tpa-1 has a lesser effect. Prolonged phosphorylation results in ubiquitination and degradation. {ECO:0000269|PubMed:17728253}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17728253}. Membrane {ECO:0000269|PubMed:17728253}. Note=Translocation to the cell membrane is required for kinase activation. {ECO:0000269|PubMed:17728253}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715};
| null | null | null | null |
FUNCTION: Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Acts in the intestine to regulate both innate immunity by promoting activation of PMK-1 and also stress response and life span by acting as an upstream, negative regulator of the daf-16 transcription factor. {ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
|
Caenorhabditis elegans
|
O45824
|
CL38_CAEEL
|
MAIFYDDPLERLNQPIKTKSYRKKQVVQRVHVFIFDNWKLILLGILNLIFLIIAIVFAILFFVGSADCAQLPDYTTSPASQLTTSAISSRTSEVQTNAITTTQGTPSNKTSTTTPSTSKVICASGFTLVGTKCGKLVSSNQPRTEADSICKGYGGSTLFSVRNEQETRDMLDFVKDSNIDFLWTGLVCNQTARTSCIWDVKSGTTADYNNFADGFPNVVYGYCIYFIVTGNSAGQWGSEQCSQLMNFVCELPTTIRDPDCKYNYNKNCYIRFDITLTIPQAQRFCNEKGADLVSIHSANENRFILTIYDIHGQILLGGLAPAVDFIVWLDGSPTTYSNLLYFYDTRSCVLMTVARGGPYDGDWYTMNCNVQEFFLCKRAIDF
| null | null |
dorsal/ventral axon guidance [GO:0033563]; motor neuron axon guidance [GO:0008045]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of gene expression [GO:0010629]; negative regulation of sensory neuron axon guidance [GO:1905490]; presynapse assembly [GO:0099054]; regulation of dorsal/ventral axon guidance [GO:1905815]; regulation of motor neuron axon guidance [GO:1905812]; regulation of sensory neuron axon guidance [GO:1905489]; sensory neuron axon guidance [GO:0097374]; synaptic vesicle localization [GO:0097479]
|
membrane [GO:0016020]
|
carbohydrate binding [GO:0030246]
|
PF00059;
|
3.10.100.10;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000303|PubMed:18434533}; Single-pass type II membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Involved in negative modulation of unc-40-mediated axon outgrowth (PubMed:18434533). Required for proper presynaptic development in axons that have reached their targets (PubMed:18434533). May function in concert with E3 ubiquitin-protein ligase rpm-1 in regulating axon outgrowth (PubMed:18434533). {ECO:0000269|PubMed:18434533}.
|
Caenorhabditis elegans
|
O45876
|
APH1_CAEEL
|
MGYLLTIACYIASFSPSIALFCSFIAHDPVRIILFFLGSFFWLVSLLFSSLAWLGLSTVLPDTFLLSLTVCIIAQELSRVAYFMLLKKAQRGLNKITRQGQISVAPGVSDLHNARHMLALVCGLGMGVISALFYTMNAFAIFSGPGTIGLPNALKTGEIDTNRAGKYLPLCYTLSAILLTLFHVTWTIMVWDSCHKIGRIPSAFVPGAAAVVSHLLVTFLSSLNSRGFHVLVFAVQFLILLICIAYCNVIMGGTISSFVNGIGQSITDAVTLKQVRTLIEERKLRTQRQSVPDEPMTERAGTSNTVNA
| null | null |
cell fate commitment [GO:0045165]; cell fate commitment involved in pattern specification [GO:0060581]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic morphogenesis [GO:0048598]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; oocyte development [GO:0048599]; pharynx development [GO:0060465]; protein localization to cell surface [GO:0034394]; protein processing [GO:0016485]
|
endoplasmic reticulum [GO:0005783]; gamma-secretase complex [GO:0070765]
|
protein-macromolecule adaptor activity [GO:0030674]
|
PF06105;
| null |
APH-1 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors (lin-12 or glp-1). It may represent a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Required for the localization of aph-2. {ECO:0000269|PubMed:11792846, ECO:0000269|PubMed:12110170}.
|
Caenorhabditis elegans
|
O45923
|
TTM1_CAEEL
|
MTISMISPSSIRLSSDKRDSSSSNLPANIEEDTQSVSSSDSGVSADSIDHHHHGHGHGHSHGGHGHSHTHNNDDSSSDCSGAGGGAHKHSHDEKYQKGRRAEKVLWAVAALSAVFIAAEFVGGFWAQSLAIMTDAGHMLSDLLSFIISIFAIRCARLPASKRLSFGYERAEVLGALTSVIILWVLTTVLVVVAIQRIVNNEHEVDADVMLITAGVGVLFNIVMGLVLHFGTGGHGHTHGGHSSHGHAHDGKNVNVRAALIHVIGDLVQSIGVLIAALIIRFTGWTLADPICTFLFSIIVLFTTVTVMRDIFFVLMEATPSHYDLSDVKKALSALEGVKGVHDLHLWSIGMDKTAFSVHLALESPNRAMENVAEARSLIRRRFGVAVATVQVEPFDEKIDSCDTCQQQETA
| null | null |
response to cadmium ion [GO:0046686]; response to nematicide [GO:0093002]; response to zinc ion [GO:0010043]; zinc ion transmembrane transport [GO:0071577]
|
apical plasma membrane [GO:0016324]; cytoplasmic vesicle membrane [GO:0030659]; plasma membrane [GO:0005886]
|
zinc ion transmembrane transporter activity [GO:0005385]
|
PF01545;
|
1.20.1510.10;
|
Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily
| null |
SUBCELLULAR LOCATION: [Isoform a]: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform b]: Apical cell membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Promotes excretion of zinc from intestinal cells into the intestinal lumen in response to increased dietary zinc (PubMed:23717214). Involved in cadmium resistance, possibly by promoting its transport from cells (PubMed:15256590). Involved in resistance to B.thuringiensis pore-forming toxin Cry5B downstream of the sek-1 and pmk-1 MAPK kinase pathway (PubMed:15256590). {ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:23717214}.
|
Caenorhabditis elegans
|
O45935
|
KLP19_CAEEL
|
MSSDASLRVVVRARPMNGRETKEGASRCVQFYENTKQIVINESATFTFDAVFADTSDQESVYETTALPLLDRIFAGFNATVLAYGQTGSGKTYTMGTEDNVGTDEMRRGIIPRLVSALFQRIMNTEAPESFAVTVSMFEVYGDNVYDLLRPDKVKLNVHGDEKNCTVVNLTAVPVIDLKGALKQLAVGCHYRTKAETAMNAMSSRSHAVFTVFVEKTATAECDSAFSAKLQLVDLAGSERLKKTEAEGNRMKEGININGGLLILSQVIAALATKQKHIPYRNSVITRVLQDSLGGNSFTVFLACISPADSNSQETLNTLRYADRAKQIKNKPIVNKNPKAEEIAILQAQLKRLQKENADLKQGIAPAEVRFNDANNSAEILSLKEEVVRKTEQLKERAMKQSECIIRMSALTQKNSRLEEDKAKLQSMLTDVRNTVLNEEMLDAAEVVRSIQQVVGDTEESTTLADDDNDETALGGQDDTIYDTERLPELQAELDDLEKQIAMKDENRQKALDEQRAFIEAMQQRESEKTQLVVRISELETEMNKLRQEGKKVTTAAKLAEERRQKLKDLERQHAEDKKVLNDMKKLQETRRRMEETLKKTEDELKNLKTQRLRLLREQRAEASKFQAFKQKHEREMAQMKSKLQKRENDVAIQKRMTDQKLTVLQMRLTEANRANKTLRELNLKRANRKSSPTNASALQNMIEEELEHEMCAQRSHWLCEDLRRQRHDLMQNINTVESMKFEGGKRRRISASADPNVSVVIEGEEEFEVKRQKELTFLRASLETLNEEIKDSLRNETIAGNEERANSRWEKVPAEMRPAFEAVYAQAVAHIRKEIELEFKLARTKSEFTAKIASKASHEEKRKKEDEEMRAKYRELAQCLEDAKSGLHEKIAFLLCLIKENRVDENAIQQFESLKNQFCDVEQKVKKASRRKTTNFMGGLTPKPELQRNERARRAVKYYGNVVNSEDVTMDDSRHQKRKDHSLLAVEMNRTTDDNVKRRVAMSPIKCDDDTRLTEEDEDIENEAMNNATFVKDSFNSATIVLDDSQPSPSNSTFVIGAAPTSEADGVPPIKRKSRRTDLGPL
| null | null |
cell division [GO:0051301]; meiotic chromosome condensation [GO:0010032]; meiotic spindle midzone assembly [GO:0051257]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]
|
chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; spindle [GO:0005819]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15452142}. Nucleus {ECO:0000269|PubMed:15452142}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15452142}. Chromosome {ECO:0000269|PubMed:15452142}. Note=Localizes to nuclei of the distal mitotic zone (PubMed:15452142). During mitotic prophase in embryos, localizes to the nucleoplasm (PubMed:15452142). In prometaphase, localizes to the body of the spindle and the periphery of chromosomes (PubMed:15452142). In anaphase, localizes to the spindle interzone (PubMed:15452142). Localizes to early meiotic prophase nuclei and to the nucleoplasm in late prophase (PubMed:15452142). Localizes to prophase chromosomes before fertilization (PubMed:15452142). During metaphase of meiosis I and meiosis II, localizes to the body of the spindle, around the periphery of chromosomes, and between homologous chromosomes (PubMed:15452142). {ECO:0000269|PubMed:15452142}.
| null | null | null | null | null |
FUNCTION: Required for chromosome movement and orientation on spindle poles in mitosis and meiosis (PubMed:15452142). May play a role in early anterior-posterior chromosome movement in mitotic embryos (PubMed:15452142). {ECO:0000269|PubMed:15452142}.
