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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
D1A4G7 | ECCC_THECD | MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGG... | null | null | localization [GO:0051179] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF01580; | 3.40.50.300; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:25865481). Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481). Might be the translocase subunit (PubMed:25865481). {ECO:... | Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) |
D1A7C3 | FGE_THECD | MPSFDFDIPRRSPQEIAKGMVAIPGGTFRMGGEDPDAFPEDGEGPVRTVRLSPFLIDRYAVSNRQFAAFVKATGYVTDAERYGWSFVFHAHVAPGTPVMDAVVPEAPWWVAVPGAYWKAPEGPGSSITDRPNHPVVHVSWNDAVAYATWAGKRLPTEAEWEMAARGGLDQARYPWGNELTPRGRHRCNIWQGTFPVHDTGEDGYTGTAPVNAFAPNGYGLYNVAGNVWEWCADWWSADWHATESPATRIDPRGPETGTARVTKGGSFLCHESYCNRYRVAARTCNTPDSSAAHTGFRCAADPL | 1.8.3.7 | COFACTOR: Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795, ECO:0000269|PubMed:28544744}; Note=The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000269|PubMed:28544744}; | post-translational protein modification [GO:0043687]; protein oxidation [GO:0018158] | null | cuprous ion binding [GO:1903136]; formylglycine-generating oxidase activity [GO:0120147] | PF03781; | 3.90.1580.10; | Sulfatase-modifying factor family | null | null | CATALYTIC ACTIVITY: Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-[sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide; Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=580 uM for [sulfatase]-L-cysteine (in presence of Cu(+)) {ECO:0000269|PubMed:27862795}; Note=kcat is 1.6 min(-1) in presence of Cu(+). {ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}; | PATHWAY: Protein modification; sulfatase oxidation. {ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}. | null | null | FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. {ECO:00002... | Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) |
D1D8L6 | CDNTP_ASPFM | MDGEMTASPPDISACDTSAVDEQTGQSGQSQAPIPKDIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEYLCLFAQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAFEPVRYQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAKDERNLNEEQLTKYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATGQTGSNACFGAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAHTRFKVYIADPLVTLARAEEHWTLGGRLTDEDAAVGLEI... | 2.5.1.-; 3.4.11.17 | null | alkaloid metabolic process [GO:0009820]; proteolysis [GO:0006508] | null | aminopeptidase activity [GO:0004177]; prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + harmol = 6-(3-dimethylallyl)harmol + diphosphate; Xref=Rhea:RHEA:72983, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:192558, ChEBI:CHEBI:192559; Evidence={ECO:0000269|PubMed:35767141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72984; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=650 uM for dimethylallyl diphosphate (DMAPP) {ECO:0000303|PubMed:17525915}; KM=300 uM for H-L-Trp-L-Gly-OH (for aminopeptidase activity) {ECO:0000269|PubMed:18635009}; KM=380 uM for L-tryptophan {ECO:0000303|PubMed:19113967}; KM=128 uM for cyclo-D-Trp-L-Tyr {ECO:00... | null | null | null | FUNCTION: Prenyltransferase that catalyzes reverse prenylation at position N-1 of tryptophan-containing cyclic dipeptides (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141). Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate s... | Aspergillus fumigatus (Neosartorya fumigata) |
