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
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G4T4R7 | AGASK_MEDGN | MAIIYNPNKKIFTLHTAHTTYQMQVDPLGYLLHLYYGEKTNSSMDYVLTYADRGFSGNPYAAGMDRTYSLDALPQEYPSLGTGDYRNIALNIKNEKGVESADLLFKSYEIRNGKYRLQGLPAVWADEKEAQTLEIVLADENAQVEVHLLYGVLEENDVITRSVRIKNTGTGQITIEKAAAACLDFVQGEFDVLRFYGKHAMERNLERTPLGHGTIAFGSRRGTSSHQYNPAVILAEKGTTETAGSCYGMLFVYSGNFSCEAEKDQFNQTRLLLGLNEELFSYPLASGETFTVPEVILSYSAEGLSALSQQYHNCIRNHVCRSKYVHMQRPVLINSWEAAYFDFTGDTIVDLAKEAASLGIDMVVMDDGWFGKRNDDNSSLGDWQVNETKLGGSLAELITRVHEQGMKFGIWIEPEMINEDSDLYRAHPDWAIRIQGKKPVRSRNQLLLDFSRKEVRDCVFDQICVVLDQGKIDYVKWDMNRSMADVYAGNLSYDYVLGVYDFMERLCSRYPDLLLEGCSGGGGRFDAGMLYYSPQIWCSDNTDAINRTRIQYGTSFFYPVSAMGAHVSAVPNHQTGRVTSFHTRGVTAMAGTFGYELNPALLSDEEKQQIREQIKTYKKYETLINEGTYWRLSDPFTDEIAAWMSVSEEQDHALVSVVRLMAEANQATVYVRLRGLKPDAVYLEEQSGRQYSGAALMHAGIPLPPFTEEYEAYQFAFTELKEAGRLYEKVQKWCDGNAENRVVISIYGGSGSGKTTLATALQQYFLNDGTECYLLSGDDYPHRIPKRNDEERMRVYKEAGEDGLRGYLGTKKEIDFDRINEVLAAFHEGKDSITLRHMGREDGEISLEETDFSGISVLLLEWTHGGSDDLHGVDLPVFLESSPGETRERRIRRNRDENAASPFICRVVELEQEKLEVQRKNAGLIVGKDGSVYEQ | 2.7.-.-; 3.2.1.22 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21931163}; | melibiose catabolic process [GO:0005995]; protein homotetramerization [GO:0051289]; raffinose catabolic process [GO:0034484]; stachyose metabolic process [GO:0033531] | null | alpha-galactosidase activity [GO:0004557]; ATP binding [GO:0005524]; carbohydrate kinase activity [GO:0019200]; magnesium ion binding [GO:0000287]; nucleotidyltransferase activity [GO:0016779]; raffinose alpha-galactosidase activity [GO:0052692] | PF16874;PF16875;PF02065;PF00485; | 3.20.20.70;2.70.98.60;2.60.40.1180;3.40.50.300; | Glycosyl hydrolase 36 family; Uridine kinase family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; Evidence={ECO:0000269|PubMed:21931163}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.37 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 6.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21931163}; Note=kcat/KM is 1850 s(1) mM(1) for p-nitrophenyl-alpha-D-galactopyranoside. {ECO:0000269|PubMed:21931163}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. Active between pH 4.0-6.5. {ECO:0000269|PubMed:21931163}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:21931163}; | FUNCTION: Bifunctional enzyme with alpha-galactosidase and sucrose kinase activities. Produces sucrose-6-phosphate directly from raffinose. Binds ATP. Phosphorylates sucrose specifically on the C6 position of glucose in the presence of ATP. Hydrolyzes melibiose, raffinose, stachyose and synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside with high activity. Low activity against locust bean gum, guar gum and synthetic substrates xylose alpha-D-4-nitrophenol, glucose alpha-D-4-nitrophenol and o-nitrophenyl-alpha-D-galactopyranoside. {ECO:0000269|PubMed:21931163}. | Mediterraneibacter gnavus (Ruminococcus gnavus) |
G4V4G2 | SDHE_SERS3 | MDIDNKPRIHWACRRGMRELDISIMPFFEHDYDTLSDDDKRNFIRLLQCDDPDLFNWLMNHGEPTDQGLKHMVSLIQTRNKNRGPVAM | null | null | antibiotic biosynthetic process [GO:0017000]; respiratory chain complex II assembly [GO:0034552]; succinate metabolic process [GO:0006105] | cytoplasm [GO:0005737] | null | PF03937; | 1.10.150.250; | SdhE FAD assembly factor family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22474332}. | null | null | PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis. {ECO:0000269|PubMed:22474332}. | null | null | FUNCTION: An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins (PubMed:24070374, PubMed:24374335). Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH (PubMed:22474332). Required for flavinylation of the flavoprotein subunit FdrA of fumarate reductase (FDR) (PubMed:24374335). Flavinylation of SDH and FDR occurs in a similar but not identical manner, as site-specific mutations display subtle differences between them (PubMed:24070374, PubMed:24374335). Flavinylates SdhA in vivo in the absence of the other SDH subunits; SdhE mutants that do not flavinylate also interfere with wild-type activity in a possible dominant-negative fashion (PubMed:24070374). Weakly binds to FAD and facilitates its binding to SdhA (PubMed:22474332). Required for production of prodigiosin antibiotic (Pig); overproduction of SdhE in a deletion mutant leads to decreased synthesis of Pig compared to wild-type (PubMed:22474332). Capable of flavinylating A.pasteurianus SdhA when the SDH operon and this gene are expressed in G.oxydans; flavinylation of SdhA is detected only in the presence of sdhE (PubMed:26399411). {ECO:0000269|PubMed:22474332, ECO:0000269|PubMed:24070374, ECO:0000269|PubMed:24374335, ECO:0000269|PubMed:26399411}. | Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida) |
G4VJD5 | PGM_SCHMA | MAPYRIVFIRHGESVYNEENRFCGWHDADLSGQGITEAKQAGQLLRQNHFTFDIAYTSVLKRAIKTLNFVLDELDLNWIPVTKTWRLNERMYGALQGLNKSETAAKHGEEQVKIWRRAYDIPPPPVDISDPRFPGNEPKYALLDSSCIPRTECLKDTVQRVLPFWFDTISASIKRREQVLIVAHGNSLRALIKYLDNTSDSDIVELNIPTGIPLVYELDANLKPTKHYYLADEATVAAAIARVANQGKKK | 5.4.2.11 | null | canonical glycolysis [GO:0061621]; symbiont-mediated activation of host plasminogen [GO:0044542] | null | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | null | SUBCELLULAR LOCATION: Tegument {ECO:0000269|PubMed:15952743, ECO:0000269|PubMed:16447162, ECO:0000269|PubMed:21468311, ECO:0000269|PubMed:25910674, ECO:0000269|PubMed:36083036}. Note=Exposed on the tegumental surface (PubMed:21468311, PubMed:25910674, PubMed:36083036). Associated with the tegumental surface membranes (PubMed:15952743, PubMed:16447162). Not secreted or released to the culture medium (PubMed:36083036). {ECO:0000269|PubMed:15952743, ECO:0000269|PubMed:16447162, ECO:0000269|PubMed:21468311, ECO:0000269|PubMed:25910674, ECO:0000269|PubMed:36083036}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000269|PubMed:36083036}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.85 mM for 3-phosphoglycerate in the presence of 2,3-bisphosphoglycerate (at pH 7.8) {ECO:0000269|PubMed:36083036}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000305|PubMed:36083036}. | null | null | FUNCTION: Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction (PubMed:36083036). Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG (PubMed:36083036). Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro (PubMed:36083036). Host-interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable). {ECO:0000269|PubMed:36083036, ECO:0000305}. | Schistosoma mansoni (Blood fluke) |
G4WJD4 | COLD_YERPU | MRKIMINFPLASSTWDEKELNAIQRIIDSNMFTMGESVKQYEKDFAEYFGSKYSVMVSSGSTANLLMIAALFFTKKPKFKRGDEVIVPAVSWSTTYFPLQQYGLNVRFVDIDKKTLNIDLDKLKSAITEKTKAILAVNLLGNPNDFDAITKITEGKDIFILEDNCESMGARLNGKQAGTYGLMGTFSSFFSHHIATMEGGCVITDDEELYHILLCIRAHGWTRNLPEFNHITGQKSIDPFEESFKFVLPGYNVRPLEMSGAIGIEQLKKLPSFIEMRRKNATIFKELFSSHPYIDIQQETGESSWFGFALILKESSPITRAELVKKLIEAGIECRPIVTGNFLKNKEVLKFFDYTIAGEVTDAEYIDKHGLFVGNHQIDLSEQIKNLFNILKK | 4.2.1.168 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:15610039}; | nucleotide-sugar metabolic process [GO:0009225]; polysaccharide biosynthetic process [GO:0000271] | plasma membrane [GO:0005886] | dTDP-4-amino-4,6-dideoxygalactose transaminase activity [GO:0019180]; glutamate binding [GO:0016595]; hydro-lyase activity [GO:0016836]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF01041; | 3.90.1150.10;3.40.640.10; | DegT/DnrJ/EryC1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=GDP-4-dehydro-alpha-D-rhamnose + L-glutamate = 2-oxoglutarate + GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NH4(+); Xref=Rhea:RHEA:49488, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57964, ChEBI:CHEBI:73931; EC=4.2.1.168; Evidence={ECO:0000269|PubMed:15610039}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.5 uM for GDP-4-keto-6-deoxy-D-mannose (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:15610039}; KM=1.4 mM for L-glutamate (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:15610039}; Note=kcat is 0.6 sec(-1) (at pH 7 and 37 degrees Celsius). {ECO:0000269|PubMed:15610039}; | PATHWAY: Nucleotide-sugar metabolism; GDP-L-colitose biosynthesis. {ECO:0000305|PubMed:15610039}. | null | null | FUNCTION: Involved in the biosynthesis of L-colitose, a 3,6-dideoxyhexose present in the O-antigen region of lipopolysaccharides (LPS), where it serves as an antigenic determinant and is vital for bacterial defense and survival. Catalyzes the removal of the C3'-hydroxyl group from GDP-4-keto-6-deoxy-D-mannose via a combined transamination-deoxygenation reaction. The catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate (PLP) is converted to pyridoxamine 5'-phosphate (PMP) in the presence of L-glutamate. This coenzyme then forms a Schiff base with GDP-4-keto-6-deoxy-D-mannose and the resulting adduct undergoes a PMP-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after tautomerization and hydrolysis to release ammonia yields GDP-4-keto-3,6-dideoxy-D-mannose as a product. {ECO:0000269|PubMed:15610039}. | Yersinia pseudotuberculosis |
G4YRX5 | PSR1_PHYSP | MRLTYVLLVAVTTLLVSCDATKPSTEATAVSKRLLRFVEAADEEERRIDFSPEKLRKMLGDETYRLKKFGKWDSDGHTFDGLKHYLLLSDSSMVKLRNMYKAWLEQ | null | null | null | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | null | PF16810; | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25902521}. Host nucleus {ECO:0000269|PubMed:25902521}. Note=The nuclear localization is required for this interaction. {ECO:0000269|PubMed:25902521}. | null | null | null | null | null | FUNCTION: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection (PubMed:23377181, PubMed:25902521, PubMed:29029698, PubMed:30963588). Interferes with secondary siRNA production by associating with host nuclear protein PINP1 that acts as a regulator of the accumulation of both microRNAs and endogenous small interfering RNAs (PubMed:25902521). {ECO:0000269|PubMed:23377181, ECO:0000269|PubMed:25902521, ECO:0000269|PubMed:29029698, ECO:0000269|PubMed:30963588}. | Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
G4ZHR2 | XEG1_PHYSP | MKGFFAGVVAAATLAVASAGDYCGQWDWAKSTNYIVYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVFSFVATKTITNFSADLQKFLSYLTKNQGLPSSQYLITLEAGTEPFVGTNAKMTVSSFSAAVN | 3.2.1.151 | null | polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576]; host cellular component [GO:0018995] | cellulase activity [GO:0008810]; xyloglucan-specific endo-beta-1,4-glucanase activity [GO:0033946] | PF01670; | 2.60.120.180; | Glycosyl hydrolase 12 (cellulase H) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26163574, ECO:0000269|PubMed:28082413}. Host {ECO:0000269|PubMed:26163574}. Note=Targeted to the host apoplast in order to trigger cell death. {ECO:0000269|PubMed:26163574}. | CATALYTIC ACTIVITY: Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151; Evidence={ECO:0000269|PubMed:26163574}; | null | null | null | null | FUNCTION: Glycoside hydrolase that exhibits xyloglucanase activity (PubMed:26163574). Acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death. XEG1-induced cell death can be suppressed by P.sojae RxLR effectors. The PAMP activity is independent of its xyloglucanase activity (PubMed:26163574). XEG1 induces plant defense responses in a RLP kinase Serk3/Bak1-dependent manner in Nicotiana benthamiana. Moreover, the perception of XEG1 occurs independently of the perception of ethylene-inducing xylanase Eix2 in Tomato (PubMed:26163574). With truncated paralog XLP1, is required to elevate apoplastic sugar during P.sojae infection (PubMed:28082413). {ECO:0000269|PubMed:26163574, ECO:0000269|PubMed:28082413}. | Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
G4ZHR3 | XLP1_PHYSP | MKSFLQLVVVVAALLSVSTADFCSQWRLSKAGKYVIYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVYQPPGLPLST | null | null | polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | cellulase activity [GO:0008810] | PF01670; | 2.60.120.180; | Glycosyl hydrolase 12 (cellulase H) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28082413}. | null | null | null | null | null | FUNCTION: Secreted XEG1-like protein that has lost enzyme activity but binds to host soybean apoplastic glucanase inhibitor protein GIP1 more tightly than does XEG1, thus it outcompetes XEG1 for GIP1 binding and frees functional XEG1 to support P.sojae infection (PubMed:28082413). With XEG1, is required to elevate apoplastic sugar during P.sojae infection (PubMed:28082413). {ECO:0000269|PubMed:28082413}. | Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
G4ZJX4 | AVH23_PHYSP | MRLTYFLTVIVVATLHAGGTALATAEAPNHAAIVNVASADNVHSLDTTAEIGGRMLRKVKEDTVSKKDHEERGPGAILERQTAFVKKLFSRQNAIVNRAQGAFQRQNAFVNRDQGAFQRQNAFVKRAIQRQNHFKLSDNA | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | null | PF16810; | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28318979}. Host nucleus {ECO:0000269|PubMed:28318979}. Host cytoplasm {ECO:0000269|PubMed:28318979}. Note=Location into the host nucleus is required for virulence. {ECO:0000269|PubMed:28318979}. | null | null | null | null | null | FUNCTION: Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts (PubMed:21653195). Acts as a modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to the ADA2 subunit of the HAT complex SAGA and disrupts its assembly by interfering with the association of ADA2 with the catalytic subunit GCN5. As such, Avh23 suppresses H3K9 acetylation mediated by the ADA2/GCN5 module and increases plant susceptibility (PubMed:28318979). {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:28318979}. | Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
G4ZSG0 | AVH52_PHYSP | MRLTSILVLVIAATFHTTGTALTLTKDSKAGIANGDSPASGDFIDANSARLLRRVEKDKVDYEQDEQRSFGALKDAVKKLNPVTAVKKFFKQRAKRKKVIQTARDADNNLAWAMKEVYKAAN | null | null | symbiont-mediated perturbation of host transcription [GO:0052026] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | null | PF16810; | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30346270}. Host nucleus {ECO:0000269|PubMed:30346270}. | null | null | null | null | null | FUNCTION: Effector that suppresses plant defense responses during the early stages of pathogen infection (PubMed:21653195, PubMed:26163574, PubMed:30346270). Suppresses cell death induced by effectors and PAMPs in plant hosts (PubMed:26163574, PubMed:30346270). Interacts with host acetyltransferase TAP1 and causes TAP1 relocation into the nucleus where it acetylates histones H2A and H3 during early infection, thereby promoting susceptibility of host plant to P.sojae (PubMed:30346270). {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:26163574, ECO:0000269|PubMed:30346270}. | Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
G5AY81 | HYAS2_HETGA | MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSSKSVCIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYSQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRRKKGQQYDMVLDV | 2.4.1.212 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | atrioventricular canal development [GO:0036302]; bone morphogenesis [GO:0060349]; endocardial cushion to mesenchymal transition [GO:0090500]; extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of urine volume [GO:0035810]; renal water absorption [GO:0070295]; vasculogenesis [GO:0001570] | cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853] | hyaluronan synthase activity [GO:0050501] | PF03142;PF00535; | null | NodC/HAS family | PTM: Phosphorylation at Thr-328 is essential for hyaluronan synthase activity. {ECO:0000250|UniProtKB:Q92819}.; PTM: O-GlcNAcylation at Ser-221 increases the stability of HAS2 and plasma membrane localization. {ECO:0000250|UniProtKB:Q92819}.; PTM: Ubiquitination at Lys-190; this ubiquitination is essential for hyaluronan synthase activity and homo- or hetero-oligomerization. Can also be poly-ubiquitinated. Deubiquitinated by USP17L22/USP17 and USP4. USP17L22/USP17 efficiently removes 'Lys-63'- and 'Lys-48'-linked polyubiquitin chains, whereas USP4 preferentially removes monoubiquitination and, partially, both 'Lys-63'- and 'Lys-48'-linked polyubiquitin chain. {ECO:0000250|UniProtKB:Q92819}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Lysosome {ECO:0000250|UniProtKB:Q92819}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane and either back to endosomes and lysosomes, or out into extracellular vesicles. Post-translational modifications control HAS2 trafficking. {ECO:0000250|UniProtKB:Q92819}. | CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000250|UniProtKB:Q92819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466; Evidence={ECO:0000250|UniProtKB:Q92819}; CATALYTIC ACTIVITY: Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000250|UniProtKB:Q92819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529; Evidence={ECO:0000250|UniProtKB:Q92819}; | null | PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000250|UniProtKB:Q92819}. | null | null | FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By similarity). This is one of three isoenzymes responsible for cellular hyaluronan synthesis and it is particularly responsible for the synthesis of high molecular mass hyaluronan (By similarity). {ECO:0000250|UniProtKB:P70312, ECO:0000250|UniProtKB:Q92819}. | Heterocephalus glaber (Naked mole rat) |
G5BQH4 | APOC3_HETGA | MQPRVFLAVTLLALLASARALETEDASLLGYMQDYMQGYMEHASKTAQDALTRVQDSQMAQQARGWMSDSLSSLQDYWSSFKGKWSGFGFWDATPEEASPTPAPEGI | null | null | cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; chylomicron remnant clearance [GO:0034382]; G protein-coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; negative regulation of cholesterol import [GO:0060621]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of high-density lipoprotein particle clearance [GO:0010987]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of triglyceride catabolic process [GO:0010897]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phospholipid efflux [GO:0033700]; regulation of Cdc42 protein signal transduction [GO:0032489]; triglyceride catabolic process [GO:0019433]; triglyceride homeostasis [GO:0070328] | chylomicron [GO:0042627]; intermediate-density lipoprotein particle [GO:0034363]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phospholipid binding [GO:0005543] | PF05778; | 6.10.90.10; | Apolipoprotein C3 family | PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-101 with a core 1 or possibly core 8 glycan. {ECO:0000250|UniProtKB:P02656}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. | null | null | null | null | null | FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. {ECO:0000250|UniProtKB:P02656}. | Heterocephalus glaber (Naked mole rat) |
G5BQH5 | APOA1_HETGA | MKAVVLAVAVLFLTGSQARHFWQGDEPQTSWDRMKDFAALYVDAIQESGKDCAAQLDASALGKQLNLNLLANWNTLTSTFNNLREQLGSVTKEFWDNLGEDTVWLRQQMNKDLEEVKQKVQSYLDNFQKKVNEEVERYRDKVQPLGKELHKDAQQKLKELQEKLAPLGQDIRQRAREYVDALRTHLGSYTQGMRQGLAKRLEALKESAPVSEYQVKASKHLKTFSEKAKPALEDLRQGLMPVMESLKASFLSSIDQASKQLSAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180] | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Heterocephalus glaber (Naked mole rat) |
G5BWH8 | APOA2_HETGA | MKLLAMTVLLVTICSLDGALVRRQAEEPDLQGLFSQYFQTVTSYGKDLLQKTKPQDLQAQVQSYFEKTQEQLVPLVKKAGTELFNMLSNMIELKKTQPATA | null | null | cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; diacylglycerol catabolic process [GO:0046340]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodeling [GO:0034374]; negative regulation of cholesterol import [GO:0060621]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid catabolic process [GO:0009395]; phospholipid efflux [GO:0033700]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of lipid catabolic process [GO:0050996]; positive regulation of phagocytosis [GO:0050766]; protein stabilization [GO:0050821]; regulation of intestinal cholesterol absorption [GO:0030300]; response to glucose [GO:0009749]; reverse cholesterol transport [GO:0043691]; triglyceride-rich lipoprotein particle remodeling [GO:0034370] | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Heterocephalus glaber (Naked mole rat) |
G5CV52 | TPS17_SOLLC | MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSKSLEKLELINTIQCLGLGYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTIAQLKQILPKLSNSQLAQQITNALKYPIKDGIVRVETRKYISFYQQNQNHNEVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFYISIIDDTYDIYGKLDELTLFTQAIERWNIDASEQLPLYMKIIYRDLLDVYDEIEKELANENKSFLVNYSINEMKKVVRGYFQEAKWYYGKKVPTMEQYMKNGISTSAYILLTTTSWLAMGNVATKDAFDWVATEPPIVVASCYIIRLLNDLVSHEEEQKRGNAASAVECYMNEYSVTKEEAHIKIRDIIENYWKDLNEEYFKVDMIIIPRVLLMCIINLTRVAEFIYKDEDAYTFSKNNLKDVISDILVDPII | 4.2.3.-; 4.2.3.106; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.47; 4.2.3.54; 4.2.3.73; 4.2.3.81 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; response to jasmonic acid [GO:0009753]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate; Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700, ChEBI:CHEBI:175763; EC=4.2.3.73; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29512; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-gurjunene; Xref=Rhea:RHEA:68400, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763, ChEBI:CHEBI:178033; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68401; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019, ChEBI:CHEBI:49238, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene + diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019, ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene + diphosphate; Xref=Rhea:RHEA:30471, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:61679; EC=4.2.3.54; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30472; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-alpha-bergamotene and (Z)-gamma-bisabolene as well as beta-bisabolene, (Z)-alpha-bergamotene and (E)-gamma-bisabolene to a lower extent (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene, terpinolene, gamma-terpinene and (Z)-beta-ocimene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
G5CV54 | TPS14_SOLLC | MATNLTLETDKEIKNMNQLSMIDTTITRPLANYHSSVWKNYFLSYTPQLTEISSQEKLELEELKEKVRQMLVETSDKSTQKLVLIDTIQRLGVAYHFDNEIKISIQNIFDEFEQNKNEDDNDLYIVALRFRLVRGQRHYMSSDVFKKFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEQILEEALSFTVTHLKSMSPKLDSSLKAQVSEALIQPIYTNVPRVVAPKYIRIYENIESHDDLLLKFVKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWATGVYFGPQYKRARRMITKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMDSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKVEMNKLIKSYLKEAEWLKNDIIPKCEEYKRNATITVANQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFVECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLQPALNLSRLVDILQEDDFTDSQNFLKDTIKLLFVDSVNSTSCG | 4.2.3.-; 4.2.3.40; 4.2.3.59 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate; Xref=Rhea:RHEA:68472, ChEBI:CHEBI:33019, ChEBI:CHEBI:49242, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68473; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:26081, ChEBI:CHEBI:33019, ChEBI:CHEBI:49238, ChEBI:CHEBI:175763; EC=4.2.3.40; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26082; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21813655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469; Evidence={ECO:0000269|PubMed:21813655}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-bisabolene, but also smaller amounts of (Z)-gamma-bisabolene, (E)-gamma-bisabolene and nerolidol (PubMed:21813655). {ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
G5DAC6 | XTH1_DIOKA | MAFMSFINGFSTLFLVALLASSMMAAKGGNFYQDFDVTWGDHRAKIFNGGQLLSLSLDKTSGSGFRSKKEYLFGRIDMQLKLVAGNSAGTVTAYYLSSQGPTHDEIDFEFLGNLSGDPYIVHTNVFTQGKGNREQQFYLWFDPTRNFHTYSVVWNPRQIIFLIDNTPIRVFKNAESIGVPFPKNQPMRIYSSLWNADDWATRGGLVKTDWTKAPFTAYYRNFNAKTCSGACTESFGDGAWQSQELDAHSRRRLRWVQKNFMIYNYCTDLKRFPEGLPKECQRRSRFL | 2.4.1.207 | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411] | apoplast [GO:0048046] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | PF00722;PF06955; | 2.60.120.200; | Glycosyl hydrolase 16 family, XTH group 2 subfamily | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5-5.5. Loses activity rapidly when pH is lowered from 5 to 4. {ECO:0000269|PubMed:25849978}; | null | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH) (PubMed:25849978). Overexpression in Arabidopsis transgenic plants results in elevated tolerance to abiotic stress, such as salt, ABA (abscisic acid) and drought stresses, and in the production of wider leaves. Overexpression in transgenic tomato plants slows down fruit ripening and softening, and the plants produce larger fruits. Both transgenic plants have larger and more irregular cells. Moreover, the fruits of the transgenic tomato have higher density of cell wall and intercellular spaces. May provide cells with more strength and thickness to maintain structural integrity (PubMed:28155115). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits (PubMed:25849978, PubMed:28155115). {ECO:0000269|PubMed:25849978, ECO:0000269|PubMed:28155115}. | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) |
G5DAC7 | XTH2_DIOKA | MAMGTHFGGLWLALLCMVSATMGAVPRKPVDVPFGRNYVPTWAFDHIKYFNGGSQIQLSLDKYTGTGFQSKGSYLFGHFSMQIKMVPGDSAGTVTAFYLSSQNSEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIFLWFDPTKEYHSYSVLWNLFLIIFFVDDVPIRVFKNSKDLGVRFPFDQPMKIYSSLWNADDWATRGGLEKTDWSKAPFVASYRSFHVDGCEASVNAKFCDTQGKRWWDQKEFQDLDSFQYRRLRWVRSKYTIYNYCTDRKRYPVMPPECKRDRDI | 2.4.1.207 | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411] | apoplast [GO:0048046] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | PF00722;PF06955; | 2.60.120.200; | Glycosyl hydrolase 16 family, XTH group 1 subfamily | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 4.5-6.5. Loses activity rapidly when pH is lowered from 5 to 4. {ECO:0000269|PubMed:25849978}; | null | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during fruit ripening and postharvest fruit softening. {ECO:0000269|PubMed:25849978}. | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) |
G5DBJ0 | CPP1_NICBE | MATTLISKLTLSSAFLGQQFSSRGNSMRSAPAGLFLRGPRCAATDTPYGGNIPQFPRVNVWDPYKRLGISRDASEEEVWSSRNFLLNQYYNHERSAESIEAAFEKILMASFINRKKTKINLKTRLKKKVEESPPWVQNLLSFVELPPPVIILRRLFLFGFMACWSVMNSTEAGPAFQVAISFGACVYFLNDKTKSLGRAALIGFGALVAGWFCGSLLVPMIPPNLLHPTWSLELLTSLFIYVSLFLGCTFLK | null | null | chaperone-mediated protein folding [GO:0061077]; chloroplast organization [GO:0009658]; de-etiolation [GO:0009704]; protein folding [GO:0006457] | chloroplast envelope [GO:0009941]; chloroplast membrane [GO:0031969]; chloroplast thylakoid membrane [GO:0009535]; plastid thylakoid membrane [GO:0055035] | protein folding chaperone [GO:0044183] | PF11833; | null | Chaperone-like protein of POR1 protein family | null | SUBCELLULAR LOCATION: Plastid, chloroplast envelope {ECO:0000269|PubMed:24151298}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24151298}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Exhibits holdase chaperone activity involved in the stabilization of POR proteins against photooxidative stress in chloroplasts. Required for chloroplast development. {ECO:0000269|PubMed:24151298}. | Nicotiana benthamiana |
G5DDC2 | ADH1B_MAIZE | MMASQAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKQELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKVAPALAAGCAAVLKPSELASVTCLELADICKEVGLPPGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMAAAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLVHTKIAKEFNEKMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFILNAKSEGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYRSPSKL | 1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.54; 1.2.1.8 | null | cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | null | 1-pyrroline dehydrogenase activity [GO:0033737]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; gamma-guanidinobutyraldehyde dehydrogenase activity [GO:0047107]; protein homodimerization activity [GO:0042803]; sodium ion binding [GO:0031402] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244, ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540, ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306; Evidence={ECO:0000269|PubMed:23408433}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; KM=11 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; KM=10 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; KM=5 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; KM=29 uM for betaine aldehyde {ECO:0000269|PubMed:23408433}; KM=79 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:23408433}; | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:23408433). {ECO:0000269|PubMed:23408433, ECO:0000305}. | Zea mays (Maize) |