|
Caenorhabditis elegans
|
O45947
|
GLT10_CAEEL
|
MVAICIKIGERERKRVHIMLLAYTWKTRVSSHQCNKSPIFGLFAIQFSNICSNLLLLQQKLSMGLSRYLSRRHHWVIQYCGLLLFLYLIYSYVATSNDGPNLHEDIPVFQGQGKDRANPNPPAALGDEALDPFEKYRGHEKIKWEDEAAYEKEKRREGPGEWGKPVKLPEDKEVEKEALSLYKANGYNAYISDMISLNRSIKDIRHKECKNMMYSAKLPTVSVIFPFHEEHNSTLLRSVYSVINRSPPELLKEIILVDDFSEKPALRQPLEDFLKKNKIDHIVKVLRTKKREGLIRGRQLGAQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYRTVVCPFVDVIDCETYEVRPQDEGARGSFDWAFNYKRLPLTKKDRESPTKPFNSPVMAGGYFAISAKWFWELGGYDEGLDIWGGEQYELSFKVWQCHGRMVDAPCSRVAHIYRCKYAPFKNAGMGDFVSRNYKRVAEVWMDDYKETLYKHRPGVGNADAGDLKLMKGIREKLQCKSFDWFMKEIAFDQDKYYPAVEPKASAEGEIRNVGTNFCIDTQFKEQNQRFGLRKCTSDDKDGGGEQDLRLTRWHDIRPKGRKICFDCSTSVDKAPVILFDCHSMKGNQLFKYRVAQKQIYHPISGQCLTADENGKGFLHMKKCDSSSDLQKWAWQTVDNELLETRQANEAKEQE
|
2.4.1.41
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
protein O-linked glycosylation [GO:0006493]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;PF00652;
|
2.80.10.50;
|
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}.
|
Caenorhabditis elegans
|
O45952
|
CSC1_CAEEL
|
MPPRKIKKDPAVVAMADTLETRVKDLLEEYKKKLREVALQTAKAESDRIIATIKPKYRDMPIMEFLASPPDDFYIESGEEEEEGEAAVAVKQELPSEPDMEIDDAAAAQKTSIPIGQNSGRNTVQVKQEPEIDDDAAHETSIPIAPSGQNSGRNTAADEHRRNEIITPAGQVLPLPTLQPEKPFRAPHVDEEIAFSVNGSPLVLAGRTTATAAGKENRKKSKKSGAASKKAAAAAGPLQPETENAGTSV
| null | null |
meiotic chromosome segregation [GO:0045132]; mitotic cell cycle [GO:0000278]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic cleavage furrow ingression [GO:1990386]; mitotic cytokinesis [GO:0000281]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic spindle midzone assembly [GO:0051256]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic sister chromatid separation [GO:1901970]
|
chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; meiotic spindle midzone [GO:1990385]; microtubule cytoskeleton [GO:0015630]; mitotic spindle midzone [GO:1990023]
| null | null | null |
Borealin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12707312}. Chromosome, centromere {ECO:0000269|PubMed:12707312}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12707312}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the central spindle from anaphase through cytokinesis.
| null | null | null | null | null |
FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis during mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation. In the complex, it may be required to direct the Aurora B/air-2 to centromeric DNA. {ECO:0000269|PubMed:12707312}.
|
Caenorhabditis elegans
|
O45962
|
RLE1_CAEEL
|
MAPTGQGGQWQEVLCCSICNRHFNETFLPVSLICGHVICRKCAEKPENQTKPCPHDDWKTTHSPSEYPNNVALLSVIFPRKQCMTLSGAVSEAEKRVDQLSIQIAKFFREADSERGGTVSSREISRTLQRKVLALLCYQWREVDGRLKTLKMCRGISERVMIEIILSIQSNTHVSSQLWSAVRARGCQFLGPAMQDDVLRLILMTLETGECIARKNLVMYVVQTLASDYPQVSKTCVGHVVQLLYRASCFNVLKRDGESSLMQLKEEFRTYESLRREHDSQIVQIAFESGLRIGPDQWSALLYADQSHRSHMQSIIDKLQSKNSYQQGVEELRALAGSQTSMLVPAYRYFLTQVIPCLEFFAGIEHEDTSMRMIGDALHQIRILLKLHCSQDDLRKMPKEERRGVILQAEVPGGMGGGPGGSGGAEAGRIGGLHPLYSQIDETGRSISRTNPKDNSHNSPQTPPKQPRQKRYQMGIPPNRMGYSSDAPPFIPSHQQQPPPQFFNSQHLPQRFRGGRQRGAPPPPPPQPMPMLIGYDMPGAPMMQATEVLTADGQMVNGTPQRVVIMQSPTHLPGGPVVMIPQQQMVPPPQSMTPVGGPMGPMGPMTPSIPVQVPPNTMWTATSPTGSVIYPAASPPGQPPHTIWIQSTDGNMFPMFDRGSGGMVWGPGTMLRESGADAEQLLAKRYEILKRLQPSEDDDDPEDGGIGHVSYTVASSVLDDRMDHHPLTMIPVPTIDLPAIPISFANMPTEETMTMIGEMVQNRPRAPSLTAPSSNQPMNVNASASATVQAECGTMSVMDSICQPISTSAIHNSATIPQPVIPMVQVPVQVPIVPAENFNPNVPPPPPPPQGQPMLVDSAIGLLTPIRPILVAHPQNVVSNSLDKIVDVKERISEAQGNASEAENAHLRMELRMAESQMAHLDPYTKNNCLLRALQQVDMELQQLHLNPTVEG
|
2.3.2.27
| null |
determination of adult lifespan [GO:0008340]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; response to heat [GO:0009408]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasmic stress granule [GO:0010494]
|
double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF18386;PF21206;
|
1.20.120.1790;3.30.40.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000303|PubMed:17276341, ECO:0000303|PubMed:24448648};
| null |
PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway. {ECO:0000269|PubMed:17276341}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase. Regulates the activity of daf-16 and is thereby involved in regulating aging and stress resistance (PubMed:17276341). Regulates nsy-1 activity and thereby attenuates the activation of sek-1 and pmk-1, two components of the p38 pathway, which results in susceptibility to pathogenic bacterial infection (PubMed:24448648). {ECO:0000269|PubMed:17276341, ECO:0000269|PubMed:24448648}.
|
Caenorhabditis elegans
|
O46036
|
CTBP_DROME
|
MDKNLMMPKRSRIDVKGNFANGPLQARPLVALLDGRDCSIEMPILKDVATVAFCDAQSTSEIHEKVLNEAVGALMWHTIILTKEDLEKFKALRIIVRIGSGTDNIDVKAAGELGIAVCNVPGYGVEEVADTTMCLILNLYRRTYWLANMVREGKKFTGPEQVREAAHGCARIRGDTLGLVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIDKSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHLINEFTIKQMRPGAFLVNTARGGLVDDETLALALKQGRIRAAALDVHENEPYNVFQGALKDAPNLICTPHAAFFSDASATELREMAATEIRRAIVGNIPDVLRNCVNKEYFMRTPPAAAAGGVAAAVYPEGALHHRAHSTTPHDGPHSTTNLGSTVGGGPTTVAQAAAAAVAAAAAAALLPSPVPSHLSPQVGGLPLGIVSSQSPLSAPDPNNHLSSSIKTEVKAESTEAP
| null | null |
chaeta development [GO:0022416]; chromatin remodeling [GO:0006338]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sensory organ precursor cell fate determination [GO:0016360]; wing disc development [GO:0035220]
|
ISWI-type complex [GO:0031010]; nucleus [GO:0005634]
|
DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713]; transcription coregulator binding [GO:0001221]; transcription corepressor activity [GO:0003714]
|
PF00389;PF02826;
|
3.40.50.720;
|
D-isomer specific 2-hydroxyacid dehydrogenase family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Corepressor targeting diverse transcription regulators. Hairy-interacting protein required for embryonic segmentation and hairy-mediated transcriptional repression. {ECO:0000269|PubMed:9524128, ECO:0000269|PubMed:9525852}.
|
Drosophila melanogaster (Fruit fly)
|
O46043
|
PARG_DROME
|
MSKSPDGGISEIETEEEPENLANSLDDSWRGVSMEAIHRNRQPFELENLPPVTAGNLHRVMYQLPIRETPPRPYKSPGKWDSEHVRLPCAPESKYPRENPDGSTTIDFRWEMIERALLQPIKTCEELQAAIISYNTTYRDQWHFRALHQLLDEELDESETRVFFEDLLPRIIRLALRLPDLIQSPVPLLKHHKNASLSLSQQQISCLLANAFLCTFPRRNTLKRKSEYSTFPDINFNRLYQSTGPAVLEKLKCIMHYFRRVCPTERDASNVPTGVVTFVRRSGLPEHLIDWSQSAAPLGDVPLHVDAEGTIEDEGIGLLQVDFANKYLGGGVLGHGCVQEEIRFVICPELLVGKLFTECLRPFEALVMLGAERYSNYTGYAGSFEWSGNFEDSTPRDSSGRRQTAIVAIDALHFAQSHHQYREDLMERELNKAYIGFVHWMVTPPPGVATGNWGCGAFGGDSYLKALLQLMVCAQLGRPLAYYTFGNVEFRDDFHEMWLLFRNDGTTVQQLWSILRSYSRLIKEKSSKEPRENKASKKKLYDFIKEELKKVRDVPGEGASAEAGSSRVAGLGEGKSETSAKSSPELNKQPARPQITITQQSTDLLPAQLSQDNSNSSEDQALLMLSDDEEANAMMEAASLEAKSSVEISNSSTTSKTSSTATKSMGSGGRQLSLLEMLDTHYEKGSASKRPRKSPNCSKAEGSAKSRKEIDVTDKDEKDDIVD
|
3.2.1.143
| null |
ATP generation from poly-ADP-D-ribose [GO:1990966]; Cajal body organization [GO:0030576]; carbohydrate metabolic process [GO:0005975]; DNA damage response [GO:0006974]; female germ-line stem cell population maintenance [GO:0036099]; heterochromatin formation [GO:0031507]; maintenance of protein location in nucleus [GO:0051457]; nucleotide-sugar metabolic process [GO:0009225]; regulation of DNA repair [GO:0006282]; regulation of RNA splicing [GO:0043484]; response to heat [GO:0009408]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]
|
ADP-ribosylserine hydrolase activity [GO:0140292]; poly(ADP-ribose) glycohydrolase activity [GO:0004649]
|
PF05028;PF20811;
| null |
Poly(ADP-ribose) glycohydrolase family
| null | null |
CATALYTIC ACTIVITY: Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143; Evidence={ECO:0000250|UniProtKB:Q867X0};
| null | null | null | null |
FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism is required for maintenance of the normal function of neuronal cells. {ECO:0000269|PubMed:14676324}.