D1FVF0 | BSLS_BEABA | MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDYFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDGHGRVFSLQPTTDLTESENGDHLSTPASERTVVIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTST... | 2.1.1.-; 6.1.2.- | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550] | cytosol [GO:0005829] | isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=4 (R)-2-hydroxy-3-methylbutyrate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + bassianolide + 8 diphosphate + 8 H(+) + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:57856, ChEBI:CHEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; KM=2.8 uM for L-leucyl-N-acetyl-cysteamine thioester(by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.41 uM/min/mg enzyme toward L-phenylalanyl-N-acety... | null | null | null | FUNCTION: Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity (PubMed:19285149, PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). BSLS first cat... | Beauveria bassiana (White muscardine disease fungus) (Tritirachium shiotae) |
D1KF50 | SRS2L_ARATH | MENLPPNRGMWNQEYSHGRISQSFRSAKPLLDRKRPIENAPNSSNPLPQRMKESMDTESVSHNINFNSTPLMELSANTPYKRLKPEIESYADGHPCGLRTPPPRFDLDKEIINGFQTDIYADVGSLSEAFVTPLKEPERVTLSNGCSTSSILDDDFDDSILEEIDLICEQSARKAACQTPTTSIYQTPSKDNKSSDPKASLDFRDVEKFEPDSNVKLKLDEETPTIAADPALLNSMPDECSKYMLSLNDRQRDAACSNISTPLMVIAGPGSGKTSTMVGRVLVLLNEGLLPSNILAMTFTKAATSEMRERIGKSAGKKAA... | 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19767619}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19767619}; | DNA recombination [GO:0006310]; DNA rewinding [GO:0036292]; recombinational repair [GO:0000725] | nucleus [GO:0005634] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; isomerase activity [GO:0016853] | PF00580;PF13361; | 1.10.10.160;3.40.50.300; | Helicase family, UvrD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; 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... | null | null | null | null | FUNCTION: ATP-dependent 3'- to 5'-DNA helicase that could disrupt recombinogenic DNA intermediates and facilitate single strand annealing. Unwinds nicked and partial Holliday junctions in vitro. Anneals two single strands into a dsDNA molecule in vitro. {ECO:0000269|PubMed:19767619}. | Arabidopsis thaliana (Mouse-ear cress) |
D1L2X1 | DPOL2_BPK32 | MLDNFNQPKGSTIGVLKDGRTIQEAFDSLPRLESFSGSTATDKLRAAITLGVSEVAIGPVEGNGGRPYEFGDVVIPYPLRIVGCGSQGINVTKGTVLKRSAGASFMFHFTGEGQAQRPMGGGLFNINLNGDTATALGDIIKVTQWSYFKANNCAFQNMAGWGIRLKDVMESNISGNLFRRLGGPSGGGILFDDVRSAVTDNVNNLHIEDNTFALMSGPWIGSTANSNPDLIWIVRNKFEFDGTPAAPNTVDSYVLDFQQLSRAFIQDNGFTHFTTERNRYVGVLRVGATAVGTIKFEDNLLFACESAGLIAGGIVVSRGN... | null | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell glycocalyx [GO:0098996] | virus tail [GO:0098015] | null | null | 2.160.20.10; | Przondovirus depolymerase 2 family; K21-specific depolymerase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Tail appendage (Probable). Depolymerase 1 is connected to the phage tail via an N-terminal anchor domain, while depolymerase 2 is attached to depolymerase 1 (PubMed:33947754). {ECO:0000303|PubMed:33947754, ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K21-type polysaccharides Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane ... | Klebsiella phage KP32 (Bacteriophage KP32) |
D1LYT2 | GBRB2_MACMU | MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMAL... | null | null | cellular response to histamine [GO:0071420]; chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; 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, GABRB2 sub-subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:P63137}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P63138}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cell membrane {ECO:0000250|UniProtKB:P47870}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P63138}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P08219}; | null | null | null | null | FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain. GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active bin... | Macaca mulatta (Rhesus macaque) |