G5E5X0 | LIMD1_BOVIN | MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGAGNNPEFEETRRVFATKMAKIHLQQQQQQQLLQEETLPRASRGPINGGARLGPPAHREAGGGSKLAADGAAKPPLAASTVAPGTTITVAPGQPSYPPQEQRAKLYVRGSRQGSQDCGSKESMVNSEMSAFHRPGPCEDPSCLTHGDYYDNLSLAGPKWADDPGVSPGIRLGVGSGWSGTPGSDPLLSKPSRDPHLYHQQLSAGSGRSLQSGQDGGPGGGNSEKPAGVWTTASSQRVSPGLPSAGPENGALPRSAQPRTPSFSAPLALNRPSQGSLPRTNSGVGSEVSGTMPKPTVDPQPWFQDGPKSYLSSSAPSSSPASMDHMQAGALPGLGPKPGSTDPGIGPKLSPNSLVHPVMSTLPELSCKEGASSWASDGSLGPVLPETPSSPRVRLPCQTLIPGPELGPTAAELKLEALTQRLEREMDAHPKADYFGACVKCSKGVFGAGQACQAMGNLYHDACFTCAACSRKLRGKAFYFVNGKVFCEEDFLYSGFQQSADRCFLCGHLIMDMILQALGKSYHPGCFRCVICNECLDGVPFTVDSENKIYCVRDYHKVLAPKCAACGLPILPPEGSDETIRVVSMDRDYHVECYHCEDCGLELNDEDGHRCYPLEDHLFCHSCHVKRLEKGPSPAALRQHHF | null | null | cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hippo signaling [GO:0035331]; negative regulation of osteoblast differentiation [GO:0045668]; osteoblast development [GO:0002076]; P-body assembly [GO:0033962]; phosphorylation [GO:0016310]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; regulation of cell shape [GO:0008360]; regulation of DNA-templated transcription [GO:0006355]; response to hypoxia [GO:0001666] | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; plasma membrane [GO:0005886]; RISC complex [GO:0016442]; transcription regulator complex [GO:0005667] | metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | PTM: Phosphorylated during mitosis. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
G5E829 | AT2B1_MOUSE | MGDMANNSVAYSGVKNSLKEANHDGDFGITLTELRALMELRSTDALRKIQESYGDVYGICTKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYINEKHYKKVPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGFLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSFRIFSKGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDVVTGLTCIAVVGIEDPVRPEVPEAIKKCQRAGITVRMVTGDNINTARAIATKCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVSEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGRNAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATSSSPGSPLHSLETSL | 7.2.2.10 | null | calcium ion export [GO:1901660]; calcium ion export across plasma membrane [GO:1990034]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of cytokine production [GO:0001818]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; positive regulation of bone mineralization [GO:0030501]; positive regulation of calcium ion transport [GO:0051928]; regulation of blood pressure [GO:0008217]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of vascular associated smooth muscle contraction [GO:0003056] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; dendrite membrane [GO:0032590]; dendritic spine membrane [GO:0032591]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body membrane [GO:0032809]; nucleoplasm [GO:0005654]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165] | PF12424;PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20020}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:23460639}. Synapse {ECO:0000269|PubMed:12209837}. Presynaptic cell membrane {ECO:0000269|PubMed:30862855}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:30862855}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with SV2A in photoreceptor synaptic terminals (PubMed:12209837). Colocalizes with NPTN to the immunological synapse (PubMed:28827723). Colocalizes with EPB41 to the basolateral membrane in enterocyte (PubMed:23460639). Preferentially sorted to recycling synaptic vesicles. {ECO:0000269|PubMed:12209837, ECO:0000269|PubMed:23460639, ECO:0000269|PubMed:28827723, ECO:0000269|PubMed:30862855}. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000305|PubMed:24805951, ECO:0000305|PubMed:30862855}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000305|PubMed:24805951, ECO:0000305|PubMed:30862855}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis (PubMed:16956963, PubMed:22311909, PubMed:23266958, PubMed:24805951, PubMed:26392310, PubMed:28827723, PubMed:29950683). Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to regulation of vascular smooth muscle cells vasoconstriction (PubMed:22311909, PubMed:24805951, PubMed:29950683). Positively regulates bone mineralization through absorption of calcium from the intestine (PubMed:23266958, PubMed:26392310). Plays dual roles in osteoclast differentiation and survival by regulating RANKL-induced calcium oscillations in preosteoclasts and mediating calcium extrusion in mature osteoclasts (PubMed:23266958). Regulates insulin sensitivity through calcium/calmodulin signaling pathway by regulating AKT1 activation and NOS3 activation in endothelial cells (By similarity). May play a role in synaptic transmission by modulating calcium and proton dynamics at the synaptic vesicles. {ECO:0000250|UniProtKB:P20020, ECO:0000269|PubMed:16956963, ECO:0000269|PubMed:22311909, ECO:0000269|PubMed:23266958, ECO:0000269|PubMed:24805951, ECO:0000269|PubMed:26392310, ECO:0000269|PubMed:28827723, ECO:0000269|PubMed:29950683, ECO:0000269|PubMed:30862855}. | Mus musculus (Mouse) |
G5E870 | TRIPC_MOUSE | MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPRAFQHIESFSETNKPHSKSKKRHLDQEQQLKSAQLPSTSKAHTRKSVAAGSSRNQKRKRTESSCVKSGSGSESTGAEERSAKPIKLASKSATSAKAGCSTITDSSSAASTSSSSSAIASASSTVPAGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPESNQETVNSSAARTDEAPQGAAASSSVAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNPLANSNTSGYSELKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSLGSTTPASSGTATAATNASADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSAQSNSNNIEPARTAGVSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKNEKDAVGREIRLKRFLHVFFSSPLPGEEPVGRVEPVGHAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGAGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSVQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESTKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVANPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLCLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGQQSFHLS | 2.3.2.26 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; heterochromatin boundary formation [GO:0033696]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of embryonic development [GO:0045995]; ubiquitin-dependent protein catabolic process [GO:0006511] | nuclear speck [GO:0016607]; nucleoplasm [GO:0005654] | ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00632;PF02825; | 3.30.720.50;3.30.2410.10;3.90.1750.10;1.25.10.10; | UPL family, K-HECT subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14669}. | 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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q14669}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q14669}. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex. {ECO:0000250|UniProtKB:Q14669}. | Mus musculus (Mouse) |
G5E8I7 | U17LC_MOUSE | MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKQVSIDMPEGRVHEVLDPEYQLKKSRRKKHKKKSPCTEDAGEPCKNREKRATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRINEILPQEQNHQKAGQSLRNTEGELDLPADAIVIHLLRSTENWGRDAPDKENQPWHNADRLLTSQDPVNTGQLCRQEGRRRSKKGKNKNKQGQRLLLVC | 3.4.19.12 | null | chordate embryonic development [GO:0043009]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF00443; | 3.90.70.10; | Peptidase C19 family, USP17 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:11443643, ECO:0000269|PubMed:8995226}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes (PubMed:11443643, PubMed:8995226). Important for preimplantation stage embryonic development (PubMed:22984479). {ECO:0000269|PubMed:11443643, ECO:0000269|PubMed:22984479, ECO:0000269|PubMed:8995226}. | Mus musculus (Mouse) |
G5E8K5 | ANK3_MOUSE | MSEEPKEKPAKPAHRKRKGKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADVESKSGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTLKVVTEEIMTTTTITEKHKMNVPETMNEVLDMSDDEVRKASAPEKLSDGEYISDGEEGDKCTWFKIPKVQEVLVKSEDAITGDTDKYLGPQDLKELGDDSLPAEGYVGFSLGARSASLRSFSSDRSYTLNRSSYARDSMMIEELLVPSKEQHLTFTREFDSDSLRHYSWAADTLDNVNLVSSPVHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLAELLNGMDEELDSPEELGTKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPEETVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDATPNLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLASQLYRELICVPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKAEKADRRQSFASLALRKRYSYLTEPSMSPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGHPSFQVELETPMGLYCTPPNPFQQDDHFSDISSIESPFRTPSRLSDGLVPSQGNIEHPTGGPPVVTAEDTSLEDSKMDDSVTVTDPADPLDVDESQLKDLCQSECAQCWASVPGIPNDGRQAEPLRPQTRKVGMSSEQQEKGKSGPDEEVTEDKVKSLFEDIQLEEVEAEEMTEDQGQAMLNRVQRAELAMSSLAGWQNETPSGSLESPAQARRLTGGLLDRLDDSSDQARDSITSYLTGEPGKIEANGNHTAEVIPEAKAKPYFPESQNDIGKQSIKENLKPKTHGCGRTEEPVSPLTAYQKSLEETSKLVIEDAPKPCVPVGMKKMTRTTADGKARLNLQEEEGSTRSEPKQGEGYKVKTKKEIRNVEKKTH | null | null | anterograde axonal transport [GO:0008089]; axon development [GO:0061564]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to magnesium ion [GO:0071286]; clustering of voltage-gated sodium channels [GO:0045162]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; magnesium ion homeostasis [GO:0010960]; maintenance of protein location in cell [GO:0032507]; membrane assembly [GO:0071709]; negative regulation of delayed rectifier potassium channel activity [GO:1902260]; negative regulation of endocytosis [GO:0045806]; neuromuscular junction development [GO:0007528]; neuronal action potential [GO:0019228]; positive regulation of action potential [GO:0045760]; positive regulation of cation channel activity [GO:2001259]; positive regulation of cell communication by electrical coupling [GO:0010650]; positive regulation of gene expression [GO:0010628]; positive regulation of homotypic cell-cell adhesion [GO:0034112]; positive regulation of membrane depolarization during cardiac muscle cell action potential [GO:1900827]; positive regulation of membrane potential [GO:0045838]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of sodium ion transmembrane transporter activity [GO:2000651]; positive regulation of sodium ion transport [GO:0010765]; protein localization to axon [GO:0099612]; protein localization to plasma membrane [GO:0072659]; regulation of potassium ion transport [GO:0043266]; regulation of protein targeting [GO:1903533]; signal transduction [GO:0007165]; synapse organization [GO:0050808] | axon [GO:0030424]; axon cytoplasm [GO:1904115]; axon initial segment [GO:0043194]; cell surface [GO:0009986]; costamere [GO:0043034]; dendrite [GO:0030425]; intercalated disc [GO:0014704]; lysosome [GO:0005764]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; node of Ranvier [GO:0033268]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; spectrin-associated cytoskeleton [GO:0014731]; synapse [GO:0045202]; T-tubule [GO:0030315]; Z disc [GO:0030018] | cadherin binding [GO:0045296]; cytoskeletal protein binding [GO:0008092]; phosphorylation-dependent protein binding [GO:0140031]; protein-macromolecule adaptor activity [GO:0030674]; spectrin binding [GO:0030507]; transmembrane transporter binding [GO:0044325] | PF00023;PF12796;PF13637;PF00531;PF17809;PF00791; | 2.60.220.30;2.60.40.2660;1.25.40.20;1.10.533.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon {ECO:0000250|UniProtKB:O70511}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q12955}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:O70511}. Lysosome {ECO:0000269|PubMed:9060470}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70511}. Note=In skeletal muscle, localized at costameres and neuromuscular junctions. In bone marrow-derived macrophages, isoforms 2 and 3 are associated with lysosomes. | null | null | null | null | null | FUNCTION: Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1 (PubMed:19109891). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368). Required for intracellular adhesion and junctional conductance in myocytes, potentially via stabilization of GJA1/CX43 protein abundance and promotion of PKP2, GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (By similarity). {ECO:0000250|UniProtKB:O70511, ECO:0000250|UniProtKB:Q12955, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:23903368}. | Mus musculus (Mouse) |
G5E8P1 | BRD1_MOUSE | MRRKGRCHRGSAARHPSSPCSIKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEVLPSTHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIINEKRKGDCVSAVSQNMFEFLMDRFEKESYCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGSATFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKTLAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRNTQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQMAMELRLTPLTVLLRSVLEQLQEKDPAKIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHAFEEDFNLIVDNCMKYNAKDTVFYRAAVRLRDQGGVVLRQARREVESIGLEEASGMHLPERPIAAPRRPFSWEEVDRLLDPANRAHMSLEEQLRELLDKLDLTCSMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQAPPTGAGTGGFEDEAAPLAPDTAEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDTGLTNGFGGARSEQEPGGGPGRKAAPRRRCASESSICSSNSPLCDSSFSTPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSNMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSEEKLFLVLFFDNKRSWQWLPKSKMVPLGVDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPASDLSDID | null | null | erythrocyte maturation [GO:0043249]; positive regulation of erythrocyte differentiation [GO:0045648]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357]; response to electrical stimulus [GO:0051602]; response to immobilization stress [GO:0035902] | dendrite [GO:0030425]; histone H3-K14 acetyltransferase complex [GO:0036409]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perikaryon [GO:0043204] | histone binding [GO:0042393]; histone H3K14 acetyltransferase activity [GO:0036408]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K5 acetyltransferase activity [GO:0043995]; histone H4K8 acetyltransferase activity [GO:0043996]; histone reader activity [GO:0140566]; metal ion binding [GO:0046872] | PF00439;PF10513;PF13831;PF00855;PF13832; | 2.30.30.140;1.20.920.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95696}. Chromosome {ECO:0000250|UniProtKB:O95696}. Note=Localizes to transcription start sites. {ECO:0000250|UniProtKB:O95696}. | null | null | null | null | null | FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a regulator of hematopoiesis (PubMed:21753189). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby promoting erythroid differentiation (PubMed:21753189). {ECO:0000269|PubMed:21753189}. | Mus musculus (Mouse) |
G5E8Q8 | AGRF5_MOUSE | MRSPRTFTFYFLLLVICSSEAALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; energy reserve metabolic process [GO:0006112]; erythrocyte development [GO:0048821]; fat cell differentiation [GO:0045444]; glomerular filtration [GO:0003094]; glucose homeostasis [GO:0042593]; macrophage activation [GO:0042116]; negative regulation of macrophage activation [GO:0043031]; pharyngeal arch artery morphogenesis [GO:0061626]; phospholipid biosynthetic process [GO:0008654]; positive regulation of phospholipid biosynthetic process [GO:0071073]; regulation of lipid metabolic process [GO:0019216]; surfactant homeostasis [GO:0043129] | apical part of cell [GO:0045177]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930] | PF00002;PF16489;PF01825;PF00047;PF01390; | 2.60.220.50;2.60.40.10;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q9WVT0}.; PTM: Proteolytically cleaved at multiple sites: one in the GPS region of the GAIN-B domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin. {ECO:0000250|UniProtKB:Q9WVT0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WVT0}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor that plays a critical role in lung surfactant homeostasis (PubMed:23590306, PubMed:23684610, PubMed:23922714). May play a role in controlling adipocyte function (PubMed:22971422). {ECO:0000269|PubMed:22971422, ECO:0000269|PubMed:23590306, ECO:0000269|PubMed:23684610, ECO:0000269|PubMed:23922714}. | Mus musculus (Mouse) |
G5E8Z2 | TAF4B_MOUSE | MPAGLTEPAGAAAPVVSSASGAVTMAPVAALPVRVEGTPVALGPVTKAPVSVCVESVAPQPLPAPVGTLVTKVVPVTALPKLGSPRLPAPQIVTVKTPGTTTIQLPANLQLPPGTVLIKSNSGQLMLVSPQQAVTGAKTTSNITPRPAVPANTQTVKICTVPNSSSQLMKKVTVAPVKNLTQIGTTVATTASSTSSGQPVALPSSVITVTPAKLVNTVSTLKSSSLGVLSTPSNDARLKAETSVAAQTALPPTVLENVKKCKNFLSMLIKLACSGSQSPEMGQNVKRLVEQLLDAEIEAEEFTRKLYIELKSAPQPHLVPFLKKSVVALRQLLPNSQSFIENCVKEVSGDVVISSCTMTTATSPVVTSTVSPVLVSGATAPRTLSVQQTLNPLAGPGVANTGVVTLHSVAPAAATGGTTAATVLLQTSKPLTTSVPNTVAAVSLQPENPVVSGAAVTLAIPSATFGEASATPLCLPSAKPAITSAGTKADKPAIGTPVQIVTQPSTLLPQAAGIPQTAKVKQLVVQQPSGSSVNHVTSISHSSPLSTQNCGQKTPVNAVMPTSSIIKQITLPGNKLLSLQAQRSSIQSNKIKENGPTCFRGEDDINDVTFMAEVNLDEENACILAAHSDFVGTLIQSCKEEPFLVIGALQKRILDIGKKHDITELNSDAVNLISHATQERLRGLLEKLTTIAQHRMTIYKGSENYILSTDTRSQLKFLEKLDQLEKQRKDLEEREMLLKAAKSRSNKEDPEQLRLKQKAKELQQLELAQIQYRDANLTALAAIGPRKKRPLESGNESFKDNPSTSGTSSLTATKPFRPRITRICLRDLIFCMEQEREMKYSRALYLALLK | null | null | mRNA transcription by RNA polymerase II [GO:0042789]; oogenesis [GO:0048477]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; spermatogenesis [GO:0007283]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF05236;PF07531; | 1.10.20.10;1.20.120.1110; | TAF4 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92750}. Cytoplasm {ECO:0000250|UniProtKB:Q92750}. Note=Export into the cytoplasm is mediated by a CRM1-independent nuclear export pathway and not by phosphorylation. {ECO:0000250|UniProtKB:Q92750}. | null | null | null | null | null | FUNCTION: Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators asond repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis. {ECO:0000250|UniProtKB:Q92750, ECO:0000269|PubMed:11557891, ECO:0000269|PubMed:15774719}. | Mus musculus (Mouse) |
G5EB19 | PPOA_EMENI | MGEDKETNILAGLGNTISQVENVVAASLRPLPTATGDGTYVAESTQTGLAKDLSHVDLKDVRTLAEVVKSAATGEPVDDKQYIMERVIQLAAGLPSTSRNAAELTKSFLNMLWNDLEHPPVSYLGADSMHRKADGSGNNRFWPQLGAAGSAYARSVRPKTMQSPSLPDPETIFDCLLRRKEYREHPNKISSVLFYLASIIIHDLFQTDPKDNSVSKTSSYLDLSPLYGNNQDEQNLVRTFKDGKLKPDCFATKRVLGFPPGVGVLLIMFNRFHNYVVDQLAAINECGRFTKPDESNVDEYAKYDNNLFQTGRLVTCGLYANIILKDYVRTILNINRTDSTWSLDPRMEMKDGLLGEAAAMATGNQVSAEFNVVYRWHACISKRDEKWTEDFHREIMPGVDPSTLSMQDFVAGLGRWQAGLPQEPLERPFSGLQRKPDGAFNDDDLVNLFEKSVEDCAGAFGASHVPAIFKSVEALGIMQARRWNLGTLNEFRQYFNLAPHKTFEDINSDPYIADQLKRLYDHPDLVEIYPGVVVEEAKDSMVPGSGLCTNFTISRAILSDAVALVRGDRFYTVDYTPKHLTNWAYNEIQPNNAVDQGQVFYKLVLRAFPNHFDGNSIYAHFPLVVPSENEKILKSLGVAEKYSWEKPSRISHPIFISSHAACMSILENQETFKVTWGRKIEFLMQRDKHQYGKDFMLSGDRPPNAASRKMMGSALYRDEWEAEVKNFYEQTTLKLLHKNSYKLAGVNQVDIVRDVANLAQVHFCSSVFSLPLKTDSNPRGIFAESELYKIMAAVFTAIFYDADIGKSFELNQAARTVTQQLGQLTMANVEIIAKTGLIANLVNRLHRRDVLSEYGIHMIQRLLDSGLPATEIVWTHILPTAGGMVANQAQLFSQCLDYYLSEEGSGHLPEINRLAKENTPEADELLTRYFMEGARLRSSVALPRVAAQPTVVEDNGEKLTIKAGQVVMCNLVSACMDPTAFPDPEKVKLDRDMNLYAHFGFGPHKCLGLDLCKTGLSTMLKVLGRLDNLRRAPGAQGQLKKLSGPGGIAKYMNEDQSGFTPFPSTMKIQWDGELPQLKEDF | 1.13.11.60; 5.4.4.5 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; | asexual sporulation resulting in formation of a cellular spore [GO:0043936]; fatty acid metabolic process [GO:0006631]; negative regulation of sexual sporulation resulting in formation of a cellular spore [GO:0043942]; oxylipin biosynthetic process [GO:0031408]; penicillin metabolic process [GO:0042316]; positive regulation of asexual sporulation resulting in formation of a cellular spore [GO:0043945]; response to oxidative stress [GO:0006979]; sexual sporulation resulting in formation of a cellular spore [GO:0043935]; sterigmatocystin biosynthetic process [GO:0045461] | null | dioxygenase activity [GO:0051213]; fatty acid peroxidase activity [GO:0047888]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; isomerase activity [GO:0016853]; linoleate 8R-lipoxygenase activity [GO:0052878]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF03098;PF00067; | 1.10.630.10;1.10.640.10; | Peroxidase family | null | null | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659; EC=1.13.11.60; CATALYTIC ACTIVITY: Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:31579, ChEBI:CHEBI:58659, ChEBI:CHEBI:63217; EC=5.4.4.5; | null | null | null | null | FUNCTION: Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively (By similarity). {ECO:0000250}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
G5EB30 | CHIA1_EMENI | MAPKLFTFVSALSGLASLASAFHAEAKSNIAVYYGQGVNQPRLAEFCAETSYDIINIGFINSFPEQNPLTGLPGSDFGNQCWADTFVVDGIASQLYSHCPNIAEDIPKCQAAGKKVFLSLGGATPTYWFDTIDASTKLADFLWGAFGPVTDAWTVADKPRPFGNAVVDGFDFDIEFFGSKGYANMIKRFRRRFGEVPDQTFYISAAPQCSIPDEQLSVAIKNAVIDFVWVQFYNTPGCSARDFVLGTKNGFNYDSWVEVIKAGANPNAKLYVGLPASGAAANLGYYLTPEEVKPLVKKYMDKYPETFGGVMLWEATQARNNQIDGVGYNEKIREILYDLDPNHPPPTTSPTPTPTPSTTTTSTTSTTSTTSATSTTSTTSTTSTTSTTPTTSTTSTTSTTTPTPSPSPSTASSSTTETVTPSPKPSPSESSTTSETSSLPSTSTPVVSETPSETKTPTSSSAPPLSSSSPVGGSSSTASSSTSTPSETPSASSTRAVSETSTHISTSTSSGPETSLTGSSTSVPATSSSVPSSAISPSSTPVISETPRPPVTSSSSSTFVSSTSTSTDCSESSTAIGTHSSSSISETPSASTPAASPSTSPETTKTLTVFPTPGSSVSTGTTSASTLSSSVPATSGGHTETSTVSTSSANQTPSASTSKPLIPTNSASSTSTGSVTSTPSAPGVPSSSAGSDETATTSTTDSEPTSTSSGSVTAKPTTTEPATTTTIIVTSYTSICPTGFTTITTTITSTYCPGTASATATAIAPTTDVPGSGSGSSPAQPTITADIPEGWTTTVTVCTVCAATPTTVTLTLPPATTTEESTSAQPTGEVPSSDGSGSGEVSTTTVVVVPAPTGNAGDGVPAPGANVGEEYTAAPGSATTSKPLIGGGASGAHTAYPYASSTFHIIPSASAHVPVPSGSGSSPSGTQGGASPTFTGAGSRYDVVKGVPALVALALSLLAVL | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | cell tip [GO:0051286]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00704; | 3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class III subfamily | PTM: O-glycosylated but not N-glycosylated. {ECO:0000269|PubMed:18420434}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18420434}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18420434}. Secreted, cell wall {ECO:0000250}. Cell tip {ECO:0000269|PubMed:18420434}. Note=Localizes at the germ tubes of conidia, at hyphal branching sites and hyphal tips. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:18420434}; | null | null | null | null | FUNCTION: GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. {ECO:0000269|PubMed:18420434}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
G5EB37 | CHMU_EMENI | MDTAIDLSDASKALDLANIRFQLIRLEDTITFHLIERVQFPLNKTIYIPGGVKIPNEQISLMDYLLRETERLQSRVRRYQSPDEYPFFPSALEKPILQPLDYPKILHDNDVNVNETIKTRYVQDILPAICPQFGGREDRGETQENYGSAATCDVSCLQALSRRIHFGKFVAESKFQKETEKFVALIKAGDRKEIDEAITDAKVEQKVLERLALKAKTYGTDPGFPEQSGPKIDVQAVQDMYKEYVIPLTKVVEVEYLMQRLKGTQWE | 5.4.99.5 | null | aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; L-phenylalanine biosynthetic process [GO:0009094]; sporocarp development involved in sexual reproduction [GO:0000909]; tyrosine biosynthetic process [GO:0006571] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chorismate mutase activity [GO:0004106]; tryptophan binding [GO:0120284]; tyrosine binding [GO:0072545] | null | 1.10.590.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:10428795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:10428795}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for chorismate (in the presence of 5 uM tryptophan and at 30 degrees Celsius); Note=kcat is 82 sec(-1) with chorismate as substrate (at 30 degrees Celsius). kcat is 92 sec(-1) with chorismate as substrate (in the presence of 5 uM tryptophan and at 30 degrees Celsius). kcat is 82.5 sec(-1) with chorismate as substrate (in the presence of 50 uM tyrosine at 30 degrees Celsius). {ECO:0000269|PubMed:10428795}; | PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:10428795}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.9 in the absence of effectors. Optimum pH is 7.1 in the presence of tryptophan. Optimum pH is 5.4 in the presence of tyrosine. Tryptophan broadens the pH range of detectable catalytic activity. {ECO:0000269|PubMed:10428795}; | null | FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:10428795). Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (By similarity). {ECO:0000250|UniProtKB:P32178, ECO:0000269|PubMed:10428795}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
G5EB89 | KAPA_EMENI | MAERYIPEHRRTQYKARNQFRPDELRRRREEQQVEIRKQKREENLAKRRGIQTRDGGIGVGGGMAAAESDDEASAIESELNVELPEMVKGVFSDQIEAQIQATTKFRKLLSKERNPPIERVIETGVVSRFVEFLRSPHTLVQFEAAWALTNIASGSAQQTQVVIEAGAVPIFVELLSSPEPDVREQAVWALGNIAGDSPQCRDFVLNAGALRPLLTLINDGRKISMLRNATWTLSNFCRGKTPQPDWNTIAPALPVLAKLIYMLDDEVLIDACWAISYLSDGPNEKIQAVIEAGIPRRLVELLMHASTSVQTPALRSVGNIVTGDDVQTQVIINCGALPALLSLLSSTKDGIRKEACWTISNITAGNSSQIQSVIDAGIIPPLVHLLANGDFKTRKEACWAISNATSGGLQKPDQIRYLVTQGCIKPLCDLLACPDNKIIQVALDGLENILKVGEMDKEAGQGDAHVNRYALFIEEAGGMEKIHDCQNNANEEIYMKAYNIIEKYFSDEDEAAGDIDELAPQQTQTGFTLGATQQQPGGFSFGGANGGDSMDM | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B6HJ92}. | null | null | null | null | null | FUNCTION: Import of proteins with classical NLS composed of one or two clusters of basic residues is initiated by binding to the importin alpha/beta heterodimer, where importin alpha acts as an adapter subunit to bridge NLS cargos to importin beta, which transports the whole complex through the nuclear envelope (PubMed:12684370). Involved in the nuclear accumulation of the light-dependent developmental regulator veA (PubMed:17163983, PubMed:19318129). Participates at different regulatory stages of asexual and sexual development, being required for the completion of both reproductive cycles with the formation of conidiospores and ascospores, respectively (PubMed:19318129). Mediates secondary metabolite gene expression with positive regulation of penicillin production and negative regulation of mycotoxin biosynthesis (PubMed:19318129). {ECO:0000269|PubMed:12684370, ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:19318129}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
G5EBF1 | SAX3_CAEEL | MFNRKTLLCTILLVLQAVIRSFCEDASNLAPVIIEHPIDVVVSRGSPATLNCGAKPSTAKITWYKDGQPVITNKEQVNSHRIVLDTGSLFLLKVNSGKNGKDSDAGAYYCVASNEHGEVKSNEGSLKLAMLREDFRVRPRTVQALGGEMAVLECSPPRGFPEPVVSWRKDDKELRIQDMPRYTLHSDGNLIIDPVDRSDSGTYQCVANNMVGERVSNPARLSVFEKPKFEQEPKDMTVDVGAAVLFDCRVTGDPQPQITWKRKNEPMPVTRAYIAKDNRGLRIERVQPSDEGEYVCYARNPAGTLEASAHLRVQAPPSFQTKPADQSVPAGGTATFECTLVGQPSPAYFWSKEGQQDLLFPSYVSADGRTKVSPTGTLTIEEVRQVDEGAYVCAGMNSAGSSLSKAALKVTTKAVTGNTPAKPPPTIEHGHQNQTLMVGSSAILPCQASGKPTPGISWLRDGLPIDITDSRISQHSTGSLHIADLKKPDTGVYTCIAKNEDGESTWSASLTVEDHTSNAQFVRMPDPSNFPSSPTQPIIVNVTDTEVELHWNAPSTSGAGPITGYIIQYYSPDLGQTWFNIPDYVASTEYRIKGLKPSHSYMFVIRAENEKGIGTPSVSSALVTTSKPAAQVALSDKNKMDMAIAEKRLTSEQLIKLEEVKTINSTAVRLFWKKRKLEELIDGYYIKWRGPPRTNDNQYVNVTSPSTENYVVSNLMPFTNYEFFVIPYHSGVHSIHGAPSNSMDVLTAEAPPSLPPEDVRIRMLNLTTLRISWKAPKADGINGILKGFQIVIVGQAPNNNRNITTNERAASVTLFHLVTGMTYKIRVAARSNGGVGVSHGTSEVIMNQDTLEKHLAAQQENESFLYGLINKSHVPVIVIVAILIIFVVIIIAYCYWRNSRNSDGKDRSFIKINDGSVHMASNNLWDVAQNPNQNPMYNTAGRMTMNNRNGQALYSLTPNAQDFFNNCDDYSGTMHRPGSEHHYHYAQLTGGPGNAMSTFYGNQYHDDPSPYATTTLVLSNQQPAWLNDKMLRAPAMPTNPVPPEPPARYADHTAGRRSRSSRASDGRGTLNGGLHHRTSGSQRSDSPPHTDVSYVQLHSSDGTGSSKERTGERRTPPNKTLMDFIPPPPSNPPPPGGHVYDDIFQTATRRQLNRGSTPREDTYDSVSDGAFARVDVNARPTSRNRNLGGRPLKGKRDDDSQRSSLMMDDDGGSSEADGENSEGDVPRGGVRKAVPRMGISASTLAHSCYGTNGTAQRFRSIPRNNGIVTQEQT | null | null | cell-cell adhesion [GO:0098609]; dorsal/ventral axon guidance [GO:0033563]; neuron migration [GO:0001764]; regulation of sensory neuron axon guidance [GO:1905489]; Roundabout signaling pathway [GO:0035385]; sensory neuron axon guidance [GO:0097374] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046] | PF00041;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, ROBO/SAX3 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required to confine migrating sex myoblasts to the ventral muscle quadrants during their migration through the body and for multiple aspects of sensory, motor, and interneuron axon guidance. {ECO:0000269|PubMed:10993679, ECO:0000269|PubMed:9458046}. | Caenorhabditis elegans |
