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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O17087 | GLD2_CAEEL | MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQSHPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPKYHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNRAPTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQPPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQTNQQKTVSSYERAAQFRASASELPTDSVDAKH... | 2.7.7.19 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | cytoplasmic polyadenylation [GO:0180011]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic cell cycle [GO:0051321]; mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; nucleus organization [GO:0006997]; positive regulation of meiosis I [GO:0060903]; positive regulation of mitotic nu... | cytoplasm [GO:0005737]; P granule [GO:0043186]; protein-containing complex [GO:0032991]; RNA polymerase complex [GO:0030880]; RNA-directed RNA polymerase complex [GO:0031379] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA polymerase activity [GO:1990817]; RNA uridylyltransferase activity [GO:0050265] | PF03828; | 1.10.1410.10;3.30.460.10; | DNA polymerase type-B-like family, GLD2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12239571}. | CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:12239571}; PhysiologicalDirection=left-to-... | null | null | null | null | FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. Acts as a regulator of mitosis/meiosis required for progression through meiotic prophase during oogenesis and spermatogenesis and for promotion of the entry into meiosis from the mitoti... | Caenorhabditis elegans |
O17185 | SUP9_CAEEL | MKRQNIRTLSLIVCTLTYLLVGAAVFDALETENEILQRKLVQRVREKLKTKYNMSNADYEILEATIVKSVPHKAGYQWKFSGAFYFATTVITTIGYGHSTPMTDAGKVFCMLYALAGIPLGLIMFQSIGERMNTFAAKLLRFIRRAAGKQPIVTSSDLIIFCTGWGGLLIFGGAFMFSSYENWTYFDAVYYCFVTLTTIGFGDYVALQKRGSLQTQPEYVFFSLVFILFGLTVISAAMNLLVLRFLTMNTEDERRDEQEAILAAQGLVRVGDPTADDDFGRLPLSDNVSLASCSCYQLPDEKLRHRHRKHTEPHGGPPTF... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of muscle contraction [GO:0006937]; stabilization of membrane potential [GO:0030322] | muscle cell projection membrane [GO:0036195]; plasma membrane [GO:0005886]; striated muscle dense body [GO:0055120] | outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Associated with dense bodies. {ECO:0000269|PubMed:14534247}. | null | null | null | null | null | FUNCTION: Potassium channel involved in coordination of muscle contraction (PubMed:14534247). Activity is regulated by sup-18 (PubMed:24586202). {ECO:0000269|PubMed:14534247, ECO:0000269|PubMed:24586202}. | Caenorhabditis elegans |
O17286 | NFYB1_CAEEL | MDPKPINEGMLLEDHDHGMPEEEEITEDDMNGIHNIEEDTRTISEIAMELHHPNKSQVLLDQERFLPIANVVRIMKTQMDPQAKLAKDAKECAQECVSEFISFIASEAAEICNITKRKTITADDLLTAMEATGFDNYAEPMRIFLQKYRQAHKITGPIHRTHPDYVRPPQFQMDPFVRPLFFDTEQGRRCTETQYVINGSEIVKNAPLGEEWNEQTGTLNTRADGYYMEEPMEPMPMEEVEIEEHEEIIEQDSLGAIALEQQGQMQIYVDPKTKQHFAAKETPNGMELYPLIIQDTPLQLENVSGPNQFVMNMPDGRAIP... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888] | CCAAT-binding factor complex [GO:0016602]; cytoplasm [GO:0005737]; perikaryon [GO:0043204] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region ... | PF00808; | 1.10.20.10; | NFYB/HAP3 subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17574230}. Cytoplasm {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}. Perikaryon {ECO:0000269|PubMed:15704008}. Note=Localizes to the cytoplasm of secretory cells and cell bodies of the small ganglia surrounding the pharynx. {ECO:0000269|PubMed:15704008}. | null | null | null | null | null | FUNCTION: Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types (PubMed:17574230). In... | Caenorhabditis elegans |
O17323 | HDA4_CAEEL | MEEASSSTGSAGGAGPSVPNLPSTSEAAIGQTNLEPESIALLQSQLQEYRQKQMDLIGHFQRAQQELSVQHMHNLYAALQQQQQLQNLQTERSAVNPLLISQQHSTEDQNSGPAAPLSLANSLTNLLSSSNGNLSVPQTPTKEHHPTAPTSNRKCDLPRSNSTTISQLTKDRLKNMIANRSKGESNSQSNLMSNSVTANGNGHDNGRKLKNSNSQVNVSSPHFEPYRLPTSLANAHNLQQASEFQLRKVNSEPNLKMRIRAKLLSKGSSPVQHVQQNNSQFNFTHPQLKRSDSETSQNVPLDFMQSSSQTNLPHLMLPSP... | 3.5.1.98 | null | chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of neuron differentiation [GO:0045664]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nucleus [GO:0005634] | calmodulin binding [GO:0005516]; histone deacetylase activity [GO:0004407]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 2 subfamily | PTM: Phosphorylated by serine/threonine-protein kinase kin-29 at Ser-251; the phosphorylation inhibits repression of transcription by mef-2 (PubMed:17170704). May be phosphorylated by either cyclic-AMP dependent or cyclic-GMP dependent protein kinases (PubMed:18832350). {ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:... | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; | null | null | null | null | FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By sim... | Caenorhabditis elegans |
O17386 | CED8_CAEEL | MFLKKHKSKLLLVPRDEEQEDAGIVAVLTDRIPSVLLVRWFDLFCFGFAMCSYALDFFSDIGIAIFHFWAGRYLSGSLVLAFALLPSVIINIISMVWMLDDEMHWKRRAHPRRTGTFELNQKRFIPLSKMIVLCICQMGPLFWYYKALYYGWMFRKSSNENTDGEKRKCFSKMVEAERDATLLRFFEAFLESAPQLIIQGSIAASYFQNYYQTGTYPYWLYFQAASLLLSIISISWSVVVQNRSLRMIRDDKVNIWPHEAVLQFCWRFLTILARIITLVALVLIFGINVVPLISVHLLVTLVHVIFLQAIHIDACTHIEK... | null | null | apoptotic process involved in development [GO:1902742]; embryo development ending in birth or egg hatching [GO:0009792]; engulfment of apoptotic cell [GO:0043652]; execution phase of apoptosis [GO:0097194]; phosphatidylserine exposure on apoptotic cell surface [GO:0070782]; programmed cell death [GO:0012501] | plasma membrane [GO:0005886] | phospholipid scramblase activity [GO:0017128] | PF09815; | null | XK family | PTM: Cleavage by ced-3 activates ced-8 function in promoting phosphatidylserine exposure at the surface of apoptotic cells. {ECO:0000269|PubMed:24225442}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10882128, ECO:0000269|PubMed:24225442}; Multi-pass membrane protein {ECO:0000269|PubMed:10882128}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000305|PubMed:23845944}; | null | null | null | null | FUNCTION: Phospholipid scramblase that acts downstream of ced-9 and caspase ced-3 to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:24225442). Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubM... | Caenorhabditis elegans |
O17389 | TYB_CAEEL | MAAVTELPKMNQELAGAVREGLELKKVETTEKNVLPTKEDVAEEKQHVERIHEIEHFDSTKLHSTPVKEKIVLPSADDIKQEKQHLELTDKINNFPSENLKKTETIEKNVLPSPTDVAREKTLQMAASFDKSALHHVETIVSTDVRVTEAQ | null | null | actin filament organization [GO:0007015] | anchoring junction [GO:0070161]; cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin monomer binding [GO:0003785] | PF01290; | 1.20.5.520; | Thymosin beta family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:15269284}. Cytoplasm {ECO:0000269|PubMed:15269284}. Cell junction {ECO:0000269|PubMed:15269284}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15269284}. Note=Localizes to the cell cortex and the cytoplasm in oocytes and at the inside edges of membrane cubi... | null | null | null | null | null | FUNCTION: Plays an important role in the organization of the cytoskeleton by regulating actin polymerization in two ways. Firstly, by binding to and sequestering actin monomers (G actin) inhibits actin polymerization. Secondly, by binding directly filamentous actin (F actin) promotes actin polymerization. Regulates the... | Caenorhabditis elegans |
O17468 | HIRA_DROME | MRLLKPAWVHHDDKQIFSVDIHKDCTKFATGGQGSDCGRVVIWNLLPVLSDKAEFDADVPKMLCQMDQHLACVNCVRWSQNGQNLASGSDDKLIMIWRKSAGSSGVFGTGGMQKNHESWKCFYTLRGHDGDVLDLAWSPNDVYLASCSIDNTVIIWDAQAFPHSVATLKGHTGLVKGVSWDPLGRFLASQSDDRSIKIWNTMNWSLSHTITEPFEECGGTTHILRLSWSPDGQYLVSAHAMNGGGPTAQIIEREGWKCDKDFVGHRKAVTCVRFHNSILSRQENDGSPSKPLQYCCLAVGSRDRSLSVWMTALQRPMVVI... | null | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription [GO:0006351]; regulation of DNA-templated transcription [GO:0006355]; sperm DNA decondensation [GO:0035041] | germinal vesicle [GO:0042585]; HIR complex [GO:0000417]; male germ cell nucleus [GO:0001673]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone chaperone activity [GO:0140713]; nucleosome binding [GO:0031491] | PF07569;PF09453;PF00400; | 2.130.10.10; | WD repeat HIR1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16251970}. Note=Maternally contributed protein localizes specifically to the male nucleus in fertilized eggs. This localization persists from the initiation of sperm nucleus decondensation to the end of pronucleus formation. | null | null | null | null | null | FUNCTION: Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly. Promotes remodeling of sperm chromatin following fertilization via the incorporation of histone H3.3 and histone H4. {ECO:0000250, ECO:0000269|PubM... | Drosophila melanogaster (Fruit fly) |
O17514 | MES2_CAEEL | MSNSEPSTSTPSGKTKKRGKKCETSMGKSKKSKNLPRFVKIQPIFSSEKIKETVCEQGIEECKRMLKGHFNAIKDDYDIRVKDELDTDIKDWLKDASSSVNEYRRRLQENLGEGRTIAKFSFKNCEKYEENDYKVSDSTVTWIKPDRTEEGDLMKKFRAPCSRIEVGDISPPMIYWVPIEQSVATPDQLRLTHMPYFGDGIDDGNIYEHLIDMFPDGIHGFSDNWSYVNDWILYKLCRAALKDYQGSPDVFYYTLYRLWPNKSSQREFSSAFPVLCENFAEKGFDPSSLEPWKKTKIAEGAQNLRNPTCYACLAYTCAIH... | 2.1.1.356 | null | epigenetic regulation of gene expression [GO:0040029]; gamete generation [GO:0007276]; germ cell development [GO:0007281]; germ-line stem cell division [GO:0042078]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of gene expression [GO:0010629]; regulation of gene expression [GO:0... | ESC/E(Z) complex [GO:0035098]; nucleosome [GO:0000786]; nucleus [GO:0005634]; PcG protein complex [GO:0031519] | chromatin binding [GO:0003682]; histone H3K27 methyltransferase activity [GO:0046976]; histone H3K27 trimethyltransferase activity [GO:0140951]; histone methyltransferase activity [GO:0042054] | PF18264;PF00856; | 2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, EZ subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9609829}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEB... | null | null | null | null | FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of a the mes-2/mes-3/mes-6 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive s... | Caenorhabditis elegans |
O17528 | TMED2_CAEEL | MNSLTWILAVLFVTPAASYFIHVDANEEQCFFDRLTSGTKMGLMFEVAEGGFLDIDVKITGPDNKEIYKGERESSGKFTFAAHMDGVYTYCFGNKMSTMTPKAVMFTVEITEPHQQAPGAAANQDAADNAKLEEMVRELSSALMSVKHEQEYMEVRERVHRNINENTNSRVVMWAAFEAFVLVGMTVGQIFYLKRFFEVRTMV | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; regulation of Notch signaling pathway [GO:0008593]; regulation of transport [GO:0051049] | COPI-coated vesicle membrane [GO:0030663]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | cargo receptor activity [GO:0038024] | PF01105; | null | EMP24/GP25L family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Golgi-derived coatomer-coated vesicles. | null | null | null | null | null | FUNCTION: May have a role in the negative regulation of lin-12 and glp-1 transport to the cell surface (PubMed:10366590). May also have a role in a quality control mechanism for endoplasmic reticulum-Golgi transport; the budding of coatomer-coated and other species of coated vesicles, could bind cargo molecules to coll... | Caenorhabditis elegans |
O17581 | SCC4_CAEEL | MNQDAVAKALLGMAEALRTQDPPKLKMAIKCARSTLSMEISDEMKAICNLQLGKLLFFYTDNFELAKNHLQCAYDKMSAMGTFYTRDKMNAISMLADLHIHYQQWPLTSIKATIRHEITTTRGFPALSNKLMFQLIELMKIDKDVEGAIEMCQLAINSSHADPKMELYFRIAKTLVTYQLMHEEPDISDVTRIGSMIKVMENSTTSDKAHLECIKDFYVCTKLAYMFYEGKSRTSRQLLRQIQKSQTSGETKIHGIRWLGEPSITLLACVMNQICALVQSNTDRVEKYYHLVIKHADEIIFKSTRSPQEPGVVRCINMIK... | null | null | anterior/posterior axon guidance [GO:0033564]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; dorsal/ventral axon guidance [GO:0033563]; egg-laying behavior [GO:0018991]; maintenance of mitotic sister chromatid cohesion [GO:0034088] | axon [GO:0030424]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMC loading complex [GO:0032116] | double-stranded DNA binding [GO:0003690] | null | null | SCC4/mau-2 family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15539489}. Cytoplasm {ECO:0000269|PubMed:15539489}. Note=Binds to chromatin from the end of mitosis until prophase. Localizes to the cytoplasm of neurons. | null | null | null | null | null | FUNCTION: Plays an important role in the loading of the cohesin complex on to DNA (By similarity). Forms a heterodimeric complex (also known as cohesin loading complex) with scc-2/SCC2 which mediates the loading of the cohesin complex onto chromatin (By similarity). Required for normal development until the fourth larv... | Caenorhabditis elegans |
O17583 | LIN10_CAEEL | MSSEAVAQATAATTSPEHGVPTSSATPTPPPSKGGGAGGGGGGEQQQVPFQMIPPGHFFANPFLNPYIPTAGAPAQEGEAQPQMVFSPAQYQEVMHHYFQQMMAASGAQFPIPFPMQFQPALQQPRPSSQASSSHRSEDDNGRQTAGSVVSSNVSPNHREVRPAEDSTETSGVVQNNDELLVPTSTSSDVTIGDVIEKSDSPENSQESAGGEEKSEEKRKLSGDRTDSLIRKQMSEMEKEITRRSQNKNIKTIDDDGLAELIGGSSTRTVADDFSPFVDKSGLSYTAPAPPSTEKSAPKESLNQLRSSFNLPDDSTTVGP... | null | null | chemical synaptic transmission [GO:0007268]; nervous system development [GO:0007399]; neuron-neuron synaptic transmission [GO:0007270]; positive regulation of backward locomotion [GO:1905852]; positive regulation of vulval development [GO:0040026]; protein localization [GO:0008104]; protein localization to basolateral ... | cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi trans cisterna [GO:0000138]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; synapse [GO:0045202]... | amyloid-beta binding [GO:0001540]; small GTPase binding [GO:0031267] | PF00595;PF00640; | 2.30.42.10;2.30.29.30; | null | PTM: Phosphorylated on multiple Ser and Thr residues by cdk-5 which regulates its localization (PubMed:17671168, PubMed:22252129). {ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22252129}.; PTM: May be hydroxylated by egl-9 isoform e on multiple Pro residues which may prevent phosphorylation by cdk-5. {ECO:0000269|Pu... | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10359617}; Peripheral membrane protein {ECO:0000269|PubMed:10359617}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10359617}; Peripheral membrane protein {ECO:0000269|PubMed:10359617}. Cytoplasm {ECO:0000269|PubMed:2225... | null | null | null | null | null | FUNCTION: Required specifically for the determination of 3 vulval precursor cell fates P5.p, P6.p and P7.p during late second and early third larval stages; required for basolateral localization of receptor tyrosine kinase let-23. Could have a general but redundant role in development, functioning in diverse cell linea... | Caenorhabditis elegans |