|
Drosophila melanogaster (Fruit fly)
|
O46084
|
PGAM5_DROME
|
MRKLTSFVCGTGAGLAAYYLQRLRDPQTVVQNSWTHSDKPVDPWALWDTNWDCREPRALVRPLRNSQPEEENRYNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKEKVVNCAFLREGAPIPPQPPVGHWKPEASQFLRDGSRIEAGFRRYFHRAYPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPAELLTNRIPRDVKNVV
|
3.1.3.16
| null |
peptidyl-threonine dephosphorylation [GO:0035970]; positive regulation of mitochondrial fission [GO:0090141]; protein dephosphorylation [GO:0006470]; regulation of mitochondrion organization [GO:0010821]; response to anesthetic [GO:0072347]; response to heat [GO:0009408]
|
membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
kinase binding [GO:0019900]; myosin phosphatase activity [GO:0017018]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00300;
|
3.40.50.1240;
|
Phosphoglycerate mutase family, BPG-dependent PGAM subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:19590015}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:19590015};
| null | null | null | null |
FUNCTION: Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity. {ECO:0000269|PubMed:19590015}.
|
Drosophila melanogaster (Fruit fly)
|
O46102
|
PAPD1_DROME
|
MNSLVRRSAQQLSLWRTYCIKHNASEAASPGRNAGRPNYEEFIGRHQRQAQCSIVVQVSSEKSYEELYNYCSSFGSIMGAHHYCVRQDETLHYILLEYATSDEAAAAIGAGVTNGELSGVPVRSPFLWFRAAGGGRRSPKLVANTAPALLSLDGTRQVDQRHLLGLLRGAADIEEQVQQLYEHTRLNELGIRMRFLAALQVQQAIAGMFPAAQAQPFGSSVNGFGRMGCDLDLILRFDSDMGAKIPLEAAVPSRLVYHTKENLSNGRSQTQRHMECFGDMLHLFLPGVCHVRRILQARVPIIKYHHEHLDLEVDLSMSNLTGFYMSELLYMFGEMDPRVRPLTFTIRRWAQTCGLTNPSPGRWISNFSLTCLVMFFLQQLRQPILPTIGALAKAAEPGDSRVTEDGINCTFTRNVDRLGFRSRNQSSLSELLLQFFEFYSQFDFHNRAISLNEGKPLSKPDHSAMYIVNPLEQLLNVSKNVSLEECERLRIEVRNAAWVLESEVENASVPEGDGQELSCGLLNLFKHPEKAVIRPNMFFKPRMVEVSDLFEQKEAGATSSSTPPTPAITYKSASVRQQVQSIKAATRSELKQLRGSGSSVPTSSPNNRRRSR
|
2.7.7.19
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4};
|
mitochondrial mRNA 3'-end processing [GO:0090616]; mitochondrial mRNA polyadenylation [GO:0097222]; mRNA polyadenylation [GO:0006378]; tRNA stabilization [GO:0036416]
|
mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]
|
PF03828;
|
1.10.1410.10;3.30.460.10;
|
DNA polymerase type-B-like family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27176048}.
|
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000250|UniProtKB:Q9NVV4};
| null | null | null | null |
FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. This is not required for transcript stability or translation but may maintain mRNA integrity by protecting 3' termini from degradation. {ECO:0000269|PubMed:27176048}.
|
Drosophila melanogaster (Fruit fly)
|
O46106
|
NOI_DROME
|
METLLEQQRRLHEERERLVKLMVDEHATKKPGEKERIHSEHRLKYLMELHHNSTSQLRDLYEDKDNERKAEIAALSGPNEFNEFYARLKQIKQFYKSHPAEVSVPLSVEFDEMIRVYNNPDDMSALVEFTDEEGGGRYLDLNECYELYLNLRSVEKLDYITYLMSFDHVFDIPRERKNREYRIYIETLNDYLHHFILRIQPLLDLEGELLKVELDFQRQWLMGTFPGFSIKETESALANTGAHLDLSAFSSWEELASLGLDRLKSALVALGLKCGGTLEERAQRLFSTKGKSTLDPALMAKKPSAKTASAQSREHERHKEIAQLEALLYKYADLLSEQRAATKENVQRKQARTGGERDDSDVEASESDNEDDPDADDVPYNPKNLPLGWDGKPIPYWLYKLHGLNISYNCEICGNFTYKGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAITLWEKLKSQKQSERWVADQEEEFEDSLGNVVNRKTFEDLKRQGLL
| null | null |
fertilization [GO:0009566]; mitotic cell cycle [GO:0000278]; mRNA splicing, via spliceosome [GO:0000398]
|
catalytic step 2 spliceosome [GO:0071013]; precatalytic spliceosome [GO:0071011]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]
|
RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
|
PF13297;PF16837;PF12108;PF11931;
| null |
SF3A3 family
| null |
SUBCELLULAR LOCATION: Nucleus. Note=Excluded from the nucleoli.
| null | null | null | null | null |
FUNCTION: Probable subunit of a splicing factor complex required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA (By similarity). Involved in male fertility. {ECO:0000250}.
|
Drosophila melanogaster (Fruit fly)
|
O46166
|
TXI1_ERAAG
|
MKLQLMICLVLLPCFFCEPDEICRARMTHKEFNYKSNVCNGCGDQVAACEAECFRNDVYTACHEAQKG
| null | null | null |
extracellular region [GO:0005576]
|
toxin activity [GO:0090729]
| null |
1.10.2010.20;
|
Helical arthropod-neuropeptide-derived (HAND) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9589602}.
| null | null | null | null | null |
FUNCTION: Toxin that paralyzes insects. May have a direct effect on the insect central nervous system. {ECO:0000269|PubMed:9589602}.
|
Eratigena agrestis (Hobo spider) (Tegenaria agrestis)
|
O46339
|
HTH_DROME
|
MAQPRYDDGLHGYGMDSGAAAAAMYDPHAGHRPPGLQGLPSHHSPHMTHAAAAAATVGMHGYHSGAGGHGTPSHVSPVGNHLMGAIPEVHKRDKDAIYEHPLFPLLALIFEKCELATCTPREPGVQGGDVCSSESFNEDIAMFSKQIRSQKPYYTADPEVDSLMVQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDTTKPPELGSANGEGRSNADSTSHTDGASTPDVRPPSSSLSYGGAMNDDARSPGAGSTPGPLSQQPPALDTSDPDGKFLSSLNPSELTYDGRWCRREWSSPADARNADASRRLYSSVFLGSPDNFGTSASGDASNASIGSGEGTGEEDDDASGKKNQKKRGIFPKVATNILRAWLFQHLTHPYPSEDQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVYTPHPGPSGYGHDAMGYMMDSQAHMMHRPPGDPGFHQGYPHYPPAEYYGQHL
| null | null |
animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; compound eye development [GO:0048749]; compound eye photoreceptor fate commitment [GO:0001752]; embryonic pattern specification [GO:0009880]; eye development [GO:0001654]; haltere morphogenesis [GO:0048735]; head morphogenesis [GO:0060323]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing morphogenesis [GO:0007476]; Malpighian tubule development [GO:0072002]; oenocyte differentiation [GO:0001742]; peripheral nervous system development [GO:0007422]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell proliferation involved in compound eye morphogenesis [GO:2000497]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to nucleus [GO:0034504]; proximal/distal pattern formation [GO:0009954]; regulation of cell fate specification [GO:0042659]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357]; salivary gland boundary specification [GO:0007432]; segmentation [GO:0035282]; somatic muscle development [GO:0007525]; specification of animal organ identity [GO:0010092]; specification of segmental identity, antennal segment [GO:0007383]; specification of segmental identity, head [GO:0007380]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator binding [GO:0001223]; transcription factor binding [GO:0008134]
|
PF05920;PF16493;
|
1.10.10.60;
|
TALE/MEIS homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936, ECO:0000269|PubMed:9463350}.
| null | null | null | null | null |
FUNCTION: All isoforms are required for patterning of the embryonic cuticle. Acts with exd to delimit the eye field and prevent inappropriate eye development. Isoforms that carry the homeodomain are required for proper localization of chordotonal organs within the peripheral nervous system and antennal identity; required to activate antennal-specific genes, such as sal and to repress the leg-like expression of dac. Necessary for the nuclear localization of the essential HOX cofactor, extradenticle (exd). Both necessary and sufficient for inner photoreceptors to adopt the polarization-sensitive 'dorsal rim area' (DRA) of the eye fate instead of the color-sensitive default state. This occurs by increasing rhabdomere size and uncoupling R7-R8 communication to allow both cells to express the same opsin rather than different ones as required for color vision. {ECO:0000269|PubMed:14636555, ECO:0000269|PubMed:16778079, ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936, ECO:0000269|PubMed:9463350}.