G5EBH0 | PLCB_CAEEL | MAKEFQFNWKPTIIPELLHGSVFDRYDDESTCLELNAQVRIDENGFFLRWLIEGKDAVVLDMGQIWEARTGGLPKDGRIMFELEQRGASETIAERTIWITHGQDLVNVQSFFLVAESVELAKTCRAGINDILKSSRIRHVCPTTQLMKYHTWLTMNVNERRKIPIKLIIKTFSSGKPEKMVQKCLNDLGLGGDKYTPARVINRSMGKKFRNFYKCSRGRKRKEREELDVDILTFEKFQRLYNKICPRTEVQELFVKLSGQKEYLTKERLINFLNEEQRDPRLNEILFPFFDSQRIVALLKKHENDIKYQEDGKMSGDGFLRFLMSDENPPVFLDRIEMFMDMDQPLCHYYINSSHNTYLTGRQYGGKSSSEIYRQVLLSGCRCIELDCWDGTGENKGEPIITHGKAMCTDVFFKDVLVQIRDTAFARSDFPVVLSFENHCSKSNQLKMAKYCMDIFGDMLLSKPFEDAPLDPGVSLPSPNRLRKKILIKNKRLKTDIERHQLDQFLREGKLDEEDELNETPEVVGEDSVSPRSGGSGGTGAPEEVDDDTSDDDDDPSVQTSLNVMRTIPTVNTTSNNGSNRSARSSLDTPSPSGGSLMVPDRATSTATSIKNAVLARSPNFSSLRQKLSFKRRQSPLAGDQRAHPEVEQPVSSSSPATPSISGPPPCATSSGSTSSITITTTGCSTSSSGPSKHILGGEMPAKENDEAHPELKQNFIAKNLKGFGFSKKQPVLTKEEEERIFAEYHYTGATTNIHPLLSSLVNYTHPVKFSGFDVAEANNLHFHMSSFSESTGLGYLKQSAPEFVNYNKRQSSRIYPKGARVDSSNFLPQIFWNAGCQMVSLNFQTPDVYMQLNMGKFEYNGGSGYLLKPDFLRRPDRTFDPFSESPVDGVIAAHCSVRVISGQFLSDRKIGTYVEVEMYGLPTDTIRKEHKTKVIPGNGLNPVYNEDPFVFRKVVLPELAVLRFAVYDENGKQLGQRILPLDGLQAGYRHISLRSDTNQSFILSPVLFVQIVIKTYVPDELSGLVDALADPRAFLSEQKKRQEALAHMGVDDSDIPDVPNTRNMALRHVKQPPRQNGSSADLLANNGQTGSARGDQTSSMASSTIRSPNEQPQPVAVDKFKVDPIEVDDLRRDKAFAKLLKRFQKELDDLRKKHQKQRDSIQKQQPARRRNSSIAWIQTNVDKLITNNRRSTKKEKGSRRSLTASVSSGCGSASGTVTVSVCSPSGASCSGYSTGGPSTPVACNSDGTGSPATIGSPVPQDLVNNDRVRSLVNTQTGEWSAMVRRHDEEEFELKKVQLKEQFDLLRKLMSEAQKNQMLALKLRLEAEGKDLKQTQTKKSMEDAKVIQLDKGIKTKAERDRRVKELNEKNLKMFVEERKRLAMKAQKHEEQLTKRHLDQLEQLDKDFHKALDAEVGNYKEEQLAAQPTSVV | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P10688}; | chemotaxis [GO:0006935]; dopamine receptor signaling pathway [GO:0007212]; lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of axon regeneration [GO:0048680]; positive regulation of locomotion [GO:0040017]; protein localization to synapse [GO:0035418]; regulation of egg-laying behavior [GO:0046662]; regulation of locomotion [GO:0040012]; regulation of nematode pharyngeal pumping [GO:0043051]; release of sequestered calcium ion into cytosol [GO:0051209]; thermotaxis [GO:0043052] | adherens junction [GO:0005912]; axon [GO:0030424]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435] | PF00168;PF06631;PF09279;PF17787;PF00388;PF00387; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:10571227}. Cell projection, axon {ECO:0000269|PubMed:10571227}. Synapse {ECO:0000269|PubMed:10571227}. Cell junction, adherens junction {ECO:0000269|PubMed:10571227}. Note=Present in neuronal cell somas and axon processes of the nerve ring in head ganglia. Present in the adherens junction of intestinal cells. {ECO:0000269|PubMed:10571227}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000250|UniProtKB:P10687}; | null | null | null | null | FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) which plays an important role in the regulation of intracellular signaling cascades (By similarity). Required in the nervous system to modulate neuronal activity. Facilitates synaptic transmission at neuromuscular junctions by regulating the release of acetylcholine from the motor neurons and thus affecting locomotion (PubMed:10571228). Plays a role in efficient egg laying and defecation (PubMed:10571227, PubMed:10571228, PubMed:24212673). Involved in axon regeneration after injury (PubMed:23072806). Plays a role in male mating behavior by regulating spicule insertion and sperm transfer (PubMed:15958491). By triggering Ca(2+) transient via IP3-mediated activation of IPR3 receptor itr-1 in ASH sensory neurons, regulates avoidance behavior in response to nose touch (PubMed:19730689). By activating tpa-1 via DAG production, required for the expression of antimicrobial peptide nlp-29 in response to fungal infection (PubMed:19380113). During embryogenesis, may play a role in epidermal morphogenesis together with plc-1 (PubMed:18369461). {ECO:0000250|UniProtKB:P10687, ECO:0000269|PubMed:10571227, ECO:0000269|PubMed:10571228, ECO:0000269|PubMed:15958491, ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:19380113, ECO:0000269|PubMed:19730689, ECO:0000269|PubMed:23072806, ECO:0000269|PubMed:24212673}. | Caenorhabditis elegans |
G5EBH1 | TAT5_CAEEL | MGKRKKNDESSSSSSQKPCVSSSSDDFSVSFVRAEEDDVATTIRDKTASLKSNATHFSAASAAKGGMFDFRCCRSLFSRRRVLHSRTVRVGYGPVGHDANVTFTPNTVCNQKYNIFSFVPIVLFQQFKFFLNLYFLLMACSQFIPAIQIGAPITYWGPLGFVLTITLIREAFDDFVRYLRDRDLNSEKYEKLTRDGTRIEIRSADIEVGDVIIMHKDRRVPADVVLLRTTDKSGACFIRTDQLDGETDWKLRIPVPHTQHLPNEADIMELNCEVYAEKPQKDIHAFVGTLKITDDDNVQDGSLNVENVLWANTVVASGTAVGIVVYTGRETRSVMNTTLPESKVGLLDLEVNNLTKLLFCFVLVLSSVMVAMKGLDNLWYRYLMRFILLFSYIIPISLRVNLDMAKLFYSWQIGRDKHIPETVIRSSTIPEELGRISFLLSDKTGTLTKNEMHFKKIHLGTVAFSSDAFEEVGQHVRSAYAGRLAKHSFSAKLQNAVEAIALCHNVTPIFENGEISYQAASPDEVALVKWTETVGVRLASRDLHAMSLSVQLPNGQTLMKQFQILYVFPFTSETKRMGIIVKDETTDEVTLLMKGADTVMSGMVQYNDWLDEECSNMAREGLRTLVVARKPLSQAELEAFDRAYHAAKMSISDRSQNMANVVNRMLERDLQLLCLTGVEDRLQDQVTTSLELLRNAGIKIWMLTGDKLETAICIAKSSGLFSRSDNIHVFGNVHNRTDAHNELNNLRRKTDVALVMPGSALNVCLQYYEAEVAELVCACTAVVCCRCSPEQKAQIVQLLRKYRAPLRVAAIGDGGNDVSMIQAAHAGIGIDANEGKQASLAADFSITQFSHVCRLLLVHGRFCYKRSCALSQFVMHRGLIISTMQAIFSCVFYFASVSLYQGVLMVAYSTCYTMLPVFSLVVDRDVTATNALTYPELYKELGKGRSLSYKTFCIWVLISLYQGAVIMYGALLVFDADFIHVVSISFSALIVTELIMVAMTVHTWHWAMLLAQALSLGLYMISLILFDQYFDRQFVLSWVFISKTTAITAVSCLPLYIVKALRRKFSPPSYAKVN | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527}; | embryo development ending in birth or egg hatching [GO:0009792]; endocytosis [GO:0006897]; phospholipid translocation [GO:0045332]; reproduction [GO:0000003]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890] | cytoplasmic vesicle [GO:0031410]; endosome [GO:0005768]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287] | PF13246;PF00122;PF00702;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22100064}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000305|PubMed:30213940}; | null | null | null | null | FUNCTION: Plays a role in regulating membrane trafficking of cargo proteins during embryogenesis (PubMed:22100064, PubMed:30213940). Regulates snx-3 retromer-mediated endosomal sorting of mig-14, a transporter of Wnt egl-20 morphogen (PubMed:30213940). Together with mon-2 and pad-1, may participate in the formation of endosomal carriers that direct mig-14 trafficking back to Golgi, away from lysosomal degradation. Required for Wnt egl-20 gradient formation along the anteroposterior body axis and migration of QL neuroblast descendants toward the posterior part (PubMed:30213940). Maintains phosphatidylethanolamine (PE) asymmetry at the cell membrane and prevents the budding of ectosome vesicles that affect intercellular communication and morphogenesis (PubMed:22100064). {ECO:0000269|PubMed:22100064, ECO:0000269|PubMed:30213940}. | Caenorhabditis elegans |
G5EBI4 | CEEH1_CAEEL | MLFESIYIQCLNKFSKYKKFVCHTTCNCPNYKIIGYLLYFLCLCRPINCSLPLSRHDLAFGSFSYYLTMFLYRILVRLLQFYYFVKFSAILFLGFAVKGRSLFEKKQREKPNVLEGWDSRYIKLKKVRLHYVQTGSDDKPLMLFIHGYPEFWYSWRFQLKEFADKYRCVAIDQRGYNLSDKPKHVDNYSIDELTGDIRDVIEGLGYDKAIVVAHDWGGLVAWQFAEQYPEMVDKLICCNIPRPGSFRKRIYTSWSQFRKSWYMFFYQNEKIPEMLCSADDMKMLELCFRAKEIGIQNNKNFTDEDLEAWKYSFSMNGASFKYPINYYRNIFNAKKQQADLVLEMPTLIIWGTADGALDIEAAVDSLNTLKQGTMKKIEGASHWVQQDEPEMVNEHIKKFLNKYQ | 3.3.2.10 | null | cellular lipid metabolic process [GO:0044255] | membrane [GO:0016020] | epoxide hydrolase activity [GO:0004301]; hydrolase activity [GO:0016787] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Epoxide hydrolase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19038; Evidence={ECO:0000305|PubMed:18267101}; CATALYTIC ACTIVITY: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-(5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44048, ChEBI:CHEBI:15377, ChEBI:CHEBI:84025, ChEBI:CHEBI:84032; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049; Evidence={ECO:0000305|PubMed:18267101}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44044, ChEBI:CHEBI:15377, ChEBI:CHEBI:76625, ChEBI:CHEBI:84031; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045; Evidence={ECO:0000305|PubMed:18267101}; CATALYTIC ACTIVITY: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15-dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:44040, ChEBI:CHEBI:15377, ChEBI:CHEBI:84024, ChEBI:CHEBI:84029; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44041; Evidence={ECO:0000305|PubMed:18267101}; CATALYTIC ACTIVITY: Reaction=12,13-epoxy-(9Z)-octadecenoate + H2O = 12,13-dihydroxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:44036, ChEBI:CHEBI:15377, ChEBI:CHEBI:84026, ChEBI:CHEBI:84028; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44037; Evidence={ECO:0000305|PubMed:18267101}; CATALYTIC ACTIVITY: Reaction=9,10-epoxy-(12Z)-octadecenoate + H2O = 9,10-dihydroxy-(12Z)-octadecenoate; Xref=Rhea:RHEA:44032, ChEBI:CHEBI:15377, ChEBI:CHEBI:84023, ChEBI:CHEBI:84027; Evidence={ECO:0000269|PubMed:18267101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44033; Evidence={ECO:0000305|PubMed:18267101}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for trans-1,3-diphenylpropene oxide {ECO:0000269|PubMed:18267101}; KM=11.4 uM for 12,13-epoxy-9-octadecenoate {ECO:0000269|PubMed:18267101}; KM=7.5 uM for 9,10-epoxy-12-octadecenoate {ECO:0000269|PubMed:18267101}; Note=kcat is 12 sec(-1) with trans-1,3-diphenylpropene oxide as substrate. kcat is 0.11 sec(-1) with 12,13-epoxy-9-octadecenoate as substrate. kcat is 0.22 sec(-1) with 9,10-epoxy-12-octadecenoate as substrate. {ECO:0000269|PubMed:18267101}; | PATHWAY: Lipid metabolism. {ECO:0000305|PubMed:18267101}. | null | null | FUNCTION: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active against epoxyeicosatrienoic acids (EETs) including 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate (8,9-EET), 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate (11,12-EET) and 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate (14,15-EET) and the linoleic acid metabolites 12,13-epoxy-(9Z)-octadecenoate (12,13-EpOME) and 9,10-epoxy-(12Z)-octadecenoate (9,10-EpOME). These epoxides function as lipid signaling molecules, the enzyme can deplete the supply of the epoxide signal by transforming them into diol species that are more readily eliminated through excretion. {ECO:0000269|PubMed:18267101}. | Caenorhabditis elegans |
G5EBK1 | PBO4_CAEEL | MWIKLLFFFTTLLVSTSGLGDDGITALLDPNSTEFSTVLPSNNSEKFSYMLASVKNMNMTASEFEEFIKVLKHRQSKDHSGEHVGNEHDESHGISVVSWHWDYVKNELVLTLFFIVIGLFKLVYHHTFVTRKILPESCCLIFIGIAIGFFFVGDATHASIKFLEFKSKVFFFYLLPPIILESAYSLKDRAFIENIGTILLYAVVGTILNIVLLAAALLILIWVGIMGKYNLSVMDILTFASLVAAVDPVAVLAVFQEVGVNKMLYFMVFGESLFNDAVTIVCYNLAIEFQTLPDFTWYHGFLGLLSFLCVSIGGLIIGLICGAISSFVTKFTTDVRVVEPVVLFGMAYLAYLGSEMFHFSGIIALIACGLFQTHYACCNISYKSFTSVMYITKVCSTLCESLIFIILGVMLVNEREWFWTDWHPVFSAVSVVLCVVVRFGVTFFLTYFVNQFTGGVRHISFQEQFIMSYGGLRGAVSFSLVFMISANPDVKNTMLGATYAVILFTNIIQGSTIKLFVKWLNIRLAKKEDHFRLFIEFNNGMVQHLSQGIEDLCGDKSLSLINRMSELSKKYVRPLLEKNYTANKAKKEGKLVELNRAVAMREALNNSPSQSSFQRQHTIDEMAESGALPHDLLDEEHQGHHHHGQVHPDNEDADQRANELIKDVSSIRQLMHNPFEDCYLDRNLTHEEEKEQARLKMKKTRAFKFSSVRKTIGFFGKKKSVRRHATQQGILHSAIATIGVQSVDRPSTSTRVSVEDEEQGLTMKEMEEEHPLMTITESEETSF | null | null | defecation [GO:0030421]; lipid transport involved in lipid storage [GO:0010877]; positive regulation of intestinal lipid absorption [GO:1904731]; positive regulation of striated muscle contraction [GO:0045989]; potassium ion transmembrane transport [GO:0071805]; regulation of cellular pH [GO:0030641]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719] | basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12021279, ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:23319594}; Multi-pass membrane protein {ECO:0000269|PubMed:12021279, ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:23319594}. | null | null | null | null | null | FUNCTION: Na+/H+ exchanger which mediates the transient acidification of the coelomic space and plays a role in contraction of posterior body muscles during defecation (PubMed:18191228, PubMed:18291648, PubMed:23319594). Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells (PubMed:25849533). {ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:18291648, ECO:0000269|PubMed:23319594, ECO:0000269|PubMed:25849533}. | Caenorhabditis elegans |
G5EBL2 | MES1_CAEEL | MKIHHFLTLLCTFLPLTTTALTNSTPLSLLGPCYKRCVTKFGETKEQLTNAETISLEYDVSNNTEFSLCKLGCNSHEYTDLNLAAFRYGQLAYQKILTTVEDVPTRGTVLNDVFIVCLDTSFMPSNNSAPSAKRLLSGTVLLVLDEDVAKADNVFLIEVLARNADKSAVQVISQQWCYSSNCNITFNAPTEVSSFDVRLRVSTFDSNGQVGGINFSKWHNINQILTKTFVDMSLKSVVWKAEKAAANFVFNLTASDHVPACSLQMIYRSSLSSELLHRNFYLDHTLEVFVNNLDFDKIYTMQLAPSGTHDRSTPSLASAVIEIPPCRHLVDDYSMCAPPPVSSLSYNWNLSPTSEYELLIKWKLLNYMDGLNVTEELSIPVAYFLLNAHPLITANNEQCEKYEKIRRVVSYGLRELVFHVPDTDCNYEVEMTAVDTNQRISEVKKIQVFRFNVPPYVSFLQASDIPTSVELMAVVLATSAIFALIALFLLYRKRKRDKKARFQMYKDAEAGVSYDYVATTESLGSVVQIRSTNFRFEPVENIDGNIEAALAQQQKFEGGTMNSMFRTYYNLDHPVKVPAHMAEASSDEDNGYENIRYSYFGSELSDDVFEEDIYMTHKSLSIYCQDSPLTTPMAPIAPYEHFDDIPSHQYRNFQVHNFNERIEKQAYWLMATVVDVVRRELYSLKVPKDYTPETISAMRKELEFLRTLAPHGNCRRFEGVVIGRWDDLPRQVIGILIENTRGGTLRNYIAAVGSVFRNCSLATDHDSFASQQDMNSTQHPFDKLSTEADENNSKKVKIQEITDSLSIRFCQFAEQVSSALEHLHSAGSVHTRVTTLNIYLLHNYSDPFDMLPDQVVKLGNFGFAVQNSEDVVLDDNLQPPEVIKGEKYEARGDIWQFGLCLAEMCSLGDLEQSEVGTLKSGHDTFKNLPSTQVLRDAAKRCLSARTRPSASDLCGVFKSVNVAATV | null | null | asymmetric cell division [GO:0008356]; asymmetric protein localization involved in cell fate determination [GO:0045167]; cell fate specification [GO:0001708]; developmental process involved in reproduction [GO:0003006]; embryonic digestive tract morphogenesis [GO:0048557]; establishment of mitotic spindle localization [GO:0040001]; establishment or maintenance of cell polarity [GO:0007163]; gamete generation [GO:0007276]; left/right axis specification [GO:0070986] | centrosome [GO:0005813]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713] | PF07714; | 1.10.510.10; | Protein kinase superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12110172}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes at the site of contact between EMS and P2 cells in the 4-cell stage embryo, between P3 and E cells in the 12-cell stage embryo and between P4 and Ep cells in the 26-cell stage embryo. {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12110172}. | null | null | null | null | null | FUNCTION: During early embryogenesis, controls asymmetric cell division and the asymmetric localization of P granules of germline precursor P2 and its descendant P3 (PubMed:7555722). Probably upstream of tyrosine kinase src-1, plays a role in endoderm development by controlling spindle orientation during EMS blastomere cell division (PubMed:12110172). Controls EMS spindle orientation probably by promoting lin-5 and gpr-1/2 enrichment at, and let-99 exclusion from the junction between P2 and EMS cells (PubMed:12730122, PubMed:14534135). {ECO:0000269|PubMed:12110172, ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135, ECO:0000269|PubMed:7555722}. | Caenorhabditis elegans |
G5EBL3 | SDC2_CAEEL | MSDESELGNQSEMESFNESDSPDEADPDVVIIHDIVHLRASTTGDYSQSEIGKLPEQNTFFLPGRVKRNISSNDSDVIIDEDEIPDGAIRITSDTHFIGSSRGTSELGDFEMDEQEFLNITIEENGNEQELEEHLRNAYRHEEEECFEEEDDIIELPPLPVKPAVKKPRRKLPKHLSIESGSTAKTSKLVAEVVHDHPRPVNYRMKPAVTDDGKVVEQKRTRVTRNIMSHTIPQYHLEGEETEFGRVKESTLSKTIEQYLQAGKLVSPKCDQFREQIVATAVEYDGSVKMLQFENALKKHSGKQKRLKYQTGWWKASKSHYERAVNGYVAMPKTPVLSISDDPVLYKHHSLFPKNQSSELEKINVQLRIRLNSKRQNNDVIPDSSYFVREFLMQKHSISLRMNRSSDLPELFVPPTLECGYFPQDAVTVQQQEHYLMMRFEEAQDEYHNITYRSIAPPVEFQVGTISAKELHKFHRIGRHIHGFFVVWENKFPEYDESGICCPRKRYLVDMFNLICFPLYTEYEQWESRLRVAFDKTIVYNLHLSEILRCNRPVFDFLSKNKSMLQPITLKEIVYLIEQSNMDAKSFAVKFGLRTFYDHGRATSNKDYLSAFLIITGGAKVVTEEIDSERLRVFNSDYMESGVLTSSGDVYTFEFDKIPNNYQISIGCNADGVAEMEQEDVRHELSECSSRITRIIGDSKKPEKIIARPLVKTNQNDGMKFFTRKDLLNYRIKLYDPSYVVPRAKKQIVNEPAKKKPGRKSKTRYDAAMQQNNFEIEGVPSDVDSEFEGYLSDSENVFQKPSKLMRSTSSDSVFIDYQYREKMFLDVSWFHQQKMIDRSLPPLKKRKRKMNRIYHKHSVRYTMLQANGCAFTEMYRCYDKILPCGTKEIARTKNAIRFPHRFRTYNIPQVYGPGDKQLITEVFGVVKDVITRATGFESASIRTANDIAQAVYDANIARRELLENLEPSDNGILPSPAYLAIEMLSHQKMSGRLCLESARKDVQNNVDKMYNDYMDLDPLDKELHFEISQSIRQSKLNESLEEYERNRERQLAKTLKTVPMDKRSQAALARREEKRRESRRKLADKYAEQRRMMASTRRLEKRTTQKQVDPETIQRLRREDEVRKRKRFEEEDRRGMIRRREERVALQEKVDRMLEEGLRLEKVREAERIRQQQEEERIEMETILISRRVREEEEEKMRLERLRKAEREREQERLKREEEEERKRLEQLREAEKLKAEIEKENERKLQEERTRKALELERKIEEIKRVSTLKDMFGPLPIAKENEQTEKDFQILLDDHELTLLTISRDPLNEKYQEARTEFERLDIKSMLLRKAEKLIDVLTIHYDVPIEQTCRYFTSSIESNENRMAVNEQLNKLFENMANCFTFNIQDGENGLQSKRKWDFQFKKCAVFDGVSQSTVNFIEEKMRENTKKKHLATPKTVISIDTSLLKQSLLRSHARFDPDISLYAQNHTANSIGDVTLKMSNYSLDFATQSIHDKELAEKATPKKGPTVRRHIKNLFGSEKVIVRRSLAAGKPASLNSEDSDSEDSREGSPVAEFLPTNPVCSFWKLVVKIENSTTDKEKTELCEDLDKLILRKDDLFSKSLKWMFPLLATFYVLLSNAVLNENEEIISDKNQTGVTKDEILKSTINDLMIIAAYFEEGSRERSNLRKMISMNGFSVVFNRVILFAKKTCTLAKELESNSRSLSGYVIEDLFESLLAEIERTMRQELGSSVRKTGKLERDFEEIVKLIQNEKKLALSHKSHKNDENRRFRLNTVVKWYDAIICHCKEELTQAIVDAFPLNAITKNKETSHVAMENGDDEAMLSDTSDNQMSTTDYQMPKNICRNSEIFPEDAFAKAYAVVRIPSKKERAQMLSVYRKKNAQSGCVENKGLSRMPKFEEPFVDSVWRTIEKRINNMTHSEEKQIKRFIPVSRSHKLNEKVKFYAMVMIQERDSRDTRLFNSKFQDDNLWHCYSKSSLNHEKMESRILQHIEHTVLSKSNFNQMKWSVQCVNGNKKDAIHYFTDLYKYRSESEFRSALSCGKLKFNFKVYTHLWFMGNLLPTSYNPDSHDDKLFVPCSGCTSGDVIIIHKCTCAYHNDTFSDKFIYANTSLPVGIDKVTRLVGRFVCEHGPSSFLILEHCSANVDANIPFESENVEFSAELRIVKRKTMHSQLVKTFAEEHTHLRDASRHRAISTVTLDSSGSGRSTRCEIFEDSPSEDENDENQLDTTRIGRKIDPIIVDSDKAYLIAEGERMALRIKRLLDPELQKFRSKNFVSRSKSVDAPKTSKQKTVIRRSQSVCDLNDVNEYAQKKVRNTKDSFATLFRDHEYSTRRTYEEQLNNELLDVVTTFGGASNVSADKKYNILASILAFEKEVQLVNDKNGELFKTVSNLVQRNSLQHVKGVILAEDNQTLRSTDNTSEVFPESKAVNEYLKFEIYKRKMMVNAKLMADTVKDLKLKHAEYRPFAKLIATYDSIFKFNVYLFEHFLNCISKHVFNPYAIYCEETRPTGTELSKFQLTLKLIETSMPTVLSMLFNTEPLRRQLSELSEIHKKVRSEDLACTIASLCRYAIERIRIPQTADKRLCDFSWLNSAEDHRETVSFIRLTLEHTLPDMKTENEQTRFVEFLKEAEGFHFSYKFVEAQCKTFVRNHGDSKQAFFTAFYNQNEAFYGSLQKFMSNGTIDPKMKLYYQHQAFLRLHNIVKKRSHIITSDDYHRSSDVCKAMLLSEIVSNPKIAQEAYISGSVLDRMYTSLCKIKAKMPLISPSYIGTSLTCFEDELLFSAVREAKVHTDTRVVFRSKSCMRPNEKAGDANFKTCKVTLLVNLETALLSMVFKSRDQSEIDKDDRLDIDILDEEVIKPIIDWNRIFETFIQPTYNTLFSRMEKRERVSILPENPLGRLENYAFTNPNQDKDCQAVLEYIDVASDTDAEESIEDPLDIVEMTLKRALPRSMSPSSKRRRMR | null | null | cell differentiation [GO:0030154]; dosage compensation by hypoactivation of X chromosome [GO:0042464]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; sex determination [GO:0007530]; sex differentiation [GO:0007548] | nuclear chromosome [GO:0000228]; X chromosome [GO:0000805] | null | null | null | null | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:10364546}. Note=Localizes specifically to X chromosomes in hermaphrodite (XX) embryos. {ECO:0000269|PubMed:10364546}. | null | null | null | null | null | FUNCTION: Component of the SDC complex that functions in sex determination and in X chromosome dosage compensation specifically in hermaphrodite (XX) animals (PubMed:10364546, PubMed:2759421). Required for the recruitment of the condensin I-like dosage compensation complex to the male sex-determining autosomal gene her-1, thereby contributing to its repression and initiating hermaphrodite sexual development (PubMed:10364546, PubMed:11937488, PubMed:14660541, PubMed:2759421). Plays a central role in X-chromosome recognition and in the recruitment and assembly of the dosage compensation complex and the dosage compensation protein dpy-21 onto the X chromosomes in hermaphrodites, which leads to a reduction of X-linked gene transcription and an equalization of X-linked gene expression between the sexes (PubMed:10364546, PubMed:14660541, PubMed:8939869, PubMed:8939870, PubMed:9056777, PubMed:9458050). May confer protection against toxicity induced by heavy metals such as arsenite (PubMed:25204677). {ECO:0000269|PubMed:10364546, ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:25204677, ECO:0000269|PubMed:2759421, ECO:0000269|PubMed:8939869, ECO:0000269|PubMed:8939870, ECO:0000269|PubMed:9056777, ECO:0000269|PubMed:9458050}. | Caenorhabditis elegans |
G5EBM1 | CSP1_CAEEL | MVLKTIEDNCKSQFDDDLVEDFNNFQTTSSMSSSTTISTEDFNTIEIESTFEICRSGSYTEEPILGENDEFLIDFEMERFLKFLKDKTKQVEKRKEPFSQKEIYAVFQRRIKSELCIETVKKKFQPLLPNAIQTCEFDEETMIRMIYGAGIRIDSVDFWNRFTSKATISLDCYSRLISYSSDSLTLSGTHRSGFTYHWISTPPVTYHRTENKDPNIQEPSPVEFLDVQSSLGSSMKPPILDKPTKLDDPAETRHDCSYSLEEYDSQSRMPRTDAKKSNHKHKYCYEMNSNPRGTVLILSNENFKNMERRVGTKQDEVNLTKLFQKLQYTVICKRNLEAESMLEAIKEFAEMAHTDSIILFLLSHGDGAGSVFGIDDMPVNVMEVSTYLAYHQNLLLKPKWVAVSACRGGKLNMGVPVDGLPALEDKCAPISKFWNLMMSRIMPGTFTSLNADVIISFSTTDGFTSYRDEEAGTWYIKSMCKVFNKHSKTMHLLDILTETGRNVVTKYENVQGNVVLKQAPEILSRLTKQWHFSRSM | 3.4.22.36 | null | activation of cysteine-type endopeptidase activity [GO:0097202]; apoptotic process [GO:0006915]; negative regulation of cellular response to manganese ion [GO:1905803]; positive regulation of apoptotic process involved in development [GO:1904747]; positive regulation of cellular response to gamma radiation [GO:1905845]; positive regulation of neuron apoptotic process [GO:0043525]; protein autoprocessing [GO:0016540]; protein processing [GO:0016485]; proteolysis [GO:0006508] | germ cell nucleus [GO:0043073] | cysteine-type endopeptidase activity [GO:0004197] | PF00656;PF04435; | 3.40.50.1460; | Peptidase C14A family | PTM: Autocatalytic cleavage removes the propeptide and generates the two active subunits p16 and p14 in vitro. Cannot be cleaved by ced-3 in vitro. {ECO:0000269|PubMed:9857046}. | null | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.; EC=3.4.22.36; Evidence={ECO:0000269|PubMed:9857046}; | null | null | null | null | FUNCTION: Cysteine protease which, in vitro, cleaves itself and caspase ced-3 into their mature active forms (PubMed:9857046). Also cleaves, in vitro, inactive caspase csp-2 isoform b (PubMed:9857046). Required maternally to induce apoptosis in a subset of cells fated to die during embryogenesis, mostly independently of the ced-9, ced-4 and ced-3 canonical apoptosis pathway (PubMed:23505386). Involved in the degeneration of dopaminergic CEP neurons in response to high Mn(2+) levels (PubMed:23721876). {ECO:0000269|PubMed:23505386, ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:9857046}.; FUNCTION: [Isoform a]: Dispensable for regulating apoptosis during embryogenesis. {ECO:0000269|PubMed:23505386}. | Caenorhabditis elegans |
G5EBN9 | SNF3_CAEEL | MGTSEHVPLPTDEAKAKELEQSQHSEEPDRGQWTGKFDFLMSMVAYAVGLGNVWRFPYLCYKNGGGSFLVVYMIFFCLAAVPIFLMEVTVGQYLQKGAMEMWLMCPLFRGVGIGNVVIAFMCIAYFCVIVAWAMFYMISSIAWVFPWETCNNYWNDATCVTGKENFTELARIKALVASAGGHTQTSVEQFWEKRVLHDTGDISEFGGIQWELFFIMAAAWLIVYFALWKGITQARKFVYFCALFPYVLIFILLIRGLTLEGAGTGIYFYLKPNATRLLDTAVWKDAGTQVFYSYGVGFGALIALGSHNKFNHNCFKDAITMCFINGCTSITAGFAVFSILGYMSHVAQKDISEIVKPGVGLAFLAYPEVASNLPMKQVFAVLFFLMITILGLDSQVCMMEGLFTALEDAFPILRKYKKQSLGIFCLFFFCIGIPMVTHSGSHWLTLFDAYGASGYALLFVVFFEVVGLAYGFGAHNIRKALHEMIGVTLPKGIEYVWKFCAPATSLVLFVFCVVYYHPVKYPDGKDFPFWANAFGWFLSSCSMVVIPGYAIYYLFFTNKHLTLKERVRKGLNLDGSFESPAKKNLVNNAEELKFIESSSQ | null | null | amino acid transport [GO:0006865]; amino-acid betaine transport [GO:0015838]; neurotransmitter transport [GO:0006836]; sodium ion transmembrane transport [GO:0035725] | neuron projection [GO:0043005]; plasma membrane [GO:0005886] | amino-acid betaine transmembrane transporter activity [GO:0015199]; gamma-aminobutyric acid:sodium:chloride symporter activity [GO:0005332] | PF00209; | null | Sodium:neurotransmitter symporter (SNF) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24212673}; Multi-pass membrane protein {ECO:0000305|PubMed:24212673}. | null | null | null | null | null | FUNCTION: Betaine transporter dependent on Na(+) and Cl(-) ions that functions primarily in the epidermis to clear betaine from the extracellular space. Elicits current in response to betaine but not in response to GABA, L-carnitine, sarcosine, glycine or dimethylglycine. {ECO:0000269|PubMed:24212673}. | Caenorhabditis elegans |
G5EBQ8 | CHS2_CAEEL | MMNTLDHRPLGRMETMEGKPDEDEVPTSSNSDAKGKGYYYSSGTVPTDDSTLEEKCQQKTFDPSCPTPKTPVIVPNREFDPNFSTVTENKGWDIFRLLPPKPDRLGHGFWHDASLQVLKLATFLVLFLLTLGSAVVAKSTFILMTSAIGWGGQTITICNQVISEATQNTVKLKNAHVVKWVWATLLALSAPEALCFVRSMHRTMFRNVKRPTFIQFVFVLIIETFHSIGVGILVFRIFPDLDAVTAAQLTNAMCFVPAILSVISRKPNKSALLLVIIDFAAIAAQSSGFWALPMFLPNLQKHLVAIPVSLTLISLAWWQNFVHRDSVFPPVRTLAKFAQRLSERRSKTYAFVSLWKICIYVVCCFLFISSRMKIEDMLQKDPFGEKLLSVAGHDMNQTQIEKFQLRINQMIEQANREAGFYAAAEKKKQPPKKQPKADEAEQVDAGEYMMKRFKRFIGDAGENEEEEPEEEEFSSYNIYSNYVERNQLTMAYDALWLVIFQFGAVFVCYHSSKFACKVMMQRMGFALPMALSVPVTVLLLSTNCRMRQKDSCYGTNVLTVELFWQCNGASMSLADFILTPQTWIWLCWLASQFWITIHLWNPKHERLAKSEKLFILPYYIGAFVDQSLAFNRRRDDKAKIKAEDLEFDAEDSSLTYETIPGLQNKTPPSVCSASSSKLENGLIRDSASSADAITKIYACATMWHETGVEMTCMLKSLFRMDEDQCARRNAQKYLKVIDPDYYEFEAHIFFDDAYDVNEYGEPEINKFVKQIVNVIDQAASAVHQTQMRLKPPKKAKTPYGGKLTYIMPGKNKLFIHLKDNQKIRHRKRWSQVMYLYYLLGYRLMMKVDDPSRKEIISENTFILTLDGDVDFTPSSVYLLVDLMKKNRRLGAACGRIHPRGDGAMVWYQKFEYAIGHWLQKATEHMIGCVMCSPGCFSLFRAYALMDDNVARRYALKSEEPKHFIQYDQGEDRWLCTLLLQRGYRVEYCAASDAQTFAPEGFNEFFNQRRRWIPSTIFNIMDLLKDYRNVVRVNESISIWYIIYQLVMLISSILGPGTIFVMIIGAISISFSIDTLISLVIVSIPVVVFIVVCLTAKPEHQLICAQTIGAIFAMLMTAVVVGTSLQLQKDGLLSPHSMFTVAVATSFLTAAILHPLEFTCIIPGTIYFLAIPCMYMLLPIYSVCNMHTVSWGTREDPRPTEKNTLAKKTPGNLESGDGAGNSENWCTRFLCCGRGTVHPMTMVINEKLNEVIKKVDRLDRKHHPSLARRASILSSTGGTIQIDKCSEADEDEQAEIEDALEMSNQSHAAKKNQKWKQAQSEAWLADKALKRAEREYLEPEEESFWNDVIERYLSPLIMDGKDMDRLRAGLIAIRNSHTVYFLMINIVFIISVLVLQIHKDCLNIEWPLGPKFNHTVRPCYANHDDNQKEEVWVMTRLQLEPIGLVFLIFFVSILVIQFLAMLCHRFGTLAHIIASTELFCFRKTMDRLSEDELVAQNAVEIARELQAIRGIDENAHNIDNPTEDRGISRRRVVQNLESSRKSMMKRKTETLDAAFKKRFFALSSEQTPDPAGFSARDNSKRLTLRKGTIRALEHRRDSLFGTLDNRKDDEVDATSMRGPAQRRLERLFTAQQDQNSPTSDGNRRKSNSRPWDQPTSSATSSGDVELRRF | 2.4.1.16 | null | cell wall chitin biosynthetic process [GO:0006038]; chitin biosynthetic process [GO:0006031]; positive regulation of nematode larval development [GO:0061063] | cell periphery [GO:0071944]; cell septum [GO:0030428]; plasma membrane [GO:0005886] | chitin synthase activity [GO:0004100] | PF03142; | null | Chitin synthase family, Class IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16098962}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evidence={ECO:0000305|PubMed:16098962}; | null | null | null | null | FUNCTION: May be involved in chitin synthesis in the pharynx during larval development. {ECO:0000269|PubMed:16098962}. | Caenorhabditis elegans |
G5EBR3 | GLUCL_CAEEL | MATWIVGKLIIASLILGIQAQQARTKSQDIFEDDNDNGTTTLESLARLTSPIHIPIEQPQTSDSKILAHLFTSGYDFRVRPPTDNGGPVVVSVNMLLRTISKIDVVNMEYSAQLTLRESWIDKRLSYGVKGDGQPDFVILTVGHQIWMPDTFFPNEKQAYKHTIDKPNVLIRIHNDGTVLYSVRISLVLSCPMYLQYYPMDVQQCSIDLASYAYTTKDIEYLWKEHSPLQLKVGLSSSLPSFQLTNTSTTYCTSVTNTGIYSCLRTTIQLKREFSFYLLQLYIPSCMLVIVSWVSFWFDRTAIPARVTLGVTTLLTMTAQSAGINSQLPPVSYIKAIDVWIGACMTFIFCALLEFALVNHIANKQGVERKARTEREKAEIPLLQNLHNDVPTKVFNQEEKVRTVPLNRRQMNSFLNLLETKTEWNDISKRVDLISRALFPVLFFVFNILYWSRFGQQNVLF | null | null | chloride transmembrane transport [GO:1902476]; locomotion involved in locomotory behavior [GO:0031987]; protein complex oligomerization [GO:0051259] | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | extracellularly glutamate-gated chloride channel activity [GO:0008068]; glutamate binding [GO:0016595]; identical protein binding [GO:0042802]; neurotransmitter receptor activity [GO:0030594]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Glutamate-gated chloride channel (TC 1.A.9.4) subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q94900}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q94900}. Cell membrane {ECO:0000255, ECO:0000269|PubMed:21572436, ECO:0000269|PubMed:25143115, ECO:0000269|PubMed:7935817}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:21572436, ECO:0000269|PubMed:25143115, ECO:0000303|PubMed:7935817}. | null | null | null | null | null | FUNCTION: Glutamate-gated chloride channel subunit; channel properties depend on the subunit composition. Glutamate binding triggers a rapidly reversible current in heteromeric channels formed by glc-1 and glc-2, while the anti-helmintic drug ivermectin and other avermectins trigger a permanently open channel configuration. Channels containing only glc-1 are activated by ivermectin, but not by glutamate alone (in vitro). The heteromeric channel formed by glc-1 and glc-2 is also activated by ibotenate, and it is blocked by picrotoxin and flufenamic acid (PubMed:7935817). Plays a role in the regulation of locomotor behavior (PubMed:16527366). {ECO:0000269|PubMed:16527366, ECO:0000269|PubMed:21572436, ECO:0000269|PubMed:7935817}. | Caenorhabditis elegans |