O17607 | RUVB1_CAEEL | MDMEVDEAISGTSSSRLAPIEEVKPTPKQIKRIAAHSHVKGLGIDTETQEAHYEAAGFVGQAPARTAASIVVDMIRLKCMAGRAVLIAGPPATGKTAIALAMSQELGDGVPFVPLVASEVFSNEVKKTEVLMRSFRRAIGLRVKETKDVYEGEVTELSPVEASDNSGMGKTISHLVLSLKTAKGSKQLKLDPSIYDSILKQRVEVGDVIYIEANSGIVKRVGRCDVYASEFDLEADEFVPMPKGDVRKSKDIVQNVSLHDLDIANARPQGRQGDVSNIVSQLMTPKKTEVTDRLRSEINKVVNEYIESGVAELMPGVLFI... | 3.6.4.12 | null | box C/D snoRNP assembly [GO:0000492]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; nematode larval development [GO:0002119]; positive regulation of translation [GO:0045727]; regulation of transcription by RNA polymerase II [GO:0006357]; TOR signaling [GO:0031929] | cytoplasm [GO:0005737]; Ino80 complex [GO:0031011]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; R2TP complex [GO:0097255]; Swr1 complex [GO:0000812] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678] | PF06068;PF17856; | 1.10.8.60;3.40.50.300;2.40.50.360; | RuvB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25437307}. Nucleus {ECO:0000269|PubMed:25437307}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P0A812}; | null | null | null | null | FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP dependent DNA helicase (3' to 5') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). May participate in several chromatin remodeling complexes that mediate the ATP-dependent exchange of histones and r... | Caenorhabditis elegans |
O17622 | KCY1_CAEEL | MYNVVFVLGPPGSGKGTICTQIHENLGYVHLSAGDLLRAERERAGSEYGALIEGHIKNGSIVPVEITCALLENAMIASKDANGFLIDGFPRNEDNWSGWNKQMGGKVNEQFVLFLSCPVDVCIDRCLHRGQGRTDDNVESLKKRVETYNQSTFPIIEHFEKVGMVREVNSERPVTEVYEDVVKVFAAANQK | 2.7.4.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; CDP biosynthetic process [GO:0046705]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; CMP kinase activity [GO:0036430]; cytidylate kinase activity [GO:0004127]; dCMP kinase activity [GO:0036431]; UMP kinase activity [GO:0033862] | PF00406; | 3.40.50.300; | Adenylate kinase family, UMP-CMP kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. | CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:C... | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}. | Caenorhabditis elegans |
O17645 | HST2_CAEEL | MLWKKRKVLYFAGISVFILILLLLKLNSKPKANVWPTSSKIVIYNRIPKTGSTTFTNAIAYDLYKENGFSVLHVNMTKNRQVMSLPDQYTFVNNITTWTERLPAFYHGHVAFIDFQRFGIANPIYINIIREPLERLLSHYYFLRYGDNYRIGLKRSRAGNNETFDECYSRGGKDCDMKQMWIQIPYFCGHYHFCTEVGNPEALRVAKQNVLEKYLLVGTTSRMRDMIALLEVTVPDFFKGALGHFDSLDANRAHLRYTKKKIPPNDQTLSMIRRDEVYKMEREFYDFINNLFDAVFKKATNGISKADDLVKLPLQYHFEK... | 2.8.2.- | null | heparan sulfate proteoglycan biosynthetic process, enzymatic modification [GO:0015015]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; positive regulation of multicellular organism growth [GO:0040018]; regulation of axon guidance [GO:1902667]; regulation of ce... | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | heparan sulfate 2-O-sulfotransferase activity [GO:0004394] | PF03567; | 3.40.50.300; | Sulfotransferase 3 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). Involved in cell adhesion and guidance by specifically modifying proteoglycans in the extracellular matrix and on the cell surface that are essential for axon migrations. {ECO:000... | Caenorhabditis elegans |
O17670 | EYA1_CAEEL | MLPDSEGQKLKTFLLGTGTTLDPSLDPTGNSNFSMATTSDSSTIWTALPASQPGDKDIPTVDLAAISEAYGSTSSTTSLTSSVTSQYQYNSYPQYAMYTSANPANYYQQVTANLRAGTTAFPYSLTTPSYYGSYPVDYTSAAAAYQNPYYTNLRGGTAAPYYNPLNATTAAAYASVASSVLGTDAVNLGTSSDGSTGVPSTVTSFSLKEKKPKVSKKKKTGSCSPGDETYARVFIWDIDDIAVISRNYLASVTHTNEFYARAANSVSHLMERIALNNFADVNEFLEGDITNIEDAVVDETTMDSGPIDNLRGLDVMRRVA... | 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU362036}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|RuleBase:RU362036}; | cell differentiation [GO:0030154]; egg-laying behavior [GO:0018991]; embryonic morphogenesis [GO:0048598]; locomotion [GO:0040011]; mesodermal cell fate specification [GO:0007501]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [G... | nucleus [GO:0005634] | metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]; transcription coactivator activity [GO:0003713] | null | 3.40.50.12350; | HAD-like hydrolase superfamily, EYA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16154558, ECO:0000269|PubMed:19427847}. | 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|RuleBase:RU362036}; | null | null | null | null | FUNCTION: Tyrosine protein phosphatase (By similarity). Acts probably as a transcription regulator in the embryonic and postembryonic development of several tissues including pharynx, vulva and gonads (PubMed:16154558). Required for the development of anterior tissues during late embryogenesis (PubMed:16154558). Togeth... | Caenorhabditis elegans |
O17679 | SET6_CAEEL | MERSRTGGSSTYSMSTANVPIITISDDDDELTIWEEPRKSPISSNSYSDERNHSLSSTSNSSVERSIIITISDDESEATERNQQEVVDRAISNNLTEKRRRSVESFHRLHSKERKLEVKSRKKSRTSSSSMEASTSCTFPARQTKTKRHKRKTYSTISSFAPHHSTICAELRNVNPARIADFRHPSIFEYSDMSLNERREHWKKEMKVIKKHNDIRLMHEEAVRFDDIIELDPTLNGYYRRFMGAEQSTRALFMAVRCLATFGRNFYEEPERDHGEEEIPEELDRYFEKLIYVAPRTRIRITDDIHLSNDTHRIPVYTDA... | 2.1.1.-; 2.1.1.366 | null | epigenetic regulation of gene expression [GO:0040029]; methylation [GO:0032259] | chromatin [GO:0000785]; nucleus [GO:0005634] | histone H3K9 dimethyltransferase activity [GO:0140942]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H3K9me2 methyltransferase activity [GO:0140947] | PF00856; | 2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32103178}. Chromosome {ECO:0000269|PubMed:32103178}. | CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically di- and trimethylates 'Lys-9' of histone H3 (H3K9me2 and H3K9me3, respectively); involved in positively modulating the rate of age-related behavioral deterioration (PubMed:32103178). May repress the expression of mitochondrial function-related genes by occupying the... | Caenorhabditis elegans |
O17695 | HDA1_CAEEL | MNSNGPLMEHGKRRVAYYYDSNIGNYYYGQGHVMKPHRIRMTHHLVLNYGLYRNLEIFRPFPASFEDMTRFHSDEYMTFLKSANPDNLKSFNKQMLKFNVGEDCPLFDGLYEFCQLSSGGSLAAATKLNKQKVDIAINWMGGLHHAKKSEASGFCYTNDIVLGILELLKYHKRVLYVDIDVHHGDGVEEAFYTTDRVMTVSFHKYGDFFPGTGDLKDIGAGKGKLYSVNVPLRDGITDVSYQSIFKPIMTKVMERFDPCAVVLQCGADSLNGDRLGPFNLTLKGHGECARFFRSYNVPLMMVGGGGYTPRNVARCWTYET... | 3.5.1.98 | null | cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; determination of adult lifespan [GO:0008340]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; gonad development [GO:0008406]; hermaphrodite somatic sex determination [GO:0042001... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; germ cell nucleus [GO:0043073]; histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]; NuRD complex [GO:0016581] | histone deacetylase activity [GO:0004407]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Sumoylated. {ECO:0000305|PubMed:15990876}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32934238}. Cytoplasm. Chromosome {ECO:0000269|PubMed:32934238}. Note=Except in the germ line where it is also cytoplasmic. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; | null | null | null | null | FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression. Plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:25446273). Histone... | Caenorhabditis elegans |
O17736 | ETC1_CAEEL | MIKSLNERDNFLNRLREMEHKREKDEKQEKAARKVQKFWRGHRVQHNQRLLFRAEFDAVSDRQRGLEETIKMAQLLVNFYETNKDEERLVMTLSELVKLKTSDKEFEKRIRETQRLLLARCCIKFLKNATENTIFFHIFRYLEDYVTCHSKLFEASSKLGLFNAEFHLLEALIGKPTGKTVERASLNPRILQLLTRIFETFVNPSRSTSVSVNVANRLLKTICVNITDLNFSNYILYYIKDHIKPTSPNFTNLFEAMKSVDILNNWKVRPEIAETASLRLQSIFVSQIVHVSNTQSEDVKQYFNSLAVFLEHHSKIMRSL... | 2.3.2.26 | null | meiotic cell cycle [GO:0051321]; positive regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902104]; protein polyubiquitination [GO:0000209]; regulation of metaphase/anaphase transition of meiosis II [GO:1905189]; ubiquitin-dependent protein catabolic process [GO:0006511] | null | ubiquitin protein ligase activity [GO:0061630] | PF00632; | 3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000255, ECO:0000269|PubMed:23578927}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23578927}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from E2 ubiquitin-conjugating enzymes, such as ubc-18, in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ify-1 and cyb-1 targeting them for degradation in post-meiotic embryos. {ECO:0000269|PubMed:23578... | Caenorhabditis elegans |
O17754 | CBPE_CAEEL | MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLA... | 3.4.17.10 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | acetylcholine secretion, neurotransmission [GO:0014055]; cellular response to carbon dioxide [GO:0071244]; larval feeding behavior [GO:0030536]; negative regulation of nematode pharyngeal pumping [GO:1903745]; neuropeptide processing [GO:0061837]; peptide metabolic process [GO:0006518]; positive regulation of acetylcho... | axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; presynapse [GO:0098793] | carboxypeptidase activity [GO:0004180]; metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:12657671}. Perikaryon {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to axons in the nerve ring. {ECO:0000269|PubMed:12657671}. | CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; Evidence={ECO:0000303|PubMed:12657671, ECO:0000303|PubMed:17564681}; | null | null | null | null | FUNCTION: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage (PubMed:12657671, PubMed:17564681). By processing neuropeptides, modulates basal acetylcholine rel... | Caenorhabditis elegans |
O17798 | FKPC1_CAEEL | MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P09958}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958}; | dendrite morphogenesis [GO:0048813]; dendrite self-avoidance [GO:0070593]; gene expression [GO:0010467]; insulin processing [GO:0030070]; negative regulation of dauer entry [GO:1905910]; negative regulation of protein localization to cell surface [GO:2000009]; peptide hormone processing [GO:0016486]; positive regulatio... | axon [GO:0030424]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26974341}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23932402}. Cell projection, axon {ECO:0000269|PubMed:23932402}. Note=In most neurons, localizes exclusively within the cell bodies, but in ventral cord neurons, localizes ... | null | null | null | null | null | FUNCTION: Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif (PubMed:24671950). During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341, PubMed:28846083). Tog... | Caenorhabditis elegans |
O17850 | ATX3_CAEEL | MSKDDPINSIFFEHQEAALCAQHALNMLLQDALYKWQDLRDLAIQMDKMEQQILGNANPTPGRSENMNESGYFSIQVLEKALETFSLKLTNIENPAMVDYKNNPLTARAYICNLREHWFVLRKFGNQWFELNSVNRGPKLLSDTYVSMFLHQVSSEGYSIFVVQGVLPRSDADDLISLCPVVPPKVTPKKEQKLEKVMTKFFNTVGKRLGGGSGAPPDSQEEKDLAIAFAMSMETKDGSEVSRSSAEIDEENLRKAIELSQAPGPSEPAEIPLLTRSRSSTPPGASEPFSNAEQQRRDRQKFLERFEKKKEERNDEK | 3.4.19.12 | null | chemical synaptic transmission [GO:0007268]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; synapse [GO:0045202] | cysteine-type deubiquitinase activity [GO:0004843] | PF02099;PF02809; | 3.90.70.40;1.10.287.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus, nucleolus {ECO:0000269|PubMed:27669035}. Note=Localizes predominantly in the cytoplasm (PubMed:17234717). In the germline, following ionizing radiation... | 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:17234717, ECO:0000269|PubMed:21317884}; | null | null | null | null | FUNCTION: Acts as a chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway (PubMed:17234717, PubMed:19545544, PubMed:21317884). ... | Caenorhabditis elegans |
O17894 | HM35_CAEEL | MTDHPPIDTSSYFDCYQQHQLPLQYTFTSSSNSNTSNSSTSPSHISDQFSSSGGPPYELSSHILTPSSVIPTPSPSVASASISSPTIPAFGCTMSEYSMEQMEAISTSLFQARDGDRLVAFFKQLESLYGPNAVDHLRSEAIIVAYTYALYHSNEFETLFHLLSNRHFQQRHYNDLQDIWHHARYKESQLKRGKELNPVEKYRLRRKFPAPKTIWDGEEIVYSFKDSSRKFLKQFFRNVSEYPTQEQKREISRATGLKIVQISNWFKNRRQRDKSNNSAKCSPPSSSSSTNGGSDFLPIITPQSFNLAAAPFNMNMIYGT... | null | null | axon guidance [GO:0007411]; egg-laying behavior [GO:0018991]; locomotion [GO:0040011]; mesodermal cell migration [GO:0008078]; neuron migration [GO:0001764]; positive regulation of locomotion [GO:0040017]; regulation of cell migration [GO:0030334]; regulation of nematode male tail tip morphogenesis [GO:0110037]; regula... | 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] | PF00046;PF16878; | 1.10.10.60; | SIX/Sine oculis homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15282156}. | null | null | null | null | null | FUNCTION: Probable transcription factor required for differentiation and migration of neuronal cells, such as RID and CAN neurons (PubMed:15282156, PubMed:2361334). Specifically, plays a role in the terminal differentiation of RID peptidergic neurons (PubMed:27855782). Also required for CAN neuron axon guidance (PubMed... | Caenorhabditis elegans |