|
Drosophila melanogaster (Fruit fly)
|
O46373
|
ADT1_RABIT
|
MSDQALSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFSGLGNCLTKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWKKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV
| null | null |
adaptive thermogenesis [GO:1990845]; ADP transport [GO:0015866]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; positive regulation of mitophagy [GO:1901526]; regulation of mitochondrial membrane permeability [GO:0046902]
|
membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial permeability transition pore complex [GO:0005757]
|
ATP:ADP antiporter activity [GO:0005471]; oxidative phosphorylation uncoupler activity [GO:0017077]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
|
PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers. {ECO:0000250|UniProtKB:P48962}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P12235}; Multi-pass membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP, ARL2 and SLC25A4/ANT1 is expressed in mitochondria (By similarity). May localize to non-mitochondrial membranes (By similarity). {ECO:0000250|UniProtKB:P12235, ECO:0000250|UniProtKB:P48962}.
|
CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48962}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P48962};
| null | null | null | null |
FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity. Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it. Probably mediates mitochondrial uncoupling in tissues that do not express UCP1. Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death. It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962}.
|
Oryctolagus cuniculus (Rabbit)
|
O46374
|
TOP2A_PIG
|
MEVSPLQPVNENMQVNKTKKNEEAKKRLSIERIYQKKTQLEHILLRPDTYIGSVESVTQQMWVYDEDIGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDEEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFHPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDLYLKDKVDETGNPLKIIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVAKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQVKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTHFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRLLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPIRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKEADKSDSVADSGPTFNYLLDMPLWYLTKEKKDELCKLRNEKEQELETLKRKSPSDLWKEDLAAFIEELEAVEAKEKQDEQIGLPGKGGKAKGKKTQMAEVLPSPCGKRVIPRVTVEMKAEAEKKIKKKIKSENTEGSPQEDGMEVEGLKQRLEKKQKREPGTKTKKQTTLPFKPIKKAKKRNPWSDSESDISSDESNFNVPPREKEPRRAAAKTKFTVDLDSDEDFSDADEKTRDEDFVPSDTSPQKAETSPKHTNKEPKPQKSTPSVSDFDADDAKDNVPPSPSSPVADFPAVTETIKPVSKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGAKKDPDLDSDVSKKPNPPKPKGRRKRKPSTSDDSDSNFEKMISKAVTSKKPKGESDDFHLDLDLAVASRAKSGRTKKPIKYLEESDEDDLF
|
5.6.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-ProRule:PRU00995};
|
apoptotic chromosome condensation [GO:0030263]; DNA topological change [GO:0006265]; negative regulation of DNA duplex unwinding [GO:1905463]; regulation of circadian rhythm [GO:0042752]; resolution of meiotic recombination intermediates [GO:0000712]; rhythmic process [GO:0048511]; sister chromatid segregation [GO:0000819]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
ATP binding [GO:0005524]; DNA binding, bending [GO:0008301]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; magnesium ion binding [GO:0000287]
|
PF00204;PF00521;PF08070;PF02518;PF01751;PF16898;
|
3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10;
|
Type II topoisomerase family
|
PTM: Phosphorylation has no effect on catalytic activity (By similarity). However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation (By similarity). {ECO:0000250|UniProtKB:P11388}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
|
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
| null | null | null | null |
FUNCTION: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (By similarity). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320}.
|
Sus scrofa (Pig)
|
O46382
|
BIG1_BOVIN
|
MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHIPQEHEGDLDPQTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGENHDCEEKPQDIVQSIVEEMVNIVVGDTGERTTINVSADGNNGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFGTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQETSEMKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFTKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPAKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGAKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGYTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPISGETAPPTPSPVSENQLDTISQKSVDIHDSIQPRSADNRQQAPLASVSTVNEEISKIKPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSRKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRASAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ
| null | null |
endomembrane system organization [GO:0010256]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; positive regulation of wound healing [GO:0090303]; protein glycosylation [GO:0006486]; protein transport [GO:0015031]; regulation of ARF protein signal transduction [GO:0032012]; regulation of establishment of cell polarity [GO:2000114]
|
cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase A regulatory subunit binding [GO:0034237]
|
PF20252;PF16213;PF01369;PF09324;PF12783;
|
1.10.220.20;1.10.1000.11;
| null |
PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O46385
|
SVIL_BOVIN
|
MKRKERIARRLEGIETDTQPILLQSCTGLVTHRLLEEDTPRYMRATDPASPHIGRSNEEEETSDSSLEKQTRSKQCTETSGIHADSPYSSGIMDTQSLESKAERIARYKAERRRQLAEKYGLTLDPEADSETPSRYSRSRKDPEAAEKRGVRSERSAESSRDAGSSYSRTELSGLRTCVAESKDYGLHRSDGVSDTEVLLNAENQRRGQEPSATGLARDLPLAGEVSSSFSFSGRDSALGEVPRSPKAVHSLPSPSPGQPASPSHSTSDLPLPAEARASIGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVREESARSSPELTSESLTQRRHQTAPGHYLAFQSENSAFDRVSGKVASSARQPIRGYVQPAEPVHTITLVTSDTPESISEGSWVGPAPQTVTKPPPSKVLEGERRDTPVLHICESKAEDVLFSDALEKTRKTLAVLEDRGSGRSQEAPSGTEDLSQPAVGIVTAEPQKESESLAHPPMAQQQPTERMGRSEMVMYVQSEAVSQGHRKEVPTRKHRVLTRSLSDYTGPPQLQALKAKAPAPKRDAESQTSKAELELGLLDTKVSVAQLRNAFLESARASRKPELHSRVEGSSEGPGVERERGSRKPRRYFSPGENRKTSERFRTQPITSAERKESDRSTSNSEMPAAEDEEKVDERARLSVAAKRLLFREMEKSFDEKSVPKRRSRNAAVEQRLRRLQDRSHTQPVTTEEVVIAAEPTPASCSVATHPVMTRHPSPTVAKSPVQPARTLQASAHQKALARDQTNESKDSAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRLDMRQRRMNARYQTQPVTLGEVEQVQSGKLMAFSPTINTSVSTVASTVPPMYAGNLRTKPLPDDSFGATEQKFASSLENSDSPVRSILKSQGWQPSVEGAGSKAMLREFEETERKGGLTGGDGGVTKYGSFEEAELSYPVLSRVREGDNHKEAIYALPRKGSLELAHPPIAQLGDDLKEFSTPKSTMQASPDWKERQLFEEKVDLENVTKRKFSLKAAEFGEPTSEQTGAAAGKPAAPTATPVSWKPQDPSEQPQEKRYQSPCAMFAAGEIKAPAVEGSLDSPSKTMSIKERLALLKKSGEEDWRNRLNRKQEYGKASITSSLHIQETEQSLKKKRVTESRESQMTIEERKHLITVREDAWKTRGKGAANDSTQFTVAGRMVKRGLASPTAITPVASPVSSKARGTTPVSRPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMQETVLTVTGKSVKEVMKPDDDETFAKFYRSVDSSLPRSPVELDEDFDVIFDPYAPRLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFVESKRMKVEKLSANSSFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKKLMLLQVKGRRHVQTRLVEPRAPSLNSGDCFLLLSPHHCFLWVGEFANVIEKAKASELASLIQTKRELGCRATYIQTVEEGINTHTHAAKDFWKLLGGQASYQSAGDPKEDELYETAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRPNEKNASELAQHKDDARAEVKPYDVTRMVPVPQTTAGTVLDGVNVGRGYGLVEGDDRRQFEIASISVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFIVSTAVGSRQKGEHSVRVAGKEKCVYFFWQGRQSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENTQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVHKALIYLWHGCKAQAHTKEVGRTAANKIKDQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGNFNFTPRLFILSSSSGDFSATEFMYPARDPSVVNSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCRGKNLKKPPPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF
| null | null |
actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; positive regulation of cytokinesis [GO:0032467]
|
actin cytoskeleton [GO:0015629]; anchoring junction [GO:0070161]; cell projection [GO:0042995]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; microtubule minus-end [GO:0036449]; midbody [GO:0030496]; podosome [GO:0002102]
|
actin filament binding [GO:0051015]; molecular adaptor activity [GO:0060090]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, invadopodium {ECO:0000250|UniProtKB:O95425}. Cell projection, podosome {ECO:0000250|UniProtKB:O95425}. Midbody {ECO:0000269|PubMed:20309963}. Cleavage furrow {ECO:0000269|PubMed:20309963}. Note=Tightly associated with both actin filaments and plasma membranes.
| null | null | null | null | null |
FUNCTION: [Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (By similarity). {ECO:0000250|UniProtKB:O95425}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6 (PubMed:16880273, PubMed:17925381). Plays a role in cytokinesis through KIF14 interaction (PubMed:20309963). {ECO:0000269|PubMed:16880273, ECO:0000269|PubMed:17925381, ECO:0000269|PubMed:20309963}.