G5EBT1 | SMA5_CAEEL | MVFADFLEKIKSLFAKTKDPITSMSPPQENRSPKAEYLNNFFNTNPTNGKSRGSQEAPRKPLGQTNLNVQGSMPAKKEGFNRVLDGLKKRQLQHDFKLERAAETYEPTQNIGSGAFGIVCEAVETSSNQKVAIKKVAHASATPTLARRTLREIRVLRYINHPNIVPLRDIFRTKGPLGIDVFLVMDLMQNNLHHIIYGNEDPLEEHYINAFLGQLLRGLEYLHAACIAHRDLKPSNLLVNQDGTLRIADFGMAKCADNSSKKHDDEEHCYYMTQHVATLPYRAPELLFVLPEHSTAVDMWAVGCIFGEMVIRNEILPGRSVQGQIKMLLTMLGQPPQEVINEVRCDRTRKLIQDFGRKADAEWDDIMFCKARGDDQIVRGNCDTIDFVKQLFQYDAQKRINIQDALLHPYIQRVIPAEAPQKKCPFRVKKDMMQVEDLNHQELISMMKQDVRSAENPITYSELHSGDSTGSTSDMSTNTSGEYSPIAQHEQLLEDVATQISICEPTCDL | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13164}; | cell population proliferation [GO:0008283]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; intracellular signal transduction [GO:0035556]; nematode larval development [GO:0002119]; organelle localization [GO:0051640]; parturition [GO:0007567]; phosphorylation [GO:0016310]; positive regulation of cell growth [GO:0030307]; positive regulation of cell size [GO:0045793]; positive regulation of multicellular organism growth [GO:0040018]; post-embryonic development [GO:0009791]; regulation of multicellular organism growth [GO:0040014] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; 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 | null | null | 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:0000250|UniProtKB:Q13164}; 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:0000250|UniProtKB:Q13164}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in the postembryonic regulation of body size, mainly through control of cell growth. In particular, controls the volume of intestine, muscles and hypodermis. In addition, regulates growth, intestinal granule distribution, lifespan and number of offspring. {ECO:0000269|PubMed:15944183, ECO:0000269|PubMed:17535251}. | Caenorhabditis elegans |
G5EBU3 | MMPC_CAEEL | MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSSGGGSRTTARPTTTTRSWFGRFFGDDDDDVRSRTTTRRTTLWPTTQSPFSGDDWGSGSGSSGRGGSSSGSSGGGCPSHIDAYTPSSSFSYAFSGSQVYTISGTKVTKVQSIHDLFPSAPTPVNAALWNPISGSMLLFSSNRVYSYYFSNIRQIFQMDSGFPKTLPSDLGFSVSGALRWINGHQILMSSGDEFAVYDEFWNQVTLKNRISSYFPNLPRGVKGVESPAGSVITAFTSNQVFEYNSRTKSIGRQSGFSSYIAC | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P03956}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; 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;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. | null | null | null | null | null | FUNCTION: Metalloproteinase. {ECO:0000269|PubMed:9573338}. | Caenorhabditis elegans |
G5EBU4 | ZAG1_CAEEL | MVDIAEAMPTTASSLPSDEALRKFKCPECTKAFKFKHHLKEHIRIHSGEKPFECQQCHKRFSHSGSYSSHMSSKKCVQQASPSMVTPFNPYQLMMYRNIMLQLQTPQVSFLPSTAANNMDYMSLLQANLFQSLENGTSPTPTQEPSAPASPEPKIEVVDEPEVSSEVKTEVKTEVKTEDSVPEESITPAVSMSLSPAPEQNGNESMNNGGSGSDGKSSPDWRPLRSRSFLNDSQVAVLQNHFKRNPFPSKYELSAVAEQIGVNKRVVQVWFQNTRAKERRSNRLPSMPRGSVASAAAAAATSPTVWQTPVQLMAAWASQFSNGNNSLTASQDERNNENTDEVMDHDGLKDGKETPLDLTLSTDDTEPEWSPEKLIGFLDQTGGVIQELLRQAGNGFVTNQEDEEEKPIKAEESPVSSGSSSIWPSFIGQYPSILDSASLSVLEKALDQQKSSEDDASSLCSNESKLLKFPTTPLKEEEGLFSCDQCDKVFGKQSSLARHKYEHSGQRPYKCDICEKAFKHKHHLTEHKRLHSGEKPFQCDKCLKRFSHSGSYSQHMNHRYSYCKPYREQPASPSDVLNGGSVTVSPSSSNTPPPST | null | null | axon guidance [GO:0007411]; dendrite development [GO:0016358]; larval development [GO:0002164]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron fate specification [GO:0048665]; positive regulation of axon extension [GO:0045773]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046;PF00096; | 3.30.160.60;1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12835394}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:12835394, PubMed:12835395, PubMed:25474681, PubMed:30291162). Down-regulates expression of genes involved in either the synthesis or reuptake of serotonin, dopamine and GABA (PubMed:12835394). Acts as a transcriptional repressor to regulate multiple, discrete, neuron-specific aspects of terminal differentiation, including cell migration, axonal development and gene expression (PubMed:12835394, PubMed:12835395, PubMed:25474681, PubMed:30291162). Promotes touch receptor neuron differentiation by repressing the expression of egl-44 and egl-46 (PubMed:30291162). As egl-44 and egl-46, probably acting as a heterodimer, repress expression of zag-1 in FLP neurons, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates (PubMed:30291162). Required for axon guidance (PubMed:12835395). Involved in the proper development of the pharynx (PubMed:12835395). Required for pharynx isthmus peristalsis, probably via a role in the differentiation of the M4 cholinergic motor neuron (PubMed:25474681). Directly represses its own transcription by interacting with conserved E-box sequence motifs 5'-CACCTG-3' in its own promoter (PubMed:12835394, PubMed:12835395). May also act as a transcriptional activator of the homeodomain ceh-28 (PubMed:25474681). {ECO:0000269|PubMed:12835394, ECO:0000269|PubMed:12835395, ECO:0000269|PubMed:25474681, ECO:0000269|PubMed:30291162}. | Caenorhabditis elegans |
G5EBV0 | EGL9_CAEEL | MSSAPNDDCEIDKGTPSTASLFTTLMLSQPSSSTAVLQCTYCGSSCTSSQLQTCLFCGTVAYCSKEHQQLDWLTHKMICKSLQTSGMVPSNLMPQAAPAVMAPIPPTVSFDDPALTTSLLLSLQNNPILNQTISNFPPTFSITSKTEPEPSIPIQIPQRISSTSTVPFSSEGSAFKPYRNTHVFNSISSESMSSMCTSHEASLEHMSSASLAMFPTSSTAQSDISRLAQVLSLAGDSPASLALVTTSVPSTASTATIPPPATTTSSATSSGKSETITVGKEKIIQTDDPDIQIIETEGGSKPTVSRTRKRPTPSNSADPKINYKDHNKNVVYSTTLQEHQKHLQNRGLALSIHQAMVLRLRYIAEHVIRSLNEFGWAVVDNFLGSDHYKFTAKEIERLYERGLFSPGQLMEAKHKDEFHIKDIRSDHIYWYDGYDGRAKDAATVRLLISMIDSVIQHFKKRIDHDIGGRSRAMLAIYPGNGTRYVKHVDNPVKDGRCITTIYYCNENWDMATDGGTLRLYPETSMTPMDIDPRADRLVFFWSDRRNPHEVMPVFRHRFAITIWYMDKSERDKALAKGKESDAACASKKENDPTSSSLNSLIGSLLRPRKNPSTHDLSKLDLRLFPSTSSDPALVSAADEDRVDISADFQSTSSLAHPESTDSGVSLSTFNVAHNHMERTTSLQSISDHFRSERSHERRSSTSSDQDLDEGLPPPPSTNPEYYI | 1.14.11.29 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:19737748}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:11595184}; | cellular response to hypoxia [GO:0071456]; regulation of protein localization [GO:0032880]; response to hypoxia [GO:0001666] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleus [GO:0005634] | ferrous iron binding [GO:0008198]; hypoxia-inducible factor-proline dioxygenase activity [GO:0160082]; L-ascorbic acid binding [GO:0031418]; peptidyl-proline 4-dioxygenase activity [GO:0031545] | PF13640;PF01753; | 6.10.140.2220;2.60.120.620; | null | null | SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:22252129}. Nucleus {ECO:0000269|PubMed:22252129}. Cell projection, dendrite {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes throughout the ventral cord dendrites. {ECO:0000269|PubMed:22252129}.; SUBCELLULAR LOCATION: [Isoform c]: Cytoplasm {ECO:0000269|PubMed:22252129}. Nucleus {ECO:0000269|PubMed:22252129}. Cell projection, dendrite {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes throughout the ventral cord dendrites. {ECO:0000269|PubMed:22252129}.; SUBCELLULAR LOCATION: [Isoform e]: Cytoplasm {ECO:0000269|PubMed:22252129}. Nucleus {ECO:0000269|PubMed:22252129}. Cell projection, axon {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes in puncta (which probably correspond to endosomes) along the ventral cord. Localization to puncta is regulated by oxygen levels. Co-localizes with lin-10 in puncta. {ECO:0000269|PubMed:22252129}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29; Evidence={ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:19737748}; | null | null | null | null | FUNCTION: Cellular oxygen sensor which regulates the stability and the activity of hypoxia-inducible transcription factor, hif-1. In normoxic conditions, hydroxylates hif-1 targeting it for vhl-1-mediated proteasomal degradation (PubMed:11595184). In addition, regulates hif-1 transcriptional activity in a vhl-1-independent manner and independently of its hydroxylase activity (PubMed:19737748). By regulating hif-1 activity, controls several cellular responses. Mediates susceptibility to B.thuringiensis and V.cholerae pore-forming toxins and enteropathogenic E.coli (PubMed:16091039, PubMed:20011506). Mediates susceptibility to P.aeruginosa PAO1-mediated killing by regulating resistance to cyanide produced by P.aeruginosa (PubMed:10611362, PubMed:11591663, PubMed:20865124). Mediates resistance to S.aureus-mediated killing (PubMed:22792069). In addition, plays a role in heat acclimation, neuronal development, behavioral responses to reoxygenation and hydrogen sulfide, iron homeostasis and aging (PubMed:12686697, PubMed:18477695, PubMed:19372390, PubMed:22396654, PubMed:22405203). In neurons, involved in mitochondrion fusion during reoxygenation (PubMed:24385935). Involved in egg laying (PubMed:10611362, PubMed:11813735). {ECO:0000269|PubMed:10611362, ECO:0000269|PubMed:11591663, ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:16091039, ECO:0000269|PubMed:18477695, ECO:0000269|PubMed:19372390, ECO:0000269|PubMed:19737748, ECO:0000269|PubMed:20011506, ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:22396654, ECO:0000269|PubMed:22405203, ECO:0000269|PubMed:22792069, ECO:0000269|PubMed:24385935}.; FUNCTION: [Isoform e]: Regulates the trafficking of the glutamate receptor glr-1, probably independently of hif-1, by regulating lin-10 subcellular localization in response to oxygen levels. May hydroxylate lin-10. {ECO:0000269|PubMed:22252129}. | Caenorhabditis elegans |
G5EBV6 | PGL3_CAEEL | MEANKRQIVEVDGIKSYFFPHLAHYLASNDELLVNNIAQANKLAAFVLGATDKRPSNEEIAEMILPNDSSAYVLAAGMDVCLILGDDFRPKFDSGAEKLSQLGQAHDLAPIIDDEKKISMLARKTKLKKSNDAKILQVLLKVLGAEEAEEKFVELSELSSALDLDFDVYVLAKLLGFASEELQEEIEIIRDNVTDAFEACKPLLKKLMIEGPKIDSVDPFTQLLLTPQEESIEKAVSHIVARFEEASAVEDDESLVLKSQLGYQLIFLVVRSLADGKRDASRTIQSLMPSSVRAEVFPGLQRSVFKSAVFLASHIIQVFLGSMKSFEDWAFVGLAEDLESTWRRRAIAELLKKFRISVLEQCFSQPIPLLPQSELNNETVIENVNNALQFALWITEFYGSESEKKSLNQLQFLSPKSKNLLVDSFKKFAQGLDSKDHVNRIIESLEKSSSSEPSATAKQTTTSNGPTTVSTAAQVVTVEKMPFSRQTIPCEGTDLANVLNSAKIIGESVTVAAHDVIPEKLNAEKNDNTPSTASPVQFSSDGWDSPTKSVALPPKISTLEEEQEEDTTITKVSPQPQERTGTAWGSGDATPVPLATPVNEYKVSGFGAAPVASGFGQFASSNGTSGRGSYGGGRGGDRGGRGAYGGDRGRGGSGDGSRGYRGGDRGGRGSYGEGSRGYQGGRAGFFGGSRGGS | 4.6.1.24 | null | null | intracellular organelle [GO:0043229]; P granule [GO:0043186] | identical protein binding [GO:0042802]; lyase activity [GO:0016829]; ribonuclease T1 activity [GO:0046589]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | null | null | null | PTM: Methylated at arginine residues in the RNA-binding RGG-box by prmt-1. Methylation promotes P-granule degradation by autophagy. {ECO:0000269|PubMed:24140420}. | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:27594427, ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:28806108, ECO:0000305|PubMed:19167332}. Note=Localizes to P granules in germ cells at all stages of development except in spermatogenesis (PubMed:15238518). Localizes to the germ precursor cells Z2 and Z3 in embryos (PubMed:19372764, PubMed:24140420, PubMed:27650246). Co-localizes with pgl-1 in P-granules, but localization in P-granules is not dependent on an association with pgl-1 (PubMed:15238518, PubMed:21402787). {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:27650246}. | CATALYTIC ACTIVITY: Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].; EC=4.6.1.24; Evidence={ECO:0000269|PubMed:26787882}; | null | null | null | null | FUNCTION: Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). P-granule component involved in germline development (PubMed:15238518, PubMed:19372764, PubMed:24746798). Together with the P-granule component pgl-1, is involved in the formation of P-granules (PubMed:21402787, PubMed:24746798, PubMed:27594427). Together with pgl-1, probably recruits other granule components such as pos-1, mex-3 and glh-1, and RNA to P-granules (PubMed:21402787, PubMed:27594427). In vitro, binds mRNA; this interaction is required for the formation of liquid-like droplets that resemble P-granules (PubMed:27594427). Most likely recruits pgl-1 into P-granules during autophagy (PubMed:19167332). Associates with adapters such as sepa-1 and is required for the accumulation and degradation of P-granules by autophagy in somatic cells (PubMed:19167332, PubMed:24140420, PubMed:28806108). This ensures exclusive localization of the P-granules in germ cells (PubMed:19167332, PubMed:28806108). In addition, may act redundantly with pgl-1 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (PubMed:26598553). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (PubMed:26598553). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246). {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:26787882, ECO:0000269|PubMed:27594427, ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:28806108}. | Caenorhabditis elegans |
G5EBX6 | EXOSX_CAEEL | MSGEESMPDEEQKQSEEEEEMIRKRTLAMRKKVEEIMRNGAGLVRESNGLPKAGADYELYNSYPTFNTFMKRSEQRLNALMNKVTKSIGCAMRVPDVGSSVEHYTECVIEAQDNIAERAATLHEALKKAELDEIVKVPEFITKAAPTNRKTEAEVSAAMRTFSANIGTVLAEKFRERREEAAQMVVLEKPQKTYNISSDNSQAPFSSKLTVKHHAIEKRTGIVLHDDDESGRRDWISAETETEEEHPYIAEILHFKVPEAQLKSAECLKFTALKDTPLTMIDTKEKLEALTKTLNSVKEFAVDLEHHQMRSYLGLTCLIQISTRDEDFIIDPFPIWDHVGMLNEPFANPRILKVFHGSDSDVLWLQRDYGVHVVNLFDTYVAMKKLKYPKFSLAYLTLRFADVVLDKQYQLADWRARPLRNAMINYAREDTHYLLYSYDMLREQLLKQDTKDLANVYSESSDLCIKVYKKPVFNPKGYLTEIKFRFTLNTRQDYALTHLFKWRDVVARAEDESPHFVLPNHMMLSLSETLPRDVGGIYACCNPLPYFVKQRTGDILKIIVEARDVKLEKVGLSAKERNDAQEARGVMNDTMDHITSVLKSKIDFSHTRFDEERGEIYIDKTDEGMDIELKDHKESLLSVLQTAEIPSVETMIVVEKGKKSDNQKVKKLLNELDKFVTPFECYQMMMITKEKQEEEERKEAERKKLEEGDLPKTMFSHHDAPINRKPEFDAKLLNVDTLKLVPDDPNKPKDPEPSPMEESSSEPQIFDPSRFTDDQLLSKKAMKRKRDAARRNIDVSVVLGESSSSSDPKKKKSDDDAPVEDFDYEKADSSAFEKPVRDNNADFDPFHQKYRLKNKTKKNMAMKKSSNRQGTINYKK | 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q01780}; | apoptotic cell clearance [GO:0043277]; apoptotic DNA fragmentation [GO:0006309]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; histone mRNA catabolic process [GO:0071044]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; nuclear polyadenylation-dependent CUT catabolic process [GO:0071039]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent snoRNA catabolic process [GO:0071036]; nuclear polyadenylation-dependent snRNA catabolic process [GO:0071037]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; RNA processing [GO:0006396] | exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | 3'-5'-RNA exonuclease activity [GO:0000175]; nucleotide binding [GO:0000166]; single-stranded RNA binding [GO:0003727] | PF01612;PF00570;PF08066; | 1.10.150.80;3.30.420.10; | Exosome component 10/RRP6 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34365510, ECO:0000269|PubMed:36763670}. Nucleus, nucleolus {ECO:0000269|PubMed:34365510, ECO:0000269|PubMed:36763670}. Nucleus, nucleoplasm {ECO:0000269|PubMed:36763670}. Note=As a part of exosome complex, translocates from the nucleolus to nucleoplasm in response to cold-warm shock. {ECO:0000269|PubMed:36763670}. | null | null | null | null | null | FUNCTION: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). Involved in apoptotic DNA degradation (PubMed:12718884). Involved in regulation of antisense ribosomal siRNA production (PubMed:30224484, PubMed:34365510). Involved in response to cold-warm shock (PubMed:36763670). {ECO:0000250|UniProtKB:Q01780, ECO:0000269|PubMed:12718884, ECO:0000269|PubMed:30224484, ECO:0000269|PubMed:34365510, ECO:0000269|PubMed:36763670}. | Caenorhabditis elegans |
G5EBX9 | PPE_CAEEL | MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLTIKSAILIQKWYRRCEARLEARRRATWQIFTALEYAGEQDQLKLYDFFADVIRAMAEENGKGGVENGRNSPLMSALSHYAKPSLMDSEGETVKKMLEDTSPTNVDIDRNYKGPTLSLPLDKPQVAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASKTHRKSTLRERLGVVEESAVKELKEKLSSFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGLNLPWIALAPKVATLSEDGKYVMYKEDRRIAQVGGTHAQEKDIVESLYRHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKYTKRPLQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRPLLR | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P36873}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:P36873}; | detection of stimulus involved in sensory perception [GO:0050906] | axon [GO:0030424]; cilium [GO:0005929]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF13499;PF00149;PF08321; | 3.60.21.10;1.10.238.10; | PPP phosphatase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11312268}; Lipid-anchor {ECO:0000269|PubMed:11312268}. Perikaryon {ECO:0000269|PubMed:11312268}. Cell projection, dendrite {ECO:0000269|PubMed:11312268}. Cell projection, axon {ECO:0000269|PubMed:11312268}. Cell projection, cilium {ECO:0000269|PubMed:11312268}. | 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:0000255|RuleBase:RU004273}; 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:0000255|RuleBase:RU004273}; | null | null | null | null | FUNCTION: Probably acts as a protein phosphatase. {ECO:0000305}. | Caenorhabditis elegans |
G5EBY8 | UN129_CAEEL | MRRLPIVLLLSVFSIANCAKVDVDLINETIRDLLHFKSSDPNVTSFHRSSHTLTEHMKNLYENFIDEDSNEDGNLVRAIEPAVGKFEGQEVLVFDVEGFDSHESIMRAELHFYLRRRDSFARRRSRQIRAKSVCVNEYCRQQTLKKIRVGGDENLEEYKVIWDATKSVFDSYHLDAKQAVFRITREHSKMRPYAEMIRKSTPFLVIYSKVNHTLDTVSVMKQTEQTKRKRRDLGNEELREYYNYNSIPLDNDDREPIKRKNGKKNSLSEEISSEDVWQGFGEETSREERERIANEELANDVRVVLLQNKNRCHKEGVLVSLKHFGWDRYVIEPKTIETSFCKGKCAKPMLTSGKASNHAMLQSLFAAEPVCCAPTNLKSLNFWYRDEKGRTVIRNYSKMLIGSCSCL | null | null | backward locomotion [GO:0043057]; dorsal/ventral axon guidance [GO:0033563]; inductive cell migration [GO:0040039]; locomotion [GO:0040011]; motor neuron axon guidance [GO:0008045]; nematode male tail tip morphogenesis [GO:0045138] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; signaling receptor binding [GO:0005102]; transforming growth factor beta receptor binding [GO:0005160] | PF00019; | 2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:19169249}. | null | null | null | null | null | FUNCTION: Required for the migration of axonal growth-cones and distal tip cells (DTC) along the dorsal-ventral axis of the body wall (PubMed:19169249, PubMed:9473333, PubMed:9685266). Acts cell nonautonomously and independently of the classical daf-4, sma-6 or daf-1 TGFbeta receptor signaling (PubMed:11018016, PubMed:19169249, PubMed:9685266). During axon migration, facilitates long-range repulsive guidance of unc-6/netrin by enhancing unc-5-unc-40 signaling at the expense of unc-5 alone signaling, probably through direct interaction with receptor unc-5 (PubMed:19169249, PubMed:9473333). Involved in cell-cell contact formation in sensory rays in the developing male tail, via a pathway involving plx-2 and mab-20/semaphorin-2A (PubMed:15030761). {ECO:0000269|PubMed:11018016, ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:19169249, ECO:0000269|PubMed:9473333, ECO:0000269|PubMed:9685266}. | Caenorhabditis elegans |
G5EBZ4 | LE418_CAEEL | MSTEEDPSLVDAEESMEEGSVTQDATEETEEEEEQEQGDEAGPSERKRSSRKKGGKGGKKGSKKSAAAASKVEIPDPYNSTSEEVCAAIGLTDVEFDYDEEEFQGISNLKTFSSIIKPQILEANPGTNVSKMYPMFQVKYKEYQDHMAAQGKPVQKQARGSKTPAVSTPVIPPRSAPTKTRSARRKRRDSDAPDSDQEFEAFIKQQEQLEDDLVKDKEDARIKRAAEREEKKKGALEAARAAKKAKLEKGEEAENNDYCEECKQDGELLLCDTCPRAYHTVCIDENMEEPPEGDWSCAHCIEHGPEVVKEEPAKQNDEFCKICKETENLLLCDSCVCSFHAYCIDPPLTEVPKEETWSCPRCETVKPEHKIEKILCWRWKEIPYPEPLEAGKEASSDDAMLKPPRKMEPRREREFFVKWKYLSYWQCSWVSEMLLEVHFRMLILLYWRKNDSDAPPEFEESVTSRHHSDNDPYKLRERFYQYGIKPEWMQIHRIINHQSYAKSQQDYLVKWKELSYDQATWERDDSNIANYEEAIIKYWQHRESKLNEDIPKNVQKMIAKHREAKGLPPKEDEKKKKKREKIDIRKKYEVQPDYVTETGGKLHPYQLEGLNWLRHCWSNGTDAILADEMGLGKTVQSLTFLYSLMKEGHCKGPFLIAAPLSTIINWEREAEQWCPDFYVVTYVGLRDARVVLREHEFSFVEGAVRSGPKASKMKTTENMKFHVLLTSYETINMDKTILSSIEWGALVVDEAHRLKNNQSLFFKNLNEYTIHYRVLLTGTPLQNNLEELFHLLNFLSKERFNQLEAFTAEFNEISKEDQIEKLHNLLGPHMLRRLKADVLTGMPSKSELIVRVELSAMQKKWYKNILTRNFDALNVKNGGTQMSLMNVLMELKKCCNHPYLFVKAELEAPKEKNGMYEGTALIKNSGKFVLLQKMLRKLKDGGHRVLIFSQMTRMLDIMEDLCEYEGYRYERIDGSIMGQMRQDAIDRYNAPGAQQFIFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRLGQKHKVMIYRFVTKKSVEEKITSVAKKKMLLNHLVVRAGLGGKEGKTMSKTELDDVLRWGTEELFSEDLDAAEGEGSEKKGAAAQEIVWDDAAVDALLDRSNKEETPAGEDGEEKAEWQNEYLSSFKVASYQTKETEGQEEEEEEETEVIKEDEKEPDPDYWEKLLKHHYEQDREIELQKLGKGKRVRKQINYASENMGTDWSKQNQTQDDDDDNESYRGSDNGDGLNSDEDDYDEKKKRRRDEEKMPPLMAKVNGQVEILGFNPRQRKAFYGAVMRWGMPPQDSHQSQWLVRDLRNKSEKVFRAYASLFMRHLCEPGADGHDTFNDGVPREGLNRQHVLGRIGLLSLVRRKVQEFEQYNGQWSMPEIQDEVLAKAANGSAQGSSRSTPKPKEEPKEEPMEKEDATETVNGATSEPATDAESEQNAPVDEPMDTDEAKEPKEEPIETEKPRAARPSFKFNICDGGFTELHSLWANEEKVARNGKEYEIWYRRHDYWLLAGVVVHGYGRFQANFNDIINDPRFSVLNEPFKEVGAEATGSDIKAKFMQRRFKLIEQSLVIEEQLRRAAHANRHLQPDNVGPLAQRFADLENIAESQANIAKESSAGNRNANAVLHKTLVQLDEILSDMKADVSRLPSTFTQLATVTERLNMTERQILSRLTTKDEDAIANRSVLPPPGPFVTPILRQQMDGIQPKFAALYSKFMSENGERMEEDEPVEAEEEEGVKQEPDDETQDSAEAPPVLSAEVNSDDSNDVPSTSAAAAVSSETAADAEPASAEDQAPTDEPEPMET | null | null | chromatin remodeling [GO:0006338]; embryonic digestive tract morphogenesis [GO:0048557]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vulval development [GO:0040027] | chromatin [GO:0000785]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; RNA polymerase II transcription repressor complex [GO:0090571] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; metal ion binding [GO:0046872]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076750, ECO:0000269|PubMed:17466968}. | null | null | null | null | null | FUNCTION: Part of a NuRD (Nucleosome Remodeling and Deacetylase) complex which is implicated in the synMuv B pathway that negatively regulates specification of vulval cell fate (PubMed:11076750, PubMed:21060680). This negative regulation is thought to be mediated via interaction with the promoter of lin-39, a key regulator in vulva development, and is dependent on the presence lin-1 (PubMed:17466968). Contributes to negative regulation of lag-2 which is expressed in the gut during larval development (PubMed:21060680). Has a broad role in development (PubMed:21060680). In association with akir-1, plays a role in regulating the transcription of antimicrobial peptide genes in response to fungal infection (PubMed:30036395). {ECO:0000269|PubMed:11076750, ECO:0000269|PubMed:12507426, ECO:0000269|PubMed:17466968, ECO:0000269|PubMed:21060680, ECO:0000269|PubMed:30036395}. | Caenorhabditis elegans |
G5EBZ8 | ARK1_CAEEL | MREEPTAGTADATLNKLLQAADLSGYESDLRRKLKLRNAADLQYVEEVDLLSVGMSRPEQKRLRKEYTKMFPSGIFGKVKKAFKRAESLDRKTSNSVANQDDNDHHVIPIEKITLCKELGQGEFGSVWQAGWKNSAGSDVIQVAVKCVGSDKLLATSSSFLQEAAIMTRMRHEHVVRLYGVVLDTKKIMLVSELATCGSLLECLHKPALRDSFPVHVLCDYAEQIAMGMSYLELQRLIHRDLAARNVLVFSPKLVKISDFGLSRSLGIGEDYYRSEFTPNLKLPIAWCAPECINFLKFTSKSDVWAYGVTIWEMFSYGEMPWKGRSGAQILELVDRKKELLTRPKACPEDIYDMLKETWTHQVQDRPTFSDIVAKFPERRAQSVRAVVDCKDSAADHLHFKKDDLIVVISRSPAQYPDGYYWFGSLRNGKLGLFRPTDTVAHLGSEPPCSNGTIENGFSEKEKGGKKNKKAEKESERERKKLLISEPVGDVRHTCHVGIDGTAFGLLQLDKKAMCPTSSSPSTSRGSQASPAPSHTSSSTTSSVHLRETVARNGVPIKETMSLRDVGPLSRDALNLRDTVSPPVARAPSQPPSYSQPRPPPRSVSSVSSGNQHSVQVHDQFSSLDRSRGSLTPTAPPLTASAANSLKDPLTGISLSIPSNNLISYMDDQEDDHRWTRSPGAISQSTTLTALSSSRKDPIPAPRGPVAAVYARGKDIPTPASKSDIALCEKIEDLNRDLTNYSIGTICDYSEDRPLLDSMNRTISSSTTHQPPPQSSEARIRFMTEQEVRKINEKSAREHRKTEDLLREERQKEQKPGEIEEPQQPAESLYSTRTPQQEGWSSAAQEAYKLLVECGTNLKQASVSPPPMSPTSSRLSTLDRSSISPAPPRPVTPPLSVRNETISMRKSQQEEMEHVTVEENSPKRVHIIETKLIDGPARGMSPIQDRHIPAFTTPMSNGSFRKAPAPTPVSPAPAGSTDQKPPPCRPPKTRQFPLVIDERNLAYDNLNGFGAGARVAPPVPPKPKVRTIFSFADDQKKQKEVAN | 2.7.10.2; 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q07912}; | embryo development ending in birth or egg hatching [GO:0009792]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of vulval development [GO:0040027]; phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF07714;PF07653; | 2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | null | 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:0000250|UniProtKB:Q07912}; 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:Q07912}; 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:Q07912}; | null | null | null | null | FUNCTION: Probable tyrosine protein kinase which plays a role in vulva development, probably by acting as a negative regulator of the let-23/EGFR and let-60/ras pathway. Involved in the negative regulation of germline development (PubMed:14657502). {ECO:0000269|PubMed:10949028, ECO:0000269|PubMed:14657502}. | Caenorhabditis elegans |
G5EC23 | HCF1_CAEEL | MDEDVGLEATNYSRGDESRSEEQEKNVVRWRIVQQSTGPNPKPRHGHRAVVLKELIVIFGGGNEGMIDELHAYNTQKREWTAPQCCGDVPTPAAAFGAISLGNKIYRFGGMTEYGKYTNDLYELQSTRWEWRRLNPRVHSNGHLPCPRIGHSFVVSQKSQKAYVFGGLSNDLNDPKRNVPHYLDDLYVINLSGPQHLIWEKLNATGPGPISRESHTAVIYEKDSISRMVVYGGMNGVRLGDLWYLNLNTLHWTEIKFDDPRTGIPPMPRSLHSSVLIGDKMFVYGGWVPLLEHASTEQQTEKEWKCTSSLGCWNITEDRWVPLHLYCSDEDTIPRGRAGHCAAAVGDRMYIWSGRDGYRKAWSNQVCCRDMWLLDTILPEQPGKVQLGRAGFNSLEISWPIVQGASGYFLQIGFGDAKEQSVSPIKRATTSPRKQPSIVPPSQKETEQSPKKPQGTAPSIISTQGTTYTAPADPKPATDEGGLPQDLFEDTEKNETASPKRSNDAQSADSSTCEQKKTDESGLEEDSEKDQKPSDAGETDEMKEENGDDDLPWFDVGIIDKATINVTHYFNDRQQSLEKQLNDLIDHNAFKCVNDSVFTTEDKIPLINGQSYRFRVSAINGLGKGAWSETASCKTCVPGYPSAPSSIRITKSHEGAQLTWEPPSNTNISGKIIEYSVYLAVKNQSANSADSQLAFMRVYCGPQADCQVLQSNLGTAFVDQTNKPAIIFRIAARNEKGYGPATQVRWLQDQQKIPVRTNYPNNSGFIYQQHGGQQKRARFDHQ | null | null | chromatin remodeling [GO:0006338]; dauer exit [GO:0043054]; defense response to other organism [GO:0098542]; determination of adult lifespan [GO:0008340]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription by transcription factor localization [GO:0010621]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; response to cadmium ion [GO:0046686]; response to endoplasmic reticulum stress [GO:0034976]; response to oxidative stress [GO:0006979] | histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor binding [GO:0140297]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription coregulator binding [GO:0001221]; transcription corepressor activity [GO:0003714] | PF13415;PF13418;PF13854; | 6.10.250.2590;2.60.40.10;2.120.10.80; | null | PTM: Phosphorylated at multiple serine residues (PubMed:11341844). Phosphorylation is developmentally regulated, occurring in embryos but not L1 larvae (PubMed:11341844). Phosphorylation may be cell-cycle-regulated (PubMed:11341844). {ECO:0000269|PubMed:11341844}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14629117, ECO:0000269|PubMed:18043729, ECO:0000269|PubMed:18828672}. Note=Localizes to nucleus, except for nucleolus. {ECO:0000269|PubMed:14629117}. | null | null | null | null | null | FUNCTION: Transcriptional coregulator (PubMed:18828672). Involved in control of the cell cycle and in modulating mitotic histone phosphorylation (PubMed:18043729). Plays a role in modulating lifespan by regulating the transcriptional activity of daf-16/Forkhead box protein O, in concert with protein deacetylase sir-2.1/SIRT1, and perhaps acting independently of the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:18828672, PubMed:21909281). Negatively modulates responses to environmental stresses, including oxidative stress, heat stress, and exposure to heavy metals; acting via regulation of the transcription factors daf-16 and skn-1 (PubMed:18828672, PubMed:21909281, PubMed:22568582). May play a role in pharyngeal development via positive modulation of expression of sup-35 (PubMed:19521497). {ECO:0000269|PubMed:18043729, ECO:0000269|PubMed:18828672, ECO:0000269|PubMed:19521497, ECO:0000269|PubMed:21909281, ECO:0000269|PubMed:22568582}. | Caenorhabditis elegans |