O17966 | TOP1_CAEEL | MSVVSNHHSNGNGNSTVYDTNGNDEIKKEVKDEPMASDSEVPFGELMKRDKKEKKQKKRKAESGSDEDDYKPEKRKSSAKNGKKKDVGSDSEDDYKPEKKKSKKNNKKKAQESSEDDDEESEGDVSEEDVKPQIHSDDELEEEDEAPTTDDEEEQKRKEKERRKKEKREKKERKEKKRLEKENRKIKEEDDEDSDDEDDEKAKKKKRKSKGAEKSKPSTSKKDAGGKKEPPKKKVKKEEDIEDIWEWWKEEKKPAGVKWNSLQHCGPLFAPPYIPLPSHVHFKYGGEKMKLTLETEEIAQFYAGVLDHEYSTKEAFNKNF... | 5.6.2.1 | null | chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; DNA topological change [GO:0006265] | chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle pole centrosome [GO:0031616] | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917] | PF14370;PF01028;PF02919; | 1.10.132.10;2.170.11.10;1.10.10.41; | Type IB topoisomerase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11387}. Nucleus, nucleolus {ECO:0000269|PubMed:16943775}. Chromosome {ECO:0000269|PubMed:16943775}. Note=Localizes around sperm chromatids. {ECO:0000269|PubMed:16943775}. | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... | Caenorhabditis elegans |
O17972 | NPHP1_CAEEL | MSIFGSILSLQDAINRFPQFEYQINRLEKEQKDTEAASRASFRKHFVRQCQELHRQLDDHRNRIEKAKTDETYKKENALEQLDKLKQRLTALSPEKEQLSFSVSVDSQSEEEKPKMAAIGRRKSTMYNDDESEDSDNDSEIIETDVQLDDPLPSQPQPPQQQHQQPQPKPRQPITITKPLESKTLNERQELDEVISRLQNPSRGDSGEVMEPVVVRGNVFVAIDSWDAEAEGDLELIKGKKYRITQTRSDGWWTALDEYGQRGLVPKTYLQHVKEKPKNVPSKVSSRLGVRDSVIGISTTTDPSRREANRQASRVDDCLG... | null | null | determination of adult lifespan [GO:0008340]; neuronal signal transduction [GO:0023041]; non-motile cilium assembly [GO:1905515]; protein localization [GO:0008104]; protein localization involved in establishment of planar polarity [GO:0090251]; response to hermaphrodite contact [GO:0034606]; turning behavior involved i... | ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytoplasm [GO:0005737]; non-motile cilium [GO:0097730] | null | PF00018; | 2.30.30.40; | Nephrocystin-1 family | null | null | null | null | null | null | null | FUNCTION: Plays a role in the extension of dendrites from phasmid ciliated sensory neurons (PubMed:34115759). May be necessary for initial assembly of the cilium. {ECO:0000269|PubMed:15659564, ECO:0000269|PubMed:34115759}. | Caenorhabditis elegans |
O18017 | BLM_CAEEL | MIKNREIEVAPPRRTIQFGGYTFVEPDLNFKAPIFSCCGSIRDPSCEEREEEYIDNGHDEEPPVEVNRIQESTSFDEPVSSPPRYRPSENPGPSSSSYEPGHYSFNEYQQFPSRPQKRLVDPPIVDLDEEPPIVDLDDSFDNFHVGSTSEEVVSGDIAPEEEEEEGHDSFDDFESVPAQPPSKNTLASLQKSDSEIALNQQRHDMHGRFRGFLQDDSEEFSDEVGLLGADMNKELYDTLKSKFGFNQFRHRQKQCILSTLMGHDTFVLMPTGAGKSLCYQLPAVILPGVTVVVSPLRSLIEDQKMKMKELGIGCEALTAD... | 5.6.2.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P54132}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P54132}; | chromosome organization [GO:0051276]; chromosome segregation [GO:0007059]; determination of adult lifespan [GO:0008340]; DNA damage checkpoint signaling [GO:0000077]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; replisome [GO:0030894] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; metal ion binding [GO:00... | PF00270;PF00271;PF00570;PF16124;PF09382; | 1.10.150.80;3.40.50.300;1.10.10.10; | Helicase family, RecQ subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}. Chromosome {ECO:0000269|PubMed:27011106}. Note=Localizes on chromosomes during pachytene in meiotic prophase I in oocytes. Co-localizes with rmh-1 at mid-pachytene and late-pachytene in meiotic prophase I (PubMed:27011106). Locali... | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:P54132}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:306... | null | null | null | null | FUNCTION: Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Stabilizes and positively regulates the localization of the BTR double Holliday Junction dissolution complex component rmh-1 at nuclea... | Caenorhabditis elegans |
O18158 | OGT1_CAEEL | MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAVNQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLPTLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSGGDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEK... | 2.4.1.255 | null | dauer larval development [GO:0040024]; energy reserve metabolic process [GO:0006112]; glycogen metabolic process [GO:0005977]; glycoprotein metabolic process [GO:0009100]; lipid storage [GO:0019915]; protein O-linked glycosylation [GO:0006493]; reproduction [GO:0000003]; response to temperature stimulus [GO:0009266] | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | protein O-acetylglucosaminyltransferase activity [GO:0097363]; protein serine/threonine phosphatase activity [GO:0004722] | PF13844;PF00515;PF13414;PF13431;PF13181; | 3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10; | Glycosyltransferase 41 family, O-GlcNAc transferase subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9083068}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.... | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. {ECO:0000250|UniProtKB:O15294}. | Caenorhabditis elegans |
O18178 | 2A51_CAEEL | MHGSGHSLTGAPHQIPPPRTQGAATGGQQLSATANQFVDKIDPFHNKRGTSRRLRINNSSRYNVDSAQELVQLALIKDTAANEQPALVIEKLVQCQHVFDFYDPVAQLKCKEIKRAALNELIDHITSTKGAIVETIYPAVIKMVAKNIFRVLPPSENCEFDPEEDEPTLEVSWPHLQLVYELFLRFLESPDFQASIGKKYIDQRFVLKLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKHINNMFLRFVYETDSFNGVGELLEILGSIINGFALPLKQEHKVFLVKVLLPLHKPKCLSLYHAQLAYCVVQFIEKD... | null | null | dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; negative regulation of insulin receptor signaling pathway [GO:0046627]; P granule assembly [GO:1903863]; regulation of lipid storage [GO:0010883]; response to heat [GO:0009408]; signal transduction [GO:0007165] | cytosol [GO:0005829]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159] | protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542] | PF01603; | 1.25.10.10; | Phosphatase 2A regulatory subunit B56 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249087}. | null | null | null | null | null | FUNCTION: Probable regulatory subunit of serine/threonine-protein phosphatase let-92 which negatively regulates the insulin receptor signaling cascade composed of daf-2, age-1, akt-1, akt-2 and sgk-1 by promoting the dephosphorylation of akt-1 on 'Thr-350' (PubMed:19249087). Negatively regulates several functions contr... | Caenorhabditis elegans |
O18191 | APC1_CAEEL | MRKYVLFFISGNNDSQIWATTPNTPRVIARGGLERNIHTRTLARMVNEDAPGTSTPAAQSRLQTTASPFHRTHLTQMCRRGDTNASLLRDFTRMIRDTPRNFSKNTQHGNDRDFGDLERDPDVDLLLSKVCLECVYVEPKEGAIPKANKIFISNFLSDMYINLVSVTGEVMKIIPIWKNAETTRKNLLEKGKHEPCVVDCVDAAFVMKSGITVVLGSDFTTAMFGGNERIAPIFIKEMSNQRVGRKFRLFSFAENRIFAVNEMRCIVVEIPETVTCKSATELMRTCFLHLDRDLSRKLLIKWRSVKRDVDTERLDLDRKE... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; asymmetric cell division [GO:0008356]; establishment of meiotic spindle localization [GO:0051295]; metaphase/anaphase transition of meiotic cell cycle [GO:0044785]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; neurotransmitter tra... | anaphase-promoting complex [GO:0005680] | molecular adaptor activity [GO:0060090] | null | 1.25.10.10; | APC1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:11861581). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (P... | Caenorhabditis elegans |
O18195 | WASH1_CAEEL | MYHVPLIPRDAGREETIFRINQSLQKLLRVSDEIFDRVEHRITRIHGKAEAIDRRTEVLEKKLESLQESDKVITFTLPRQLPKLPEEPPTSTSLFRINIDTEHFPGSEELPAFRRADDHVLRPCEPIDFTYELNKPDKFFLTSQVLKEYEQKGWERYKKRLLGGLRELSRSPEHIAELFYAGTSIPAFEGVSGDFSKKALDADDDGGTSRSGRTTDELAQLRLHEQLLEDTALSSTLMQEDSLDDNHPLAFRINFNEKKKKTAKMVEMPDSLPNLKGHAHDFTLRDPEIDEDRLLDILPADDQIPEASEPTEAEADAPTT... | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; cytoplasmic sequestering of protein [GO:0051220]; determination of adult lifespan [GO:0008340]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; regulation of gene expression [GO:0010468]; retrograde transport, endosome to Golgi [GO:0042147] | cytosol [GO:0005829]; early endosome [GO:0005769]; recycling endosome [GO:0055037]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015] | PF11945; | null | WASH1 family | null | null | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome ... | Caenorhabditis elegans |
O18209 | PMY13_CAEEL | MDDTEGNSSMDSIRNGQSSPLPQVTPRLPQIPMMMRETPLSTKRERQAITPRFRRPAPKMIKTMPPTRSIWSVRKESVPLLVTPQGPKPLESPKYDHTNAQSFFEQVFQIDEIIGRGSFGEVFAARCREDSQLYAVKVSLAPIRQHSISKYREAESHMIIPPHKNLVKFYRAWEETGRLYIQTELCDQSLLKYCTEKHALPEDEIWNIFVDLLQAVHHLHSNDMIHDDIKPENIFLTKDMICKLGDFGLVINLKNPNDVKSAEEGDSKYLAPEVLNGRPTKSSDIFSLGMTILEATTDLDVPSNGDSWHQIRNGQIPDRF... | 2.7.11.1 | null | embryo development ending in birth or egg hatching [GO:0009792]; meiotic cell cycle [GO:0051321]; meiotic nuclear membrane disassembly [GO:0051078]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]; n... | condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; extrinsic component of membrane [GO:0019898]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:00047... | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16466390}. | 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; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase during oocyte maturation (PubMed:16338136, PubMed:16421191, PubMed:16466390). Required for oocyte maturation, embryonic development, germline proliferation and initiation of meiosis during spermatogen... | Caenorhabditis elegans |
O18214 | MAB3_CAEEL | MLTEDPVSEICEAKAVDELAEQEKNYYCQRCLNHGELKPRKGHKPDCRYLKCPCRECTMVEQRRQLNNLLSKKKIHCTPATQTRDGKRVRDPHCARCSAHGVLVPLRGHKRTMCQFVTCECTLCTLVEHRRNLMAAQIKLRRSQQKSRDGKEPKRNSRRKSKDMDMEMMVVTATDGQKIIGTSASPSPSSTTDTMSPSLSMSPPCSPSPLLAQYTLTLAAPIPIYPPIPMNQQLISLQQQQFLMSIIQNMAPSIGQQAPLLPGISAGSVSSAAILNEFWSMYLKNYGLQA | null | null | cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of nematode male tail tip morphogenesis [GO:0110039]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of tr... | 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]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00751; | 4.10.1040.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. | null | null | null | null | null | FUNCTION: Transcription factor which binds the DNA motif 5'-[CGA][TCA][TA]ACAATGT[AT][TGA]C-3', probably as a monomer (PubMed:9490411). Acts partially redundantly with the transcription factor dmd-3 to coordinate tail tip cell fusion and retraction and thereby regulate male tail tip morphogenesis (PubMed:18550714, PubM... | Caenorhabditis elegans |
O18276 | GBRB_CAEEL | MRRSKTRRIFHVSITLLLVSTIFCQNGTKPHNNSTSDQMSSSWSNRSQTMYSNASSLLSDLLLDYDIRLRPGFGGDALLLTMDIIIASFDSISEVDMDYTLTMYLHQYWTDERLRWSNEIPIDEMTLSGEFSQNIWVPDTFLANDKHSYLHEVTERNKMLRINVDGKVAYGMRLTSTLSCSMNLRNFPLDSQNCTVEIESYGYTTSEVLMKWNYPLAVHGVEQADVPQFTITGFHTEDSIVSTATGSYQRLSLVFQLRRSVGYFIFQTYLPCVLIVMLSWVSFWINHEATSARVALGITTVLTMTTISTGVRQSLPRISY... | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; monoatomic ion transport [GO:0006811]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; 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: Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. {ECO:0000250, ECO:0000269|PubMed:12421359}. | Caenorhabditis elegans |
O18330 | MRJP1_APIME | MTRLFMLVCLGIVCQGTTGNILRGESLNKSLPILHEWKFFDYDFGSDERRQDAILSGEYDYKNNYPSDIDQWHDKIFVTMLRYNGVPSSLNVISKKVGDGGPLLQPYPDWSFAKYDDCSGIVSASKLAIDKCDRLWVLDSGLVNNTQPMCSPKLLTFDLTTSQLLKQVEIPHDVAVNATTGKGRLSSLAVQSLDCNTNSDTMVYIADEKGEGLIVYHNSDDSFHRLTSNTFDYDPKFTKMTIDGESYTAQDGISGMALSPMTNNLYYSPVASTSLYYVNTEQFRTSDYQQNDIHYEGVQNILDTQSSAKVVSKSGVLFFG... | null | null | caste determination, influence by environmental factors [GO:0048650]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | null | PF03022; | 2.120.10.30; | Major royal jelly protein family | PTM: Glycosylated. {ECO:0000269|PubMed:9395329}.; PTM: Jellein-2 is probably processed to yield jellein-1 and jellein-4. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15203237, ECO:0000269|PubMed:9395329}. Note=Royal jelly. {ECO:0000269|PubMed:9395329}. | null | null | null | null | null | FUNCTION: [Major royal jelly protein 1]: Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces development... | Apis mellifera (Honeybee) |
O18333 | RAB2_DROME | MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQEAFRSITRSYYRGAAGALLVYDITRRETFNHLTTWLEDARQHSNSNMVIMLIGNKSDLDSRREVKKEEGEAFAREHGLVFMETSARTAANVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGQQHSPTNPSLPGAGGAAGAANSGCC | 3.6.5.2 | null | autophagosome-lysosome fusion [GO:0061909]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; eye pigment granule organization [GO:0008057]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of glutamate receptor clustering [GO:0106104]; regulation of postsyn... | autolysosome membrane [GO:0120281]; autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum exit site [GO:0070971]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynapse of neuro... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Vesicle {ECO:0000269|PubMed:33822845}. Cytoplasmic vesicle {ECO:0000269|PubMed:33822845}. Cell projection, axon {ECO:0000269|PubMed:33822845}. Presynapse {ECO:0000269|PubMed:33822845}. Presynaptic active zone {ECO:0000269|PubMed:33822845}. Golgi apparatus {ECO:0000269|PubMed:33822845}. Golgi appar... | CATALYTIC ACTIVITY: [Ras-related protein Rab-2]: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P53994}; | null | null | null | null | FUNCTION: May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking (PubMed:33822845). Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex (PubMed:28063257, PubMed:28483915, PubMed:31194677, Pub... | Drosophila melanogaster (Fruit fly) |
O18334 | RAB6_DROME | MSSGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNTNSFHQTSKWIDDVRTERGSDVIIMLVGNKTDLSDKRQVSTEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMDSTENKPSEDMQEVVLKDSPNETKDPEGGCAC | null | null | axon guidance [GO:0007411]; compound eye morphogenesis [GO:0001745]; defense response to fungus [GO:0050832]; exocytosis [GO:0006887]; germarium-derived egg chamber formation [GO:0007293]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; oocyte microtubule cytoskeleton ... | autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; synapse [GO:0045202] | actin binding [GO:0003779]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Synapse {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Perikaryon {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Protein transport (PubMed:17329360, PubMed:17827179, PubMed:18833296, PubMed:21835342, PubMed:22928698, PubMed:33704067, PubMed:9685396). Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (PubMed:21795785). Mediates membrane trafficking during egg chamber growth and... | Drosophila melanogaster (Fruit fly) |