|
Bos taurus (Bovine)
|
O46392
|
CO1A2_CANLF
|
MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPTGDRGPRGERGPPGPPGRDGDDGIPGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGASGAPGPQGFQGPAGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGNPGPAGPAGPRGEVGLPGVSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGIVGEPGPAGSKGESGNKGEPGSAGAQGPPGPSGEEGKRGPNGEAGSAGPSGPPGLRGSPGSRGLPGADGPAGVMGPPGPRGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGAPGNVGPAGKEGPMGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPAGTAGEVGKPGERGLPGEFGLPGPAGPRGERGPPGESGAAGPSGPIGSRGPSGPPGPDGNKGEPGVLGAPGTAGASGPGGLPGERGAAGIPGGKGEKGETGLRGEIGNPGRDGARGAPGAMGAPGPAGATGDRGEAGPAGPAGPAGPRGTPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPIGSAGPSGPNGPPGPAGSRGDGGPPGATGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGLRGPRGDQGPVGRTGETGASGPPGFTGEKGPSGEPGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGSVGEPGPLGIAGPPGARGPPGAVGAPGVNGAPGEAGRDGNPGNDGPPGRDGQAGHKGERGYPGNIGPVGAVGAPGPHGPVGPTGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGLAGQHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGQPGTVGPAGIRGSQGSQGPAGPPGPPGPPGPPGPSGGGYDFGYEGDFYRADQPRSPPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRNSKVKKHIWLGETINGGTQFEYNVEGVTTKEMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWRKTIIEYKTNKPSRLPILDIAPLDIGDADQEFRVDVGPVCFK
| null | null |
extracellular matrix organization [GO:0030198]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O46409
|
APOA4_PIG
|
MFLKAVVLSLALVAVTGARAEVNADQVATVMWDYFSQLGSNAKKAVEHLQKSELTQQLNTLFQDKLGEVNTYTEDLQKKLVPFATELHERLTKDSEKLKEEIRRELEELRARLLPHATEVSQKIGDNVRELQQRLGPFTGGLRTQVNTQVQQLQRQLKPYAERMESVLRQNIRNLEASVAPYADEFKAKIDQNVEELKGSLTPYAEELKAKIDQNVEELRRSLAPYAQDVQEKLNHQLEGLAFQMKKQAEELKAKISANADELRQKLVPVAENVHGHLKGNTEGLQKSLLELRSHLDQQVEEFRLKVEPYGETFNKALVQQVEDLRQKLGPLAGDVEGHLSFLEKDLRDKVNTFFSTLKEEASQGQSQALPAQEKAQAPLEG
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of triglyceride catabolic process [GO:0010898]; regulation of intestinal cholesterol absorption [GO:0030300]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361]
|
cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
|
Sus scrofa (Pig)
|
O46411
|
5NTC_BOVIN
|
MTTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE
|
2.7.1.77; 3.1.3.5; 3.1.3.99
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8031149}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49902};
|
adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; dGMP metabolic process [GO:0046054]; GMP metabolic process [GO:0046037]; IMP catabolic process [GO:0006204]; IMP metabolic process [GO:0046040]; negative regulation of defense response to virus by host [GO:0050689]; protein K48-linked ubiquitination [GO:0070936]
|
cytosol [GO:0005829]
|
5'-nucleotidase activity [GO:0008253]; ATP binding [GO:0005524]; GMP 5'-nucleotidase activity [GO:0050484]; identical protein binding [GO:0042802]; IMP 5'-nucleotidase activity [GO:0050483]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; ubiquitin protein ligase activity [GO:0061630]; XMP 5'-nucleosidase activity [GO:0106411]
|
PF05761;
|
3.40.50.1000;
|
5'(3')-deoxyribonucleotidase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; Evidence={ECO:0000305|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside; Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274, ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719; Evidence={ECO:0000305|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714, ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; CATALYTIC ACTIVITY: Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate; Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; CATALYTIC ACTIVITY: Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; CATALYTIC ACTIVITY: Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530, ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57464; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531; Evidence={ECO:0000250|UniProtKB:D3ZMY7}; CATALYTIC ACTIVITY: Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584, ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP; Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596, ChEBI:CHEBI:57673, ChEBI:CHEBI:58053; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572, ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053, ChEBI:CHEBI:61194; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588, ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865, ChEBI:CHEBI:58053; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592, ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:60377; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}; CATALYTIC ACTIVITY: Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for IMP (in absence of allosteric activator) {ECO:0000269|PubMed:8031149}; KM=0.09 mM for IMP (in the presence of 4.5 mM ATP) {ECO:0000269|PubMed:8031149}; Vmax=12.5 umol/min/mg enzyme for the hydrolysis of IMP (in the presence of 4.5 mM ATP) {ECO:0000269|PubMed:8031149}; Vmax=1.48 umol/min/mg enzyme for the hydrolysis of IMP (in absence of the allosteric activator ATP) {ECO:0000269|PubMed:8031149};
| null | null | null |
FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates (PubMed:8031149, PubMed:9371705). In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (PubMed:8031149, PubMed:9371705). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP (PubMed:8031149, PubMed:9371705). Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (PubMed:8031149, PubMed:9371705). Through these activities regulates the purine nucleoside/nucleotide pools within the cell (PubMed:8031149, PubMed:9371705). {ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705}.
|
Bos taurus (Bovine)
|
O46419
|
LIPT_BOVIN
|
MLIPFSMKNCFQLLCNLKVPAAGFKNTVKSGLILQSISNDVYHNLAVEDWIHDHMNLEGKPVLFLWRNSPTVVIGRHQNPWQECNLNLMREEGVKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLVVRALKAVHPHLDVQATKRFDLLLDGQFKISGTASKIGRNAAYHHCTLLCGTDGTFLSSLLKSPYQGIRSNATASTPALVKNLMEKDPTLTCEVVINAVATEYATSHQIDNHIHLINPTDETVFPGINSKAIELQTWEWIYGKTPKFSVDTSFTVLHEQSHVEIKVFIDVKNGRIEVCNIEAPDHWLPLEICDQLNSSLIGSKFSPIETTVLTSILHRTYPGDDELHSKWNILCEKIKGIM
|
2.3.1.-; 2.3.1.200
| null |
protein modification process [GO:0036211]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
lipoate-protein ligase activity [GO:0016979]; lipoyltransferase activity [GO:0017118]
| null |
3.30.390.50;
|
LplA family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:8206978}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H protein] + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein]; Xref=Rhea:RHEA:16413, Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501, Rhea:RHEA-COMP:10502, ChEBI:CHEBI:29969, ChEBI:CHEBI:83099; EC=2.3.1.200; Evidence={ECO:0000250|UniProtKB:Q9Y234}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16414; Evidence={ECO:0000250|UniProtKB:Q9Y234}; CATALYTIC ACTIVITY: Reaction=(R)-lipoyl-5'-AMP + L-lysyl-[lipoyl-carrier protein] = AMP + 2 H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein]; Xref=Rhea:RHEA:20473, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:83091, ChEBI:CHEBI:83099, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:17570395, ECO:0000269|PubMed:8206978};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for (R)-lipoyl-5'-AMP {ECO:0000269|PubMed:8206978}; Vmax=135 nmol/min/mg enzyme for the reaction with (R)-lipoyl-5'-AMP as lipoyl donor {ECO:0000269|PubMed:8206978};
|
PATHWAY: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:8206978};
| null |
FUNCTION: Lipoyl amidotransferase that catalyzes the transfer of lipoyl moieties from lipoyl-protein H of the glycine cleavage system (lipoyl-GCSH) to E2 subunits of the pyruvate dehydrogenase complex (PDCE2). Unable to catalyze the transfer of octanoyl from octanoyl-GCSH to PDCE2 (By similarity). In vitro, it is also able to catalyze the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes but this reaction may not be physiologically relevant (Probable) (PubMed:8206978). {ECO:0000250|UniProtKB:Q9Y234, ECO:0000269|PubMed:17570395, ECO:0000269|PubMed:8206978, ECO:0000305}.
|
Bos taurus (Bovine)
|
O46420
|
CP51A_PIG
|
MVLLGLLQAGGSVLGQAMEQVTGVNLLSSLLLACAFTLILVYLFRQAIGHLAPLPAGAKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFRQHVSIIEKETKEYFQSWGESGERNLFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKNIFYKAIQKRRQSEEKIDDILQTLLDSTYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQEKCYLEQKTVCGEDLPPLTYDQLKDLNLLDRCIKETLRLRPPIMTMMRMAKTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK
|
1.14.14.154
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q16850};
|
bile acid biosynthetic process [GO:0006699]; cholesterol biosynthetic process [GO:0006695]; cholesterol homeostasis [GO:0042632]; sterol metabolic process [GO:0016125]
|
endoplasmic reticulum membrane [GO:0005789]
|
heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=24,25-dihydrolanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:45960, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45961; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxy-24,25-dihydrolanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75079, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87057; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75080; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=32-hydroxy-24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxo-24,25-dihydrolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75087, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87057, ChEBI:CHEBI:87060; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75088; Evidence={ECO:0000250|UniProtKB:Q64654}; CATALYTIC ACTIVITY: Reaction=32-oxo-24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75083, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904, ChEBI:CHEBI:87060; Evidence={ECO:0000250|UniProtKB:Q64654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75084; Evidence={ECO:0000250|UniProtKB:Q64654};
| null |
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. {ECO:0000250|UniProtKB:Q64654}.
| null | null |
FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the cholesterol biosynthesis pathway, being cholesterol the major sterol component in mammalian membranes as well as a precursor for bile acid and steroid hormone synthesis. Cytochrome P450 monooxygenase that catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of sterols such as lanosterol (lanosta-8,24-dien-3beta-ol) and 24,25-dihydrolanosterol (DHL) in the form of formate, and converts the sterols to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol and 4,4-dimethyl-8,14-cholestadien-3beta-ol, respectively, which are intermediates of cholesterol biosynthesis. Can also demethylate substrates not intrinsic to mammals, such as eburicol (24-methylene-24,25-dihydrolanosterol), but at a lower rate than DHL. {ECO:0000250|UniProtKB:Q64654}.
|
Sus scrofa (Pig)
|
O46421
|
EST1_MACFA
|
MWLRALVLATLAAFTAWGHPSSPPVVDTVHGKVLGKFVSLEGFTQPVAVFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCSQDAVAGQVLSELFTNRKENTPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLVVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQLAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTAVLVKKGDVKPLAEQIAIAAGCQTTTSAVMVHCLRQKTEEELLETTLKMKFFSLDLHGDPRESHPFLGTVIDGLLLPKTPEELQAERKFNTVPYMVGFNKQEFGWIIPMLMGYPLSEGKLDQKTAMSLLWKSYPLVYIAKELIPEATEKYLGGTDDPVKKKDRFLDLLADVMFSVPSVIVARHHRDAGVPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPRWPEYNQEEGYLQIGANTQAAQKLKDKEVAFWTTLFAKKAVEKPPQTEHIEL
|
3.1.1.1; 3.1.1.13
| null |
cholesterol metabolic process [GO:0008203]; lipid catabolic process [GO:0016042]; negative regulation of cholesterol storage [GO:0010887]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; regulation of bile acid biosynthetic process [GO:0070857]; regulation of bile acid secretion [GO:0120188]; reverse cholesterol transport [GO:0043691]
|
cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; lipid droplet [GO:0005811]
|
carboxylesterase activity [GO:0106435]; sterol esterase activity [GO:0004771]
|
PF00135;
|
3.40.50.1820;
|
Type-B carboxylesterase/lipase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P23141}. Cytoplasm {ECO:0000250|UniProtKB:P23141}. Lipid droplet {ECO:0000250|UniProtKB:P23141}. Note=Moves from cytoplasm to lipid droplets upon lipid loading. Associates with lipid droplets independently of triglycerides (TG) content of the droplets and hydrolyzes cholesteryl esters more efficiently from mixed droplets. {ECO:0000250|UniProtKB:P23141}.