G5EC24 | PTP2_CAEEL | MPRLALRQYNFYYRVNGEKAEELLKEYGEDGDFLLRYSESNPQNFSISVRVAEDKILHIKVTKYESDMLSIFEDERTTPNQFGSITELAEFYMEFPEKLREKNGLFLELKKPVYVPYHLEACAEEQRRTQLYRWWHGNLPASSANKLLQTEKNGTYLLRASQHIPGALVISAKTEGQVVHLTIYQDPSTGRFNIDGDRTKFQSAWLLIDSYSKNPIVEKGEASRVLYLEEPLFNTFIEADLFVDRFEIIRRPINPRESMEKTGISEEFDRLSQEALPAEQYLSKREGRRPVNAEKNRYKNIVPFDHTRVILTDRPNTPGSDYINASYVRFENSQRTKNVTFACEKSFIATQGCLETTISDFWSMVWQENSRVIVMPTMENERKEKCARYWPAEVNKPEVHGDISLTCTIERKVQRAVSDEVKAELEQEKTNRIAKGLVPEAELNGDGISYILRTLVMKKGKDTREIRQLQYLTWPDHGCPLHPYAVLNFLEDVDREYDYFNAQPIAASLPQGPIVVHCSAGIGRTGTVLVLDALLNQVKKVGLLCPMDVYKMVKYVRTYRSGLVQTEQQYQFLYKALAFYLKNNNPYPVKSFIDGDTDAFDFPRRLRPTPNASRPSSARQVTSSRPSSSASSRTSHSRPRTGPQAEPIFERSTSSTSSSSTLLKSTKK | 3.1.3.48 | null | cell differentiation [GO:0030154]; dephosphorylation [GO:0016311]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; muscle organ development [GO:0007517]; nematode larval development [GO:0002119]; oogenesis [GO:0048477]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of vulval development [GO:0040026]; regulation of cell projection organization [GO:0031344] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410] | non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; phosphotyrosine residue binding [GO:0001784] | PF00017;PF00102; | 3.90.190.10;3.30.505.10; | Protein-tyrosine phosphatase family, Non-receptor class 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR000929, ECO:0000269|PubMed:20380830}. Note=Localizes to vesicle-like structures. {ECO:0000269|PubMed:20380830}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PIRNR:PIRNR000929}; | null | null | null | null | FUNCTION: Involved in embryonic and larval development (PubMed:20380830, PubMed:9472025). Plays a role in oogenesis by regulating mpk-1 phosphorylation and oocyte maturation in response to major sperm protein (MSP) (PubMed:20380830, PubMed:9472025). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles probably downstream of receptor egl-15 (PubMed:16495308). Plays a role in fluid homeostasis probably downstream of receptor egl-15 and adapter soc-1 (PubMed:11689700). Promotes vulva induction and negatively regulates fertility probably downstream of receptor let-23 (PubMed:16547100, PubMed:9472025). Negatively regulates daf-2-mediated repression of dauer formation (PubMed:16547100). {ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100, ECO:0000269|PubMed:20380830, ECO:0000269|PubMed:9472025}. | Caenorhabditis elegans |
G5EC32 | SRBS1_CAEEL | MMHHPHPFGSNLANSSEPQQPSGQYLNPAADAYNFDTFEDSDKFSPKGNVAALRNVIHGQLDMKTPTGNSSRYQKPAPPPVDSTPSWAKNVKVYEPNGYVDPHLNKHNMGRVLDGPVNPNKYFQGVPPASYSQVKHNESKPPVPPSTKPPHSAAQALQAQVLQSSKAPSQPQQSQKTSYRIPYDVALDPRHHLGEFDIDDSASIISSCISTFGESSEIAGFSAAAEQRHLYEQYRKKLMEEKNELKEGSETPCVSLSEKVMTSSTENLKNGNNQQNQQPEPQPPSSSIFNSELTPFGHVAPVAKQFEPTNFPPFSPEKESEIKRSIDLESSQLLVKSKSPAPYSTSSTDHYGTIRRKHKPVAIDLSKSSPNLASQSPSNLFFGASFEEKQNRSPMTSTPSYKEQGFKNDSLNDSLNQAFEIASSIETTKNAYEAPPTPKSASHDRSISDTYPVSSSTTSTWPSHTTTPTTTTAAAPIAAVAPQTYTEQQPMSTSMSSSVMSTNMDEPIVVGSHQQIPQQSPDSSPERNEDMSQWYRKMFKQMHRKGEDGSNEGKEQHFINPSNVTDGIGRTTPTASNLGRSRENLSFNQHRPDHPSSYFDSLEHGPNDQYNNQERVKQSNEEELLRLKAEKLAEELRKEKERKHSFIPSSAPSLQNNMDRLNSLLYDFSSDIQEPAHRDYTPQPVMTATAVYKFEPRSARELPLNRGDIIRIIREVDGYWMEGERNGRSGIFPTSYVQINTGNQGDSQKMRAIYPFTARSDTELSLKRGEIITRRRQIDSNWLEGSNQIGIVGIFPASYVEPIEQVEQHIPTIVPNRPKTPKIEDQVYNQVYKPNETVIMQSNQGYYDKAAVVPNNKVRFDLPSGSDSNLQMSLNPHQNQFPPTHTQTSTQQPSNYGMKKIEYEREKVVEEVPPMHMDQYRKLNDEPKNPKKDTNILMNAASLIPKGSEMYRAVYPYQPQKEDELQLYTNDIIFVVEKCDDGWFIGTSLRTGDFGIFPGNYVKRH | null | null | maintenance of mitochondrion location [GO:0051659]; sarcomere organization [GO:0045214] | adherens junction [GO:0005912]; dense body [GO:0097433]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886] | null | PF14604; | 2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:28978740}. Cell membrane {ECO:0000269|PubMed:28978740}. Cell junction, focal adhesion {ECO:0000269|PubMed:28978740}. Note=Localizes to adhesion plaques and dense bodies between myocytes (PubMed:28978740). Co-localizes with deb-1 and atn-1 at dense bodies (PubMed:28978740). Predominantly localizes to the membrane-proximal region of dense bodies (PubMed:28978740). {ECO:0000269|PubMed:28978740}. | null | null | null | null | null | FUNCTION: Required for organization of sarcomeres in body wall muscles and for maintaining normal mitochondrial position in myocytes. {ECO:0000269|PubMed:28978740}. | Caenorhabditis elegans |
G5EC36 | LIM7_CAEEL | MNICMRNGYEQFSLTSPGTSDLEIGGSFWKDEPDTKYLCLDSPVEQRQHQPPMAVCAGCRLEISDRYFLRVNPNLEFHAQCLKCVQCSRPLDENQTAFVKNGQTYCRDDYRRLFTTRCSRCHGDFDKTDLVMRAGPQNVFHLNCFACVACEKRLQTGEEFQIKNNSLYCRSDCRGLDNPDTSASVPDYSKLNNNNNNDNNNSSSNFDEDEWDEERSTLTSLDNNTSSPLGSPKSDGVRTPLFGHHNSGSGGSTSSCGKKKKDKQATRVRTVLNENQLKILRDCYSINSRPDATLKERLVEMTGLSARVIRVWFQNKRCKDKKRQIQITENRLNSEREEVLNRVRVNGIGPLMVQPATPHIDNTLGGPIDIQHFAQWNGTPPPPPPQYGNPMMFNSPSTFDVSVILAPVAPNVTSPSEALGPLGASVFPHFSPQHAPFTATSHDISSPAPCGE | null | null | axonogenesis [GO:0007409]; body morphogenesis [GO:0010171]; gonad morphogenesis [GO:0035262]; head morphogenesis [GO:0060323]; locomotion [GO:0040011]; nematode larval development [GO:0002119]; neuron fate specification [GO:0048665]; pharynx development [GO:0060465]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872] | PF00046;PF00412; | 2.10.110.10;1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}. | null | null | null | null | null | FUNCTION: Probable DNA-binding transcriptional activator. {ECO:0000250|UniProtKB:P61372}. | Caenorhabditis elegans |
G5EC37 | SEPA1_CAEEL | MTPLSALTSNPAPSPPPKFALGKCPATAIHVVSVLRPNRQRFCYEKTDAGDLIPHKCLICQPILTEKHISPYYAVYSDLLEDFVLFGYNTMTGKMEQFIYAFKTDCFVEVNRPEIKYNPAFLVKGNVVVALNGPEGELVVIERDCRGLLSKESTSYGQFRTLPTAALRTLTLQDLERDRWDRAANSDEVKISSGNESFDRLYAEYQKNLPRFQVRQCLHLNKEFLCVYSKTSGDYTRLEYIDETGDFQKISCTLCTCEVTESNLIPLYVERNASELVIHVHNTENNQIEQYIYDVRTFGFVQVKRNLVYDPKKITSGLNLFMAENIDNRKVYMIMRGRDGRLQKETSGSGGFEKMQPVAVKTFQVQWVEMKTEFEKKKASTERVEPQHPVQTEGEDIMETVLAMVESFNCDLRKELGLTQDQEIPRKAPRVESAETEENIVKNLEKLQIAKDPEEPTTAASEGGNTYGYQELDDTMSEGLLEKEAESKHQDANEPEPVKNVTYEPDVAAMDKKKKRRELKSRLNKINAQIDELEKRRMERAGKKQVVSSSVPSEEAAQVEAPASPALAENTNQISNEETPKIDIFEGYNGSFLFGTNTSKEWIVEDIRNHMVGKLLKAFWPRIQNVEEMNGELFKKLIANARKCETEILEASNDRDEYYRLMQLTVDQILKKTLKKDQRATEHNHQQPTQSSDELAKNHEKN | null | null | autophagy [GO:0006914]; regulation of DNA-templated transcription [GO:0006355] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | protein self-association [GO:0043621]; protein-macromolecule adaptor activity [GO:0030674]; transcription coregulator activity [GO:0003712] | PF02172; | 1.10.246.20; | null | PTM: Degraded by autophagy. {ECO:0000269|PubMed:19167332}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00311}. Cytoplasm {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24140420}. Cytoplasmic granule {ECO:0000305|PubMed:19167332}. Note=Diffuse cytoplasmic localization, but also localized to cytoplasmic aggregates throughout development (PubMed:19167332, PubMed:21802374). Co-localizes with epg-2 and lgg-1 in cytoplasmic aggregates (PubMed:19167332, PubMed:24140420). {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24140420}. | null | null | null | null | null | FUNCTION: Adapter protein that connects P-granules in somatic cells with the autophagic machinery (PubMed:19167332, PubMed:19372764, PubMed:19377305, PubMed:24140420). Association with other adapters such as epg-2 and P-granule components such as pgl-3 is required for the accumulation and degradation of P-granules by autophagy in somatic cells (PubMed:19167332, PubMed:19372764, PubMed:24140420, PubMed:28806108). This ensures exclusive localization of the P-granules in germ cells (PubMed:19167332, PubMed:19372764, PubMed:24140420, PubMed:28806108). {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:28806108}. | Caenorhabditis elegans |
G5EC44 | MRT2_CAEEL | MMELETGQCTIMELKKENVKELAQVFKTVAFKDTGTWHASEAGMKITVDDGSYQLASVFINPAFFSSFKVREEIVSMKISIKSISEFLSISENSSSSVKVSYPGMFQPVKMLVEDADGWVARGNFTTTLADQELDFEFDDAGVLATYLLKTQVLKEIIKDFDDTSRTVRIQFTKNSLCFTTFGDVGETTVSIPSRSLQMESVKCLEEVEFSYLLSLIQRMTTAFILATKLILRVDERGVLSCQFSIDHGEGNASYIEFLTVPADEEE | 3.1.11.2 | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; nucleotide-excision repair [GO:0006289]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004] | checkpoint clamp complex [GO:0030896]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311] | PF02144; | 3.70.10.10; | Rad1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:O60671}; | null | null | null | null | FUNCTION: May be a component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:12445383, PubMed:16951081). Promotes DNA double strand break-induced cell cycle arrest and apoptosis, thereby playing a role in genome stability (PubMed:10646593, PubMed:10882129, PubMed:16951081). Also required for telomere length maintenance and germline immortality (PubMed:10646593, PubMed:16951081, PubMed:22547822). May possess 3'->5' double stranded DNA exonuclease activity (By similarity). {ECO:0000250|UniProtKB:O60671, ECO:0000269|PubMed:10646593, ECO:0000269|PubMed:10882129, ECO:0000269|PubMed:12445383, ECO:0000269|PubMed:16951081, ECO:0000269|PubMed:22547822}. | Caenorhabditis elegans |
G5EC86 | MOE1_CAEEL | MNVNGENNEKIDEHHLESSLAGVPTLPVSPLDHAKDLSQTNPNAQIGDLVTQTANLIAIKKQLLEDIAFNQHIQSMQVRAIQSFPQNNQVAPPFQQFDPRRRGLARMQKPESYKTVICQAWLESKTCSFADNCRFAHGEEELRPTFVEPLQNNKYKTKLCDKYTTTGLCPYGKRCLFIHPDHGPNAYIRADKLLEVSQRHALADIRDQMEQHIMTNGRIAAPPLSAIQHPLEMFARPSTPDEPAAKLPLGPTPVSTRGPRYELPTKELHDAEGAMTYPPSRWPLDPSMFALDAWNMAHRPASPLDSMVLGSAPNAGSFGMLGKQNTPGGVSGYSSAGSTPSQDLSSSSLNAASAAAAAAYFANSAVAQSLLMKSVATDPMMSCNGPFSPMPGFDQLAENMTKHLNLW | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; endodermal digestive tract morphogenesis [GO:0061031]; establishment of chromosome localization [GO:0051303]; meiotic nuclear membrane disassembly [GO:0051078]; negative regulation of endodermal cell fate specification [GO:0042664]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]; negative regulation of mesodermal cell fate specification [GO:0042662]; negative regulation of ovulation [GO:0060280]; negative regulation of smooth muscle cell differentiation [GO:0051151]; negative regulation of translation [GO:0017148]; nematode pharyngeal muscle development [GO:0160096]; oocyte growth [GO:0001555]; oocyte maturation [GO:0001556]; oocyte morphogenesis [GO:0048601]; positive regulation of embryonic development [GO:0040019]; positive regulation of fertilization [GO:1905516]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904146]; positive regulation of oocyte development [GO:0060282]; positive regulation of oocyte maturation [GO:1900195]; protein destabilization [GO:0031648]; protein localization to chromatin [GO:0071168]; regulation of endodermal cell differentiation [GO:1903224]; regulation of mesodermal cell fate specification [GO:0042661] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; messenger ribonucleoprotein complex [GO:1990124]; nucleus [GO:0005634]; P granule [GO:0043186] | metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA regulatory element binding translation repressor activity [GO:0000900] | PF00642; | 4.10.1000.10; | null | PTM: Phosphorylation by mbk-2 and by gsk-3 are required for its rapid degradation following meiosis II. {ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:16343905}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18854162}. Cytoplasmic granule {ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:25261697}. Nucleus {ECO:0000269|PubMed:18854162}. Note=Expressed in cytoplasmic P-granules in developing oocytes, and remains in P-granules following fertilization when cytoplasmic expression is abolished (PubMed:12296824, PubMed:12781695, PubMed:16611242, PubMed:25261697). When phosphorylated, increased levels in the cytoplasm of embryos after meiosis II and before anaphase of the first mitotic division (PubMed:16289132). {ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:25261697}. | null | null | null | null | null | FUNCTION: Zinc-finger RNA-binding protein that binds to 5'-UA[AU]-3' motifs in the 3'-UTR of maternal mRNAs to suppress translation in oocytes and embryos (PubMed:18417623, PubMed:18854162, PubMed:19786575, PubMed:20826530, PubMed:24014033). Acts as a ribonucleoprotein particle component that may exert part of its function within cytoplasmic foci of unfertilized oocytes (PubMed:25261697). Acts redundantly with oma-2 to control the temporal expression and distribution of maternal proteins and thereby promote meiotic progression, oocyte maturation, fertilization and embryonic development (PubMed:11702779, PubMed:12296824, PubMed:12781695, PubMed:16289132, PubMed:16611242, PubMed:19786575, PubMed:20826530, PubMed:25261697). Recruits the translational repressor ifet-1 to the 3'-UTR of mei-1 and zif-1 to negatively regulate their translation (PubMed:19786575, PubMed:20826530). By suppressing the translation of the E3 ligase zif-1, may in turn play a role in the stabilization of zif-1 targets such as the maternal transcriptional repressor protein pie-1 (PubMed:16343905, PubMed:20826530). Following fertilization, sequesters the transcription initiation factor, taf-4, in the cytoplasm, which prevents its nuclear localization and thus allows for transcriptional suppression in early embryos, but not in oocytes (PubMed:18854162). Also, together with oma-2, is involved in P-granule distribution during embryonic development (PubMed:16611242). {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16343905, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18417623, ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:19786575, ECO:0000269|PubMed:20826530, ECO:0000269|PubMed:24014033, ECO:0000269|PubMed:25261697}. | Caenorhabditis elegans |
G5EC89 | CEH17_CAEEL | MMMEYGGYFSSSAVAQQSGDVPTTAPSAVTNSFFYTPQSHNIYHQYATPYLQSGRALTTAHNTSSSSAGNSTSSSSSSSNYRNTTHDSLQAFFNTGLQYQLYQKSQLIGSDTIQRTSSNVLNGLPRSSLVGALCSTGGAPLNPAERRKQRRIRTTFTSGQLKELERSFCETHYPDIYTREEIAMRIDLTEARVQVWFQNRRAKYRKQEKIRRVKDEEEDPLKKEPGQISLEEIIDQI | null | null | axon guidance [GO:0007411]; neuron development [GO:0048666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of axon extension [GO:0030516]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | 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]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF12413;PF00046; | 1.10.10.60; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:10887091}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in postembryonic differentiation of the ALA neuron, and regulation of genes that contribute to behavioral quiescence, a sleep-like behavior mediated by ALA (PubMed:20501595). Regulates its own expression and also that of homeodomain ceh-14, together forming an autoregulatory loop in the ALA neuron (PubMed:20501595). Involved in fasciculation-independent longitudinal axonal navigation in many neurons (PubMed:10887091). {ECO:0000269|PubMed:10887091, ECO:0000269|PubMed:20501595}. | Caenorhabditis elegans |
G5ECB2 | GABR2_CAEEL | MSRWLSLLLFAVQAVGGYEAGEELSCKRRHGGIPLPLGVFTVQKEGFPDALPAIRTALSHVHSRSCILQGYRLEMIVKDTHCKTSQGMKALFDLIASRPRPVAILGGQCTEVNEPIAMALKYWQIVQLSYAETHAKFASSDSHELFTTFFRVVPGSRNTNMAKCKFVNHFGWKRVGTVKQNDQPRYALPHEALTTRLEHGFGVKIVHTAGVNWEQIETVGGELDELKERDVRIILVDVDEEMAATVLCAGYHRGMYGDNYVWILPGYHSDKWLNQTHDNCTVEEMREAAKNHFSVEFALTRRDVDTKIVGNTRAGDVWNEITQLDPNNTWRGYLYDGLWTLAIALSHSMGDNAEFSHHKMMEAIDNSSFQGLTGKVKFANNERLGLVDIKQWSDGQYVPFAVYDGADDEFKIIDSTTKGWSPPLDSTITERRREHISSILFLAMSLLALIGIFLALIFLLINFRYRNHRFIKMSSPNLNNIIIAGSICTFASVIMLGLDTRIVSPDVFVWLCYTKTWTLCIGFTLSFGAMFSKTWRVHSIFTNIRMDRKAIKDSKLFIILGILLFIDICVLVTWAFVSPFSYTVTELPHIPEDNIVIIPEVEKCNSSHSGVFQAVLYAVKGVLMILGCFLAWETRHVNVPALNDSKYIGTSVYCCVVMSVLGLSTSVILQERVNEMFSLASFFVIFSTTLTLCLVFVPKVIELARNPVGNEPRAYRRGLMKSVVAKTSQPMSPQPRSDSSGDLIGKAESENKLRRRYLHQKSTQLWDLVEKLRAQGDTRFLQQEWCLSSASPSSQERETSLLLRQPSSSNNREETSLTAAGPNGERSSDWPWVDPDEPSTKL | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; negative regulation of synaptic transmission, cholinergic [GO:0032223]; regulation of locomotion [GO:0040012]; response to xenobiotic stimulus [GO:0009410] | G protein-coupled GABA receptor complex [GO:1902712]; G protein-coupled receptor heterodimeric complex [GO:0038039] | G protein-coupled GABA receptor activity [GO:0004965] | PF00003;PF01094; | 3.40.50.2300; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75899}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-1, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons (PubMed:18614679). As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior (PubMed:18614679). Regulates locomotory behavior in response to GABA release by GABAergic motor neurons (PubMed:18614679, PubMed:21613582). {ECO:0000250|UniProtKB:O88871, ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:21613582}. | Caenorhabditis elegans |
G5ECD6 | CHS1_CAEEL | MNDGENYWNAFRSHKRSATDGPTLSPWMVTVLQATKLLLFALCNIVLTLGSVFSKLIVLIMATNIVPRAHLIGKFARKCTKAAVRRTSTTTAGIYLSLLLIQCFPDTINLIRSGIDMWKGQCGQLVKSVVVLESLRAIGLAVLSFHVFPQLDLARCLVLSACFPLVAVLQRSLVAMVSAARTGRSFRNRLGRCFVAIPHVIMFLVLMSSCYVWALFDNKFTAIIALPIGVICTSAGFWESWIDTTHSGTSFDELYRLKYAVRKMNTTTKLIVSLMRIVCTVSVLVSAVYINDHKKLNSSHFVKAFFSFSTRQPHTRLLLLATGIIVLHFVMRGISRFLAALDLHPFSFVHPLSIAPLIAYGYVRYACQSPTCSIARRLARFGLHWVCDQWFQSARGIASPDFYICLIWLLVGCYRGWRLVRQRYFDTNEEIISSMPPVCNGLCIEQSLVVFQHSLNRQEKTMLTEEEDISDENDELRIRNDEVDRVSTVYGCATMWHETETEMRQVLRSILKLDVDHATRMNNKKANELRYRLEGHIFFDDAWEDVEEDGIEKRQPNEYFNMFFDLLNEMTGERLNEEGKMETRILVNTPYGGRLVVKLPSGTLLFVHLKDKKMIRHKKRWSQVMYMYYLLGHRIMDCPLSIEDRQQMADNTFILAIDGDSKFEPDALLRLLHLMNAKSDIGCACGRIHPIGNGIMVWYQKFEYAIAHWFQKAAEHVFGCVLCAPGCFSLFRASALMDDNIMHKYTKTASEPRHYVQYDQGEDRWLSTLLLKQGYRIEYAAASDAETYAPEGFEEFFNQRRRWTPSSIANTVDLLMDYKRASENNDAISYAYIAYQFLVIFFSMLGPAIIFTMLVFAQVAAFELRGSDVMLYNGIPIGFFIVLCFTTESNIQLIYAKYMSIAYAFVMLAVLVATSSQIVLETVLAPTSLFIVTMVGIFFFAACLHPKEFTNIIHGVVFFLMIPSTYVFLTLYSLINLNVITWGTREAVAKATGQKTKKAPMEQFIDRVIDIVKKGFRLISCREKKEHEERREKMEKKMQRMELALRSIESGADVKKILDATEEKEKREEETQTADFPIEENVEKTQKEIQKANRYVWMTSHSLKVCERGKLKSAEKVFWNELINAYLKPIKTTPAEMKAVAEGLASLRNQIAFTILLVNSLLALAIFLIQKHKNVLSIKFSPIKNFRWTKMNEMTGQYEETDEPLKIDPLGMGIVVFLLIILFVQTLGMLLHRLNTMIGAFQEVKNLYEYGVSPVINTKNDDERIMNNARLMINSLGVSTGHAADGYTRHRGEESDTGNVLYKLQKARLAKRMQRSALSTTE | 2.4.1.16 | null | cell wall chitin biosynthetic process [GO:0006038]; chitin biosynthetic process [GO:0006031]; eggshell formation [GO:0030703]; positive regulation of protein localization to cell cortex [GO:1904778] | cell cortex [GO:0005938]; cell periphery [GO:0071944]; cell septum [GO:0030428]; plasma membrane [GO:0005886] | chitin synthase activity [GO:0004100] | PF03142; | null | Chitin synthase family, Class IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:20971008}; Multi-pass membrane protein {ECO:0000255}. Note=egg-1, egg-2 and egg-3 maintain the homogenous distribution of chs-1 at the unfertilized oocyte cell membrane, thus ensuring the formation of a continuous and cohesive eggshell chitin layer (PubMed:17869112, PubMed:20971008). In the fertilized embryo, co-localizes with egg-3 to cytoplasmic foci in an egg-3-dependent manner (PubMed:17869112). {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:20971008}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evidence={ECO:0000305|PubMed:16098962, ECO:0000305|PubMed:20971008}; | null | null | null | null | FUNCTION: Essential for the embryonic synthesis of chitin, a component of the eggshell. {ECO:0000269|PubMed:16098962, ECO:0000269|PubMed:20971008}. | Caenorhabditis elegans |
G5ECD9 | AEX2_CAEEL | MNSTDIIANVTKPFVENLTLGETAFYISCGIVGTVFNALVLWIALTYINTEDKPRQIIVINMTVADLLMCIVYMKTRPWLSHFNLWLCHPYYVIIWTCQMCSCLNLVWLNVDKLIYIQFPLHYYQIVNRKRLLWITAATWGGLYAMNIALVTFLKITRGSCLGVSLNPYVYLLSPIFYVVMILTSFSLSALIYCIAHNLTHMEERQRSKLFRRLFFLFSSTLWTFFTCLPYRLLYLFSIFCGETCQINNYYKTATNLFFRLLIVGIMINPVITIWTQRIYRLRLMRMFGRLRENSSTEVLMVSNRRASERPPEHTPLRCDM | null | null | lipid transport involved in lipid storage [GO:0010877]; neuropeptide signaling pathway [GO:0007218]; positive regulation of defecation [GO:2000294]; positive regulation of intestinal lipid absorption [GO:1904731]; positive regulation of triglyceride transport [GO:1905885]; regulation of defecation [GO:2000292] | cilium [GO:0005929]; plasma membrane [GO:0005886] | neuropeptide receptor activity [GO:0008188] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23583549}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:18852466}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor for the nlp-40 neuropeptide (PubMed:23583549). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (PubMed:23583549). Plays a role in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds (PubMed:18852466, PubMed:23583549). Specifically, acts in GABAergic neurons, such as AVL and DVB, to control the expulsion step of defecation (PubMed:18852466, PubMed:23583549). Required for fatty acid uptake and metabolism by intestinal cells and therefore regulates the levels of triglycerides in the intestine (PubMed:25849533). {ECO:0000269|PubMed:18852466, ECO:0000269|PubMed:23583549, ECO:0000269|PubMed:25849533}. | Caenorhabditis elegans |
G5ECE3 | LAM3_CAEEL | MRLWLGLLAVSNIALGGWNTSEDASIWENYVEDSNYHEFISSESERGLFPNIFNLATNSLITATDTCGQYTAEEYCKLVEHVLLRKTTNTQSPQCDICDANNVHKRHPIEYAIDGTRRWWQSPSLANGLRFEKVNITIDLRQEYQVAYIILKMGNSPRPGTWVLEKSLDGEYYEPWQYYAMQDAECMRQFGIPATTGVPRFQKEDEVHCTSEYSKITPLENGEIHTSLVNGRPGAENTSLELQKFTRARFVRLRLISPRTLNADLMIINKKSDSLDKSVTMRYFYSISDISIGGQCICYGHAESCPSDPVTGQFKCECRHNTCGESCNRCCPLFNQLPWKPGTNSHPNVCQQCQCFNHAHSCVYDDELDRNKWSITPEGVYEGGGRCLECAHNTEGFNCERCKDGYYRPSGLSHYREDACRTCECDPVGSVSDACVRDDQSAENGQKPGDCICKPGFGGRRCERCAPGYRNHPTCEPCPCNRAGSVNFDTCDGASCQCKANVEGIYCDRCKAGTIHLSASNPLGCQPCFCFGHSSTCTQGKWNKAQIINNIGWHLTDLTGGKDVKPEVENGEVLMFNANQNQDRSLYYWKAPDSFKGNMLNSYGGYLHYDVYYVPTEQGATVFVADVAIEGNGIKIEYHSRIEFLPREKMTVAIPMSELSGWYNAEARSPVDKADMMRALANVDRFTVRATYHQPQLQSSIFGLSLDTAVPAPDEIVEEDTSLKALAYHTQDTLMGGVEVCECPENFAGNSCESCVPGYRRVNNQLYGGRCEKCDCHGNSEECDPFTGECLNCRHNTTGSRCELCKPGHVGNPSRGGELGACEQCECPSLDLNPNPECISTELAVLGSVASNEDNYVCINCPLGYEGNKCEYCSDGFFEDPLTGKCIECTCNGNIDPMGIGNCDSETGKCLKCIGHTTGDSCESCKEHHWGNAQLHTCKPCGCHTQGAVNPQCSEENGECECKENYIGAQCDRCKENHGDVENGCPACDCNDTGSIGSDCDQVSGQCNCKQGVFGKQCDQCRPSYFNFTDAGCQFCHCNIYGSIEDGKCDQTTGKCECRENVEGTMCEKCADGYFNITSGDGCEDCGCDPTGSEDVSCNLVTGQCVCKPGVTGLKCDSCLPNFYGLTSEGCTECEPCPAPGQVCDPIDGSCVCPPNTVGEMCENCTTNAWDYHPLNGCKLCDCSDIGSDGGMCNTFTGQCKCKAAYVGLKCDLCTHGFFNFPTCEPCGCNAAGTDPLQCKDGQCLCNEIGECPCKKNVHGTKCDQCGEGTFSLDSSNLKGCTECFCFNRTSNCEQSDLVWQQMYAEDRRAVFQEPWEFYTKKHNINLLREKPSHFNSYPTDATPLYWPLPSTMLGDRTASYNGFLRFKIWNEDNRRGLHGIRPDQQYFRHFPQVIIFGNNRIELEHIPMEINDDGIYKIRLHESEWRVRHSPELTLTRKQMMVALQDTQGIYIRGTYTYPARGDAINIQEVSLDVAVPESKIVAGLSTTKAIGVEKCLGCPQGYTGLSCQNPEVGYYRKKHREYLNQADDIALIGWSEPCSCHGHSQTCNPDTSVCTDCEHNTFGDFCEHCLPGYIGDAREGGANACTKCACPLVENSFSDSCVAVDHGRGYVCNSCKPGYTGQYCETCVAGYYGDPQHIGGTCSPCDCHPDGSLHGACNPLSGQCECKPGVTGRTCSMCQERHAFINRVCTSCDQGCYLPLMETMDTMEEHLGRQNFSGLKPIPWKRVWRIGNESQDLSTFVGGIDKDGEIVKDSKWAKDAFALLDEVNFQMGRSNKSAVSIKQFTGIAEQLILDAQIHYANAFNTTNFLKMFAEHGATTVGGAALDGMLMEAEAHLNATVERGEYVEKRLNRAQQEHKKAEELLKMVTAQKLNETIFEDLKNRIDVLEQWMNDYRETIYDVSKKDTADAERMSLVVGKRINRYKEVSNEIEKLRVEAEDQIAYSRNSIEKARSEELMNMFEDKEKINMTLAELPDLVEQCQNITLLYSQLIDEYDEEYVQTAGRHAEKLEVQAQKIVDRFVDTRTETENPLKASHAYENIVEALKNATEAVDSAAEASEAVSKMLGSEGSESGDANEESLRSQLEKLKNESSLSNVDNSNAVKIVEELKKEKKDLTDRLGHLNELKTSIVKRLGVIKNEASSWDDKHDRMHSILKNGAKTAHERSANVKKESEGIKTEVSAIKAEVEKLMNSTSSGVQEDMEKIRASRTGMEYGAQKLTKVNKLSTANQGRTDKMARNIAILKAKIEQAREKAYQIRLSLNSGERGLCKRSYISPASPSPVNTFHVSYRPLQQVSDAVILVSKTKGRRTQPSEHLAVEIRDKRVVVHWDIGSGKKMITNSHPINYVPSNDRVTWYHIDVLRIGNAVNLTVALKESYDGGFKPRGAPVSVFVGNSKDDNSIFNTIPGETTIDVGTDETVASDIGLTTHKFSGIVGGLRIDEVPLPLWSFESTTGECEGATSPPKTSQRGHLFRDGFANVSMSVSERTMSAITVIFNAFSPNGLLYFRGSEASGDFVAIYLNDGKVMFKINLGGGSVAELTSQNVYNDGKEHTVKAIRTGSEMYLQVDSDADRFNTVITGENTALNIENENHYVAGVPMTLNKEVFGDINWNGFIGCILTVKPSQVGELDLDHPEHSQGKTDGCSQVSGVTDKIIGFPKPGYLITKGISIDNSSTFAFSFRTREENGTLVYQSSKLQKVSKRDSEDDGKGYIAFYLFRGYLVLHFGKDASSRKEVVTFRSSHPYNDGQVHAVFMERNGKIISVKVDDKEIGDSQSLSDETSVGTTSGRLILGGFSDDLKPPNNEIPITSFFIGCISDVFLNMKRVSLAPEKHNAQIGMCSMDDTQGLSPIDDPIDGNGHNGHRKSSKLSFEATNRNYYEVSTQSSHLVMNPNGEETVEKTCETSLGSLQGAVRYGLSKSSHSRINFEAPYPNITDFTVKLSLQTETSNGMIWAWANYKNYTRYIFLDIIDGFATLEVKGHKQPKILKHLGNRINDGQWHDITVEKKNRSLKLIIDSLGPVEMTDCPTPKVMKKRVYVGGVISRHRRQFGLTTPGLDGCIRDFEMNNRIFNNLDEPSTSKNVMPCAKACKLKRSSKRKRNSKN | null | null | animal organ morphogenesis [GO:0009887]; axonogenesis [GO:0007409]; tissue development [GO:0009888] | basement membrane [GO:0005604]; extracellular region [GO:0005576] | extracellular matrix structural constituent [GO:0005201] | PF00052;PF00053;PF00054;PF02210;PF00055; | 2.60.120.200;2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12783803}. Secreted, extracellular space {ECO:0000269|PubMed:12783803}. Secreted {ECO:0000269|PubMed:12783803}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:12783803}. Note=May be localized to neuronal cell surfaces by specific receptors. {ECO:0000269|PubMed:12783803}. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity). Required to assemble a stable basement membrane and for organizing receptor complexes and cytoskeletal components to the proper cell surfaces (PubMed:12783803). During embryogenesis, does not require the presence of collagen type IV in order to associate with cell surfaces, prior to assembly of the prototypical basement membrane (PubMed:12783803). Plays an important role in muscle contraction of the body (PubMed:34723150). Probably plays a distinct role from the related laminin subunit alpha epi-1 (PubMed:12783803). {ECO:0000250|UniProtKB:P25391, ECO:0000269|PubMed:12783803, ECO:0000269|PubMed:34723150}. | Caenorhabditis elegans |
G5ECG0 | TACC1_CAEEL | MSLNTTFTKEDGTEVVIPFNGSQNGHPENEEPEVEEAAEPSSSVETLCGATRGDIIVMKHTTKALTELIERLLHSDEFEVRRCSNGQIISQGRCNGTTPGNGIGGGGASSEELEKALKDRDAARAEADKLHANYATLFASFNTVREAANDIRGEYEDARDKLKLAAAEVDEWQAKFLAVKDNANSELERASVEYDDLLRSHDENTKGLRLRVKRQEIELSSKNDEIKVLTNRVSELSQICDQLLNDVDVSDGMSVISTDA | null | null | astral microtubule organization [GO:0030953]; cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic cell cycle [GO:0051321]; microtubule-based process [GO:0007017]; mitotic spindle elongation [GO:0000022]; mitotic spindle organization [GO:0007052]; negative regulation of microtubule depolymerization [GO:0007026]; pronuclear migration [GO:0035046]; regulation of microtubule polymerization [GO:0031113] | axon [GO:0030424]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; mitotic spindle astral microtubule [GO:0061673]; mitotic spindle microtubule [GO:1990498]; perikaryon [GO:0043204]; spindle [GO:0005819]; spindle pole [GO:0000922] | protein domain specific binding [GO:0019904] | PF05010; | null | TACC family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432}. Cytoplasm {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:17666432}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12956952}. Cell projection, axon {ECO:0000269|PubMed:26339988}. Perikaryon {ECO:0000269|PubMed:26339988}. Note=Initially enriched at meiotic spindle poles, but then recruited to the sperm centrosome (PubMed:12956950, PubMed:12956951). Localized to centrosomes early in pronuclear migration (PubMed:12956952). Centrosomal localization is dependent on air-1, tbg-1 and zyg-9 and is also controlled during the cell cycle, with high expression during prophase and metaphase, but with expression reducing from anaphase to telophase (PubMed:12956950, PubMed:12956951, PubMed:12956952). Accumulates at the centrosome during interphase, ready for the next mitotic cycle (PubMed:12956951). Cycles between cytoplasm and centrosome during mitosis in a cell cycle-dependent manner (PubMed:12956950, PubMed:17666432). Diffuse localization along the axon and localizes to perinuclear spots in the perikaryon (PubMed:26339988). Following injury co-localizes with efa-6 and ptrn-1 in puncta of the perikaryon (PubMed:26339988). The zyg-9/tac-1 complex localizes to centrosomes throughout the cell cycle and the kinetochore of metaphase and early anaphase chromosomes (PubMed:12956952). {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:26339988}. | null | null | null | null | null | FUNCTION: Involved in microtubule formation, polymerization and assembly, regulating microtubule nucleation and length (PubMed:12956950, PubMed:12956951, PubMed:16054029). Plays a role in pronuclear migration and mitotic and meiotic spindle elongation during early embryogenesis (PubMed:12956950, PubMed:12956951). In complex with zyg-9, functions during the early stages of embryonic development to regulate microtubule assembly throughout the cell cycle (PubMed:12956950, PubMed:12956952). Specifically, the complex is required for the formation and growth of astral microtubules and spindle microtubules during mitotic spindle assembly (PubMed:12956952). At anaphase, the complex is required for mitotic spindle positioning in one-cell stage embryos (PubMed:17666432). The complex acts in a partially redundant manner with the tac-1/zyg-8 complex to regulate microtubule assembly and processes during interphase, mitosis and meiosis in embryos (PubMed:17666432). Plays a role in injury-induced axonal regrowth, regeneration and microtubule stability in PLM neurons and this may be downstream of efa-6 (PubMed:26339988). {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:23155404, ECO:0000269|PubMed:26339988}. | Caenorhabditis elegans |