O18381 | PAX6_DROME | MRNLPCLGTAGGSGLGGIAGKPSPTMEAVEASTASHRHSTSSYFATTYYHLTDDECHSGVNQLGGVFVGGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATAEVVSKISQYKRECPSIFAWEIRDRLLQENVCTNDNIPSVSSINRVLRNLAAQKEQQSTGSGSSSTSAGNSISAKVSVSIGGNVSNVASGSRGTLSSSTDLMQTATPLNSSESGGASNSGEGSEQEAIYEKLRLLNTQHAAGPGPLEPARAAPLVGQSPNHLGTRSSHPQLVHGNHQALQQHQQQSWP... | null | null | adult walking behavior [GO:0007628]; brain development [GO:0007420]; brain morphogenesis [GO:0048854]; central complex development [GO:0048036]; compound eye development [GO:0048749]; compound eye morphogenesis [GO:0001745]; eye-antennal disc morphogenesis [GO:0007455]; glial cell migration [GO:0008347]; glucose homeos... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046;PF00292; | 1.10.10.60;1.10.10.10; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00381, ECO:0000269|PubMed:7914031}. | null | null | null | null | null | FUNCTION: Involved in eye morphogenesis. {ECO:0000269|PubMed:7914031}. | Drosophila melanogaster (Fruit fly) |
O18388 | IMB_DROME | MTSDIAMQLIAILEKTVSPDKNELLSAKNFLEQAAASNLPEFLKALSEILVNTANSAVARMAAGLQLKNHLTSKDEKVSQQYQDRWHQFPSEIRELIKNNILAALGTENTRPSCAAQCVAYVAVIELPINRWPMLIQTLVNKVVSEGSSEMHRESALEAIGYICQDIRFGVMENQSNDVLTAIIHGMRKVEPSNHVRLAATTALHNSLEFTKSNFEKDMERNFIMEVVCEATQCQDSQICVAALQCLVKIMTLYYQYMEPYMAQALFPITLAAMKSDNDAVALQGIEFWSNVCDEEIDLAIESQEATDQGRAPQRVSKHY... | null | null | chorion-containing eggshell formation [GO:0007304]; mitotic cell cycle [GO:0000278]; NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; regulation of nucleocytoplasmic transport [GO:0046822] | cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P granule [GO:0043186] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]; small GTPase binding [GO:0031267] | PF13513;PF03810; | 1.25.10.10; | Importin beta family, Importin beta-1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11102382}. Note=In cleavage embryos. | null | null | null | null | null | FUNCTION: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins (PubMed:11102382). In Drosophila, may not function as a snRNP import receptor as it does not interact with components of the snRNP complex such as snRNP U1, U2, U4/U6 and Snup (PubMed:23885126). {ECO:0000269|... | Drosophila melanogaster (Fruit fly) |
O18404 | HCD2_DROME | MIKNAVSLVTGGASGLGRATAERLAKQGASVILADLPSSKGNEVAKELGDKVVFVPVDVTSEKDVSAALQTAKDKFGRLDLTVNCAGTATAVKTFNFNKNVAHRLEDFQRVININTVGTFNVIRLSAGLMGANEPNQDGQRGVIVNTASVAAFDGQIGQAAYSASKAAVVGMTLPIARDLSTQGIRICTIAPGLFNTPMLAALPEKVRTFLAKSIPFPQRLGEPSEYAHLVQAIYENPLLNGEVIRIDGALRMMP | 1.1.1.-; 1.1.1.35; 1.1.1.51; 1.1.1.53; 1.1.1.62 | null | acyl-CoA metabolic process [GO:0006637]; androgen metabolic process [GO:0008209]; ecdysone metabolic process [GO:0008205]; estrogen metabolic process [GO:0008210]; fatty acid metabolic process [GO:0006631]; mitochondrial tRNA processing [GO:0090646]; steroid catabolic process [GO:0006706]; steroid metabolic process [GO... | cytosol [GO:0005829]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739] | 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; acetoacetyl-CoA reductase activity [GO:0018454]; dihydrotestosterone 17-beta-dehydrogenase activity [GO:0035410]; estradiol 17-beta... | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27131785, ECO:0000269|PubMed:34199774}. Note=Localizes to the lipid droplet fraction in early embryos (PubMed:16979555). {ECO:0000269|PubMed:16979555}. | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=101 uM for (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:000... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.3 for the dehydrogenase reaction, and 6.4 for the reductase reaction. {ECO:0000269|PubMed:12917011}; | null | FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, and steroid metabolism (PubMed:12917011). Versatile enzyme presenting two types of activity; L-3-hydroxyacyl-CoA dehydrogenase ((3S)-3-hydroxyacyl-CoA dehydrogenase) activity and hydroxysteroid dehydrogenase (HSD) activity with a wide substrate s... | Drosophila melanogaster (Fruit fly) |
O18412 | FZO_DROME | MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRY... | 3.6.5.- | null | mitochondrial fusion [GO:0008053]; mitochondrion localization [GO:0051646]; Nebenkern assembly [GO:0007287]; positive regulation of mitochondrial fusion [GO:0010636]; sperm mitochondrion organization [GO:0030382]; spermatogenesis [GO:0007283] | membrane [GO:0016020]; mitochondrial envelope [GO:0005740]; mitochondrial outer membrane [GO:0005741] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00350;PF04799; | 1.20.5.110;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:9230308}; Multi-pass membrane protein {ECO:0000269|PubMed:9230308}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q8IWA4}; | null | null | null | null | FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis (PubMed:18799731, PubMed:9230308). In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusio... | Drosophila melanogaster (Fruit fly) |
O18413 | PRS8_DROME | MTVTNRMEIESAYHKGEGFRSYYIQKIEELQLVVAEKHQNLRRLQAQRNELNAKVRMLREELQLLQEQGSYVGEVVKPMDKKKVLVKVHPEGKFVVDLDKNIDINDVTPNCRVALRNESYTLHKILPNKVDPLVSLMMVEKVPDSTYEMVGGLDKQIKEIKEVIELPVKHPELFDALGIAQPKGVLLYGPPGTGKTLLARAVAHHTECTFIRVSGSELVQKFIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRIESGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPN... | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome regulatory particle [GO:0005838]; proteasome regulatory particle, base subcomplex [GO:0008540] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proteasome-activating activity [GO:0036402] | PF00004;PF17862;PF16450; | 1.10.8.60;2.40.50.140;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
O18423 | TXL_EISFE | MSAKAAEGYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQVSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIVGRQIILGKTEIRIKHAERKEYMTVVSRKSWPAATLGHSKLFKFVLYEDWGGFRIKTLNTMYSGYEYAYSSDQGGIYFDQGTDNPKQRWAINKSLPLRHGDVVTFMNKYFTRSGLCYDDGPATNVYCLDKREDKWILEVVG | null | null | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; monoatomic ion transport [GO:0006811] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | null | 2.60.120.980;2.80.10.50; | Lysenin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9210594}. Target cell membrane {ECO:0000269|PubMed:9210594}. Note=Forms a beta-barrel pore in the membrane. {ECO:0000269|PubMed:27048994, ECO:0000269|PubMed:27176125}. | null | null | null | null | null | FUNCTION: Pore-forming toxin that defensively acts against parasitic microorganisms by forming pores in sphingomyelin-containing membranes (PubMed:12676961, PubMed:9478988). Has hemolytic activity and is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larv... | Eisenia fetida (Red wiggler worm) |
O18475 | DPOLQ_DROME | MAFSQSFNFGNSTLMALEKGMQADDKENAQPGNGNIQVQSAGNEVNSEIQEINSEFFRDEFSYEVNQAHKPAEQSVVNVSQVQQHMAVVSNQDSEDQSRSSALNDQICTQSSFEGEDAGADAVLDQPNLDENSFLCPAQDEEASEQLKEDILHSHSVLAKQEFYQEISQVTQNLSSMSPNQLRVSPNSSRIREAMPERPAMPLDLNTLRSISAWNLPMSIQAEYKKKGVVDMFDWQVECLSKPRLLFEHCNLVYSAPTSAGKTLVSEILMLKTVLERGKKVLLILPFISVVREKMFYMQDLLTPAGYRVEGFYGGYTPPG... | 2.7.7.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10343651}; | DNA biosynthetic process [GO:0071897]; DNA synthesis involved in DNA repair [GO:0000731]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; nucleotide-excision repair involved in interstrand cross-link repair [GO:1901255]; replication fork processing [GO:0031297] | nucleus [GO:0005634] | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; hydrolase activity [GO:0016787]; single-stranded DNA helicase activity [GO:0017116] | PF00270;PF00476;PF00271;PF20470;PF21099; | 1.10.3380.20;3.30.70.370;1.10.150.20;3.40.50.300;3.30.420.10; | DNA polymerase type-A family | PTM: In adult males, cleaved to produce a 100 kDa form. {ECO:0000269|PubMed:15961355}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15961355}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:10343651, ECO:0000269|PubMed:15961355, ECO:0000269... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10343651}; | null | FUNCTION: Multifunctional protein with both DNA polymerase and ATPase activities (PubMed:10343651, PubMed:15961355). Might have 3' to 5' exonuclease activity (PubMed:10343651). Plays a role in different DNA repair pathways such as DNA strand cross-link repair and microhomology-mediated end-joining (MMEJ), an alternativ... | Drosophila melanogaster (Fruit fly) |
O18497 | MAN2_SPOFR | MRTRVLRCRPFSTRILLLLLFVLAFGVYCYFYNASPQNYNKPRISYPASMEHFKSSLTHTVKSRDEPTPDQCPALKESEADIDTVAIYPTFDFQPSWLRTKEFWDKSFEDRYERIHNDTTRPRLKVIVVPHSHNDPGWLKTFEQYFEWKTKNIINNIVNKLHQYPNMTFIWTEISFLNAWWERSHPVKQKALKKLIKEGRLEITTGGWVMPDEACTHIYALIDQFIEGHHWVKTNLGVIPKTGWSIDPFGHGATVPYLLDQSGLEGTIIQRIHYAWKQWLAERQIEEFYWLASWATTKPSMIVHNQPFDIYSIKSTCGPH... | 3.2.1.114 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|RuleBase:RU361199}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU361199}; | mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139] | carbohydrate binding [GO:0030246]; mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity [GO:0004572]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074; | 3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | PTM: N-glycosylated. {ECO:0000269|PubMed:9061370}. | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9061370}; Single-pass type II membrane protein {ECO:0000269|PubMed:9061370}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q24451}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-bet... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P28494}. | null | null | FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. {ECO:0000250|UniProtKB:P28494}. | Spodoptera frugiperda (Fall armyworm) |
O18498 | MA1A1_SPOFR | MTGILPTYQRFVNGVPVPSISRRSFRLREKYLIVSVLLTFGIVWLGALFYLPEFKSSNSVNDSVYNVYKRIQKAGPELLMPPPLAQNDVGDFPVIGIAHHGEGGDDPHVIEDRNRLRAKIEEDMGMKVLERPQFDVAPSVSSSRGPSKPPVDAIEEPAVGNNAANKDVSPSGPKAESSDKFVAVALAPGADPEIKHKLETVKKMMLHAWYNYKLYAWGKNELKPMSKRAHLSSVFGAGELGATIVDGLDTLYLMGLNDEFREGRDWVAEHLHINEIDSDLSVFETTIRFVGGLLSCYALTGDTMFRDKAAEVGDALLPAF... | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q2ULB2}; | carbohydrate metabolic process [GO:0005975]; N-glycan processing [GO:0006491]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | PTM: N-glycosylated (PubMed:10764822, PubMed:11222938). Contains high mannose-type oligosaccharides (PubMed:11222938). {ECO:0000269|PubMed:10764822, ECO:0000269|PubMed:11222938}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:11222938}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8H116}. Note=Localizes in cytoplasmic punctate structures representing Golgi elements. {ECO:0000269|PubMed:11222938}. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Converts Man(9)GlcNAc(2) to Man(5)GlcNAc(2) primarily through the Man(7)GlcNAc(2) isomer C processing intermediate. {ECO:0000269|PubMed:10764822}. | Spodoptera frugiperda (Fall armyworm) |
O18640 | GBLP_DROME | MSETLQLRGTLIGHNGWVTQIATNPKDPDTIISASRDKTLIVWKLTRDEDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWDLAAGKTTRRFEGHTKDVLSVAFSADNRQIVSGSRDKTIKLWNTLAECKFTIQEDGHTDWVSCVRFSPNHSNPIIVSCGWDRTVKVWNLANCKLKNNHHGHNGYLNTVTVSPDGSLCTSGGKDSKALLWDLNDGKNLYTLEHNDIINALCFSPNRYWLCVAYGPSIKIWDLACKKTVEELRPEVVSPTSKADQPQCLSLAWSTDGQTLFAGYSDNTIRVWQVSVSAH | null | null | cellular response to starvation [GO:0009267]; cuticle development [GO:0042335]; cytoplasmic translation [GO:0002181]; egg-laying behavior [GO:0018991]; IRES-dependent viral translational initiation [GO:0075522]; locomotory behavior [GO:0007626]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of prot... | autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | protein kinase C binding [GO:0005080]; protein-macromolecule adaptor activity [GO:0030674]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735]; translation regulator activity [GO:0045182] | PF00400; | 2.130.10.10; | WD repeat G protein beta family, Ribosomal protein RACK1 subfamily | null | null | null | null | null | null | null | FUNCTION: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
O18696 | PDE1_CAEEL | MNRARKTSSCGCFRSAFCLLKPSTSSASEEHGDSDKKLLSVQLITPRDEEEQTSSRSIKIPPLDLNGLDCKKNAVAARRAGRRRTSEGGGVRGKGHFAEVVLDGLQRPVSLLRNQKEKSNSDDNCQEKEPTSPSSSRKKSYDNAPALESLEKLRYILHQLNSGQLPLEDLKRNIEYAALVLETAYMDETRRICDEDDDLAEVTPETVPDEVREWLAATFTRQNAGKKRDKPKFKSVANAIRTGIFFEKLFRKQQVVQCPIPPEIAELMKEVCTWSFSPFQLNEVSEGHALKYVGFELFNRYGFMDRFKVPLTALENYLSA... | 3.1.4.17 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250}; | cAMP-mediated signaling [GO:0019933]; chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; determination of adult lifespan [GO:0008340]; microvillus organization [GO:0032528]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of protein kinase C signaling [GO:0090038]; phototransd... | neuronal cell body [GO:0043025] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; calmodulin binding [GO:0005516]; calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity [GO:0048101]; calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase a... | PF00233;PF08499; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | null | CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; | null | null | null | null | FUNCTION: Redundantly with pde-5, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cGMP levels. {ECO:0000269|PubMed:27062922}. | Caenorhabditis elegans |