|
CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P23141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:P23141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) + prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P23141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=a cholesterol ester + H2O = a fatty acid + cholesterol + H(+); Xref=Rhea:RHEA:36403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:28868; EC=3.1.1.13; Evidence={ECO:0000250|UniProtKB:P23141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404, ChEBI:CHEBI:90233; Evidence={ECO:0000250|UniProtKB:P23141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301; Evidence={ECO:0000250|UniProtKB:P23141};
| null | null | null | null |
FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins. Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process. First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile. {ECO:0000250|UniProtKB:P23141}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
O46427
|
CATH_PIG
|
MWAVLSLLCAGAWLLGPPACGASNLAVSSFEKLHFKSWMVQHQKKYSLEEYHHRLQVFVSNWRKINAHNAGNHTFKLGLNQFSDMSFDEIRHKYLWSEPQNCSATKGNYLRGTGPYPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVAIATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRYNKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMNDEEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKTPDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV
|
3.4.22.16
| null |
bradykinin catabolic process [GO:0010815]; dichotomous subdivision of terminal units involved in lung branching [GO:0060448]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; immune response-regulating signaling pathway [GO:0002764]; membrane protein proteolysis [GO:0033619]; metanephros development [GO:0001656]; negative regulation of apoptotic process [GO:0043066]; neuropeptide catabolic process [GO:0010813]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidase activity [GO:0010952]; protein destabilization [GO:0031648]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to retinoic acid [GO:0032526]; surfactant homeostasis [GO:0043129]; T cell mediated cytotoxicity [GO:0001913]; zymogen activation [GO:0031638]
|
alveolar lamellar body [GO:0097208]; cytosol [GO:0005829]; extracellular space [GO:0005615]; lysosome [GO:0005764]
|
aminopeptidase activity [GO:0004177]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; HLA-A specific activating MHC class I receptor activity [GO:0030108]; serine-type endopeptidase activity [GO:0004252]; thyroid hormone binding [GO:0070324]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
| null | null | null | null |
FUNCTION: Important for the overall degradation of proteins in lysosomes.
|
Sus scrofa (Pig)
|
O46432
|
MA2B1_FELCA
|
MGADARPLGVRAGGGGRGAARPGTSSRALPPPLPPLSFLLLLLAAPGARAAGYETCPMVHPDMLNVHLVAHTHDDVGWLKTVDQYFYGIHNDVQHAGVQYILDSVISSLLVEPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIIDQMTLGLRFLEDTFGKDGRPRVAWHIDPFGHSREQASLFAQMGFDGLFFGRLDYQDKRVREENLGLEQVWRASASLKPPAADLFTSVLPNIYNPPEKLCWDTLCADKPFVEDRRSPEYNAEELVNYFLQLATAQGQHFRTNHTIMTMGSDFQYENANMWFRNLDRLIQLVNAQQQANGSRVNVLYSTPACYLWELNKANLTWSVKQDDFFPYADGPHQFWSGYFSSRPALKRYERLSYNFLQVCNQLEALAGPAANVGPYGSGDSAPLNQAMAVLQHHDAVSGTSKQHVADDYARQLAAGWDPCEVLLSNALARLSGSKEDFTYCRNLNVSVCPLSQTAKNFQVTIYNPLGRKIDWMVRLPVSKHGFVVRDPNGTVVPSDVVILPSSDGQELLFPASVPALGFSIYSVSQVPGQRPHAHKPQPRSQRPWSRVLAIQNEHIRARFDPDTGLLVEMENLDQNLLLPVRQAFYWYNASVGNNLSTQVSGAYIFRPNQEKPLMVSHWAQTRLVKTPLVQEVHQNFSAWCSQVVRLYRGQRHLELEWTVGPIPVGDGWGKEIISRFDTVLETKGLFYTDSNGREILERRRDYRPTWKLNQTETVAGNYYPVNSRIYIRDGNMQLTVLTDRSQGGSSLRDGSMELMVHRRLLKDDGRGVGEALLEDGLGRWVRGRHLVLLDKVRTAATGHRLQAEKEVLTPQVVLAPGGGAPYHLKVAPRKQFSGLRRELPPSVHLLTLARWDQKTLLLRLEHQFAVGEDSGNLSSPVTLDLTDLFSAFTITYLQETTLVANQLRASASRLKWTPNTGPTPLPSPSRLDPATITLQPMEIRTFLASVQWEEHG
|
3.2.1.24
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]
|
Golgi membrane [GO:0000139]; lysosome [GO:0005764]
|
alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]
|
PF09261;PF07748;PF01074;PF21260;
|
2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180;
|
Glycosyl hydrolase 38 family
|
PTM: Processed into 3 peptides of 72 kDa, 41 kDa and 12 kDa.
|
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24;
| null | null | null | null |
FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. {ECO:0000250}.
|
Felis catus (Cat) (Felis silvestris catus)
|
O46480
|
NDEL1_RABIT
|
MDGEDIPDFSSLKEETAYWKELSLKYKQTFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVMNSNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPLSAPGMLPLSV
| null | null |
cell differentiation [GO:0030154]; cell migration [GO:0016477]; centrosome localization [GO:0051642]; chromosome segregation [GO:0007059]; establishment of chromosome localization [GO:0051303]; establishment of mitotic spindle orientation [GO:0000132]; lysosome localization [GO:0032418]; microtubule nucleation [GO:0007020]; mitotic centrosome separation [GO:0007100]; nervous system development [GO:0007399]; positive regulation of ruffle assembly [GO:1900029]; regulation of neuron projection development [GO:0010975]; vesicle transport along microtubule [GO:0047496]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; microtubule [GO:0005874]; spindle [GO:0005819]
|
microtubule binding [GO:0008017]
|
PF04880;
|
6.10.250.1080;
|
NudE family
|
PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and YWHAE (By similarity). {ECO:0000250}.; PTM: Palmitoylation at Cys-273 reduces affinity for dynein. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the interphase centrosome and the mitotic spindle. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Colocalizes with DISC1 in the perinuclear region, including the centrosome. Localizes to the kinetochore in a CENPF-dependent manner (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1}.
|
Oryctolagus cuniculus (Rabbit)
|
O46491
|
CP7A1_PIG
|
MMSISLLGGIVTAVCCCLWLLLGMRRRQTGEPPLENGIIPYLGCALQFGANPLEFLRANQRKHGHIFTCQLMGNYVHFITNPLSYHKVLCHGKYLDWKKFHFTASAKAFGHRSIDPSDGNTTDNINKTIIKTLQGDALNLLAAAMMENLQLVLRPQVAPQPEKPAWVTEGMYSFCYRVMFEAGYVTLFGKDPIGHDAQKALILNNLDNFKQFDKIFPALVAGFPIHVFKTGHYAREKLAEGLRLQKLRKRDHISELVRFLNDTLSTLDDAEKAKSLLAVLWASQANTIPATFWCLFQTIRSPEAMKAASEEVNKTLEKAGQKISLDDKPIYLNQIELDSMPVLDSIIKESLRLSSASLNIRTAKEDFTLHLQDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTKTTFYSHGLKLKYYYMPFGSGATICPGRLFAVQEIKQFLILMLSYFDLELVESHVKCPPLDQSRAGLGILPPSNDIEFRYKLKHL
|
1.14.14.23; 1.14.14.26
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P22680};
|
bile acid biosynthetic process [GO:0006699]; cellular response to cholesterol [GO:0071397]; cellular response to glucose stimulus [GO:0071333]; cholesterol catabolic process [GO:0006707]; cholesterol homeostasis [GO:0042632]; regulation of bile acid biosynthetic process [GO:0070857]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
24-hydroxycholesterol 7alpha-hydroxylase activity [GO:0033782]; cholesterol 7-alpha-monooxygenase activity [GO:0008123]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22680}; Single-pass membrane protein {ECO:0000250|UniProtKB:P22680}. Microsome membrane {ECO:0000250|UniProtKB:P22680}; Single-pass membrane protein {ECO:0000250|UniProtKB:P22680}.
|
CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21812, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17500, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.23; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21813; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=4beta-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 4beta,7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46120, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:85778, ChEBI:CHEBI:85779; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46121; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,8alpha-epoxy-5alpha-cholestan-3beta-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53256, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17168, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137063; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53257; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] = 5alpha-cholestan-7-oxo-3beta-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53252, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17168, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137062; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53253; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=7-dehydrocholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7-oxocholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53248, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17759, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:64294; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53249; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46124, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:34310, ChEBI:CHEBI:37640, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.26; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46125; Evidence={ECO:0000250|UniProtKB:P22680}; CATALYTIC ACTIVITY: Reaction=(24R)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24R)-7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:16093, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50516, ChEBI:CHEBI:50518, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P22680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16094; Evidence={ECO:0000250|UniProtKB:P22680};
| null |
PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:P22680}.; PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000250|UniProtKB:P22680}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Functions as a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen bond at 7-alpha position of cholesterol, a rate-limiting step in cholesterol catabolism and bile acid biosynthesis. 7-alpha hydroxylates several oxysterols, including 4beta-hydroxycholesterol and 24-hydroxycholesterol. Catalyzes the oxidation of the 7,8 double bond of 7-dehydrocholesterol and lathosterol with direct and predominant formation of the 7-keto derivatives. {ECO:0000250|UniProtKB:P22680}.