G5ECG2 | FOS1_CAEEL | MFEQPSSTTNTTTSSGSGSDSNHYFELGPRNPINQAHPTSVIVPPRQHHHQIHQQQTDNSPLTPCTPYYPSNAYGLPLFFGTDFLQFQPSDIPSPLTPNISSPLTPHPFGPIPAIPTNQIYNRTFTDFYSTAASSPMVQYSTVKKSSAGRKPKEEDNMEDDDDDKRLKRRQRNKEAAARCRQRRIDLMKELQDQVNDFKNSNDKKMAECNNIRNKLNSLKNYLETHDCKLSREERTHEINRLIIPPSTVPPSQPYLQHSLRVHPPRADSVPYSIRSGHSSSSSEQHSPVEDYKPSIDQLLLPPISCIQNIKDRNINSMPPPALPASTSAAGIHVITSIPVSHANSLHGRSENVFAEPERKIPKIELDQTLTSLTMPDDVERPSALPTLSRIVENQPITTPSRPFRLGGEYQNQTPQSTGNGLFGGPPGPFDLLSSNTGLTPSGQPTMNFVSTPTPIQPHPDADLRPL | null | null | anatomical structure morphogenesis [GO:0009653]; basement membrane disassembly [GO:0034769]; cell fate specification [GO:0001708]; determination of adult lifespan [GO:0008340]; innate immune response [GO:0045087]; negative regulation of stress response to copper ion [GO:1903854]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of syncytium formation by plasma membrane fusion [GO:0060142]; regulation of transcription by RNA polymerase II [GO:0006357]; response to starvation [GO:0042594]; vulval development [GO:0040025] | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565] | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: May be phosphorylated by kgb-1. Phosphorylation at Thr-440 increases sensitivity to heavy metal stress. Phosphorylation inhibits homodimer formation, and promotes association with target promoters. {ECO:0000269|PubMed:23437011}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15960981}. | null | null | null | null | null | FUNCTION: Developmentally regulated transcription factor which binds and recognizes the enhancer DNA sequence 5'-TGA[CG]TCA-3' (PubMed:23437011). {ECO:0000269|PubMed:23437011}.; FUNCTION: [Isoform a]: Plays a role the development of the reproductive system, controlling events including anchor cell (AC) fusion and invasion (PubMed:15960981, PubMed:17488621). Regulates downstream transcriptional targets, including zmp-1, cdh-3, him-4 and mig10b, to promote the removal of the gonadal basement membrane during AC invasion (PubMed:15960981, PubMed:24553288). Regulates aff-1 expression to promote AC fusion (PubMed:17488621). With jun-1 regulates egl-1 and lin-12 expression to allow uterine cell specification and development (PubMed:17942488). {ECO:0000269|PubMed:15960981, ECO:0000269|PubMed:17488621, ECO:0000269|PubMed:17942488, ECO:0000269|PubMed:24553288}.; FUNCTION: [Isoform b]: Required for ovulation (PubMed:19570917). Controls plc-1 expression in the spermatheca to regulate spermathecal valve dilation (PubMed:19570917). Acts with hda-1 as a downstream repressor of the kgb-1 mediated stress response pathway that transcriptionally represses genes involved in the response to heavy metals, such as kreg-1 (PubMed:23437011). {ECO:0000269|PubMed:19570917, ECO:0000269|PubMed:23437011}. | Caenorhabditis elegans |
G5ECG7 | MTP_CAEEL | MFSSRIWLLLAVTVGVCLAVPDLDEIKKNLRKHGPDYYKNQPKMNENTVRLLKVDYWFRTESMIYDDIDNKEKDPSTVIAGNFSFETLHHDVEGGMLGRFTLTQCNTDNCGNPSPIYIAFRQGGNNAEHILKASDESDATWNFLYAIVNTIYTPAEYGEGDEQTVDTIYGRCFVNFGRPEDKRFRRIIEKCDLGYGTNFTKFEGIESVQYDQDVWYTQNTKVDADIIMVDAIEMLAFKSPLHEKYGFTLESRTHVEITNRTRVFVTSYCNDTVPSAKCAEQAFGAVRVGGKLYEHVKIAQEQSNKLTKLIGTYRRHLQDMGDSHICEKHSLLYSQIAQEARLAKRQDWEAAIQYPENDHVLSLIASALGGVGTAESITTAREVLLTASPDYLDDLLFGISQSSSNNEKWHKQLMYWLGSLDKKSEEYWKVANTIATVLNKRCEASTSSLNSCNKGKETIVNKFITDLTAGGVEVRVLEVLENIPIFGSYTFAKKFICETESEDVQKAALNVILAASKNLYETQLTHKLIKLFRNTCSQETPTSHSQLAIDILLKCVPDHQNVATLILRTETLNPDDQEKWHYLYKAIEASGNKDELKAEFWSRMRKFKVFRPNFLHRALQADSHVHWQEIADASNFQLFSTANTEFLQKSFKRSIFELSMKKGRKEHNLFSLSIDTEHLEQFVTGSASSRSGAPQGSVRIGVAGHKLPTHHIFKGSTDLLSTVWEADGRTHKAFEGHVPVRDVRLSVPLLSGLTLDVDSVGAISMRVLASAEVSLWNQRSNAKAEAYTSGSLHLTASLYHHSEPVRHVESTISALSTFTTDTRAIFETLPYDFCLRTSNSNVDINQKTVVQDQIGKHKKKTLNRKRVHPGVTYRLDDSTIRQCNSYLEQFRL | null | null | endoplasmic reticulum unfolded protein response [GO:0030968]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; plasma lipoprotein particle assembly [GO:0034377] | basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794] | lipid binding [GO:0008289]; phospholipid transporter activity [GO:0005548] | PF19444; | null | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17924655}. | null | null | null | null | null | FUNCTION: Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Does not catalyze transport of triglycerides (PubMed:17924655). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:14657502, PubMed:17924655). Required for normal expression of klf-3 (PubMed:23639358). {ECO:0000250|UniProtKB:P55157, ECO:0000269|PubMed:14657502, ECO:0000269|PubMed:17924655, ECO:0000269|PubMed:23639358}. | Caenorhabditis elegans |
G5ECH5 | PP4R1_CAEEL | MIKSQFATLIRVLIDFQKFWVFLSIFCTFLVVFKFDNLMFQKVRRVFQQNRKNSESIQPKLSTVSGSNSGEGMDKRNTGFSNLQQLGGAIFIDDAEDEPPRVKSSEDSRPAPHWLDSPRDSTTLPDIIASTYSDFIDEAEYATKQMLAILETLNPIEEYIELFESSFKAIEVRLPFDVILNDEKKPDWDAIRRKLIMGSLTVNTTSEKPGITTNQMTAIFDAIPFLFDAVACNPELYEYQNTLSMIVMIAMTGNSMIRRQSINAVQALMERNMLDQDFMRDGVVPGLFNIYQSGVGAFQSNDLRMECVQALCQVISYDAIHDRRWLFDNFLPRFSQMLKDPTMHVRKSALHIFGNLGNMFGQKFTEVFLVPHLITLSCDMTWAVRKVACEIFVKVAECASNQVRIDILSPNFVRLLNDPNKWVSFIAYQQLGPFISLFANPDITGLELRNGQVVVRDPVVLEPSVTEQEDPSNSTFSEDTSDDFRTLPKDTWLPEVDFNDDFEYQLGSIDNTQNQKELTTVTTALVKTPKRGERVMDSVLSGINKMFGSLERSSPKSKEVEKIAATFSSPSKRSPLSLHSAVSLIDKFSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCSSTDDLTKLGLEDDDSPDAAEDSDDFTSETRTTSPRGRRIATNAWSKLDIRQKIFLRRLGALPPSFPKKKATHSSSSSPRKSPTRSPLLSSRKKGLLFDFAAPIEIKSSSSDHSETIPVRTANQQQEKADDDKLNTDERQQYMENSGPKFNTDEDSTNDSDSDDEDNDFEKSFVADEDDGEQDDSPLSIEIKSSSSSDFESVSAATPTSQEPVSNEFSLTYWSSNYAISSIEDELKPFGSSSSFTNSPTSNSYLESRFDVMKVNLSPRARSVSFGTNGSPISTSPRRKANSTSEPSPPNTGNLKSDDSIVMLNTEEKEKLGILDFDEMNMSISSNSSIHGEAAMTEDSDISLTSIEQAALQHVPVDLVESYMRVMGPIGGSGSGGGGNGSSTTIATGDPSLCAETYRHCAHNFPAVCYTLGRAAWPRLKLVFRKLAMDEQARVRQSISHSIHEIANMLGQEITDEDLLPVFYDLRNDQNPDVRNGILIHLYDFVKFLSPEKRDEMILSLPQFFPIGAQPGNQAQNGDWRSRFELISQLSKLCSLYSIQDVNFHMSGIALTLADDRVAEVRREAVMLVSTIVGALVTAEWDNIKGVRDIENGHVDVKKKSNKTDFLSEQFVDDIVSSFAKTQKWTRRQTFCFICAQILRDKQCDGIQFRYFFATPLQQLAQDKVPNVRLASCEALSVWRKTLIAARAQERRGQSPISSPASEPSAIRRDINLVSDMMVKLSNDSDIDAAFIAKKCQGLTDDHQPVDVASRTTRMREREEQFFGDIILSYSPGCNARVSGKEIKQLIRHDQGAVQKAAPLQSMEDFGDEILAHAADSVNIQTPPEVVATVQRVSITNEQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDIPMDPAPTLPPPVTSKNQSSSPITASSSDNNETSA | null | null | embryo development ending in birth or egg hatching [GO:0009792]; establishment of mitotic spindle orientation [GO:0000132]; negative regulation of meiotic spindle elongation [GO:1902120]; polar body extrusion after meiotic divisions [GO:0040038]; regulation of mitotic spindle elongation [GO:0032888] | cytoplasm [GO:0005737] | protein domain specific binding [GO:0019904]; protein phosphatase activator activity [GO:0072542]; protein phosphatase regulator activity [GO:0019888] | null | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23918937}. Note=Localizes to the cytoplasm during meiosis and mitosis. {ECO:0000269|PubMed:23918937}. | null | null | null | null | null | FUNCTION: Probable regulatory subunit of serine/threonine-protein phosphatase PP4 which may play a role in meiosis and embryonic mitosis. Probably in association with catalytic subunit pph-4.1, regulates microtubule severing during oocyte meiosis II by dephosphorylating and likely activating mei-1, a component of the katanin microtubule severing complex. {ECO:0000269|PubMed:19087961, ECO:0000269|PubMed:23918937}. | Caenorhabditis elegans |
G5ECH7 | CDK5_CAEEL | MLNYDKMEKIGEGTYGTVFKARNKNSGEIVALKRVRLDDDDEGVPSSALREICILRELKHRNVVRLYDVVHSENKLTLVFEYCDQDLKKFFDSLNGYMDAQTARSLMLQLLRGLSFCHAHHVLHRDLKPQNLLINTNGTLKLADFGLARAFGVPVRCFSAEVVTLWYRPPDVLFGAKLYNTSIDMWSAGCIFAEISNAGRPLFPGADVDDQLKRIFKQLGSPSEDNWPSITQLPDYKPYPIYHPTLTWSQIVPNLNSRGRDLLQKLLVCNPAGRIDADAALRHAYFADTSDV | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20510931}; Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941}; | anterograde neuronal dense core vesicle transport [GO:1990048]; axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cell division [GO:0051301]; chemical synaptic transmission [GO:0007268]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; negative regulation of dense core granule transport [GO:1904810]; neuron apoptotic process [GO:0051402]; phosphorylation [GO:0016310]; positive regulation of dense core granule transport [GO:1904811]; positive regulation of protein transport [GO:0051222]; positive regulation of synapse assembly [GO:0051965]; regulation of gene expression [GO:0010468]; regulation of neuron remodeling [GO:1904799]; regulation of protein localization [GO:0032880]; regulation of synaptic vesicle transport [GO:1902803]; regulation of terminal button organization [GO:2000331]; retrograde synaptic vesicle transport [GO:0048491]; synaptic transmission, GABAergic [GO:0051932]; synaptic vesicle transport [GO:0048489]; vesicle-mediated transport [GO:0016192] | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleus [GO:0005634]; protein kinase 5 complex [GO:0016533]; synapse [GO:0045202] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20510931}. Cell projection, dendrite {ECO:0000269|PubMed:20510931}. Note=Localizes predominantly to presynaptic sites and in dendrites as faint puncta. {ECO:0000269|PubMed:20510931}. | 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:20510931}; 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:0000269|PubMed:20510931}; | null | null | null | null | FUNCTION: Proline-directed serine/threonine-protein kinase which, in several motor neurons, promotes the polarized trafficking of synaptic vesicles and dense-core vesicles (DCV). In the ventral nerve cord, phosphorylates lin-10 and thereby prevents lin-10-mediated anterograde trafficking of the glutamate receptor glr-1 (PubMed:17671168, PubMed:21609829). Involved in the inhibition of glr-1 trafficking in hypoxic conditions (PubMed:22252129). In DA motor neurons but not in DB motor neurons, regulates axonal transport of synaptic vesicle precursors by inhibiting dynein-mediated retrograde transport (PubMed:20510931). Regulates the trafficking of dense-core vesicles in DA and DB motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite (PubMed:22699897). May regulate these processes in association with cdka-1/p35 (PubMed:17671168, PubMed:20510931). Activity may be regulated by cyy-1 (PubMed:20510931). Involved in synapse formation during DD motor neuron remodeling by regulating transport of disassembled synaptic material to the new synaptic sites probably by activating the motor protein unc-104/kinesin-3 (PubMed:21609829). Regulates microtubule polarity in the dendrite of DB motor neurons (PubMed:22699897). May also play a role in GABAergic synaptic vesicle localization in the ventral nerve cord (PubMed:16996038). {ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:20510931, ECO:0000269|PubMed:21609829, ECO:0000269|PubMed:22252129, ECO:0000269|PubMed:22699897}. | Caenorhabditis elegans |
G5ECJ0 | GBR1_CAEEL | MSASILILATCHQVLADFNSYVVPQPHAQRDHRQDISQHYDYLMEENDEPLGRGAAPSKYRSSHGQAQHRPEMTESENFAQPNTESVFSSGGVDSYGETRDFLQFLRRIQYDHRQVPENEKGEATYVEVSVVVSNIRAVSEVTMDYALELFYRESWRDPRLQYDRKLFKNKTELALHESYTNFLWFPDTFVPNAIASKNPQRNSISHRSLLRLDETGKLLYSRRISLVCECTMDLTLFPFDKQLCKLGIESYGYTADHVVYKWSKGARTALELKKIRLPDFTIQEAYVTSQMESYATGNYSRLYVCFVFSRSSGFCFLQLIIPSTAVVITSWVSLWMETETEFQDMISIILAITFLIFSYNEMMPRVSYIKAMDIYLGVCFMIVFLSLIKLALVKYMRQKIMLTSDSGNSLREMSQMSTRQRLRARKTSNMNFRNNGGGSIPINEEHQQMLTVPNGEDKMANGDDKEANNNGKSHLSDMLEIRITQRTMHRFHWISQMLFFFGFVIFCLFYFLIYPNLHIVSVDPACDKNLAEWFADIY | null | null | chloride transmembrane transport [GO:1902476]; defecation [GO:0030421]; lipid transport involved in lipid storage [GO:0010877]; positive regulation of intestinal lipid absorption [GO:1904731]; positive regulation of muscle contraction [GO:0045933]; potassium ion transport [GO:0006813]; sodium ion transport [GO:0006814] | GABA-A receptor complex [GO:1902711]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; GABA receptor activity [GO:0016917]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily | null | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14555952}. Cell membrane {ECO:0000250|UniProtKB:P18505}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18505}. | null | null | null | null | null | FUNCTION: GABA receptor that functions as an excitatory cation channel. Permeable to monovalent cations such as Na(+) and K(+) (PubMed:14555952). Has negligible divalent cation permeability (PubMed:14555952). Does not act as a chloride channel (PubMed:14555952). Mediates enteric muscle contractions required for defecation (PubMed:14555952, PubMed:16236771, PubMed:2323555). Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells (PubMed:25849533). {ECO:0000269|PubMed:14555952, ECO:0000269|PubMed:16236771, ECO:0000269|PubMed:2323555, ECO:0000269|PubMed:25849533}. | Caenorhabditis elegans |
G5ECJ6 | CSK1_CAEEL | MSNGNSYNHHHQFPMSIPISCSSHSIQSQSRMNTLNANRDLLSPGNDVIVTRTVSPSFYSHGMPARDNVFRKDDHVRILGNTTDPAWYRARNANQEEGLVHADCVVRINGQAYDNGIVRMRASGCDVAPGAASTTSSTSSHHSTAANHQPWFHSMISRENTEKLLRGKPDGTFLVRESTNFPGDFTLCMSFHGKVEHYRIEQTSGGQLTCDKEEYFSNLTQLVSHYKRDADGLCHRLVTPIICETATFSSNGSSSFGSSSTVDLEDRTSVFRHAGLVISSNDIDVGDTIGHGEFGDVRLGTYKNRKVALKVSKRHGNGMLDSLLDEAKFMVGLSHPNLVTLVGVVLDDVNVYMITEYMANGNLIDLLRSRGRHALERRQLMMFAMDICQGMCYLESKQIVHRDLAARNVLLDDDLVAKVSDFGLAKKANSQSHDSASGKFPIKWTAPEALRHSQFTTKSDVWSFGILLWEIFSFGRVPYPRIPIQDVVRYIEKGYRMEAPEGCPPEIFKVMNETWALSAQDRPSFGQVLQRLTTIRNTV | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P41240}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P41240}; | embryo development ending in birth or egg hatching [GO:0009792]; larval feeding behavior [GO:0030536]; muscle cell development [GO:0055001]; nematode larval development [GO:0002119]; nematode pharyngeal pumping [GO:0043050]; phosphorylation [GO:0016310] | cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF07714;PF00017; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSK subfamily | null | 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 plays a role in pharynx function by regulating pumping and the orientation of pharyngeal muscle fibers, independently of src-1 and src-2 (PubMed:19210548). May phosphorylate and thereby negatively regulate src-1 and src-2 activities (PubMed:12527374). {ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548}. | Caenorhabditis elegans |
G5ECK3 | MAB23_CAEEL | MPKEQYMCQLCANHGIFNQPKKGHKQKCPYRTCPCSLCALNTKRRALDQIERQLKHTNEPMTGQTATSMASPTPECPLSPTTPKMTPHTPTSGKDTFRNSISSSNMAFTVQLPATITKKELKLLRRDDTPLQNSLERPFPRSIDEAIETIKKEKMSSIFHSAEMLAVGESATSLI | null | null | negative regulation of gene expression [GO:0010629]; neuron fate determination [GO:0048664]; regulation of male mating behavior [GO:1902435]; regulation of nematode male tail tip morphogenesis [GO:0110037]; sex differentiation [GO:0007548] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00751; | 4.10.1040.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. | null | null | null | null | null | FUNCTION: Probable transcription factor that plays a role in the development of the dopaminergic neurons of the male-specific genital sensilla (simple sense organs) known as rays, by negatively regulating the activity of the transcription factor ast-1 (PubMed:12231628, PubMed:22069471). Involved in male mating behavior, probably as a result of a role in the differentiation of male-specific diagonal muscles (PubMed:12231628, PubMed:22069471). Required for development of the male proctodeum (PubMed:12231628). May be dispensable in hermaphrodites (PubMed:12231628). {ECO:0000269|PubMed:12231628, ECO:0000269|PubMed:22069471}. | Caenorhabditis elegans |
G5ECL2 | SYNJ_CAEEL | MSVRGIRIWRRNDARFQPSILVEKNGLDGSLLFQGGAIATLDSDSTDVERRSYQKIVDAYGILGVLAITKDEAVLVAVTGVLSVGQLYGADILKITNVEFISLRTFGSVENVDSRIIDLQRLLSSQMFYFSSLQSYDLTRSAQHRDSHDCSDARFFWNRSLHFSFQRYGIDTDNWLLKCMAGSVLVRVVYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKLRAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFAPLVDFIDFDYHAQMKISKEAIVQLKKKMSPHMTKHGFFYSMGKEIVKRQTGVIRTNCLDCLDRTNAVQTAIGLQMSHDQVAFLNLNAGKVNVEQRVEEILRDLWQKNGDQCSTIYAGTGALDGKSKLKDASRSLARTIQNNLMDGAKQESFDLFLTGAAYDPRLFDRACNILPPSLIQESYYYHEYADAVSQLVERSPEIAEPQSIKIFVGTWNVNGGKNIHNVAFRNESSLSHWIFANSMTRLVSVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKKGKTQLLSYDRSELKTSDHRPVGAVFKVETFKVGGRKCVELIEDVVESMGPPDGTIIVSIAGKPRFPPQMFPPIHEKLKELGAQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGGTDQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDGAVFEFADEDEDAISVSSLTLTGSAPDRPRPPSARSEAISVAKLEWPTEQPNVLSTSMPTRASSASLANSSWYEHVPPLAPPQSNNNKSPPQACLFNPFTQSAPSPAPPPSTIPLPPTRGASVGPGPPAVPVRKAPPPPPRPVIPPRPKNM | 3.1.3.36 | null | acetylcholine transport [GO:0015870]; cytoskeleton organization [GO:0007010]; endosome organization [GO:0007032]; gamma-aminobutyric acid transport [GO:0015812]; Golgi vesicle uncoating [GO:0048212]; locomotion [GO:0040011]; muscle contraction [GO:0006936]; necroptotic process [GO:0070266]; phosphatidylinositol dephosphorylation [GO:0046856]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of muscle contraction [GO:0045933]; positive regulation of neurotransmitter secretion [GO:0001956]; protein localization to synapse [GO:0035418]; regulation of backward locomotion [GO:0043058]; regulation of forward locomotion [GO:0043059]; synaptic vesicle budding from presynaptic endocytic zone membrane [GO:0016185]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle transport [GO:0048489]; synaptic vesicle uncoating [GO:0016191]; vesicle organization [GO:0016050] | membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; synapse [GO:0045202]; synaptic vesicle [GO:0008021] | phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; SH3 domain binding [GO:0017124] | PF08952;PF02383; | 3.30.70.330;3.60.10.10; | Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:25918845}. Note=Localizes to puncta at neuromuscular junctions in the nerve cord. {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniProtKB:Q9D2G5}; | null | null | null | null | FUNCTION: Probable inositol 5-phosphatase which regulates synaptic vesicle recycling in neurons by regulating clathrin-mediated endocytosis. {ECO:0000269|PubMed:10931870, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:25918845}. | Caenorhabditis elegans |
G5ECL4 | BRAM2_CAEEL | MSSERRKDNPLRFALILHLLAVLVQGDIQPRFSCYNHYLAGIRTSSVLPISGHSSAPSNVKCIFENDVAFTEIHSALENSYQVMGKKSVNFQVLDLFHLRELVRRSHCTQTLTVTWKNVPEAGKGGLKVVSLLNETTRIEYSGDERQDFLFDETFAGVRHLIPDEDDNESNPTVTTTRLLCKHIPQPECLVRGKFEVDLEANLEWSYAFSFKTDITNQTLFTLRCGDTTSEVRLENDFFIRADGNAPVAVTHLSDATWHTAIVKHNQPDSHFLKIDDFPEIELGKSISDDTDKTITLSISVNGNIQLIDPTDTNDDCMYSFDKPQKRLQETVSTRTMCVGCGCPKLSGTFDGLSKCDEEDENSYNLRRDVDRLSFIHIDNAFDIDSNGAAIPAISTSFKSDSDVGLIFFGYWQNFHGKGRLQVYYHYDTISAVFCKHTDDEECSSCSIRSSEGFGKDQWIQTILWGGGDEIHLAVDSSVCRLQQLSNISLAEVYAIPQISGGAGLFIGGTWHEKKRRGLYKADAEQKYFENTREKAPVLRGCIKDVFVRGSKTDVSEMFEVQKQAMLNEPDDSNAFAVRKYCQSCIPACSEGTRCRSRAPLQDSAMICDCADELQFNTSEGTCNRERDTPVALSTAFLSENQIVLDIQNTKAILSKVWLKFALPKQINQAQRIVEFNSHRETLFNINLETDGTVNVQLHGQDTASRQLNLLDDRVHLLQLQRRTPMGTRHSAKKYDLYIDGFHTVVSDIGKLVLNNVSVTAAETEDEWSSVIVHDLGLSYEYDEHFAISHPSNVIHQVDLHSQLLPYQIRAPDLSKTGILDDSLWEKPAYVTDSEAAPVLESSPHGEVVDFTADIIEPEQLLSGRWILYSLFLTILLCLFILMCIVCYWCVLRPRAMRRTDTGSQRTIIRDSPDYAPVKMRRDSIGGISIDDDGSIGTDDTDLQAYRDIPSHRVKIYRESMVSILVPSIDQPAEAAIVKRSHSTISDQTPSRPHDTSHAPLVAVNDD | null | null | nervous system development [GO:0007399] | axon [GO:0030424]; plasma membrane [GO:0005886] | null | null | 2.60.120.200; | Neurexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14551437}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:28901288}. | null | null | null | null | null | FUNCTION: Maintains the normal guidance and termination of axonal branches of VC motorneurons (PubMed:14551437). By associating with cell adhesion protein casy-1, mediates axonal interactions to establish synaptic connections between the male-specific sensory neuron HOA and the AVG interneuron (PubMed:28901288). Plays a role in regulating male mating behavior (PubMed:28901288). {ECO:0000269|PubMed:14551437, ECO:0000269|PubMed:28901288}. | Caenorhabditis elegans |
G5ECM9 | CPI2_CAEEL | MKAILVFALIAISIISVNAGMMTGGSVEQDASQKEYSDKAWKAVKGINDQASNNGPYYYAPIKVTKASTQVVAGISTKLEVLVGESNCKKGELQAHEITSSNCQIKDGGSRALYQVTIWEKPWENFEQFTVEKIRDVTADEQF | null | null | positive regulation of vitellogenesis [GO:1903188]; regulation of oocyte development [GO:0060281]; regulation of protein processing [GO:0070613] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; vesicle [GO:0031982]; yolk granule [GO:0042718] | cysteine-type endopeptidase inhibitor activity [GO:0004869] | PF00031; | 3.10.450.10; | Cystatin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16857685}. Secreted {ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=Localizes to the sheath cell cytoplasm surrounding germ cells and oocytes. Localizes to yolk granules in the developing oocyte. {ECO:0000269|PubMed:16857685}. | null | null | null | null | null | FUNCTION: Cysteine protease inhibitor which inhibits members of the peptidase C1 family (PubMed:12704112, PubMed:15664654). Does not inhibit asparaginyl endopeptidase (PubMed:15664654). Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1 (PubMed:16857685). May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation (PubMed:24001183). {ECO:0000269|PubMed:12704112, ECO:0000269|PubMed:15664654, ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24001183}. | Caenorhabditis elegans |
G5ECN5 | STRD1_CAEEL | MADTTILDTTCSSTLAANVEFSHATDSAIGISLKNATITEAEGVPNLKETGYDCVRYMGTCNGGQIYLGRERKKLKDYVAIKKFAIDDVDDYAAIAKESSNLRLMHHPNIIELCECFVYERSIYQITPAMNLGSLFDIVFEYMKWGINEKSAAAITRQLLDALSYLHQRRYIHRDLKPKHILIDSSGNVKLSGFRFMIELNHHLDCVFEFDAHLQNQLYYLAPEVLAQNIHGYTSKSDIYMLGISICEAINGVMPFGELEPLEMLHRKLNGQVPRPVDMISLKDDQKMGLDISHRPQEHLTRRFSKEMHEFIANCLDYDPQQRGSASDLKSSAWLGSKIHKNLGPVDVRQELNLDYAHFDLSLWEQEPLIPMEPDQKYEIVFDYSPIS | null | null | asymmetric neuroblast division [GO:0055059]; establishment or maintenance of cell polarity [GO:0007163]; maintenance of dauer [GO:0043055]; negative regulation of apoptotic process involved in development [GO:1904746]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; protein localization to synapse [GO:0035418]; stress-activated MAPK cascade [GO:0051403]; synapse organization [GO:0050808] | axon [GO:0030424]; cell body [GO:0044297]; cell cortex [GO:0005938]; dendrite [GO:0030425]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perikaryon [GO:0043204]; synapse [GO:0045202] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:20023164}. Nucleus {ECO:0000269|PubMed:20023164}. Cell projection, dendrite {ECO:0000269|PubMed:20023164}. Cell projection, axon {ECO:0000269|PubMed:20023164}. Synapse {ECO:0000269|PubMed:20023164}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20110331}. Cytoplasm {ECO:0000269|PubMed:20110331}. Note=Localizes in punctate structures along the neurites of GABAergic motoneurons. Co-localizes with sad-1 at synapses (PubMed:20023164). Co-localizes with par-4 at the cell cortex of the early embryo. Cell cortex localization is regulated by par-4 (PubMed:20110331). {ECO:0000269|PubMed:20023164, ECO:0000269|PubMed:20110331}. | null | null | null | null | null | FUNCTION: Pseudokinase which may act as an adapter for kinases sad-1 and par-4 and thereby is involved in several developmental processes. Regulates cell-autonomously both neuronal polarity and synaptic organization when bound to sad-1. Required for sad-1 localization to synapses (PubMed:20023164). Required to establish germline stem cell (GSC) quiescence during dauer development, to promote cell shedding during embryogenesis and to control asymmetric cell division of the Q.p neuroblast lineage, probably when bound to par-4 (PubMed:20110331, PubMed:22801495, PubMed:23267054). May be involved in maintaining the integrity of the early embryonic cortex when bound to par-4 (PubMed:20110331). {ECO:0000269|PubMed:20023164, ECO:0000269|PubMed:20110331, ECO:0000269|PubMed:22801495, ECO:0000269|PubMed:23267054}. | Caenorhabditis elegans |
G5ECN9 | NEC2_CAEEL | MKNTHVDLICVFLSIFIGIGEAVDVYTNHFHVHLKEGGGLEDAHRIAKRHGFINRGQVAASDNEYHFVQPALVHARTRRSAGHHAKLHNDDEVLHVEQLKGYTRTKRGYRPLEQRLESQFDFSAVMSPSDPLYGYQWYLKNTGQAGGKARLDLNVERAWAMGFTGKNITTAIMDDGVDYMHPDIKNNFNAEASYDFSSNDPFPYPRYTDDWFNSHGTRCAGEIVAARDNGVCGVGVAYDGKVAGIRMLDQPYMTDLIEANSMGHEPSKIHIYSASWGPTDDGKTVDGPRNATMRAIVRGVNEGRNGLGSIFVWASGDGGEDDDCNCDGYAASMWTISINSAINNGENAHYDESCSSTLASTFSNGGRNPETGVATTDLYGRCTRSHSGTSAAAPEAAGVFALALEANPSLTWRDLQHLTVLTSSRNSLFDGRCRDFPSLGINDNHRDSHGNCSHFEWQMNGVGLEYNHLFGFGVLDAAEMVMLAMAWKTSPPRYHCTAGLIDTPHEIPADGNLILEINTDGCAGSQFEVRYLEHVQAVVSFNSTRRGDTTLYLISPMGTRTMILSRRPKDDDSKDGFTNWPFMTTHTWGENPTGKWRLVARFQGPGAHAGTLKKFELMLHGTREAPYNLIEPIVGQTNKKLDTVQKAHKRSH | 3.4.21.94 | null | arg-arg specific dibasic protein processing [GO:0090474]; determination of adult lifespan [GO:0008340]; dibasic protein processing [GO:0090472]; insulin processing [GO:0030070]; larval feeding behavior [GO:0030536]; negative regulation of dauer entry [GO:1905910]; negative regulation of dense core granule transport [GO:1904810]; negative regulation of turning behavior involved in mating [GO:0061096]; neuromuscular synaptic transmission [GO:0007274]; neuropeptide processing [GO:0061837]; peptide hormone processing [GO:0016486]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of backward locomotion [GO:1905852]; positive regulation of digestive system process [GO:0060456]; positive regulation of egg-laying behavior [GO:1901046]; positive regulation of forward locomotion [GO:1905850]; positive regulation of lipid localization [GO:1905954]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; regulation of backward locomotion [GO:0043058]; regulation of eating behavior [GO:1903998]; regulation of locomotion involved in locomotory behavior [GO:0090325]; regulation of muscle contraction [GO:0006937]; regulation of neuromuscular synaptic transmission [GO:1900073]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; response to mechanical stimulus [GO:0009612]; response to serotonin [GO:1904014] | axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; synapse [GO:0045202] | FBXO family protein binding [GO:0098770]; serine-type endopeptidase activity [GO:0004252] | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | PTM: Ubiquitinated. {ECO:0000269|PubMed:23665919}. | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:11717360}. Secreted {ECO:0000303|PubMed:24671950}. | CATALYTIC ACTIVITY: Reaction=Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.; EC=3.4.21.94; Evidence={ECO:0000303|PubMed:12657671, ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111, ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950}; | null | null | null | null | FUNCTION: Serine endoprotease which cleaves preproteins at paired basic amino acids (PubMed:12657671, PubMed:15180830, PubMed:16945111, PubMed:23665919, PubMed:24671950). Processes FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides (PubMed:12657671, PubMed:16945111). Probably by processing flp-1 and flp-18, modulates the neuronal excitation-inhibition balance and thus the level of activity of the locomotor circuit (PubMed:23658528). Regulates sensitivity to mechanosensory stimuli (PubMed:11717360). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671). Probably by processing flp neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Cleaves pro-insulin-like proteins ins-3, ins-4 and ins-6 into their mature active forms (PubMed:23665919, PubMed:24671950). Together with convertase kpc-1, cleaves pro-insulin-like protein ins-18 (PubMed:24671950). By controlling ins-4 and ins-6 processing and thus the activation of the daf-2/InsR pathway, negatively modulates synapse development and synaptic transmission at neuromuscular junctions (PubMed:23665919). Similarly, by controlling ins-4 and ins-6 processing, negatively regulates dauer formation under optimal environmental conditions (PubMed:24671950). Under adverse environmental conditions, may promote dauer formation by processing ins-18, a daf-2/InsR antagonist (PubMed:24671950). May cleave dense-core vesicle membrane protein ida-1 (PubMed:15180830). Involved in egg-laying, fat storage and locomotion (PubMed:11717360, PubMed:11813735, PubMed:17564681). {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:15180830, ECO:0000269|PubMed:16945111, ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:23658528, ECO:0000269|PubMed:23665919, ECO:0000269|PubMed:24671950}. | Caenorhabditis elegans |