O18733 | MMP9_CANLF | MSPRQPLVLVFLVLGCCSAAPRPHKPTVVVFPGDLRTNLTDKQLAEEYLFRYGYTQVAELSNDKQSLSRGLRLLQRRLALPETGELDKTTLEAMRAPRCGVPDLGKFQTFEGDLKWHHNDITYWIQNYSEDLPRDVIDDAFARAFAVWSAVTPLTFTRVYGPEADIIIQFGVREHGDGYPFDGKNGLLAHAFPPGPGIQGDAHFDDEELWTLGKGVVVPTHFGNADGAPCHFPFTFEGRSYSACTTDGRSDDTPWCSTTADYDTDRRFGFCPSEKLYAQDGNGDGKPCVFPFTFEGRSYSTCTTDGRSDGYRWCSTTADY... | 3.4.24.35 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P14780}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14780}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; response to stimulus [GO:0050896] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270] | PF00040;PF00045;PF00413;PF04886; | 3.40.390.10;2.10.10.10;2.110.10.10; | Peptidase M10A family | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P14780}. | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780}; | null | null | null | null | FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjur... | Canis lupus familiaris (Dog) (Canis familiaris) |
O18734 | PP14A_PIG | MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELESEEERSRKIQGLLKSCTNPTENFVQELLVKLRGLHKQPGLRQPSPSGDGSLSPRQDRARTAPP | null | null | regulation of phosphorylation [GO:0042325] | cytoplasm [GO:0005737] | protein serine/threonine phosphatase inhibitor activity [GO:0004865] | PF05361; | 1.10.150.220; | PP1 inhibitor family | PTM: Phosphorylation of Thr-38 induces a conformation change. {ECO:0000269|PubMed:10869555, ECO:0000269|PubMed:10924361, ECO:0000269|PubMed:8720121}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11517233}. | null | null | null | null | null | FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000269|PubMed:10869555, ECO:0000269|PubMed:10924361, ECO:0000269|PubMed:8720121, ECO:0000269|P... | Sus scrofa (Pig) |
O18735 | ERBB2_CANLF | MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQLCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQ... | 2.7.10.1 | null | cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; ERBB signaling pathway [GO:0038127]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; neurogenesis [GO:0022008]; neuron differentiation [GO:... | basal plasma membrane [GO:0009925]; early endosome [GO:0005769]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587] | ATP binding [GO:0005524]; RNA polymerase I core binding [GO:0001042]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00757;PF14843;PF07714;PF01030;PF21314; | 1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1252. Dephosphorylated by PTPN12. {ECO:0000250... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cyto... | 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=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowt... | Canis lupus familiaris (Dog) (Canis familiaris) |
O18738 | DAG1_BOVIN | MRMSVGSAVPLPLWGRTFLLLLSVAVTQSHWPSEPSEAVRDWENQLEASMHSALSDLHETVPTVVGIPDGTAVVGRSFRVTIPTDLIASNGEVIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHSEPQSLRAASPDPGEVVSLVCAADEPVTVLTVILDADLTKMTPKQRIDLLRRMRGFSEVEPHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCCLNQNSVPDIRGVEVPAREGAMSAQLGYPVVGWHIANKKPSLPKRIRRQIHATPTP... | null | null | axon guidance [GO:0007411]; morphogenesis of an epithelium [GO:0002009]; muscle attachment [GO:0016203]; nerve development [GO:0021675] | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystroglycan complex [GO:0016011]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:004... | calcium ion binding [GO:0005509]; laminin binding [GO:0043236] | PF18424;PF05454;PF05345; | 3.30.70.1040;2.60.40.10; | null | PTM: [Alpha-dystroglycan]: O-glycosylated (PubMed:16709410, PubMed:8999917). POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. Heavily O-glycosylated comp... | SUBCELLULAR LOCATION: [Alpha-dystroglycan]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0... | null | null | null | null | null | FUNCTION: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. {ECO:0000250}.; FUNCTION: [Alpha-dystroglycan]: Extracellular periph... | Bos taurus (Bovine) |
O18756 | GLCE_BOVIN | MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQVPRHLSSGFRVDALEKKAAASESNNYVNHMAKQSEEAFPQEQQKAPPVVGGFNNNGGGRVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNSKPNDWTVPKGCFMASVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFT... | 5.1.3.17 | null | heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | calcium ion binding [GO:0005509]; heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; protein homodimerization activity [GO:0042803]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857] | PF06662;PF21174; | null | D-glucuronyl C5-epimerase family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}. | CATALYTIC ACTIVITY: Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n); Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557, ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17; Evidence={ECO:0000269|PubMed:10727403}; | null | PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:10727403}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305|PubMed:10727403}. | null | null | FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269... | Bos taurus (Bovine) |
O18757 | SCMC1_RABIT | MLRWLRGFVLPTAACQGAEPPTRYETLFQALDRNGDGVVDIRELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVADIEEIIRFWKHSTGIDIGDSLTIPDEFTEEERKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMIKEGGVRSLWRGNGTNVIKIAPETAVKFWVYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTG... | null | null | adenine nucleotide transport [GO:0051503]; cellular response to calcium ion [GO:0071277]; mitochondrial ATP transmembrane transport [GO:1990544] | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778] | adenine nucleotide transmembrane transporter activity [GO:0000295]; ADP:inorganic phosphate antiporter activity [GO:0140988]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509] | PF13499;PF00153; | 1.10.238.10;1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:9238007}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:9238007}; Multi-pass membrane protein {ECO:0000255}. Note=The physiological relevance of the localization to the peroxisome is unclear. {ECO:0000269|PubMed:... | CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) + ph... | null | null | null | null | FUNCTION: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleo... | Oryctolagus cuniculus (Rabbit) |
O18766 | OPSD_PIG | MNGTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAYMFMLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGLALTWVMALACAAPPLVGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFSIPLVIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVVAFLICWLPYASVAFYIFTHQGSDFGPIFMTIPAFFAKSASIYNPVIYIMMNKQFRNCMLTT... | null | null | absorption of visible light [GO:0016038]; adaptation of rhodopsin mediated signaling [GO:0016062]; cellular response to light stimulus [GO:0071482]; detection of temperature stimulus involved in thermoception [GO:0050960]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; microtub... | cell-cell junction [GO:0005911]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment membrane [GO:0060342]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]; rod photoreceptor ... | 11-cis retinal binding [GO:0005502]; G protein-coupled photoreceptor activity [GO:0008020]; metal ion binding [GO:0046872] | PF00001;PF10413; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff... | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P02699}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membran... | null | null | null | null | null | FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (PubMed:9335046). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylati... | Sus scrofa (Pig) |
O18778 | PAHX_BOVIN | MDRNRASARLTVLLRHLGCRSAGTIIAHHTSGVGSLASFHPQQFQYTRENNVLSLEQRKFYEENGFLVIKNLVSDADIQRFRNEFERICRKEVKPLGLSVMRDVTITKSEYVPSEKVVSKVQDFQEDEELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSNSIVCAWTAMEHIDRNNGCLVVLPGTHKGPLQPHDYPQWEGGVNIMFHGIQDYDKNNARVHLVMEKGDTVFFHPLLIHGSGRNKSQGFRKAISCHFADANCHYIDVEGTSQENIEKEVVDIVRKKYGFKDVTLK... | 1.14.11.18 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evid... | 2-oxoglutarate metabolic process [GO:0006103]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089] | 9+0 non-motile cilium [GO:0097731]; peroxisome [GO:0005777] | ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; phytanoyl-CoA dioxygenase activity [GO:0048244] | PF05721; | 2.60.120.620; | PhyH family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O14832}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirect... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono- branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon a... | Bos taurus (Bovine) |
O18793 | CCR2_MACMU | MLSTSRSRFIRNTNGSGEEVTTFFDYDYGAPCHKFDVKQIGAQLLPPLYSLVFIFGFVGNMLVVLILINCKKLKSLTDIYLLNLAISDLLFLITLPLWAHSAANEWVFGNAMCKLFTGLYHIGYLGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWLVAVFASVPGIIFTKCQEEDSVYICGPYFPRGWNNFHTIMRNILGLVLPLLIMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWTPYNIVILLNTFQEFFGLSNCESTRQLDQATQVTETLGMTHCCINPIIYAFVGEKFRRYLSMFF... | null | null | blood vessel remodeling [GO:0001974]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; inflammatory response to wounding [GO:0090594]; macrophage migration [GO:1905517]; monocyte extravasation [GO:0035696]; positive regulation of cy... | cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41597}.; PTM: Sulfation increases the affinity for both monomeric and dimeric CCL2 with stronger binding to the monomeric form (By similarity). Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer to monomer (By similarity). {ECO:0000250|UniProtKB:P41597}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41597}; Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant receptors are distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:00... | null | null | null | null | null | FUNCTION: Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a rec... | Macaca mulatta (Rhesus macaque) |
O18796 | IL6RA_PIG | MLAVGCALLTALLAAPGMALAPRGCSKLEVAQDVLTSLPGASVTLTCPGGEPGDNATIHWVLRNQVTGSPDGRPAGVGRRLLLKSVQLSDSGNYSCYQDGVPAGSVRLLVDAPPEEPQLSCFRKSPLSNVGCEWRPRSPPSPTTKAVLLVRKFQNSPVEDFQEPCQYSLEAQRFFCQLAVPEGDNSFHIVTLCVANSAGSQSSTPQTFEGYGILQPDPPVNITVSAVDRNPRWLSVTWQDPPSWNSYFYRLQFELRYRAERSKTFTTWMVKELQHHCIIHDAWSGMRHVVQLRAQEEFGHGLWSEWSQEVTGIPWTESRS... | null | null | ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; interleukin-6-mediated signaling pathway [GO:0070102]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; T-helper 17 cell lineage commitment [GO:0072540]; v... | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; interleukin-6 receptor complex [GO:0005896]; receptor complex [GO:0043235] | interleukin-11 binding [GO:0019970]; interleukin-11 receptor activity [GO:0004921]; interleukin-6 binding [GO:0019981]; interleukin-6 receptor activity [GO:0004915] | PF00047;PF09240; | 2.60.40.10; | Type I cytokine receptor family, Type 3 subfamily | PTM: A short soluble form is also released from the membrane by proteolysis. The sIL6R is formed by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding. mIL6R is cleaved by the proteases ADAM10 and ADAM17. {ECO:0000250|UniProtKB:P22272}.; PTM: Glycosylated. Glycosylation is dis... | SUBCELLULAR LOCATION: [Interleukin-6 receptor subunit alpha]: Cell membrane {ECO:0000250|UniProtKB:P22272}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted {ECO:0000250|UniProtKB:P22272}. | null | null | null | null | null | FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6... | Sus scrofa (Pig) |
O18805 | DAXX_CHLAE | MATANSIIVLDDDDENEAAAQPGPSHPLPSTASPEAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFQEFLELCKTQTADHPEVVPFLCNRQQRAHSLFLASAEFCNILSRVLSRAQSRPFKLYVYINELCTVLKGHSAKKKLNLAPVATTSNEPSGNNPPTHLSLDPTNAENTASQAPRTRGSRRQIQRLEQLLALYVAEIRRLQERELDLSELDDPDSTYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIKQRIPYRGTRYPKVNRRIERLINKPGPDTFPDYGDVLRAVKKAAARHSLGLPRQQLQLMAQDAFRNV... | null | null | apoptotic process [GO:0006915]; cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to diamide [GO:0072738]; cellular response to heat [GO:0034605]; cellular response to sodium arsenite [GO:1903936]; cellular response to unfolded protein [GO:0034620]; negative ... | chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605] | histone binding [GO:0042393]; nuclear androgen receptor binding [GO:0050681]; protein homodimerization activity [GO:0042803]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714] | PF03344;PF20920; | 1.20.58.2170;1.10.8.810; | DAXX family | PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the nucleoplasm, in P... | null | null | null | null | null | FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies th... | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) |
O18823 | AOAH_RABIT | MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYL... | 3.1.1.77 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29343645}; Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role. {ECO:0000269|PubMed:29343645}; | fatty acid metabolic process [GO:0006631]; lipopolysaccharide catabolic process [GO:0009104]; negative regulation of inflammatory response [GO:0050728] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576] | acyloxyacyl hydrolase activity [GO:0050528]; calcium ion binding [GO:0005509] | PF00657;PF20825; | 1.10.225.10;3.40.50.1110; | null | PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28039}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}. | CATALYTIC ACTIVITY: Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675; EC=3.1.1.77; Evidence={ECO:0000250|UniProtKB:P280... | null | null | null | null | FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important fo... | Oryctolagus cuniculus (Rabbit) |