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Sus scrofa (Pig)
|
O46512
|
CP19A_HORSE
|
MILEMLNPMHYNLTSMVPEVMPVATLPILLLTGFLFFVWNHEETSSIPGPGYCMGIGPLISHLRFLWMGLGSACNYYNKMYGEFVRVWISGEETLVISKSSSTFHIMKHDHYSSRFGSTFGLQYMGMHENGVIFNNNPAVWKALRPFFVKALSGPSLARMVTVCVESVNNHLDRLDEVTNALGHVNVLTLMRRTMLDASNTLFLRIPLDEKNIVLKIQGYFDAWQALLIKPNIFFKISWLSRKHQKSIKELRDAVGILAEEKRHRIFTAEKLEDHVDFATDLILAEKRGELTKENVNQCILEMMIAAPDTLSVTVFFMLCLIAQHPKVEEALMKEIQTVLGERDLKNDDMQKLKVMENFINESMRYQPVVDIVMRKALEDDVIDGYPVKKGTNIILNIGRMHKLEFFPKPNEFTLENFEKNVPYRYFQPFGFGPRSCAGKFIAMVMMKVMLVSLLRRFHVKTLQGNCLENMQKTNDLALHPDESRSLPAMIFTPRNSEKCLEH
|
1.14.14.14
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P11511};
|
female gonad development [GO:0008585]; lipid metabolic process [GO:0006629]; response to estradiol [GO:0032355]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P11511}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250|UniProtKB:P11511}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16469, ChEBI:CHEBI:17347, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38192; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38195, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16422, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38196; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxyandrost-4-ene-3,17-dione + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38199, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:27576, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38200; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=19-hydroxyandrost-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein reductase] = 19-oxo-androst-4-ene-3,17-dione + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38203, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27576, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38204; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=19-oxo-androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein reductase] = estrone + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38207, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38208; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 17beta,19-dihydroxy-3-oxo-5alpha-androstanone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53200, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16330, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137031; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53201; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=17beta,19-dihydroxy-3-oxo-5alpha-androstanone + O2 + reduced [NADPH--hemoprotein reductase] = 17beta-hydroxy-3,19-dioxo-5alpha-androstanone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53204, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137031, ChEBI:CHEBI:137032; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53205; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-3,19-dioxo-5alpha-androstanone + O2 + reduced [NADPH--hemoprotein reductase] = 17beta-hydroxy-3-oxo-19-nor-5alpha-androst-1-ene + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53276, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137032, ChEBI:CHEBI:137110; Evidence={ECO:0000250|UniProtKB:P11511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53277; Evidence={ECO:0000250|UniProtKB:P11511};
| null |
PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P11511}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). {ECO:0000250|UniProtKB:P11511}.
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Equus caballus (Horse)
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O46522
|
CY24B_BOVIN
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MGNWVVNEGISIFVILVWLGMNVFLFVWYYRVYDIPDKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVNNSDPYSIALSDIGDKPNETYLNFVRQRIKNPEGGLYVAVTRLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAQRIVRGQTAESLLKHQPRNCYQNISQWGKIENCPIPEFSGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPVVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFKACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNKAPNLRLKKIYFYWLCRDTHAFEWFADLLQLLETQMQEKNNTDFLSYNICLTGWDESQASHFAMHHDEEKDVITGLKQKTLYGRPNWDNEFKTIGSQHPNTRIGVFLCGPEALADTLNKQCISNSDSGPRGVHFIFNKENF
|
1.-.-.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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defense response [GO:0006952]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; monoatomic ion transmembrane transport [GO:0034220]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]
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lysosome [GO:0005764]; membrane raft [GO:0045121]; monoatomic ion channel complex [GO:0034702]; NADPH oxidase complex [GO:0043020]; plasma membrane [GO:0005886]
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metal ion binding [GO:0046872]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]
|
PF08022;PF01794;PF08030;
|
3.40.50.80;2.40.30.10;
| null |
PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000250|UniProtKB:Q61093}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04839}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04839}. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P04839}.
| null | null | null | null | null |
FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes.
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Bos taurus (Bovine)
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O46540
|
ANF_SHEEP
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MGSSAITTSFLLFVAFQLPGQTGANPVYGSVSNADLMDFKNLLDRLEDKMPLEDEAVPSQVLSEQNEEAGAPLSPLSEVPPWDGGRSTQPREMGAPSDGDPGNPPRSVLLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRYRR
| null | null |
cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
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hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-122 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing gives rise to the auriculin and atriopeptin peptides (By similarity). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). During IDE degradation, the resulting products can temporarily stimulate NPR2 to produce cGMP, before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Phosphorylation on Ser-128 decreases vasorelaxant activity. {ECO:0000250|UniProtKB:P01160}.
|
SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. {ECO:0000250|UniProtKB:P01161}.
| null | null | null | null | null |
FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (By similarity). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
|
Ovis aries (Sheep)
|
O46550
|
CAV2_CANLF
|
MGLETEKADVQLCMDDDAYSRHSAVDFGDLEQLADSGSDRDPRRLNSHLQVGFEDVIAEPVSTHSFDKVWICSHALFEVSKYVIYKFLTLLLAMPMAFAAGVLFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSVTDAVIAPLCSSVGRSFSSVSLQVSHD
| null | null |
caveola assembly [GO:0070836]; cell differentiation [GO:0030154]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of dopamine receptor signaling pathway [GO:0060161]; positive regulation of MAPK cascade [GO:0043410]; regulation of cytosolic calcium ion concentration [GO:0051480]; skeletal muscle fiber development [GO:0048741]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]
|
caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sarcolemma [GO:0042383]
|
D1 dopamine receptor binding [GO:0031748]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
|
PF01146;
| null |
Caveolin family
|
PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:9472032}; Peripheral membrane protein {ECO:0000269|PubMed:9472032}. Cell membrane {ECO:0000269|PubMed:9472032}; Peripheral membrane protein {ECO:0000269|PubMed:9472032}. Membrane, caveola {ECO:0000269|PubMed:9472032}; Peripheral membrane protein {ECO:0000269|PubMed:9472032}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O46559
|
LIPC_RABIT
|
MGSPLCVPIFLAVCILIQSSTHGQSLRPEPFGRRARVTATKKTLLETETRFLLFKDKANKGCQIRLHHADTLQECGFNSSLPLVMIVHGWSVDGLLESWIWQMVAALKSQPARPVNVGLVDWISLAHSHYAVAVRNARLVGQEVAALLQWLEESAPFSRSNVHLIGYSLGAHVAGFAGSYISGKHKIGRITGLDAAGPLFEGTSASDRLSPDDATFVDAIHTFTREHMGLSVGIKQPVGHYDFYPNGGSFQPGCHFLELYKHIAQHGLNALSQTIKCAHERSVHLFIDSLLHPSMQSTAYQCSDMDSFSQGLCLGCTKGRCNTLGYHIRQEPLSKGKRLFLVTQAQSPFRVYHYQFKIQFINQIEKPLEPTFTMSLLGTKEEMQKIPITLGEGITSNKTYSFLITLNLDIGELMVIKFKWENSAVWANVWNTVQTIIPWGIKPRNSGLILKTIRVKAGETQQRMTFCSENMDDLQLHPTQEKNFVRCEVNPKKLKLKIK
|
3.1.1.3; 3.1.1.32; 3.1.1.5
| null |
fatty acid biosynthetic process [GO:0006633]; triglyceride catabolic process [GO:0019433]
|
high-density lipoprotein particle [GO:0034364]
|
1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; triglyceride lipase activity [GO:0004806]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:1770315}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P11150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:P11150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P11150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P11150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:P07867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:P07867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:P07867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:P07867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:P07867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; Evidence={ECO:0000250|UniProtKB:P07867};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (PubMed:1770315). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity). {ECO:0000250|UniProtKB:P07867, ECO:0000250|UniProtKB:P11150, ECO:0000269|PubMed:1770315}.
|
Oryctolagus cuniculus (Rabbit)
|
O46560
|
PDXK_PIG
|
MQAGSWVVGGGDSDSRVLSIQSHVVRGYVGNRAATFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLNSDELHALYEGLKLNNVNQYDYVLTGYTRDKSFLAMVVDIVRELKQQNPRLVYVCDPVMGDKWDGEGSMYVPEDLLPVYREKVVPVADIITPNQFEAELLTGRRIHSEEEALAVMDMLHAMGPDTVVITSSDLPSPRGKDYLIALGSQRTRSPDGSVATQRIRMEICKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSAMHHVLRRTIQCAKAKAGEGLKPSPAQLELRMVQSKRDIEDPEVVVQATVL
|
2.7.1.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9924807}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9924807}; Note=Divalent metal cations. Zn(2+) is more efficient than Mg(2+). {ECO:0000269|PubMed:9924807};
|
phosphorylation [GO:0016310]; pyridoxal 5'-phosphate salvage [GO:0009443]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; pyridoxal kinase activity [GO:0008478]
|
PF08543;
|
3.40.1190.20;
|
Pyridoxine kinase family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00764}.
|
CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:9924807}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225; Evidence={ECO:0000305|PubMed:9924807}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105; Evidence={ECO:0000250|UniProtKB:O00764}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109; Evidence={ECO:0000250|UniProtKB:O00764};
| null |
PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. {ECO:0000250|UniProtKB:O00764}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (Probable) (PubMed:9924807). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity). {ECO:0000250|UniProtKB:O00764, ECO:0000269|PubMed:9924807, ECO:0000305}.