G5ECP4 | PIK1_CAEEL | MDDSLGVSEVVMIPFMKREVLQQICAILDTDNTWETIAPYMPGIELRDVEGCKRYSSYNQSPSELLLRIWSSKGYSTTHLYQLFAKTKLIRLMRMMRSQVHEKYHYLENKVTNSTSRVSKQMVQPPGSQSASRLKKTEIKESSPSPAAAAASQLSRSNTDDTLRVAIEGTLPVTYCELLEATNGFAVSNVIGKGGYGTVYKGELKGTGGIVAVKRLHSGNDTSQNGSRERLRQSLTELRTLARFRHDNILPIYAYSLEGSEPCLVYQFMSNGSLEDRLLCRKGSVPLTWIQRKEISIGAGRGLGFLHSFGKTPIIHGDIKTANILLDKHMEPKIGDFGLCRDGHVEAEAMEKHPLIASHIKGTLAYLAPEFITSKILTTKLDVYSFGIVLLEIASGQRAYSDSRETRGLVEYCQVNKELAAHRKIPVREIFIDRRAPPLVGDEEKSFLDALIEVGLAGANNDRKVRPTMSQIVEYLCKNSIPPVV | 2.7.11.1 | null | cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; regulation of response to stimulus [GO:0048583]; Toll signaling pathway [GO:0008063] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00531;PF00069; | 1.10.533.10;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, Pelle subfamily | null | null | 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:Q05652}; 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:Q05652}; | null | null | null | null | FUNCTION: Through association with the adapter actl-1, may act downstream of the receptor complex composed of ilcr-1 and ilcr-2, which is a signaling complex that modulates neuronal activity and animal behavior in response to sensory neuron input. {ECO:0000269|PubMed:28099418}. | Caenorhabditis elegans |
G5ECQ2 | FRIZ2_CAEEL | MLLRISVLFLLLGSCGALFGKRQKCEQITIPLCKGIGYNMTSFPNSYGHEKQEEAGLEVHQFYPLVEVGCFQHLKFFLCTMYTPICQENYDKPILPCMELCVEARSKCSPIMAKYGFRWPETLSCEALPKMSDQMSTGNICAAPPDTPKKQHKGHHHKNQNQNQNQNHNYSPDGPEVGISKIDNEVIAGPSECQCTCNQPFQFVASEKSKVGNVTNCAYSCHSPALAESHSLVSNWMAFWSITCCVLASFTFLTFLIETDRFQYPERPIFMLAFCQLMVAVGFMIRYFVGHEEIACDSMRIKGADDNSGSLCFVVFLLTYFFGMAASVWWVILSLTWVLSAASKWSPEAISSFSFHFHVVGWCLPAIQTVLVIVFNAIDGDPITGICYVGNTDLQFQRIFVLFPLLVYFIVGVLFLVIGFCNLWSIRNEVQKQHPSLESAHKITQLMSKIGIFSLLYTIPSLLIICVLFYEQNHRSLWEQSQLCSCSPKQTIGDSSLIISLIKTCCMCILGWTSGFWVCSTKTLSSWKNAICCLGSSRSLPKYQPADILYAKSDMSSSQFYNTSLRHNHLYGGIPDKL | null | null | canonical Wnt signaling pathway [GO:0060070]; motor neuron migration [GO:0097475]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of motor neuron migration [GO:1905485]; sensory neuron migration [GO:1904937] | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF01534;PF01392; | 1.10.2000.10;1.20.1070.10; | G-protein coupled receptor Fz/Smo family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for Wnt proteins (PubMed:19855022, PubMed:20711352). Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of gsk-3 kinase. Both pathways seem to involve interactions with G-proteins (Probable). Required for the migration and axon formation and guidance of different neuronal cell types including canal-associated neurons (CAN), hermaphrodite-specific neurons (HSN), anterior lateral microtubule neurons (ALM), and the right Q neuroblast (QR) and its descendants (PubMed:16109397). Directs ALM migration through frizzled protein mom-5 and Wnt ligands cwn-1, cwn-2 and egl-20 (PubMed:16109397). May act redundantly with mom-5 to direct CAN migration (PubMed:16109397). Plays a role in the organization of head ganglion cells (PubMed:16109397). Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring and may in addition positively regulate the neurite outgrowth of RME GABAergic motor neurons along the anterior-posterior axis of the body (PubMed:19855022, PubMed:20711352). {ECO:0000269|PubMed:16109397, ECO:0000269|PubMed:19855022, ECO:0000269|PubMed:20711352, ECO:0000305}. | Caenorhabditis elegans |
G5ECQ3 | SEL5_CAEEL | MPLGLFSSGKAQVLCDEKIPGGKKKEPKQLSENKCKGVTLKLDHTRVTIEKQIAEGGFAIVYVASDRKNNKFALKRQFTKDNEKQLEACCREHSFLKQCIGHKNIVEFVDSYTNCLGNGIWECMLLTEYHQKNVLQLMNERISQNQYLTNDEILSIFTDLCEAVSFIHNRPQPIIHRDLKVENVLISSHKPPHYVLCDFGSATTQILSVEKYGVEYVKSEVERNTTMCYRSPEMIDFYSGLEIGLKSDIWALGVLLYRLCFFCVPFEESPLAIQSVNYQFPSVPNIPDEIKVLIYMLLDIDVNRRPSIYQTSVLAFEANHRKPLSEEIQNKKCTDAVPSLKSCIQLMRDGSNPRNKRDSSPRNPEAPPIQSSSKMASLSQQVPSISNISMPSGSGTVETSVAPRLRPKATTVVPNVPSISPVPPVGLPHLRLPSKGSTDETDGSQVRKVPIDFHHRQSFSGEEQLKPAAEADSAGPLSCPLIKPTDLGFTDLDKPALPRDRAQTDGKRRLPHESDIIFQQQHRRNVSDTSQISRSAFKPYSSQQTTSKTSSQVVRSVEDMSQRQNGGSGEWNPFLVAPFSNNSISRKDGQESAFMMDDSHFGMVFDEIRRKEIPAELDSETSSIDSRDPFGAAPFDQLTVSTSSSAQPVSLPPATDEDDERQLLSETDEEEKYEIDEKEEIQTKKDETINEEDSEIDEQRMNDRRRYSYENIDGVGDDASSDSRGKTDRDDSEEEEDDDSRRGGDTSHDEDSQNTVGSEDGEGGSRPLLEDDGLEDDDDHELISSFSSSSTNYPPLFIGTSTPHTQNPITNPFLRDELTPKMIITAPLPTAKNNLDDDWDLGDRWTDRRDTVFERPASEHQNVFAPATLPRQATPLVCRFKPDLPTAAPVSIIPSMSNTSFPEAVRDSDTVPCEPIIGTLISVGAPTDPPPPPLPKKPTEASPTQETTATIPVALGKKEKLLKKEKKKEKKDGKKDKLKLEEYREKGSSEPETDGSEAEIWTNDGATTFSNKKKKKSTFGLRSSHPSIVANDLQFSSPMPPVVKKSSKDKKSSLTGKNASFVNTSFQPEDHDDPTDL | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | actin cortical patch assembly [GO:0000147]; actin filament organization [GO:0007015]; phosphorylation [GO:0016310]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of clathrin-dependent endocytosis [GO:2000369] | cytoplasm [GO:0005737] | AP-2 adaptor complex binding [GO:0035612]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:10581273}. | 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:0000305}; 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:0000305}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which may play a role in lin-12-mediated cell-fate decisions. {ECO:0000269|PubMed:10581273}. | Caenorhabditis elegans |
G5ECR9 | UNC55_CAEEL | MQDGSSGAASLGNSSPDATDCVVCGDKSSGKHYGQFSCEGCKSFFKRSIRRSLSYTCRATKNCAIDVQHRNQCQYCRLTKCIRMGMRKEGRRSNETQTAVSAVQRGRLPVTMPSLFPPNMFLRSPFPFMSVPFNPLMTAQFTKPSIKESIFEFAAQTIFATVNWARTSMSNLVKGDQLILLRHSWTPIFIFALAQSNFALNLSTHLTAVTATAASTENGSSSLGSKSEDEEKSEEKPERVFDEPQFQGFQAKIDKIRDFHLDVVESSSLRAVLLFSCDEEALEEKGKIEEIVEKLKSAVDEYCKMNKRSERYHQICECLQLLKSTRNLPISRLFFSRLLGTTPLETILSDLLITPPPPTLPFFPQLPSRN | null | null | cell differentiation [GO:0030154]; cell fate specification [GO:0001708]; hormone-mediated signaling pathway [GO:0009755]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | 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, ECO:0000255|RuleBase:RU004334}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:28056346, PubMed:29033363). Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factors unc-3 or irx-1 in subsets of motor neurons (PubMed:22031882, PubMed:28056346). Probably acts by binding to specific promoter elements (PubMed:28056346). Required for ventral D (VD) motor neurons to adopt their normal synaptic pattern (PubMed:22031882, PubMed:7869081). Suppresses expression of flp-13 in VD motor neurons to ensure formation of the correct synaptic pattern (PubMed:15882588). Maintains low cAMP levels in VD motor neurons by enhancing expression of pde-4 which hydrolyzes cAMP and repressing expression of acy-1 which catalyzes cAMP formation (PubMed:29033363). This prevents respecification of synapses by VD neurons (PubMed:29033363). During copulation, required in males for correct movement of the spicules, a pair of prong-like structures which are inserted into the vulva of the hermaphrodite and anchor the male to the hermaphrodite (PubMed:18652814). Required for spicule prodding which allows detection of the vulva location and for spicule insertion into the vulva (PubMed:18652814). {ECO:0000269|PubMed:15882588, ECO:0000269|PubMed:18652814, ECO:0000269|PubMed:28056346, ECO:0000269|PubMed:29033363, ECO:0000269|PubMed:7869081}.; FUNCTION: [Isoform a]: Required for normal locomotion. {ECO:0000269|PubMed:18652814}. | Caenorhabditis elegans |
G5ECT0 | PBO5_CAEEL | MTRLSILQHLLTFLILSKINATSTTESYFDSSEEAPNVLLNHLNNESEGEELTQINDTQPAFVPGSSKRLTEYLLSRHNLNAPPDGLLYVEYELELVHILGIDELKQTMTVLIYVDEHWVDPSLTWDPALFGGITKTWIPLDKIWVPDIIVFNMVKSNRLAHEDLLSAVRAPARIHYNGTIVASHPAVHTVSCEINIRHFPLDDQRCAIEIASWAYGQEKIRLHAHTDHSLEHYKRNEEWHLLNLNVSEEKYEHEGVEVSEVKFEISLKRRPLFYMVTLTFPSYIMCAISVVGLFARFSTTGEREERFTLGVTAILTMAVLSLVVSEKVPHSSTHVPLLVAYFLFNMVIVSIAAMTTGIVMKVHRLGRYGDEPSDFWMRCFLLKPVFRTSNRRKYRMNPEEPTQVILVSEAKNGEVLTKKSTELNGTVVKEIMLSSRLEALEEYIRKMVNRCETIKWELDEIDAAENIELVRRRSTNGYVRISERLDILFMFLFLSTVTIPVAVLFYLT | null | null | defecation [GO:0030421]; lipid transport involved in lipid storage [GO:0010877]; positive regulation of intestinal lipid absorption [GO:1904731]; positive regulation of striated muscle contraction [GO:0045989] | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; neurotransmitter receptor activity [GO:0030594]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18191228}; Multi-pass membrane protein {ECO:0000269|PubMed:18191228}. | null | null | null | null | null | FUNCTION: Forms a proton-gated ion channel with pbo-6 that is activated by acidification of the posterior coelomic space, leading to posterior body wall muscle contraction (pBoc) during the defecation cycle (PubMed:18191228). Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells (PubMed:25849533). Does not bind neurotransmitters such as acetylcholine, gamma-aminobutyric acid, glycine, serotonin, glutamate or choline (PubMed:18191228). {ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:25849533}. | Caenorhabditis elegans |
G5ECU1 | SKR1_CAEEL | MADQKKVSEAAKEREIKISSSDNEIFLVPRNVIRLSNTINTLLMDLGLDDEEGTNAEPIPVQNVTASILKKVISWCNHHHSDPISTEDSDNREKRTDDIGSWDVEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKSPEEIRRTFNIKNDFTPEEEEQIRKENAWCED | null | null | female sex differentiation [GO:0046660]; mitotic cell cycle [GO:0000278]; negative regulation of centrosome duplication [GO:0010826]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; nervous system development [GO:0007399]; positive regulation of apoptotic process [GO:0043065]; regulation of protein stability [GO:0031647]; regulation of synapse maturation [GO:0090128]; regulation of synapse pruning [GO:1905806]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | cullin family protein binding [GO:0097602] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | null | null | null | FUNCTION: Probable essential component of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:17626846). Regulates cell proliferation during embryonic and larval development (PubMed:11864566, PubMed:11864567). Involved in synapse elimination in early synapse development (PubMed:17626846). May negatively regulate the apoptotic activity of cep-1 in response to genotoxic stress (PubMed:18340346). Plays a role in sex determination (PubMed:18718460). {ECO:0000269|PubMed:11864566, ECO:0000269|PubMed:11864567, ECO:0000269|PubMed:17626846, ECO:0000269|PubMed:18340346, ECO:0000269|PubMed:18718460}. | Caenorhabditis elegans |
G5ECU7 | JUN_CAEEL | MEEDQEEPPSSSTSSESPEVVLKAPKAPTRRRKNSKKDRRQDMEVDDGEKESTAQYCKGFYDALRVMQTTNKYEFTGGAVSSPVLPVLQTAAFSPITPASASDMHTIVMSLLGNTPITSGPSIAPLSSPTLLPLVTSGDLDDLSMKILASSAIPGPPIISSSNSPDSSTTAVTTSQITAFQPLLNNFVSSTTASTSRPDKLNLTPPQQSAEIYAFNGVNSDDSDGGLDSRSASRCGMALDDQEKKKLERKRARNRQAATKCRQKKMDRIKELEEQVLHEKHRGQRLDAELLELNRALEHFRRTVEHHSGNGCPNNSIRV | null | null | determination of adult lifespan [GO:0008340]; nitrogen catabolite activation of transcription from RNA polymerase II promoter [GO:0001080]; positive regulation of cellular response to amino acid starvation [GO:1903833]; positive regulation of gene expression [GO:0010628]; positive regulation of RNA splicing [GO:0033120]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; response to starvation [GO:0042594]; response to toxic substance [GO:0009636] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565] | null | 1.20.5.170; | BZIP family, Jun subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:24178943}. | null | null | null | null | null | FUNCTION: Transcription factor that recognizes and binds to the AP-1 non-canonical enhancer heptamer motif 5'-TTAGTCA-3' (PubMed:17942488). Required for ovulation (PubMed:19570917). Controls plc-1 expression in the spermatheca to regulate spermathecal valve dilation (PubMed:19570917). {ECO:0000269|PubMed:17942488, ECO:0000269|PubMed:19570917}. | Caenorhabditis elegans |
G5ECW5 | CSP3_CAEEL | MFFGKLGGFAFFLQRAVRCDGFIDNFFDRIPKFFQFMKSKFPSHQTSSSQADLLVSFSTSPGFLSFKDETKDTWYIQELYRVIIENAKDTHLADLLTETNRRVVEKYEADKVVFVCKQAPEFWSRFTKQLFFMSRNDVF | null | null | inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; negative regulation of apoptotic process [GO:0043066]; negative regulation of apoptotic process involved in development [GO:1904746]; positive regulation of apoptotic process involved in development [GO:1904747]; positive regulation of egg-laying behavior [GO:1901046]; positive regulation of embryonic development [GO:0040019]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of neuron apoptotic process [GO:0043525]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | caspase binding [GO:0089720]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; zymogen binding [GO:0035375] | PF00656; | 3.30.70.1470; | Peptidase C14A family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18776901}. | null | null | null | null | null | FUNCTION: Non-catalytic caspase homolog which does not contain the region necessary for caspase activity (PubMed:9857046). Acts as an inhibitor of caspase ced-3 zymogen autoactivation and delays ced-4-induced ced-3 processing (PubMed:18776901). Has no effect on active ced-3 (PubMed:18776901). Probably by preventing ced-3 activation, protects cells, whose fate is to live, from apoptosis during embryonic and larval development (PubMed:18776901). {ECO:0000269|PubMed:18776901, ECO:0000303|PubMed:9857046}. | Caenorhabditis elegans |
G5ECX0 | LPLT2_CAEEL | MAKQLKYPFLIFIISLAQCQVSNQNVNLCQSNICQNGGTCLVASSVPATATCPKNSIYYMGSCYVFDTTLRNWNDAALYCNNMNSATLPLVESAEDQAFFAGYLQAMIPSNPPADMRPPPDGIWTAVRGVNNVTRASWVYYPGSFLVTDTFWAPQEPNIYVNYNDVCVALQSDSFYREWTTALCTILKYTVCKVAPTQIQAKYVAQCSCPNGYGGQTCETQSTTNQQASTQRTCGSNDFQFSCPNDQTITVDFASFGAQESSMCNQASQSREQTCSNVNSLQTVINACQGLQSCEIRNLTSTFSNTPCPVPQEQYLETRMRCETAQQPSCLSGLIQFDSRCYSMTIETNEKKQRTMEDAQTYCSQSGGSIITSPPDALLQQIVQKVNAETKKTVNFWIGTPNNCQLLMVTGSSTSYSQCPSSPSSTANVICSTVPQSTASVSARPTQSAPVDPVSQTMARREVYTGVQPPSVPDSINKPRYCKKEKKDGITYEQTRACMLHEQPCPDPQNVEGTVTRYCNCQTAKWETPDTTNCTHRWVAEMETAIKDNQPVEDISSTVNRQLKSTIERTLFGGDITGTVRLSNDMLSLARNQFSVLNDRNLRENKARNFTENLGGSGDQLLSPVAATVWDQLSSTIRIQHASKLMSVLEQSVLLLGDYMTDQKLNLQYINWAMEVERSEPEVQTFGAAASPNVQDDMGMMRVMAAAPPAPQPETNTTIMFPSLKLSPTITLPSASLLSSLASPTPVAGGGPSILSSFQDDTPVGMASTPNLNRNPVKLGYYAFAGFGQLLNNNNDHTLINSQVIGASIQNATQSVTLPVDHPVTFTFQHLTTKGVSNPRCVYWDLMESKWSTLGCTLIATSSNSSQCSCTHLTSFAILMDISGQVGRLSGGLASALDVVSTIGCAISIVCLALSVCVFTFFRNLQNVRNSIHRNLCLCLLIAELVFVIGMDRTGNRTGCGVVAILLHYFFLSSFCWMLLEGYQLYMMLIQVFEPNRTRIFLYYLFCYGTPAVVVAISAGIKWEDYGTDSYCWIDTSTPTIWAFVAPIIVIIAANIIFLLIALKVVLSVQSRDRTKWGRIIGWLKGSATLLCLLGITWIFGFLTAVKGGTGTAFAWIFTILNCTQGIFIFVLHVVLNEKVRASIVRWLRTGICCLPETSSAAYNSRSFLSSRQRILNMIKVNGHSYPSTASTDDKEKQLTPITKTTDWLSRLPNQDSVSIPESNFNNLNGTLENSNLNSAEIKEEDEIPELRRRVTVDLNPMIVSNNEIERMSHASSDPRGSQIIEVTAVEKKAPVKRIKFPLGAKQSERGSQHRTKAKVIAPPESPVSESGSKDYRF | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; self proteolysis [GO:0097264] | plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; endopeptidase activity [GO:0004175]; G protein-coupled receptor activity [GO:0004930] | PF00002;PF16489;PF02140;PF01825; | 2.60.120.740;2.60.220.50;4.10.1240.10;3.10.100.10;1.20.1070.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: May have a role in pharyngeal pumping during feeding. {ECO:0000269|PubMed:17583712}. | Caenorhabditis elegans |
G5ECY0 | DLG1_CAEEL | MSHESSEKAHKAIENVEDYCQTLTRHGNEELRTNLERVITTFKSNLMHSLLDIHDLYEQTLLSERKSDAEKNMEVRRVIERLEGGPHSYNSRPAATTSTSNYNLSSTTPLISDLRDRGGFSYLNGGGLGNGLGNGLGNGLLSSPYNSSSTHYLHERQRQTSHDGTWRETTTRTVDTPSGLERRVVEHTGVIDDHGRKWELENIVLEKGHTGLGFSITGGMDQPTEDGDTSIYVTNIIEGGAALADGRMRKNDIITAVNNTNCENVKHEVAVNALKSSGNVVSLSLKRRKDEAFLPIGGNFGGSTSYLRSGVTPSVSAGNLQHAIHSPSAPIHPPPPPPVHHGSLSQLSVGQYRSTRPNTSVIDLVKGARGLGFSIAGGQGNEHVKGDTDIYVTKIIEEGAAELDGRLRVGDKILEVDHHSLINTTHENAVNVLKNTGNRVRLLIQQGTGAIFNDSASQQFMPTTPILRPSSVQDYNRSQMGSQSHLSYGGPLNTSYSSQAPIAIPLEPRPVQLVKGQNGLGFNIVGGEDNEPIYISFVLPGGVADLSGNVKTGDVLLEVNGVVLRNATHKEAAEALRNAGNPVYLTLQYRPQEYQIFESKIEKLRNDVIAQSRMGTLSRKSEYVRALFDYDPSRENSVAPHRSMGFNYGDILHIINSSDDEWWTARKVHENGEETAEGVIPSKKRVEKRERLRRKQVNFNSGSQSLGRNSSTTGLENRRGSRSQLSFSRKFPFVKSTDRLNDLNEESSNVAEEPVWSYQAVEQQAINYVRPVIILGALKDRINDELVNRDPSKFSSCVPHTSRPPREGEVNGRDYYFVNKHNMEEDVKNNLFIEAGQFQNNLYGTSIQSVRDVANQGRHCILDVSGNAIRRLQSNANIQPISIFIKPSSAQQILELDSQLATNRQDDRAMSGEEAQAQYSRCHRIEQTFGDLFTQEISNVHSANDVLSKVYSIISRESQTPIWVPRH | null | null | cell-cell adhesion [GO:0098609]; chemical synaptic transmission [GO:0007268]; embryo development ending in birth or egg hatching [GO:0009792]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; receptor clustering [GO:0043113]; receptor localization to synapse [GO:0097120]; zonula adherens assembly [GO:0045186] | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; lateral plasma membrane [GO:0016328]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; postsynaptic density membrane [GO:0098839] | guanylate kinase activity [GO:0004385] | PF00625;PF09058;PF00595;PF00018; | 2.30.42.10;3.30.63.10;1.10.287.470;3.40.50.300;2.30.30.40; | MAGUK family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane {ECO:0000269|PubMed:11715019}. Cell junction, adherens junction {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}. Lateral cell membrane {ECO:0000269|PubMed:18411252}. Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Note=Localizes at the apical junctions (PubMed:11715019, PubMed:18411252). Localization at the adherens junctions requires PDZ domains, lateral distribution requires SH3 domain and is let-413 dependent (PubMed:18411252). {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}. | null | null | null | null | null | FUNCTION: Essential multidomain scaffolding protein required for normal development (Probable). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells (By similarity). Required for proper embryonic elongation. Acts upstream of ajm-1 and becomes localized to apical junctions independently of ajm-1. With let-413, cooperatively regulates ajm-1 localization to apical junctions (PubMed:11715019, PubMed:18411252). {ECO:0000250|UniProtKB:Q12959, ECO:0000269|PubMed:11715019, ECO:0000305|PubMed:11715019, ECO:0000305|PubMed:18411252}. | Caenorhabditis elegans |
G5ECZ4 | DYF2_CAEEL | MSLKVIPCTLTKNQEVFKCVSAQLQYRRGEEEHGSGPIIHRWRPNGHTVAVACANNTVIYYDKKGNVIDALNPTGKLIDIAWDKEGDVLAIAVANTGTIYLWDVNSRNTDTVESGATSSKELPTCLAWSPSTPTLVIGNNAGNIVVYNHRTSRRIAVMGKHQRSVTQITVTPEDYVISCSDDNTLSVTTLEGTTVSTTTTNGEPTNMDYGSVNGKGGSGVTMVSVVIGKKILMLAHYNALDEPVNLQFQEKYGNIHSYRWFNDGYILIGFDRGYIISISAHNNEIGSELVSFLEYRGYLASIAVSTSFNKLLTIGDNMVKVRDLDELTTVTMLTEIETEKNLSEIEVTEDGQLVAVSSQSGVLSIFVTKMPTLAASYNNSICYLTNLTQVTVVAEVEKKGSSTLELNIEPTVMGLGPLNLAVANNNTVFFYDYHTPAQMQAAQQLQSTQSAAEKPTIVAAEPINRVEYLSTVTNIQLNYMYAAVNFGSRLRLHRIRNSEDNVSIEFPEANRNATLYSYALTENFLIFTTSNNYIVYFSLSEWAIVSEYRHVVPVRSIFPHPTNVVCCCFDDRLEAMIYSAVDDEVFRLPSVGSSAHYKGAIWETFTIDKNTFAVFDSQNIYVFLLSKQHIQGESVIYVSATRLPHAYVPLSLNKGIVTCLMSNGKLSSVLLDSHKTESVISDKSETVIDDILTRSLLMHRWSTAWKICIHSNDGSHWNQFAMAALLDSDVGMAIKIFREIGDAAMVTALELIETIEEKNLLHAQIYTILSRYDDAEQLYLESSRPMEALNMRRDLLEWPKALVLAETMNPKEIPYLSKEYAQELELTGDHANSLANYEKGVMENPQNLPELQEHNEICQSGIARMAIKTGDLRRGVQLAKQLEGRVVKRDCAIILEQMKQYTEAAQLYEVGLFYDRAAAVCLKANAWAKVGELLDHVKSPKIHIQYGKIMEKEKKYKVAVKCYETGRDYDNQVRLLLDPLNDPDEAVRVVRESRSIEGAKLVAKFFVKLGDYNSAIQFLVMSQCVQEAFELAEKNNAVREYAKAIEQHGNISQALELAEYYNRVNDMFMAAKFYTQAGQYNNAINLLFKNGDDENCVALAVDCGIKSKDKTLNNKLVKFLLGEDGNVKDPAQLFRLYVGLGRTKDAAQTAVVVAQIHQAKGNYRIARDLLFQMHQQLREKMMRIPLDMNKSLMAIHSYIIVKALINRKETLLAARLLIRTCGEIQRFPTHVVPILTSSVVICTQANLKKSAHKFAAQLMTPEYRPKIHEKYKKKIEDIVRKGGNQKDLVEENTPCPICDDLMPAYAMSCDNCKSLVPYCILTGRHIVASDFSRCPHCEMPGFYSEFRKLSILNENCYMCGGDLKGAIPEDAKAYLEKMEQDYK | null | null | chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; cilium assembly [GO:0060271]; intraciliary retrograde transport [GO:0035721]; intraciliary transport [GO:0042073]; non-motile cilium assembly [GO:1905515]; olfactory behavior [GO:0042048]; protein localization [GO:0008104]; protein transport [GO:0015031] | cilium [GO:0005929]; intraciliary transport particle A [GO:0030991]; intraciliary transport particle B [GO:0030992]; non-motile cilium [GO:0097730] | null | PF15911; | 1.25.40.470;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:22922713}. | null | null | null | null | null | FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport (PubMed:28479320). Moves along the ciliary axoneme and is involved in the assembly, localization and the movement of other intraflagellar transport (IFT) proteins along the cilia axoneme (PubMed:16957054, PubMed:22922713). May also associate with the BBSome complex in order to mediate ciliary transport (PubMed:22922713). Regulates cilia biogenesis, morphology and sensitivity to environmental cues (PubMed:16957054, PubMed:22922713). {ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:28479320}. | Caenorhabditis elegans |
G5ED14 | PAX5H_CAEEL | MEPIWRNYPYPTYPGHHNFQFDPLLSDGSHTGVNQLGGVFVNGRPLADTVRAQIVEMSQHGTRPCDISRQLKVSHGCVSKILGRYYSTGSVRPGVIGGSKPKVATPRVVECIAGYKRANPTMFAWEIRQKLIEDQICGEENVPSVSSINRIVRNKSFMAQLAAPTSVTSSAARPSSATSHHQRSPPRGVQQHMQQSTSVQQLQQLQLTSAATVNSLMTPPAFAMPGTAYSINGLLGTLPQPSLLDDKFTNLSTQSADMSLVYSTGLVGEHDWTMRTPMVILPQNYCGQL | null | null | apoptotic process [GO:0006915]; cell fate specification [GO:0001708]; embryo development ending in birth or egg hatching [GO:0009792]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; uterus development [GO:0060065]; vulval development [GO:0040025] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00292; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00381, ECO:0000305|PubMed:11532910, ECO:0000305|PubMed:17021039, ECO:0000305|PubMed:31398431}. Chromosome {ECO:0000269|PubMed:17021039}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:17021039). Binds to specific DNA sequence motifs in regulatory elements, for example in the genes encoding transcription factor lin-48, apoptosis regulator ced-9 and neuropeptide-like protein nlp-2 (PubMed:11532910, PubMed:15923112, PubMed:17021039, PubMed:31398431). Specifies cell fate, playing an essential role in embryonic and larval development (PubMed:10511553, PubMed:17020758, PubMed:31398431, PubMed:9374390). Involved in morphogenesis of the vulva and uterus in hermaphrodites and of the rectal epithelium of the tail in males (PubMed:15923112, PubMed:17020758, PubMed:31398431, PubMed:9374390). Plays multiple roles in the development of the egg-laying system, acting in both lin-3/EGF-pathway-dependent and -independent processes (PubMed:17020758, PubMed:31398431). Positively regulates expression of neuropeptide-like proteins nlp-2 and nlp-7 in uvl cells in an EGF-pathway-dependent manner (PubMed:31398431). Involved in negatively modulating apoptosis in germline and somatic cells, acting in partial redundancy with transcription factor pax-2, probably by directly regulating transcription of ced-9 (PubMed:17021039). Positively regulates transcription of lin-48 in hindgut cells and functions in the development of the hindgut (PubMed:10511553, PubMed:11532910, PubMed:15923112). {ECO:0000269|PubMed:10511553, ECO:0000269|PubMed:11532910, ECO:0000269|PubMed:15923112, ECO:0000269|PubMed:17020758, ECO:0000269|PubMed:17021039, ECO:0000269|PubMed:31398431, ECO:0000269|PubMed:9374390}. | Caenorhabditis elegans |
G5ED29 | ATX2_CAEEL | MSTPTGLPALNGDVLSAINDMIGRVIIINTTDKKRYSGVLGAVSQDFDFGMQCVVEITKENENNLLRTESECRDKMVFHYSDIVDFAYVTQEIKKQHAVSKFVTDRQYHGDTPIEGEELQEWNGGEEDGLGGSIEDDVVVAGGQTAARRSNNHNNGTGWSVNDMFAANEKMNVVSTFKEDLTQYTTVEVVGTDEDRARAERLAREIESNSSSKFMANLENDDDERDLDKITRQEDFENGNGRKRNNNSFNQQQQQRRNPNIAPNGQPVNRRAEGLRGDRRNSGSSSANNSRYGAPAAAQQNYSQNQQQQQGQKGYRRQNEENDWQMAKGKGQNQGHDHSFRQQQKQMLDPRPNNNVKPADDKAQSATTATAAAGGSRVTDLKNWGNEFSIATAPKDQAPAVPAGNSGSAWNRGPPSSLVAKGSSNESTPPPTTNGEEAETKKEEAPSTSVDVAAAPVQNVQNDAEKHQEDDNVSVTSENDSVITSKSSSFKFNINAPEFKPRVAPATPTATTPVQNEYHPQQQPHPAMMAPQQGPPAPGMGMVPPHMGGPQNQGQPPMMMWQQTGQQQQGGGGYPQNHQFPIQHVPMQGVPGQMYGPGAATPVTVAQQPNQQHQVPTSAAGGQNHQLRDGEYREKQPLYMPYGPPQMVPVTSQQFYHSQYQGQMQQAAPYQMKMMPQQAPQGAYQQRYQQPQVYMMPPQGQQQQPRYQGPPPPQQQQQQQPQQQQFSGEQSRPQSHPNSQPTTPGPRGELPKMSGAPQNGNMQAESSSNASHSGSTSSQSGQRSGSPPGAVPPPPPPQQQHQQQQHPPHHAPPHVGAPPPQMMQQQQQHIQQYMVMQGPHQMHPQIPNYYQQPQQVFYPMIMPQQMPMQQNQHPQQSLMGERSDQGFPTSGYFDYRTMPNYQQQQQQQQQQMHRQNSLPQQFQGNQGVNPSGQQSGPPPPPPPSQQGTPRDQQHSQSPP | null | null | astral microtubule organization [GO:0030953]; chromosome segregation [GO:0007059]; detection of temperature stimulus [GO:0016048]; establishment of mitotic spindle localization [GO:0040001]; female gonad development [GO:0008585]; maintenance of centrosome location [GO:0051661]; negative regulation of centrosome duplication [GO:0010826]; negative regulation of gene expression [GO:0010629]; negative regulation of microtubule nucleation [GO:1905833]; negative regulation of protein localization to centrosome [GO:1904780]; oocyte development [GO:0048599]; oocyte fate determination [GO:0030716]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of female gonad development [GO:2000196]; positive regulation of fertilization [GO:1905516]; positive regulation of gene expression [GO:0010628]; positive regulation of germ cell proliferation [GO:1905938]; positive regulation of meiosis I [GO:0060903]; positive regulation of mitotic cell cycle, embryonic [GO:0045977]; positive regulation of mitotic cytokinetic process [GO:1903438]; positive regulation of mitotic spindle elongation [GO:1902846]; positive regulation of oocyte development [GO:0060282]; protein localization to centrosome [GO:0071539]; regulation of centrosome duplication [GO:0010824]; regulation of gene expression [GO:0010468]; regulation of germ cell proliferation [GO:1905936]; regulation of mitotic cell cycle, embryonic [GO:0009794]; regulation of mitotic cytokinetic process [GO:1903436]; regulation of protein localization to centrosome [GO:1904779]; regulation of spindle assembly [GO:0090169]; spermatogenesis [GO:0007283]; stress granule assembly [GO:0034063] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634] | mRNA binding [GO:0003729] | PF14438; | null | Ataxin-2 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15342467, ECO:0000269|PubMed:27457958, ECO:0000269|PubMed:27689799}. Nucleus {ECO:0000269|PubMed:27457958}. Note=Co-localizes with szy-20 and pab-1 in the cytoplasm. {ECO:0000269|PubMed:27689799}. | null | null | null | null | null | FUNCTION: Probable RNA-binding protein that negatively regulates the translation of targets (PubMed:15342467, PubMed:27689799). Functions with RNA-binding protein szy-20 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation (PubMed:27689799). Required for gonad development, germ cell proliferation and for the production of oocytes (PubMed:11303786, PubMed:15342467, PubMed:15514056). Regulates whole body growth and fat accumulation in response to food availability, and this may be through the mTOR pathway, upstream of daf-15 and rheb-1 (PubMed:27457958). {ECO:0000269|PubMed:11303786, ECO:0000269|PubMed:15342467, ECO:0000269|PubMed:15514056, ECO:0000269|PubMed:27457958, ECO:0000269|PubMed:27689799}. | Caenorhabditis elegans |