O18836 | GDF8_BOVIN | MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQK... | null | null | myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of fibroblast proliferation [GO:0048147]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759] | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}. | null | null | null | null | null | FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}. | Bos taurus (Bovine) |
O18839 | KCNJ2_PIG | MGSVRTNRYSIVSSEEDGMKLATLAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEI... | null | null | cardiac muscle cell action potential involved in contraction [GO:0086002]; magnesium ion transport [GO:0015693]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; protein homotetramerization [GO:0051289]; regulation of heart rate by cardiac conduction [GO:0086091]; regulati... | membrane [GO:0016020]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization [GO:0086008] | PF01007;PF17655;PF08466; | 1.10.287.70;2.60.40.1400; | Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ2 subfamily | PTM: S-nitrosylation increases the open probability and inward rectifying currents. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor {ECO:0000250|UniProtKB:P63252}. | null | null | null | null | null | FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentratio... | Sus scrofa (Pig) |
O18840 | ACTB_CANLF | MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL... | 3.6.4.- | null | axonogenesis [GO:0007409]; cell motility [GO:0048870] | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dense body [GO:0097433]; focal adhesion [GO:0005925]; membrane [GO:0016020]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protei... | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; protein kinase binding [GO:0019901]; structural constituent of postsynaptic actin cytoskeleton [GO:0098973] | PF00022; | 3.30.420.40; | Actin family | PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP. {ECO:0000250|UniProtKB:P60709}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P60709}.; PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filame... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the... | Canis lupus familiaris (Dog) (Canis familiaris) |
O18866 | KCMA1_PIG | MSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGASQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLL... | null | null | positive regulation of membrane hyperpolarization [GO:1902632]; potassium ion transmembrane transport [GO:0071805]; regulation of membrane potential [GO:0042391]; relaxation of vascular associated smooth muscle [GO:0060087]; vasodilation [GO:0042311] | monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211] | large conductance calcium-activated potassium channel activity [GO:0060072]; metal ion binding [GO:0046872] | PF03493;PF00520;PF21014; | 1.10.287.70;3.40.50.720; | Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily | PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity (By similarity). {ECO:0000250|UniProtKB:Q12791, ECO:0000305}.; PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q12791}; | null | null | null | null | FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membr... | Sus scrofa (Pig) |
O18867 | KCMA1_MACMU | MSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLM... | null | null | potassium ion transmembrane transport [GO:0071805]; regulation of membrane potential [GO:0042391]; vasodilation [GO:0042311] | monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211] | large conductance calcium-activated potassium channel activity [GO:0060072]; metal ion binding [GO:0046872] | PF03493;PF00520;PF21014; | 1.10.287.70;3.40.50.720; | Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily | PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity (By similarity). {ECO:0000250|UniProtKB:Q12791, ECO:0000305}.; PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q12791}; | null | null | null | null | FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membr... | Macaca mulatta (Rhesus macaque) |
O18868 | KCNB1_PIG | MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQTTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSL... | null | null | action potential [GO:0001508]; cellular response to glucose stimulus [GO:0071333]; cellular response to nutrient levels [GO:0031669]; glucose homeostasis [GO:0042593]; glutamate receptor signaling pathway [GO:0007215]; negative regulation of insulin secretion [GO:0046676]; positive regulation of calcium ion-dependent e... | axon [GO:0030424]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; lateral plasma membrane [GO:0016328]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]; voltage-gated potassium channel complex [GO:000807... | delayed rectifier potassium channel activity [GO:0005251]; protein heterodimerization activity [GO:0046982] | PF02214;PF00520;PF03521; | 1.10.287.70;1.20.120.350; | Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.1/KCNB1 sub-subfamily | PTM: Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphoryla... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15387}. Perikaryon {ECO:0000250|UniProtKB:P15387}. Cell projection, axon {ECO:0000250|UniProtKB:P15387}. Cell projection, dendrite {ECO:0000250|UniProtKB:P15387}. Membrane; Multi-pass membrane protein. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P15387}.... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of more than 20 msec. After that, inac... | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neuro... | Sus scrofa (Pig) |
O18896 | SOX9_PIG | MNLLDPFMKMTDEQEKGLSGAPSPTMSEGSRGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQPGKADLKREGRPLPEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYG... | null | null | cAMP-mediated signaling [GO:0019933]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate specification [GO:0001708]; cellular response to BMP stimulus [GO:0071773]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to heparin [GO:0071504]; cellular res... | nucleus [GO:0005634]; protein-containing complex [GO:0032991] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polyme... | PF00505;PF12444; | 1.10.30.10; | null | PTM: Acetylated; acetylation impairs nuclear localization and ability to transactivate expression of target genes. Deacetylated by SIRT1. {ECO:0000250|UniProtKB:Q04887}.; PTM: Phosphorylation at Ser-64 and Ser-211 by PKA increases transcriptional activity and may help delay chondrocyte maturation downstream of PTHLH/PT... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04887, ECO:0000255|PROSITE-ProRule:PRU00267}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL... | Sus scrofa (Pig) |
O18910 | OPSG_RABIT | MTQPWGPQMLAGGQPPESHEDSTQASIFTYTNSNSTRGPFEGPNFHIAPRWVYHLTSAWMILVVIASVFTNGLVLVATMRFKKLRHPLNWILVNLAVADLAETVIASTISVVNQFYGYFVLGHPLCVVEGYTVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLAIAGIAFSWIWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIIPLSVIVLCYLQVWMAIRTVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYSFHPLVAAIPSYFAKSATIYNPI... | null | null | cellular response to light stimulus [GO:0071482]; phototransduction [GO:0007602]; visual perception [GO:0007601] | photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: O-glycosylated. {ECO:0000250|UniProtKB:O35599}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light. | Oryctolagus cuniculus (Rabbit) |
O18924 | PPARG_MACMU | MGETLGDSPIDPESDSFTDTLSANISQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRTDPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEA... | null | null | cell differentiation [GO:0030154]; cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of in... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | PF00104;PF12577;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000250|UniProtKB:P37238}.; PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic ac... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxi... | Macaca mulatta (Rhesus macaque) |
O18927 | MMP13_HORSE | MHPGVLAAFLFLSWTRCWSLPVPNDDDDDDDMSEEDFQLAERYLKSYYYPLNPAGILKKTAANSVVDRLREMQSFFGLEVTGKLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWPKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLYNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFVLPDDDVQGIQYLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMVFKDRFFWRLHPQLVDAE... | 3.4.24.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | bone morphogenesis [GO:0060349]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercu... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV a... | Equus caballus (Horse) |
O18937 | RNAS2_AOTTR | MVPKLFTSQICLLLLLGLLGVEGSLHAAPQKFTRAQWFSIQHIQTTPLRCTNAMRAINKYQHRCKNQNTFLHTTFAAVVNVCGNTNITCPRNASLNNCHHSRVQVPLTYCNLTGPPTITNCVYSSTQANMFYVVACDNRDQRDPPQYPVVPVHLDTTI | 4.6.1.18 | null | chemotaxis [GO:0006935]; defense response to virus [GO:0051607]; innate immune response in mucosa [GO:0002227] | extracellular space [GO:0005615]; lysosome [GO:0005764] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:9254715}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for yeast tRNA (in the presence of 40 mM sodium phosphate at pH 7.0) {ECO:0000269|PubMed:9254715}; | null | null | null | FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. {ECO:0000269|PubMed:9254715}. | Aotus trivirgatus (Three-striped night monkey) (Douroucouli) |
O18956 | ENTP1_BOVIN | MEDRRESELKVFCSKNILSILGFSCIIAVIALLALGLTQNKALPENVKFGIVLDAGSSHTSLYIYRWPAEKENDTGVVTQIEESNVKGPGISGFAKKVNEINVYLTACMERAQKVIPSIQHMETPVYLGATAGMRLLRMENKQMADKILAAVASSISEYPFDFQGARIISGQEEGAYGWITVNYLLGKFTQKLSWFNLKPSKDDTQETYGALDLGGASTQITFVPQNETTESPNNNLYFRLYGKNYSVYTHSFLCYGKDQALLQKLALGLQGTNGIIHEPCFHSRYMRKIKMSVLNEGFCTKRHELNSSFYPLVDIEIRG... | 3.6.1.5 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P49961}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49961}; | nucleoside diphosphate catabolic process [GO:0009134]; platelet aggregation [GO:0070527] | caveola [GO:0005901]; plasma membrane [GO:0005886] | ADP phosphatase activity [GO:0043262]; apyrase activity [GO:0004050]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; CDP phosphatase activity [GO:0036384]; CTPase activity [GO:0043273]; GDP phosphatase activity [GO:0004382]; GTPase activity [GO:0003924]; IDP phosphatase activity [GO:1990003]; ITPase ac... | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P97687}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P49961}.; PTM: Palmitoylated on Cys-13; which is required for caveola targeting. {ECO:0000250|UniProtKB:P49961}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P49961}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49961}. Membrane, caveola {ECO:0000250|UniProtKB:P49961}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=l... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates and participates in the regulation of extracellular levels of nucleotides. By hydrolyzing pr... | Bos taurus (Bovine) |
O18963 | CP2E1_BOVIN | MAALGITVALLVWMATLLFISIWKHIYSSWKLPPGPFPLPIIGNLLQLDIKNIPKSFTRLAERYGPVFTLYLGSQRAVVVHGYKPVKEVLLDYKNEFSGRGENPGFQMHKNNGIIFNNGSTWRDTRRFSLTTLRDLGMGKQGNEQRIQREAHFLLEVLRKTQGQPFDPTFVVGFAPYNVISDILFHKRFDYKDQTSLRLMSLFNENFYLLSSPWIQLYNNFPDYLQYLPGSHRKLLKNVSEVKSYALERVKDHQKSLEPSCPRGFLDTMLIEMAKERHSVDPMYTLENIAVTVADLLFAGTETTSTTLRYGLLILMKYPE... | 1.14.13.n7; 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, re... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Microsome membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05182}; Per... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:P05181}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Cataly... | Bos taurus (Bovine) |
O18964 | SYNJ1_BOVIN | MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDIMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDSSDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSLQEHTTDNRFSWNQSLHLHLKHYGVNCADWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLK... | 3.1.3.36 | null | phosphatidylinositol dephosphorylation [GO:0046856]; synaptic vesicle endocytosis [GO:0048488] | perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793] | phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; RNA binding [GO:0003723]; 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: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9199318}. | 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:0000269|PubM... | null | null | null | null | FUNCTION: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:9199318). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory protei... | Bos taurus (Bovine) |
O18965 | KCNH1_BOVIN | MTMAGGRKGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA... | null | null | cellular response to calcium ion [GO:0071277]; potassium ion transmembrane transport [GO:0071805]; regulation of cell population proliferation [GO:0042127]; regulation of membrane potential [GO:0042391] | axon [GO:0030424]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; nuclear inner membrane [GO:0005637]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076] | calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; phosphatidylinositol bisphosphate binding [GO:1902936]; voltage-gated potassium channel activity [GO:0005249] | PF00027;PF00520;PF13426; | 1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20; | Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv10.1/KCNH1 sub-subfamily | PTM: Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6. {ECO:0000250|UniProtKB:O95259}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9524140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon... | null | null | null | null | null | FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9524140). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differ... | Bos taurus (Bovine) |