|
Sus scrofa (Pig)
|
O46561
|
PRLR_SHEEP
|
MKENAASRVLFILLLFLFASLLNGQSPPEKPKLIKCRSPGKETFTCWWEPGADGGLPTNYTLTYRKEGETLIHECPDYKTGGPNSCYFSKKYTSIWKMYVITVSAINQMGISSSDPLYVDVTYIVEPEPPVNLTLELKHPEDRKPYLWIKWSPPTLTDVKSGWFSIQYEIRLKPEKATDWETHFAPKLTQLKIFNLYPGQKYLVQIRCKPDHGYWSEWSPESFIQIPNDFPVKDTSMWIFVGVLSAVICLIMVWAVALKGYSMVTCILPPVPGPKIKGFDIHLLEKGKSEELLRALESQDFLPTSDCEDLLMEFIEVDDSEDQHLMPHPSKEHMEQGVKPMHLDPDTDSGRGSCDSPSLLSEKCDEPQAYPSKFHIPEGPEKLEDPETNHTCLQAPQSTSGEGKIPYFLANGPKSSTWPFPQPPSLYSPRYSYHNIADVCELALGMAGTTATLLDQTDQHAFKPSKTIETGGEGKAAKQSESEGYSSEPDQDMAWPLLQDKTPLFSAKPLEYVEIHKVSQDGVLALFPKQNEKVDAPETSKEYSKVSRVTDSNILVLIPDLQAQNLTLLEESAKKAPPALP
| null | null |
positive regulation of cell population proliferation [GO:0008284]
|
external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
|
cytokine binding [GO:0019955]; metal ion binding [GO:0046872]; peptide hormone binding [GO:0017046]; prolactin receptor activity [GO:0004925]
|
PF09067;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 1 subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: This is a receptor for the anterior pituitary hormone prolactin.
|
Ovis aries (Sheep)
|
O46564
|
BMP2_RABIT
|
MVAGTRCLLALLLPQVLLGGAAGLIPELGRRKFAASSGRPSPQPSDDILSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGAPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLTSIPPEEFITSAELQVFREQMQEALGDDSGFHHRINIYEIIKPATANSKFPATRLLDTRLVNQNTSRWESFDVTPAVMRWTAQGHANHGFVVEVTHLEEKQGVSKRHVRISRSLHPDEHSWSQIRPLLVTFGHDGKGHPLHRREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
| null | null |
BMP signaling pathway [GO:0030509]; cardiac epithelial to mesenchymal transition [GO:0060317]; cardiocyte differentiation [GO:0035051]; cartilage development [GO:0051216]; epithelial to mesenchymal transition [GO:0001837]; heart development [GO:0007507]; heart induction [GO:0003129]; lung vasculature development [GO:0060426]; mesenchymal cell differentiation [GO:0048762]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone mineralization [GO:0030501]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of cartilage development [GO:0061036]; positive regulation of odontoblast differentiation [GO:1901331]; positive regulation of ossification [GO:0045778]; positive regulation of phosphatase activity [GO:0010922]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; telencephalon development [GO:0021537]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]
|
BMP receptor binding [GO:0070700]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; phosphatase activator activity [GO:0019211]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P12643}.
| null | null | null | null | null |
FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Also acts to promote expression of HAMP, via the interaction with its receptor BMPR1A/ALK3 (By similarity). Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Also stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (By similarity). {ECO:0000250|UniProtKB:P12643, ECO:0000250|UniProtKB:P21274}.
|
Oryctolagus cuniculus (Rabbit)
|
O46567
|
GCR_SAISC
|
MDSKESLTPGKEENPSSVLTQERGNVMDFCKILRGGATLKVSVSSTSLAAASQSDSKQQRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLQLLEESIANLNRSTSVPENPKSSASSSVSAAPKEKEFPKTHSDVSSEQQNLKGQTGTNGGNVKLYTADQSTFDILQDLEFSSGSPGKETNQSPWKSDLLIDENCLLSPLAGEEDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSSSNVTLPQVKTEKEDFIELCTPGVIKQEKLSTVYCQASFPGANIIGNKMSAISIHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIIKGIQQATTGVSQETSENPANKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSTVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQASSNLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQLPKYSNGNIKKLLFHQK
| null | null |
cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle [GO:0005819]
|
DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270]
|
PF02155;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000250|UniProtKB:P04150}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203, Ser-226 and Ser-404-phosphorylated forms are mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear. Phosphorylation at Ser-211 increases transcriptional activity. Phosphorylation at Ser-203, Ser-226 and Ser-404 decreases signaling capacity. Phosphorylation at Ser-404 may protect from glucocorticoid-induced apoptosis. Phosphorylation at Ser-203 and Ser-211 is not required in regulation of chromosome segregation. May be dephosphorylated by PPP5C, attenuates NR3C1 action. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.; PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.; PTM: Sumoylation at Lys-277 and Lys-293 negatively regulates its transcriptional activity. Sumoylation at Lys-704 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-277 and Lys-293 is dispensable whereas sumoylation at Lys-704 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner. {ECO:0000250|UniProtKB:P06536}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15857751}. Nucleus {ECO:0000269|PubMed:15857751}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus (PubMed:15857751). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:15857751}.
| null | null | null | null | null |
FUNCTION: Receptor for glucocorticoids (GC) (PubMed:10775802, PubMed:11703081). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:10775802, PubMed:11703081, PubMed:15857751). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (By similarity). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (By similarity). May act as a tumor suppressor (By similarity). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:10775802, ECO:0000269|PubMed:11703081, ECO:0000269|PubMed:15857751}.
|
Saimiri sciureus (Common squirrel monkey)
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O46576
|
BMP4_RABIT
|
MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRHPQPSKSAVIPDYMRDLYRLQSGEEEEEEQMPSGGLEYPERPASRANTVRSFHHEEHLENIPGTSENSAFRFLFNLSSIPENEAISSAELRLFREQVDQGPDWERGFHRINIYEVMKPPAEAVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNHGLAVEVTHFHHTRTHQGQHVRLSRSLLQGSGDWAQFRPLLVTFGHDGRGHALTRRRRAKRSLKHHPQRARKKNKNCRRHALYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHFNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR
| null | null |
blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; BMP signaling pathway [GO:0030509]; chondrocyte differentiation [GO:0002062]; deltoid tuberosity development [GO:0035993]; endochondral ossification [GO:0001958]; glomerular capillary formation [GO:0072104]; heart induction [GO:0003129]; hematopoietic progenitor cell differentiation [GO:0002244]; kidney development [GO:0001822]; lung vasculature development [GO:0060426]; lymphoid progenitor cell differentiation [GO:0002320]; negative regulation of branching involved in ureteric bud morphogenesis [GO:0090191]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of glomerular mesangial cell proliferation [GO:0072125]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; negative regulation of mesenchymal cell proliferation involved in ureter development [GO:0072200]; negative regulation of metanephric comma-shaped body morphogenesis [GO:2000007]; negative regulation of metanephric S-shaped body morphogenesis [GO:2000005]; negative regulation of mitotic nuclear division [GO:0045839]; negative regulation of thymocyte apoptotic process [GO:0070244]; osteoblast differentiation [GO:0001649]; positive chemotaxis [GO:0050918]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of branching involved in lung morphogenesis [GO:0061047]; positive regulation of cardiac muscle fiber development [GO:0055020]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epidermal cell differentiation [GO:0045606]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of odontoblast differentiation [GO:1901331]; positive regulation of protein localization to nucleus [GO:1900182]; regulation of cell fate commitment [GO:0010453]; secondary heart field specification [GO:0003139]; tendon cell differentiation [GO:0035990]; type B pancreatic cell development [GO:0003323]
|
extracellular space [GO:0005615]
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BMP receptor binding [GO:0070700]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis (By similarity). Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (By similarity). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Positively regulates the expression of odontogenic development regulator MSX1 via inducing the IPO7-mediated import of SMAD1 to the nucleus (By similarity). Required for MSX1-mediated mesenchymal molar tooth bud development beyond the bud stage, via promoting Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (By similarity). Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity). Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt, or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response (By similarity). {ECO:0000250|UniProtKB:P12644, ECO:0000250|UniProtKB:P21275}.
|
Oryctolagus cuniculus (Rabbit)
|
O46598
|
HAVR1_CHLAE
|
MADPIMHLQVVILSLILHLADSVADSVNVDGVAGLSITLPCRYNGAITSMCWNRGTCSVFSCPDGIVWTNGTHVTYRKETRYKLLGNLSRRDVSLTIANTAVSDSGIYCCRVKHSGWFNDMKITISLKIGPPRVTIPIVRTVRTSTTVPTTTTTTLPTTTTLPTTTTLPTTMTLPTTTTLPMTTTLPTTTTVPMTTTLPTTLPTTTTLPTTLPTTTTLPTTLPTTTTLPTTMTLPMTTTLPTTTTLPTTTTLPTTTTLPTTTTLPTTTLPTMTLPTTTTLPTTMTLPMTTTLPTTTTLPTTTTLPTTTMVSTFVPPTPLPMQDHEPVATSPSSAQPAETHPVTLLGATRTQPTSSPLYSYTTDGSDTVTESSDGLWNNNQTQLSPEHSPQMVNTTEGIYAGVCISVLVLLAVLGVVIAKKYFFKKEIQQLSVSFSNHQFKTLQNAVKKEVHAEDNIYIENNLYAMNQDPVVLFESLRP
| null | null |
phagocytosis, engulfment [GO:0006911]; positive regulation of mast cell activation [GO:0033005]
|
cell surface [GO:0009986]; motile cilium [GO:0031514]; plasma membrane [GO:0005886]
|
phosphatidylserine binding [GO:0001786]; virus receptor activity [GO:0001618]
|
PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, TIM family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D42}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96D42}.
| null | null | null | null | null |
FUNCTION: Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (By similarity). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses. Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (By similarity). Regulates also expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10. Acts as a regulator of T-cell proliferation (By similarity). May play a role in kidney injury and repair (By similarity). {ECO:0000250|UniProtKB:Q5QNS5, ECO:0000250|UniProtKB:Q96D42}.
|
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
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