G5ED35 | TTR52_CAEEL | MSRFLIYFLPFFIYSGNVLSKTSCLMATGVLKCPTDPEAVKKVHIDLWDEDSLPLESDDLMGRTWSDRNGNFQVTGCASDFGPINTPDPYLYIQHNCPHRDSNATNPIQIDVIPLFLPSIVRLGNVYLDRYLEDY | null | null | aminophospholipid transport [GO:0015917]; apoptotic process involved in development [GO:1902742]; recognition of apoptotic cell [GO:0043654] | cell surface [GO:0009986]; extracellular vesicle [GO:1903561] | phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; scavenger receptor binding [GO:0005124] | PF01060; | 2.60.40.3330; | Nematode transthyretin-like family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20526330, ECO:0000269|PubMed:22713871, ECO:0000269|PubMed:22727702}. Cell surface {ECO:0000269|PubMed:20526330, ECO:0000269|PubMed:22713871, ECO:0000269|PubMed:22727702}. Note=Detected almost exclusively on the surface of apoptotic cells. In some embryos, also observed on surface of cells adjacent to dying cells. {ECO:0000269|PubMed:20526330, ECO:0000269|PubMed:22713871, ECO:0000269|PubMed:22727702}. | null | null | null | null | null | FUNCTION: Plays a role as a bridging molecule that mediates recognition and engulfment of apoptotic cells by cross-linking the surface-exposed phosphatidylserine with the extracellular domain of the phagocyte receptor ced-1. Important for the generation of extracellular phosphatidylserine vesicles that promote loss of the exoplasmic leaflet from apoptotic cells in a time-dependent manner. Required for the exposure of exoplasmic leaflet on the phagocytic cells surrounding the apoptotic cells. Does not affect the phosphatidylserine externalization in living cells. May play a role in mediating transfer of phosphatidylserine from phosphatidylserine vesicles to ced-1 bearing phagocytes or alternatively result in the activation of a phosphatidylserine transporter in the phagocyte that promotes phosphatidylserine externalization. {ECO:0000269|PubMed:20526330, ECO:0000269|PubMed:22727700, ECO:0000269|PubMed:22727702}. | Caenorhabditis elegans |
G5ED39 | SEP1_CAEEL | MKITNKSVDKQHIEKLDELRKNVSCTVIGFAEQTAELQQEISELFIAEFGVNGPIDMNSLSKLARITSYYASSEYFQGLAKYQRTACKMFITWQTLRKEAMECRSKDREIFASIPAKLCFFYFYNGELCRAVVCLLDYIDLSDDTLAKEAALRWLMFLGETELIEKKLKTWKMDKSSKDMFSATEFAMNYLKKSEYRVEMLEKLMKLRDKVKSDPTRSFSRYELASYVSWLCSTLSNVPVGSALRECEFPDRVSHIQEAALKSDSLVRNRIPGLASSQFDNSVNASIWPFLDGHQEDSNYYVHIGSTIAWHFEMRRECALVNVTTAQTRDSMSAMILNLRVALKSASFFRVLQTTNTLAYYSSIIEEAGSEKNAKLMRVSCVNLLSSNPIIVRCSTPKETGATSRAHTPMAGSSVSEKQNTMRPDLADLLGDLELLDEQSFHPITRSCVCNVCTIYPLHSSFAAEYMMSYAIHSDFSQLSIKHFNDEFARIRERGMSSQVLMHRDSSVRPRPNIIQNEIFGMCVIRWLTKKLDSKESADEDTMEIFNNALKIVRYLQQRTTDMILAVTQLGRQLEFPMECNYSWMRPTIRKPRVKATIDCAVDILRAVSPFGRRPKVEKLEKNLQPFDKERFEKVRLAMRNEMNHYGHILYREWRCRLFAYVGRTSRDPWEAAYAWAESTQIGARNAVQSRLEKCKRGLVTMSGHDRFKTCVQSMPDEMTLVQIAMADDKTIYLVKLHADRDPIIMPLAHYSQAVELMDKFTFLLDEDEMIAKYPGDITPEEFWKRRKIVDGRMMTFVDEVQKHFLGVAASLLMPSGQLGPKAAELAIKIHKLSKGGLLLGEAKEMVYQSKLMDAKSWEALILRFCEMRTTDEKFKSFLPLMHRNSVEVMNQDDSIVTEKKYTYLVICPHLSQFCWERLPIFDEYPYVGRQVSIHSTFSQLEAMKSQEKQIPLQIDVQNAYYILDPDNNLGETQKRMVEYINKFNWEGTVGSAPKSNEISAALSQRDAFFFIGHGSGSSVMPRSVLKQSTCNAISLLMGCGSVRTIPQALGFDGKTAILDYAMAKCPLIVGCLWTVTDGEIDRFLIRMIDDCFEDSKSLTGIDKLRQLSEAMHEARSKARLKYLTGAAVVMYGLPVVAKQTTPFVEKDQRNLPQTPKTSARTSMRMETVPKTPKQEFVTSKSVPMTPIFSNNENKSPSRARMPSRVLKTPRQVKTFQEEDDEAPKRSTTRQLKPLVAPPIPATPTTRTTRSSARTPSRSRNL | 3.4.22.49 | null | cortical granule exocytosis [GO:0060471]; eggshell formation [GO:0030703]; maintenance of meiotic sister chromatid cohesion [GO:0034090]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; meiotic chromosome separation [GO:0051307]; mitotic cytokinesis [GO:0000281]; mitotic sister chromatid separation [GO:0051306]; multicellular organismal reproductive process [GO:0048609]; polar body extrusion after meiotic divisions [GO:0040038]; polarity specification of anterior/posterior axis [GO:0009949]; protein localization [GO:0008104]; protein processing [GO:0016485]; regulation of centriole-centriole cohesion [GO:0030997]; regulation of exocytosis [GO:0017157]; regulation of locomotion [GO:0040012]; regulation of nematode larval development [GO:0061062] | cell cortex [GO:0005938]; centrosome [GO:0005813]; chromosome [GO:0005694]; cleavage furrow [GO:0032154]; condensed nuclear chromosome [GO:0000794]; cortical granule [GO:0060473]; cytoplasm [GO:0005737]; meiotic spindle [GO:0072687]; metaphase plate [GO:0070090]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; separase-securin complex [GO:1990520]; spindle [GO:0005819] | cysteine-type endopeptidase activity [GO:0004197] | PF03568; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:23401519}. Chromosome {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:23401519}. Cytoplasmic granule {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:21878498}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17913784}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:23401519}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498}. Cleavage furrow {ECO:0000269|PubMed:20116245}. Midbody {ECO:0000269|PubMed:20116245}. Note=Before ovulation, accumulates on chromosomes and cortical filaments in oocytes (PubMed:17913784). By metaphase I, dissociates from filaments and transiently localizes to cortical granules until their exocytosis during anaphase I followed by an accumulation at the cortex near the polar body (PubMed:17913784). Localizes to meiotic spindle matrix (PubMed:21878498). During mitotic metaphase and anaphase, localizes to chromosomes, centrosomes and the spindle matrix (PubMed:17913784, PubMed:20116245, PubMed:21878498). During spermatogenesis, localizes to the spermatocyte cytoplasm throughout meiotic prophase I (PubMed:23401519). At the diplotene stage of prophase I accumulates at low levels in puncta around the nuclear envelope (PubMed:23401519). At diakinesis, transiently localizes to centrosomes until nuclear envelope breakdown (PubMed:23401519). At metaphase I and II becomes highly enriched around chromosomes (PubMed:23401519). At anaphase I and II, chromosomal localization is reduced and centrosome localization is highly increased (PubMed:23401519). Localizes to residual body during the budding division leading to spermatid formation (PubMed:23401519). {ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498, ECO:0000269|PubMed:23401519}. | CATALYTIC ACTIVITY: Reaction=All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.; EC=3.4.22.49; Evidence={ECO:0000305|PubMed:25919583}; | null | null | null | null | FUNCTION: Cysteine protease, which plays a central role in homologous chromosome separation during meiosis I and in sister chromatid separation during embryonic mitosis (PubMed:11728305, PubMed:12498686, PubMed:20116245, PubMed:21878498). Promotes chromosome/sister chromatid segregation by cleaving the scc-1 (mitosis) and rec-8 (meiosis) subunits of the cohesin complex at the onset of anaphase (Probable). May cleave histone H3-like protein cpar-1 during meiosis I metaphase-anaphase transition (PubMed:25919583). Promotes cortical granule exocytosis after oocyte fertilization during the first meiotic anaphase (PubMed:17913784, PubMed:21878498). Essential for embryonic cytokinesis by regulating rab-11-positive vesicle trafficking at the plasma membrane at the cleavage furrow and midbody (PubMed:20116245). Regulates centriole segregation during spermatocyte meiosis (PubMed:23401519). Required for embryonic anterior-posterior axis formation (PubMed:11832245). {ECO:0000269|PubMed:11728305, ECO:0000269|PubMed:11832245, ECO:0000269|PubMed:12498686, ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498, ECO:0000269|PubMed:23401519, ECO:0000269|PubMed:25919583, ECO:0000305}. | Caenorhabditis elegans |
G5ED46 | CASY1_CAEEL | MRTAYFIFVGALLGVSYAKHHHAARAPIINLQGAEELVAVVREDENIISTVPDFAILSETGPVCNYLLTSQNNEPVPFDIQVVDKYTGAAVLRVKDAATLDCKKPEYNLQVQAVKCDNDNVKSEGVSLKIRVKDTNNHAPEIENPWYTFHVEEGKVVEEVGVLKASDKDCGHPNGEICEYEITNGLKELPFAINNHGVLRTTQPLNFTQSKSYILTVVAIDCAMRKSKSSLVTVHVDEKCVQGITAMNERVNYAPGVGSKLLLPDVSLEFCEKETICEPKSVQSVIELRAGHVTQGCARDTVYDNQTIQSCGLSTATVKLLNEEALTSSAENQILADQGIEFDGARGVTVSDENHQGLIPDHFTLSFSMKHAAGTKDEQSNKQNILCESDDFNMNRHHFSVYIRHCKLEVVLRREAGATSDFRAAEWRWSMPEVCDNEWHSYSLLFNGIDDVNVIVDGKSFKADERNPEILDDWPLHKTKATKTKLVVGACWHGRQQKLAQFFRGQLSSLYLLSGAVESERAIKCAHTCPEQLQFTGVDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQAAEPTLSISASSQLKSNQHMVKVGQAMVPDLTITISQNNADGELEDVTQSHKIDYCKMHLQPARDMDVEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGRVLSNQLFVTMTIDGVTTTTSTTTEAPAPAQPDPIQFNFNSGETALDSLELIERHFEPAFDQLGSSRLQNILEMDLPRPKALLSHHGYDVGQGAIAGGAVAVVVVVCVGFLLVLLVIGVLKMRDTPMPRRRRQKRQSDGGMHWDDSGMNITVNPLDDVEKNGGAIDEFSDEEEEEETDGESECSYRDEEDDVSEDEEDQTEVLPHLDANQRVVGGLEWDDEDAISTNARSYRV | null | null | associative learning [GO:0008306]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; olfactory learning [GO:0008355]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of synaptic vesicle transport [GO:1902805]; regulation of synaptic transmission, glutamatergic [GO:0051966]; synaptic transmission, GABAergic [GO:0051932] | axon [GO:0030424]; cell surface [GO:0009986]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; postsynaptic membrane [GO:0045211]; synaptic cleft [GO:0043083] | amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988] | PF00028;PF19699; | 2.60.120.200;2.60.40.60; | Calsyntenin family | PTM: A proportion of the protein is proteolytically cleaved before the transmembrane domain in neurons, leading to release in the extracellular space. {ECO:0000269|PubMed:18381821, ECO:0000269|PubMed:29529030}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25035490}; Single-pass type I membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:18381821, ECO:0000269|PubMed:25035490}. Cell projection, axon {ECO:0000269|PubMed:25035490}.; SUBCELLULAR LOCATION: [Secreted calsyntenin-1]: Secreted {ECO:0000269|PubMed:18381821}. Synaptic cleft {ECO:0000269|PubMed:29529030}. Note=Released in the extracellular space following proteolytic cleavage. {ECO:0000269|PubMed:18381821}. | null | null | null | null | null | FUNCTION: Cell adhesion molecule involved in associative learning and memory (PubMed:18381821, PubMed:19287492, PubMed:25035490, PubMed:29529030). Acts as a regulator of GABAergic synaptic transmission at neuromuscular junctions by regulating GABA synaptic vesicle precursor transport: possibly functions as a cargo adapter for unc-104-mediated transport of synaptic vesicle precursors (PubMed:29529030). Promotes localization of isoform c of daf-2 (daf-2c) to synaptic regions by acting as a signaling adapter between klc-2 and daf-2c (PubMed:25035490). {ECO:0000269|PubMed:18381821, ECO:0000269|PubMed:19287492, ECO:0000269|PubMed:25035490, ECO:0000269|PubMed:29529030}.; FUNCTION: [Isoform a]: Acts as aregulator of glutamate signaling in the sensory neurons by inhibiting the activity of command interneurons, thereby negatively regulating motor circuit activity and locomotion. {ECO:0000269|PubMed:29475851}. | Caenorhabditis elegans |
G5ED47 | HIZR1_CAEEL | MQKVMNDPEDLGNCKICLQRADGIHFAVSSCRACAAFFRRTVILKLNYTCKEKGNCTVEKSLRNLCRSCRYTRCINEGMKIELVQLQRDSIGRKKSGASISIDPLFTPNVASSLSAIFKNEKEDVLSTSCTILSQMTSGYAMFLNIRRSTNTLVQSSVITPTFKMPKIELHASRFDSAKQVCKAEAHLVTDIVNSYFSPFNSLKFEDKVALFKNFFCYFSHTDRAYQSFKQFESDNLNDKILMPDGGFIKRTELGRFYENAEGVHTSAEDAAKIFQPALNYILDVIVDYMRRIHIIETEYLALLGFCLWDDAVPGLSKEAKSLAVQTQSKLLAELQNFYSSQNKDAVEITQRVGVLLLLVPKLTKCVIMLRENSVLAELFNYYEADVCCKNFKEDASVDLDCTSQCIVHTKND | null | null | intracellular zinc ion homeostasis [GO:0006882]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; 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, ECO:0000269|PubMed:28095401}. Cytoplasm {ECO:0000269|PubMed:28095401}. Note=Localizes to the cytoplasm in the absence of excess zinc, but accumulates in the nucleus when zinc is in excess. {ECO:0000269|PubMed:28095401}. | null | null | null | null | null | FUNCTION: Nuclear receptor transcription factor that binds to DNA enhancer elements to promote the transcription of genes required to maintain micronutrient homeostasis. Direct binding to its ligand zinc allows for nuclear accumulation and activation, which thereby induces the transcription of genes required to promote the storage and detoxification of excess dietary zinc. This in turn, allows for internal zinc levels to be detected and regulated. {ECO:0000269|PubMed:28095401}. | Caenorhabditis elegans |
G5ED68 | MTMR6_CAEEL | MRFEDIGISKVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLFLAESISRGTSCVVHCSDGWDRTSQVVALCQLLLDPYYRTIHGFQVLIEKDWLGFGHKFDDRCGHVGALNDEAGKEVSPIFTQWLDCIWQIMQQKPRAFQFNERYLIEMHEHVYSCQFGTFIGNCDKDRRDLNLSKRTKSLWTWMDARHDDYMNPFYSPTAHVALLDLDTRAARFTVWTAMYNRFDNGLQPRERLEDLTMAAMEHVGVLESHVAQLRTRLAELKTQQNQQITSTNTPTNMVDSGMSSATDDLKNLSLSHPLDPLSSTLPILERATSQESGVMDSSLYYPDEALTKYSLKWQPLRGADRCSNPACRGEFSSTIERRIHCHLCGMIFCRRCLKVSADERERVCDKCKTD | 3.1.3.64 | null | endocytosis [GO:0006897]; nematode larval development [GO:0002119]; phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol metabolic process [GO:0046488]; regulation of cell migration [GO:0030334]; regulation of Wnt signaling pathway [GO:0030111]; synapse assembly [GO:0007416] | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphatidylinositol phosphate phosphatase complex [GO:1904144]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; phosphatase binding [GO:0019902]; phosphatidylinositol-3,5-bisphosphate phosphatase activity [GO:0106018]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438] | PF01363;PF06602;PF21098; | 2.30.29.30;3.30.40.10; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565969}. Membrane {ECO:0000269|PubMed:14565969}; Peripheral membrane protein {ECO:0000269|PubMed:14565969}. Apical cell membrane {ECO:0000269|PubMed:12788949}; Peripheral membrane protein {ECO:0000269|PubMed:12788949}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000305|PubMed:12788949}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911, ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q9Y217}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000250|UniProtKB:Q9Y217}; | null | null | null | null | FUNCTION: May dephosphorylate phosphatidylinositol-3-phosphate (PI3P) (PubMed:12788949, PubMed:14565969). In association with mtm-9, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels (PubMed:14565969, PubMed:21076391). Regulates fluid phase endocytosis in coelomocytes (PubMed:14565969). Controls the endosomal localization of sorting nexin snx-3 and the levels of sorting receptor mig-14 (PubMed:21076391). By regulating the retrograde transport of mig-14, may be involved in the secretion of Wnt ligands such as egl-20 (PubMed:21076391). Regulates posterior migration of QL neuroblast descendants and the anterior migration of QR neuroblast descendants and HSN neurons during larval development (PubMed:21076391). Involved in the formation of correct synapse number in DA9 motor neurons probably in part by regulating the secretion of Wnt ligand egl-20 (PubMed:25479419). {ECO:0000269|PubMed:12788949, ECO:0000269|PubMed:14565969, ECO:0000269|PubMed:21076391, ECO:0000269|PubMed:25479419}. | Caenorhabditis elegans |
G5EDA5 | KSRB_CAEEL | MSDEKKKKRGFFRYSVLTTSSFSSWRRSSTSGSISQSSRTTSKTTTSSSVTSSNPINAPPPTATSSSSVLPSTSSEPPPPASAPPRISIYHKMVPSKSKFRQCDVCEHIFIFDFVRKQHLDDVYACNVCGIRVHKGCLDRVKNDCKITTQYMGGILENAVIQSNKKQWEKPTTASISKSLTTSPTCSTSTTMSPAGVEKNVHKTRKLISMTTSTLDDVTTFNSEINEEMDEETVLMTWEDVTIKLTDVDVMTKIGDGRFGSVYFGGYHGNAAVRFVNMNYLSQEDRRADVFATEIVSAYKNSRHDHIALFYGYVSDPVTNTYAIVTNFYQHNTLYHRIHEQLSEDFDQSWTFQISLQICQAMSYLHKKKILHRDLRTKNILLDNPNRVVVTDFALMKLERLENPRRNCTLLIPNHWIDYLSPEIAGNLMIDWRGDVLFQHELPFSQESDVYSFGTIFFELLLRRMPTGCDSWDQKLYAKMCGQKAALQRLDAQLQKIDGKLHELLLECWSSQPEKRPSFQQIVKRITVQMPRKESNKQKRRSTAHENPLF | null | null | meiotic cell cycle [GO:0051321]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of vulval development [GO:0040026]; Ras protein signal transduction [GO:0007265]; vulval development [GO:0040025] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713] | PF07714; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family | null | null | null | null | null | null | null | FUNCTION: Probable inactive protein kinase which positively regulates Ras-mediated signaling probably acting at the level of let-60/ras or/and lin-45/raf (PubMed:11882296, PubMed:23900546). In the germline, regulates meiotic progression during oogenesis and mpk-1 (isoform b) phosphorylation (PubMed:11882296, PubMed:26510792). Plays a role in meiotic recombination events (PubMed:26510792). Functions redundantly with ksr-1 in the Ras-mediated regulation of larval survival, the development of excretory canal, in determining vulval precursor cell fate during vulval induction and in mpk-1 phosphorylation in somatic cells (PubMed:11882296). {ECO:0000269|PubMed:11882296, ECO:0000269|PubMed:23900546, ECO:0000269|PubMed:26510792}. | Caenorhabditis elegans |
G5EDB2 | MADD3_CAEEL | MPILHQKIASTGGQPSTNSLALRRLPLVVIPRKRKYKNYVSRRRNTQLLASLRRCVSDPNVYKSYNHWKALLRPMTPIKSGAPTPKTVTPMPVPQIPPHQKMTPNPTPTQNPVQLPLPHAVSEKPGDKKSTGPTPSPVPSKAPISAAKLPGTVTKVAPLLSAAQPPPKTLAPAPGASETNSGSGPVSKQVSGKLTELKSKNGTVTEKTEKAVLRIPSSASTRAKAASAVAPEANPAPVPTATKPSPFAPAIAPLRDGAPAQPPAPIQASAPLRPPVAKQNSLQKPPEPKRSVGAPPKALPSELVNKIDGIEFLPQSSNQNTDDGQQPTTSTGGAKALRRAYGSKSGTTICAIGSPNVPSTSQPQQGDNEKRLIEKKLSLRKKKLSGEGVPPAGSMLTGSKSGVEIGLSSNLTTTNNNNNKEQTDEQRAKKTVNAVAAAFSTQAGSGNATTVDDPASTTTSKENPAAQPPKPKSAAVQNLISQLQLPASVSAKVDKIIACGDKARKPSRSGLQASQARPKVPEIVSSQRTQHQDDKDGHLIYSKGDFILNRFTIYDTLGEGTFGKVVRVNDSLSDTFMALKIIKNVSKYREAAKLEVKVLQKLAEKDPEKKNWVIHMGSYFDYNGHICLLFDLMGSSIFDFLKANHYKPYPMEQTLHITWQLCNAVKFLHDNKLTHTDLKPENILFVDSRYTTKLVDKKPLRVLHSTHVRLIDFGSATFDHEHHSIIVSTRHYRAPEVILELGWSQPCDVWSIGCILYELYTGVTLFQTHENREHLAMMERVLGDIPLRMAKRTKTKFFINGRLDWVNTSADAAYVRDNCKPLRRSMSCTDPEHVELFELIENMLMFEPLARMKLPEALQHRYFNRLPENLKIPCKMDASTNPRINGD | 2.7.11.- | null | phosphorylation [GO:0016310]; regulation of RNA splicing [GO:0043484] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, Lammer subfamily | null | SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:27123983}. Nucleus {ECO:0000269|PubMed:27123983}. Note=Enriched in the cytoplasm. {ECO:0000269|PubMed:27123983}. | null | null | null | null | null | FUNCTION: [Isoform a]: Probable dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Negatively regulates p38 MAPK signaling to allow for the plasma membrane of body wall muscle cells to form projections, also called muscle arms, that extend and connect the body wall muscles to target motor neurons. Negative regulation of p38 MAPK signaling may in turn modulate the trafficking of the muscle specific receptor eva-1 to the lysosome, to ensure proper display of the eva-1 receptor on the plasma membrane of muscle cells and allow for muscle arm extension towards guidance cues. {ECO:0000269|PubMed:27123983}. | Caenorhabditis elegans |
G5EDB9 | RPGF_CAEEL | MDPRKPRQDPVNDARFYESLIKPPHLRTPDDIRNVYEQLRQLDTFSNLFIGPLKALCKTARYERHPAQYILFRDGDVARSWYILLSGSVFIENQIYMPYGCFGKRTGQNHRRTHNCLLLQESEMIVIDYPTEPQSNGMSPRTPPRGIHHSGEPVHQKTPRKSAPNMSVDSIAMPPPPVPPRPLRLPQTAAKGPAPLPPRGLPRTYPLDFPVDIPTTSSSSSNTSYNDQHRSQVYLNGLSADEDTLVRVKHRREKSNSVGGQAQNGISTARRLRGRSTASSTTTEGETASNEGADSDEDEGSMPSQESSSGGFMDLRDSVRECLEKEPSERNSEDLAVLLDFMQHMSAFAALPMSIKRQLCLKMVFAVVNDAGTVVLAHNEKLDSWSVIVNGCVEVVKPSGERVEYKLGDSFGAEPTPATQIHIGEMRTMVDDCEFVLVEHRDFCSIMSTIGDHIEKDRDGLTGEVVSEVERRTVGTHCGQVLIKGKPDKLIHHLVDERDHNVDPHYVDDFLLTYRVFIRDPTTIFEKLMLWFADSIYRDKVARLVLLWVNNHFNDFETNDEMWNLLERFEGALERDGMHSQLSLLNIACSVKAKPRQVILTRRKDDKMMMRLVGGQESGNSVYVAEVFPDTSAAREGVKRADEMLEVNQQSAKYLSAKKAEDLLTGSLSLTLMLKNNVLGYKETIGKIEHNKPKNGTSRSGAGIPMVIPVHKTSITGKKSSTTSSKSGMMEKLMTILKSSKEDSMDFTDEAKISSADLRPSRSNPDITSISQYYGPVRSECPEHVLKIYRNDQTFKYLPVYKETSAQNVVQLALQEFNMTAEGSPEWSLCECTVTIDGVIKQRRLPPQMENLAERIALNSRYYLKNNSRSEPLVPDELAPELLKEAQTQLLSLNAQVVAAQLTLQDFSVFSAIEPTEFLDNLFKLDSKYGSPKLEEFEQLFNREMWWVATEICTERHVQKRAKLIKKFIKVARYCRDLRNFNSMFAIMSGLDKPAVRRLHSSWERVSSKYIRMLDEIHQLVDPSRNMSKYRQHLAEVAQEPPVVPIYPVIKKDLTFAHDGNATYSEKLINFEKLRLIAKSIRGVMKLSSAPYEIASMAERSGGVVMDALLHMNSFENSNVATMRKGMSGKQNQPRKKVYEQALMVRKVKSYLEGLHVVDNEMELDSMSYDIEPQVQTAHRGANSSSTANIRRVPSPTPSSLSSQSAGSADQSSRHRLLFNGTGSISSAGGGSKFGVESPQAVQKMLSLVQNSKVKGAPPQITSPSTSARSSLQRNMPRVTGRQATSSAQGPVQLNEETSTVTTYYQSDNGRRQRSGSEGRFDNIPPSTFYLTSDGLTVSPRQSLSVVIPTHPHGHSPTSPRCRSRSPASSGCSSFSTIASIAATSMAAAPSAFVSNPYQHHQTVRGHVIGHRPMPIVTSGSATLPNHVSPRGLPPKSRPTILPGSHTNSSSRMGTIKEATFLTSEQVSRV | null | null | collagen and cuticulin-based cuticle development [GO:0040002]; epidermis development [GO:0008544]; molting cycle, collagen and cuticulin-based cuticle [GO:0018996]; Ras protein signal transduction [GO:0007265] | apical plasma membrane [GO:0016324]; collagen and cuticulin-based cuticle extracellular matrix [GO:0060102]; endocytic vesicle [GO:0030139]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF00595;PF00788;PF00617;PF00618; | 2.30.42.10;2.60.120.10;1.10.840.10;1.20.870.10; | RAPGEF2 family | null | null | null | null | null | null | null | FUNCTION: Acts as a guanine nucleotide exchange factor for small G protein GTPases like rap-1 and rap-2. Required in the hypodermis, especially in the seam cells, for proper formation of the cuticle. {ECO:0000269|PubMed:15525675}. | Caenorhabditis elegans |
G5EDE1 | GFI1H_CAEEL | MSTEHVSNVYSVESLLSNVEKSSVSPTESIEDRNEFMITEDVMSSWQRMAATISLQQKLLMMQQTMPRPPPVNILGNFPFGFLNAPMFWQQYLRSMAMGIIPQNPESPSASVWNRTPTPPVEIKPFHCQKCTKLFSTIAALEQHQQVHVSDKQFECKQCGKTFKRSSTLSTHLLIHSDTRPYPCEYCGKRFHQKSDMKKHTYIHTGEKPHKCTVCGKAFSQSSNLITHTRKHTGFKPFACDVCGRTFQRKVDRRRHRESHHPGHPEECVSASQISSDLSPKGYMTPPTSNGYLDSSDEFLNVFRLPAELLAIKAEMGEEMEEADDEEEKVLNLSVS | null | null | negative regulation of apoptotic process [GO:0043066]; negative regulation of insulin secretion [GO:0046676]; negative regulation of neurotransmitter secretion [GO:0046929]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast fate specification [GO:0014018]; regulation of backward locomotion [GO:0043058]; regulation of forward locomotion [GO:0043059]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357] | axon [GO:0030424]; nucleus [GO:0005634]; perikaryon [GO:0043204] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9169852}. Cell projection, axon {ECO:0000269|PubMed:9169852}. Perikaryon {ECO:0000269|PubMed:9169852}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:26096732). Plays a role in the determination of neuroblast cell fate and neuronal differentiation (PubMed:11923211, PubMed:26096732). Negatively modulates expression of several components of dense-core vesicles (DCVs), thereby, in a DCV membrane protein ida-1-dependent manner, regulating neurosecretion (PubMed:19343207). Negatively modulates the transcription of its own gene, the mechanosensory gene mec-3, and also other touch neuron-specific genes in the BDU neurons; required for coordinated movement (PubMed:26096732, PubMed:8770591, PubMed:9169852). Required to determine the identity of BDU sensory neurons in concert with transcription factor unc-86, regulating expression of a number of genes, including transcription factors ceh-14 and ahr-1, neuropeptides flp-10, nlp-1 and nlp-15, and tyramine receptor-encoding ser-2 (PubMed:26096732). Acts in concert with non-canonical WNT signaling to negatively modulate transcription of mec-3 gene in BDU neurons (PubMed:26096732). May act in concert with transcription factor unc-3 in motor neuron fate determination (PubMed:18817768). May play a role programmed cell death (PubMed:11923211). {ECO:0000269|PubMed:11923211, ECO:0000269|PubMed:18817768, ECO:0000269|PubMed:19343207, ECO:0000269|PubMed:26096732, ECO:0000269|PubMed:8770591, ECO:0000269|PubMed:9169852}. | Caenorhabditis elegans |
G5EDE2 | CBXH2_CAEEL | MSSKSTKRAKIEDPKDNVFMVEKVLDKRTGKAGRDEFLIQWQGFPESDSSWEPRENLQCVEMLDEFEREFSKREKPIRKRHSQKPEPSEDQADPEEDKDEKKETNQNDKFSLEGKQLKCIVGLTKGPGELHFLCKFSDDTARLLPAKEVNSRYPSQVIRYYESKLTIQDPKADEL | null | null | chromatin organization [GO:0006325]; chromosome attachment to the nuclear envelope [GO:0097240]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; germ cell development [GO:0007281]; gonad development [GO:0008406]; negative regulation of gene expression [GO:0010629]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of vulval development [GO:0040027]; nematode larval development [GO:0002119]; nematode male tail mating organ morphogenesis [GO:0090597]; olfactory learning [GO:0008355]; phospholipid metabolic process [GO:0006644]; positive regulation of gene expression [GO:0010628]; positive regulation of growth rate [GO:0040010]; regulation of cell differentiation [GO:0045595]; regulation of gene expression [GO:0010468]; reproduction [GO:0000003]; response to endoplasmic reticulum stress [GO:0034976]; RNA splicing [GO:0008380]; vulval cell fate specification [GO:0072327] | chromosome [GO:0005694]; nuclear inner membrane [GO:0005637]; nuclear periphery [GO:0034399]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; H3K27me3 modified histone binding [GO:0061628]; methylated histone binding [GO:0035064] | PF00385;PF01393; | 2.40.50.40; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11850401, ECO:0000269|PubMed:16890929, ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:25467431, ECO:0000269|PubMed:26476455, ECO:0000269|PubMed:29760282}. Chromosome {ECO:0000269|PubMed:11850401, ECO:0000269|PubMed:16890929, ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:25467431, ECO:0000269|PubMed:26476455}. Note=Localizes to distinct nuclear foci, not overlapping significantly with hpl-1, in embryonic cells (PubMed:16905130, PubMed:26476455). Localization to nuclear foci overlaps partially with zinc finger protein lin-13 (PubMed:16890929). Localizes to foci in a lin-13-dependent manner (PubMed:16890929). Localization along chromosomal arms correlates with localization of histone H3 methylated at 'Lys-9' (H3K9me), however, hpl-2 can associate with chromatin in an H3K9me-independent manner (PubMed:25467431). Localization on chromosome correlates with sequences enriched in repetitive elements, or in well-expressed genes (PubMed:25467431). Localized to gene bodies (PubMed:29760282). {ECO:0000269|PubMed:16890929, ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:25467431, ECO:0000269|PubMed:26476455, ECO:0000269|PubMed:29760282}. | null | null | null | null | null | FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes (PubMed:11850401). Probably does not act as global transcriptional repressor, instead targeting a subset of genes (PubMed:19064713, PubMed:22185090, PubMed:23028351, PubMed:25467431). Involved in RNA processing mediated by Tar DNA-binding protein homolog tdp-1 (PubMed:29760282). Plays a role in linking epigenetic regulation with the innate immune response (PubMed:22083954). Involved in the endoplasmic reticulum (ER) stress response via modulation of the unfolded protein response (UPR), acting mainly through the IRE1-XBP1 pathway and perhaps, to a lesser extent, through the autophagy pathway (PubMed:24715729). May act in a common pathway with retinoblastoma-like protein homolog lin-35 and zinc finger protein lin-13 to influence the ER stress response in the intestine (PubMed:24715729). Plays a role in the formation of the vulva and in fertility, acting together with a CoREST-like complex, and chromobox protein homolog hpl-1 (PubMed:11850401, PubMed:16890929, PubMed:16905130, PubMed:26476455). Acting in concert with hpl-1 and histone H1 protein his-24, involved in reproduction, somatic gonad development, male tail development and vulval cell fate specification; perhaps as a result of modulating expression of Hox genes mab-5 and egl-5 (PubMed:11850401, PubMed:16890929, PubMed:16905130, PubMed:19064713, PubMed:23028351). In vulval cell fate specification may act by repressing transcription, of EGF family gene lin-3 in hypodermal hyp7, and of homeobox lin-39 in vulval precursor cells (VPC) (PubMed:19064713). Role in growth and somatic gonad development is antagonized by histone-lysine N-methyltransferase set-2/SET1 (PubMed:17967446). Required for larval development, acting redundantly with hpl-1 (PubMed:16905130). Plays a role in regulation of the developmentally arrested larval state known as dauer, longevity, and lipid metabolism (PubMed:22185090). {ECO:0000269|PubMed:11850401, ECO:0000269|PubMed:16890929, ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:17967446, ECO:0000269|PubMed:19064713, ECO:0000269|PubMed:22083954, ECO:0000269|PubMed:22185090, ECO:0000269|PubMed:23028351, ECO:0000269|PubMed:24715729, ECO:0000269|PubMed:25467431, ECO:0000269|PubMed:26476455, ECO:0000269|PubMed:29760282}. | Caenorhabditis elegans |
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