O18971 | PPARG_BOVIN | MGETLGDALIDPESEPFAVTVSARTSQEITMVDTEMPFWPTNFGISSVDLSMMDDHSHAFDIKPFTTVDFSSISTPHYEDIPFPRADPMVADYKYDLKLQEYQSAIKVEPVSPPYYSEKTQLYSKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHISPLQEPSKEVAIRIFQGCQFRSVEA... | null | null | cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cellular response to insulin stimulus [GO:0032869]; epithelial cell differentiation [GO:0030855]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; n... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-sp... | PF00104;PF12577;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase compl... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxi... | Bos taurus (Bovine) |
O18973 | RABX5_BOVIN | MSLKSERRGIHVDQSELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGAKKAEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEAMHYKRDLSIEEQSECTQDFYQNVAERMQTRGKVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALHWVTPQMLCVPVNEEIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTL... | null | null | endocytosis [GO:0006897]; protein transport [GO:0015031] | cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; recycling endosome [GO:0055037] | DNA binding [GO:0003677]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267]; zinc ion binding [GO:0008270] | PF18151;PF02204;PF01754; | 1.10.246.120;1.20.5.4770;1.20.1050.80; | null | PTM: Monoubiquitinated. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9323142}. Early endosome {ECO:0000269|PubMed:9323142}. Recycling endosome {ECO:0000269|PubMed:9323142}. | null | null | null | null | null | FUNCTION: Rab effector protein acting as linker between gamma-adaptin and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase. {ECO:0000269|PubMed:16462746, ECO:0000269|PubMed:9323142}. | Bos taurus (Bovine) |
O18998 | DNAS1_RABIT | MRSEMLTALLTLAVLLQVAGSLKIAAFNIRSFGETKMSNATLTSYIVRILQRYDIALIQEVRDSHLTAVGKLLDKLNEKAADTYRFVASEPLGRRTYKERYLFVYRPDQVSVLDSYYYDDGCEPCGTDTFSREPAVVRFSSPSTKVREFAIVPLHSAPEDAVAEIDALYDVYLDVQKKWGLQDVMLMGDFNADYSYVTSSQWSSIRLRTNPAFKWLIPDTADTTATSTNCAYDRIVVAGPLLQDAVVPNSAAPFNFQAAYGLSNQLAQAISDHYPVEVTLA | 3.1.21.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P24855}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24855}; Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+). {ECO:0000250|UniProtKB:P24855}; | apoptotic process [GO:0006915]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948] | extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; zymogen granule [GO:0042588] | actin binding [GO:0003779]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677] | PF03372; | 3.60.10.10; | DNase I family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:9230129}; | null | null | null | null | FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9230129). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-... | Oryctolagus cuniculus (Rabbit) |
O19011 | TGFB1_HORSE | MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRAQVAGESAETEPEPEADYYAKEVTRVLMVEKENEIYKTVETGSHSIYMFFNTSELRAAVPDPMLLSRAELRLLRLKLSVEQHVELYQKYSNNSWRYLSNRLLTPSDSPEWLSFDVTGVVRQWLSQGGAMEGFRLSAHCSCDSKDNTLRVGINGFSSSRRGDLATIDGMNRPFLLLMATPLERAQQLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | null | null | ATP biosynthetic process [GO:0006754]; cell-cell junction organization [GO:0045216]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic si... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | antigen binding [GO:0003823]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta receptor binding [GO:0034714] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; P... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Re... | Equus caballus (Horse) |
O19045 | FA10_RABIT | MANPLHLVLLGAALAGLLLSGSSVFISRRAANDVLARTRRANSFLEELKKGNLERECMEENCSYEEALEVFEDREKTNEFWNKYVDGDQCESNPCQNQGTCKDGLGMYTCSCVEGYEGQDCEPVTRKLCSLDNGGCDQFCKEEENSVLCSCASGYTLGDNGKSCISTELFPCGKVTLGRWRRSPATNSSEGPPEAPGPEQQDDGNLTATENPFNLLDSPEPPPEDDSSSLVRIVGGQDCRDGECPWQALLVNEENEGFCGGTILSEYHVLTAAHCLHQAKRFKVRVGDRDTEHEEGNEETHEVEVVVKHNRFVKETYDFD... | 3.4.21.6 | null | blood coagulation [GO:0007596]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. | Oryctolagus cuniculus (Rabbit) |
O19052 | PPARG_RABIT | MVDTEMPFWPTNFGIGSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDLPFARADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKTHEEPSNSLMAIECRVCSDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVSLDLNDQVTLLKYGV... | null | null | cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of inflammatory response [GO:0050728]; p... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [G... | PF00104;PF12577;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase compl... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxi... | Oryctolagus cuniculus (Rabbit) |
O19053 | ADHX_RABIT | MANKVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIFATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTNLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPSAPLDKVCLLGCGISTGYGAALNTAKVEPGSTCAVFGLGGVGLAAIMGCKAAGASRIIAVDINKDKFARAKEFGATECINPQDFSKPIQEVLVEKTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAGAGEEISTRPFQLVTGRTWKGTAFG... | 1.1.1.-; 1.1.1.1; 1.1.1.284 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P11766}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766}; | ethanol oxidation [GO:0006069]; fatty acid omega-oxidation [GO:0010430]; formaldehyde catabolic process [GO:0046294] | cytosol [GO:0005829] | alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; S-(hydroxymethyl)glutathione dehydrogenase NAD activity [GO:0106322]; S-(hydroxymethyl)glutathione dehydrogenase NADP activity [GO:0106321]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ket... | null | null | null | null | FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraened... | Oryctolagus cuniculus (Rabbit) |
O19058 | FUT3_PANTR | MDPLGAAKPQWPWRRCLAALLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPSGSSRQDTTPTRPTLLILLWTWPFHIPVALSRCSEMVPGAADCHITADRKVYPQADAVIVHHWDIMYNPKSRLPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKLDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQEL... | 2.4.1.-; 2.4.1.152; 2.4.1.65 | null | fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; oligosaccharide metabolic process [GO:0009311]; positive regulation of cell-cell adhesion [GO:0022409]; protein N-linked glycosylation [GO:0006487]; protein O-linked glycosylation [GO:0006493]; regulation of cell migration [GO:0030334]; regulation of cell... | Golgi cisterna membrane [GO:0032580] | 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity [GO:0017060]; 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920] | PF17039;PF00852; | 3.40.50.11660; | Glycosyltransferase 10 family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P21217}. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P21217}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P21217}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:P21217}. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:13350... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P21217}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-... | Pan troglodytes (Chimpanzee) |
O19064 | JAK2_PIG | MGMACLTMTEMEGTSTSPVHQNGDIPGNANSVKQIDPVLQVYLYHSLGKAEGDYLKFPAGEYVAEEICVAASKACGITPVYHSMFALMNETERIWYPPNHVFHVDESTRHNVLYRIRFYFPYWYCNGSNRTYRHGISRGAEAPLLDDFVMSYLFAQWRHDFLYGWVKIPVTHETQEECLGMAVLDMMRIAKEKDQTPLDIYSSVSYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIEQFSHCKATARNLKLKYLINLETLQSAFYTEQFEVKEPGRGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDF... | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305}; | activation of Janus kinase activity [GO:0042976]; adaptive immune response [GO:0002250]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to interleukin-3 [GO:0036016]; cellular response to lipopolysaccharide [GO:0071222]; collagen-activated signaling pathway [GO:0038065]; cytokine-mediated s... | caveola [GO:0005901]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; nucleoplasm [GO:0005654]; nucleus... | ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; heme binding [GO:0020037]; histone binding [GO:0042393]; histone H3Y41 kinase activity [GO:0035401]; identical protein binding [GO:0042802]; interleukin-12 receptor binding [GO:0005143]; metal ion binding [GO:0046872]; non-membrane spanning protein... | PF18379;PF18377;PF17887;PF07714;PF00017; | 2.30.29.30;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, JAK subfamily | PTM: Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813. Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity. Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (... | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | 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:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I recepto... | Sus scrofa (Pig) |
O19069 | SUCA_PIG | MTAALVAAPAAATMASGSSGLAAARLLSRSFLLQQNGIRHCSYTASRKHLYVDKNTKVICQGFTGKQGTFHSQQALEYGTNLVGGTTPGKGGKTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIDAEVPLVVCITEGIPQQDMVRVKHRLLRQGKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFTDCLEIFLNDPATEGIILIGEIGGNAEENAAEFLKQHNSGPKSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKITALQS... | 6.2.1.4; 6.2.1.5 | null | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; succinate-CoA ligase complex (ADP-forming) [GO:0009361] | nucleotide binding [GO:0000166]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776] | PF02629;PF00549; | 3.40.50.720;3.40.50.261; | Succinate/malate CoA ligase alpha subunit family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}. | CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_03222}; CATALYTIC ACTIVITY: Reaction=CoA + GTP + s... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.76 mM for succinate {ECO:0000269|PubMed:27487822}; Vmax=5.99 umol/min/mg enzyme {ECO:0000269|PubMed:27487822}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_03222}. | null | null | FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... | Sus scrofa (Pig) |
O19073 | IL18_PIG | MAAEPEDNCISFVEMKFINNTLYFVAENDEDLESDYFGKLEPKLSIIRNLNDQVLFINQGHQAVFEDMPDSDCSDNAPQTVFIIYMYKDSLTRGLAVTISVQCKKMSTLSCKNKTLSFKEMSPPDNIDDEGNDIIFFQRSVPGHDDKIQFESSLYKGYFLACKKENDLFKLILKEKDECGDKSIMFTVQNKN | null | null | angiogenesis [GO:0001525]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; establishment of skin barrier [GO:0061436]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; inflammatory response [GO:00... | cytosol [GO:0005829]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; interleukin-18 receptor binding [GO:0045515] | PF00340; | 2.80.10.50; | IL-1 family | PTM: The pro-IL-18 precursor is processed by CASP1, CASP4 or CASP5 to yield its mature, active form. The pro-IL-18 precursor features autoinhibitory interactions between the propeptide and the post-cleavage-site region, preventing recognition by the IL18R1 receptor. Processing by CASP1, CASP4 or CASP5 induces conformat... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14116}. Secreted {ECO:0000250|UniProtKB:Q14116}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GS... | null | null | null | null | null | FUNCTION: Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes... | Sus scrofa (Pig) |
O19105 | AAAT_RABIT | MVADPPKGDPKGLAAVEPTANGAPAQDPLEDSGAAVGRCCSSRDQVRRCLRANLLVLLTVVAVVAGVALGLAVSGAGGALALGPARLIAFAFPGELLLRLLKMIILPLVVCSLVGGAASLDPSALGRLGAWALLFFLVTTLLASALGVGLALALQPGAAFAAMNASLSSTGAVEQTPSKQVLDSFLDLLRNIFPSNLVSAAFRSYSTSYEEKNFNGTLVKVPVAHEEEGMNILGLVVFAIVFGVALRKLGPEGEPLIRFFNSFNDATMVLVSWIMWYAPVGILFLVASKIVEMDDVGVLFASLGKYILCCLLGHAIHGLL... | null | null | glutamine transport [GO:0006868]; L-aspartate import across plasma membrane [GO:0140009]; protein homotrimerization [GO:0070207] | melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamine transmembrane transporter activity [GO:0015186]; metal ion binding [GO:0046872]; symporter activity [GO:0015293] | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A5 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9227483}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome {ECO:0000250|UniProtKB:Q15758}. | CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in) + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-g... | null | null | null | null | FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:9227483). The preferred substrate is the essential ... | Oryctolagus cuniculus (Rabbit) |
O19111 | KPCZ_RABIT | MPSRAGPKMDGSGGRVRLKAHYSGDIFITSVDAATTFEELCEEVRDMCGLHQHHPLTLKWVDSEGDPRTVSSQMELGEAFRLAGQHRDDGLILHVFPSTPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRRHMDSVMPSQEPPVADKSDDADLPSQETDGIAFISTRKQDSGQEDAEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNGQVYAMKVVKKELVHDDEDIDWVQTEKHVFEQASGNPFLVGLHSCFQ... | 2.7.11.13 | null | establishment of cell polarity [GO:0030010]; inflammatory response [GO:0006954]; long-term synaptic potentiation [GO:0060291]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of insulin re... | cell-cell junction [GO:0005911]; endosome [GO:0005768]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00564;PF00069;PF00433; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: CDH5 is required for its phosphorylation at Thr-409. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-409 by PI3K activates the kinase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05513}. Endosome {ECO:0000250|UniProtKB:Q05513}. Cell junction {ECO:0000250|UniProtKB:Q05513}. Membrane {ECO:0000250|UniProtKB:P09217}; Peripheral membrane protein {ECO:0000305}. Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarit... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q05513}; CATALYT... | null | null | null | null | FUNCTION: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and... | Oryctolagus cuniculus (Rabbit) |
O19116 | SFRP1_BOVIN | MGGGRWAAAGALLALAAGLLAAGSASEYDYVSFQSDIGAYQSGRFYTKPPQCVDIPADLRLCHNVGYKRMVLPNLLEHETMAEVKQQASSWVPLLNKNCHIGTQVFLCSLFAPVCLDRPIYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGDVCIAMTPPNATEASKPQGTTVCPPCDNELKSEAIIEHLCASEFALRMKIKEVKKENGDKKIVPKKKKPLKLGPIKKKELKKLVLYLKNGADCPCHQLDNLSHHFLIMGRKVKSQYLLTAIHKWDKKNKEFKTFMKKMKNHECPTFQSVFK | null | null | actin cytoskeleton organization [GO:0030036]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of G... | extracellular space [GO:0005615]; plasma membrane [GO:0005886] | frizzled binding [GO:0005109]; Wnt-protein binding [GO:0017147] | PF01392;PF01759; | 2.40.50.120;1.10.2000.10; | Secreted frizzled-related protein (sFRP) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10381896}. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding. | null | null | null | null | null | FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vas... | Bos taurus (Bovine) |
O19131 | TNR1A_BOVIN | MGLPTVPGLLLPLVLPALLADVYPAGVQGLVPHPGDLEKRESPCPQGKYNHPQNSTICCTKCHKGTYLYNDCPGPGRDTDCRVCAPGTYTALENHLRRCLSCSRCRDEMFQVEISPCVVDRDTVCGCRKNQYREYWGETGFRCLNCSLCPNGTVNIPCQERQDTICHCHMGFFLKGAKCISCHDCKNKECEKLCPTRPSTGKDSQDPGTTVLLPLVIVFGLCLASFASVVLACRYQRWKPKLYSIICGQSTLVKEGEPELLVPAPGFNPTTTICFSSTPSSSPVSIPPYISCDRSNFGAVASPSSETAPPHLKAGPILPG... | null | null | apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]; inflammatory response [GO:0006954]; positive regulation of inflammatory response [GO:0050729]; positive regulation of transcription by RNA polymerase II ... | Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | tumor necrosis factor binding [GO:0043120]; tumor necrosis factor receptor activity [GO:0005031] | PF00531;PF00020; | 1.10.533.10;2.10.50.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specifi... | Bos taurus (Bovine) |
O19132 | NOS1_RABIT | MEEHVFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGVASETHVVLILRGPEGFTTNLETTFTGDGTPKTIRVTQPLGAPTKAVDLSHQPPSAGKEQPRPVDGAAGPGSWPQPTQGHGQEAGSPSRANGLAPRTSSQDPAKKSGWAGLQGSGDKNELLKEIEPVLTLLAGGSKAVDGGGPAKAETRDTGVQVDRDFDAKSHKPLPLGVENDRVFSDLWGKGSAPVVLNNPYSEKEQPPASGKQSPTKNGSPSKCPRFLKVKNWETDVVLTD... | 1.14.13.39 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P29475}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1... | nitric oxide biosynthetic process [GO:0006809] | dendritic spine [GO:0043197]; sarcolemma [GO:0042383] | calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517] | PF00667;PF00258;PF00175;PF02898;PF00595; | 2.30.42.10;3.40.50.360;3.90.440.10;3.40.50.80;2.40.30.10; | NOS family | PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro). {ECO:0000250|UniProtKB:P29476}. | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z0J4}; Peripheral membrane protein {ECO:0000255}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glyco... | CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={... | null | null | null | null | FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR (B... | Oryctolagus cuniculus (Rabbit) |
O19179 | GUC2D_CANLF | MSACALLAGGLPDPRLCAPARWARSPPGVPGAPPWPQPRLRLLLLLLLLPPSALSAVFTVGVLGPWACDPIFARARPDLAARLAAARLNRDAALEDGPRFEVTLLPEPCRTPGSLGAVSSALGRVSGLVGPVNPAACRPAELLAQEAGVALVPWSCPGTRAGGTTAPAGTPAADALYALLRAFRWARVALITAPQDLWVEAGRALSAALRARGLPVALVTTMEPSDLSGAREALRRVQDGPRVRAVIMVMHSVLLGGEEQRCLLQAAEELGLADGSLVFLPFDTLHYALSPGPEALAVLANSSQLRRAHDAVLILTRHCP... | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; visual perception [GO:0007601] | endoplasmic reticulum membrane [GO:0005789]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07701;PF07714; | 3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | PTM: There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds. | SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P55203}; | null | null | null | null | FUNCTION: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-associated proteins to the photoreceptor outer segment membrane. {ECO:0000250|UniProtKB:P52785}. | Canis lupus familiaris (Dog) (Canis familiaris) |
O19183 | PGH2_HORSE | MLARALLLCVALALGHAANPCCSNPCQNRGVCMSVGFDQYQCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGVWNIVNSFPFLRNAVMKYVLVSRSHLIESPPTYNAQYGYKSWESFSNLSYYTRALPPVADGCPTPMGVKGKKELPDSKEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDPKRGPAFTKGLGHGVDLSHIYGETLDRQHKLRLFKDGKMKYQIINGEVYPPTVKDTQVEMIYPPHIPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRL... | 1.14.99.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q05769}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250|UniProtKB:Q05769}; | cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of blood pressure [GO:0008217]; regulation of neuroinflammatory response [GO:0150077]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666] | PF03098;PF00008; | 1.10.640.10;2.10.25.10; | Prostaglandin G/H synthase family | PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}. | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Periphera... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=... | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P35354}. | null | null | FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endope... | Equus caballus (Horse) |
O19477 | HMR1_RAT | MMFLLPFLTVFLAKQSHTRTHSLRYFRLAISDPGPGVPEFISVGYVDSHPITTYDSVTRQKEPRAPWMAENLAPDHWERYTQLLRGWQRTFQTELRHLQRHYNHSGLHTYQRMIGCELLEDGSTTGFLQYAYDGQDFIVFDKDTLSWLAMDNVAHITKRAWEANLHELQYQKNWLEEECIAWLKRFLEYGSDALERTEHPVVRTTRKETFPGITTLFCRAHGFYPPEISMIWKKNGEEIVQEVDYGGVLPSGDGTYQMWVSVDLDPQTKDIYSCHVEHCGLQMVLEAPQESGNTLLVANTISGTIILIIVLAGVGALIWR... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous antigen [GO:0019884]; defense response to Gram... | early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; MHC class I protein complex [GO:0042612]; plasma membr... | beta-2-microglobulin binding [GO:0030881]; T cell receptor binding [GO:0042608] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q95460}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q95460}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass t... | null | null | null | null | null | FUNCTION: Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TCRs on MAIT cells, guiding... | Rattus norvegicus (Rat) |
O20250 | TKTC_SPIOL | MAASSSLSTLSHHQTLLSHPKTHLPTTPASSLLVPTTSSKVNGVLLKSTSSSRRLRVGSASAVVRAAAVEALESTDIDQLVEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHILYDEIMRYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVLEEDLKTFRQWGSRIPGHPENFETPGVEVTTGPLGQGIANAVGLALAEKHLAARFNKPDAEIVDHYTYVILGDGCQMEGIAQEACSLAGHWGLGKLIAFYDDNHISIDGDTAIAFTESVDLRFEALGWHVIWVKNGNTGYDEIRAAIKEAKTVTDKPTLI... | 2.2.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divale... | pentose-phosphate shunt, oxidative branch [GO:0009051]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829] | metal ion binding [GO:0046872]; transketolase activity [GO:0004802] | PF02779;PF02780;PF00456; | 3.40.50.920;3.40.50.970; | Transketolase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:9523694}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000269|PubMed:8980496}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for xylulose 5-phosphate {ECO:0000269|PubMed:9523694}; KM=330 uM for ribose 5-phosphate {ECO:0000269|PubMed:9523694}; | PATHWAY: Carbohydrate biosynthesis; Calvin cycle. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:9523694}; | null | FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively. {ECO:0000269|PubMed:8980496, ECO:0000303|PubMed:8980496}. | Spinacia oleracea (Spinach) |
O22040 | ANP1_ARATH | MQDFFGSVRRSLVFRPSSDDDNQENQPPFPGVLADKITSCIRKSKIFIKPSFSPPPPANTVDMAPPISWRKGQLIGRGAFGTVYMGMNLDSGELLAVKQVLIAANFASKEKTQAHIQELEEEVKLLKNLSHPNIVRYLGTVREDDTLNILLEFVPGGSISSLLEKFGPFPESVVRTYTRQLLLGLEYLHNHAIMHRDIKGANILVDNKGCIKLADFGASKQVAELATMTGAKSMKGTPYWMAPEVILQTGHSFSADIWSVGCTVIEMVTGKAPWSQQYKEVAAIFFIGTTKSHPPIPDTLSSDAKDFLLKCLQEVPNLRP... | 2.7.11.25 | null | protein autophosphorylation [GO:0046777]; response to oxidative stress [GO:0006979] | null | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase 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=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: May be involved in an oxidative stress-mediated signaling cascade that phosphorylates downstream MAP kinases MPK3 and MPK6. May suppress auxin signaling that promotes cell cycle. Functionally redundant to ANP2 and ANP3 in the positive regulation of cytokinesis. {ECO:0000269|PubMed:10717008, ECO:0000269|PubMed... | Arabidopsis thaliana (Mouse-ear cress) |
O22042 | M3K3_ARATH | MQDILGSVRRSLVFRSSLAGDDGTSGGGLSGFVGKINSSIRSSRIGLFSKPPPGLPAPRKEEAPSIRWRKGELIGCGAFGRVYMGMNLDSGELLAIKQVLIAPSSASKEKTQGHIRELEEEVQLLKNLSHPNIVRYLGTVRESDSLNILMEFVPGGSISSLLEKFGSFPEPVIIMYTKQLLLGLEYLHNNGIMHRDIKGANILVDNKGCIRLADFGASKKVVELATVNGAKSMKGTPYWMAPEVILQTGHSFSADIWSVGCTVIEMATGKPPWSEQYQQFAAVLHIGRTKAHPPIPEDLSPEAKDFLMKCLHKEPSLRLS... | 2.7.11.25 | null | cortical microtubule organization [GO:0043622]; protein autophosphorylation [GO:0046777] | apoplast [GO:0048046]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Involved in cortical microtubules organization and stabilization by regulating the phosphorylation state of microtubule-associated proteins such as MAP65-1. {ECO:0000269|PubMed:20215588}. | Arabidopsis thaliana (Mouse-ear cress) |
O22043 | GGPP6_ARATH | MRPRYSLILSAMRLIRPSNRRLSSIASSDSEFISYMKNKAKSINKALDNSIPLCNNFVPLWEPVLEVHKAMRYTLLPGGKRVRPMLCLVACELVGGQESTAMPAACAVEMIHAASLILDDLPCMDDDSLRRGKPTNHKVFGEKTSILASNALRSLAVKQTLASTSLGVTSERVLRAVQEMARAVGTEGLVAGQAADLAGERMSFKNEDDELRYLELMHVHKTAVLVEAAAVVGAIMGGGSDEEIERLKSYARCVGLMFQVMDDVLDETKSSEELGKTAGKDLITGKLTYPKVMGVDNAREYAKRLNREAQEHLQGFDSDK... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324}; | carotenoid biosynthetic process [GO:0016117]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid biosynthetic process [GO:0008299] | mitochondrion [GO:0005739] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:9349257}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. {ECO:0000269|PubMed:9349257}. | Arabidopsis thaliana (Mouse-ear cress) |
O22049 | AOX2_ARATH | MSQLITKAALRVLLVCGRGNCNMFVSSVSSTSVMKSPYEITAPMRIHDWCGGFGDFKIGSKHVQGNFNLRWMGMSSASAMEKKDENLTVKKGQNGGGSVAVPSYWGIETAKMKITRKDGSDWPWNCFMPWETYQANLSIDLKKHHVPKNIADKVAYRIVKLLRIPTDIFFQRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIR... | 1.10.3.11 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q39219}; Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219}; | alternative respiration [GO:0010230] | chloroplast [GO:0009507]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | alternative oxidase activity [GO:0009916]; metal ion binding [GO:0046872]; superoxide-generating NADPH oxidase activity [GO:0106292]; ubiquinol:oxygen oxidoreductase activity [GO:0102721] | PF01786; | 1.20.1260.140; | Alternative oxidase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11434463}; Multi-pass membrane protein {ECO:0000269|PubMed:11434463}. Note=Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. | CATALYTIC ACTIVITY: Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O; Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.10.3.11; | null | null | null | null | FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperature... | Arabidopsis thaliana (Mouse-ear cress) |
O22056 | SIGB_ARATH | MSSCLLPQFKCPPDSFSIHFRTSFCAPKHNKGSVFFQPQCAVSTSPALLTSMLDVAKLRLPSFDTDSDSLISDRQWTYTRPDGPSTEAKYLEALASETLLTSDEAVVVAAAAEAVALARAAVKVAKDATLFKNSNNTNLLTSSTADKRSKWDQFTEKERAGILGHLAVSDNGIVSDKITASASNKESIGDLESEKQEEVELLEEQPSVSLAVRSTRQTERKARRAKGLEKTASGIPSVKTGSSPKKKRLVAQEVDHNDPLRYLRMTTSSSKLLTVREEHELSAGIQDLLKLERLQTELTERSGRQPTFAQWASAAGVDQK... | null | null | cellular response to light stimulus [GO:0071482]; chloroplast organization [GO:0009658]; DNA-templated transcription initiation [GO:0006352]; regulation of RNA biosynthetic process [GO:2001141]; response to red light [GO:0010114]; tRNA metabolic process [GO:0006399] | chloroplast [GO:0009507] | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04542;PF04539;PF04545; | 1.10.601.10;1.10.10.10; | Sigma-70 factor family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:12602869}. | null | null | null | null | null | FUNCTION: Required for the transition of plastids into chloroplasts by coordinating nuclear and chloroplastic genomes under light conditions. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Promotes the biosynth... | Arabidopsis thaliana (Mouse-ear cress) |
O22059 | CPC_ARATH | MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK | null | null | epidermal cell differentiation [GO:0009913]; positive regulation of trichoblast fate specification [GO:0010063]; stomatal complex formation [GO:0010376] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16291794}. Note=Moves from developing non-hair cells (atrichoblasts) to developing hair cells (trichoblasts). | null | null | null | null | null | FUNCTION: Transcription factor. Determines the fate of epidermal cell differentiation. Represses trichome development by lateral inhibition. Together with GL3 or BHLH2, promotes the formation of hair developing cells (H position) in root epidermis, probably by inhibiting non-hair cell formation. Represses the expressio... | Arabidopsis thaliana (Mouse-ear cress) |
O22130 | AHL22_ARATH | MDQVSRSLPPPFLSRDLHLHPHHQFQHQQQQQQQNHGHDIDQHRIGGLKRDRDADIDPNEHSSAGKDQSTPGSGGESGGGGGGDNHITRRPRGRPAGSKNKPKPPIIITRDSANALKSHVMEVANGCDVMESVTVFARRRQRGICVLSGNGAVTNVTIRQPASVPGGGSSVVNLHGRFEILSLSGSFLPPPAPPAASGLTIYLAGGQGQVVGGSVVGPLMASGPVVIMAASFGNAAYERLPLEEDDQEEQTAGAVANNIDGNATMGGGTQTQTQTQQQQQQQLMQDPTSFIQGLPPNLMNSVQLPAEAYWGTPRPSF | null | null | flower development [GO:0009908]; photomorphogenesis [GO:0009640]; skotomorphogenesis [GO:0009647]; vegetative to reproductive phase transition of meristem [GO:0010228] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; histone deacetylase binding [GO:0042826]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein self-association [GO:0043621] | PF03479; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19517252, ECO:0000269|PubMed:22442143}. | null | null | null | null | null | FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter (PubMed:22442143). Acts redundantly with AHL18, AHL27 and AHL29 in the regulation of flowering and regulation of the... | Arabidopsis thaliana (Mouse-ear cress) |
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