D1MEI7 | MASTA_EUMPO | MRGTSFILFAVVVILGFLNANAEPLANPAPLANPDPLANPDPLANPEAFDLLGLVKKVASALG | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | null | null | MCD family, Mastoparan subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20096300}. Target cell membrane {ECO:0000250|UniProtKB:P0CJ38}. Note=Has an amphipathic alpha-helical conformation in hydrophobic environment. {ECO:0000305|PubMed:21184791}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide. Shows activities against Gram-positive bacteria (S.aureus MIC=50 uM and 200 ug/ml, and B.subtilis MIC=200 ug/ml), Gram-negative bacterium E.coli (MIC=100 uM and 200 ug/ml) and fungi (B.cinerea MIC=5 uM, S.cerevisiae MIC=128 ug/ml, S.pombe MIC=128 ug/ml, A.nidulans MIC=128 ug/ml, and C.a... | Eumenes pomiformis (Potter wasp) (Vespa pomiformis) |
D1ZA70 | ARO1_SORMK | MAESSSNPTRINILGKDNIIIDHGIWLNFVAQDLLQNIKSSTYILITDTNLYATYVPSFQSVFEKAAPQDVRLLTYAIPPGEYSKGRDTKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDVPMGKNLIGAFWQPERIYIDLTFLNTLPVREFINGMAEVIKTAAIWDESEFTTLEENAKAILEAVRSKNKSADRLAPIRDILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEAILTPQVLHGEAVAIGMVKEAELARFLGVLKPSAVARLTKCIAS... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) |
D2CLZ9 | ATOH8_DANRE | MKNPHLNSPCKILNTVSGDKKMKRKAREPIKHVSEDHYPYFKLYKNPHLMAETLGDGSPQETHRSEIITSRDDSVRNDVLNTAVDMRINTITAAEVPDSKLRSVSEKTVNSKIVQASPQVSVLSAPQVFPLERVVLSQRAASQAPAGGSERAESPRKRAGEPSGVVTEIKAIQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLAQLADLDYTPDHRNMSFRECVEQCTRTLQAEGRSKKRKE | null | null | anatomical structure morphogenesis [GO:0009653]; axon development [GO:0061564]; heart development [GO:0007507]; heart looping [GO:0001947]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neural retina development [GO:0061074]; regulation of skeletal muscle cell differentiation [GO... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99NA2}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q99NA2}. | null | null | null | null | null | FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). During development, is required for heart looping and swim bladder formation by acting in concert with GATA4 and ZF... | Danio rerio (Zebrafish) (Brachydanio rerio) |
D2CSU4 | CM1_PETHY | METQLLRFPSHTITSSITTNSSRNTTPFLPHKKWSHFVKFQLVNSSSSIKHGIRPLQASATSLGLGNKNRVDETESYTLDGIRHSLIRQEDSIIFSLVERAQYCYNAETYDPDVFAMDGFHGSLVEYIVRETEKLHATVGRYKSPDEHPFFPKVLPEPVLPPMQYPKVLHPIADSININVKIWEMYFENLLPRLVKEGDDGNYGSTAVCDTICVQALSKRIHYGKFVAEAKYRASPEVYNAAIRAQDRNGLMDLLTYPAVEEAIKRRVEIKTRTYGQELHINGPENGGDPVYKIKPSLVAELYGDWIMPLTKEVQVQYLL... | 5.4.99.5 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; green leaf volatile biosynthetic process [GO:0010597] | chloroplast stroma [GO:0009570] | chorismate mutase activity [GO:0004106] | null | 1.10.590.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:19811620}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU00516, ECO:0000269|PubMed:19811620}; | null | PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:19811620}. | null | null | FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBPs) biosynthetic pathway (PubMed:19811620). Mediates the conversion of chorismate to prephenate, thus coupling metabolites from the shikimate pathway to the synthesis of FVBPs in the corolla (PubMed:19811620). {ECO:0000269|PubMed:19811620}. | Petunia hybrida (Petunia) |
D2CVN6 | TEB1_TETTS | MKLTKGGSYILKKVDRKQFYQDEEIVMQIKKILGQKTTDCKQYIKCECIDGLGDEALIYFEMLANQNQHLQKNDVIMIQDYLNDKTQNDKIVVLVTRFQFCKASHVQPKTAQKESIQLLNTEKTIIQKSKITKNPAEEVLKFIEVNEKDNSSNSEDMIIEQQKQEIKNNQKEKQSINGFNLEDSYSNISDITNFGGKSNFNIGSLSDQLSKQTLLISQLQVGKNRFSFKFEGRVVYKSSTFQNQQDSKYFFITAQDANNQEINLSFWQKVDQSYQTLKVGQYYYFIGGEVKQFKNNLELKFKFGDYQIIPKETLSANYVQ... | null | null | telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric region [GO:0000781]; telomerase holoenzyme complex [GO:0005697] | single-stranded telomeric DNA binding [GO:0043047]; zinc ion binding [GO:0008270] | PF08646; | 2.20.25.10;2.40.50.140; | Replication factor A protein 1 family | null | SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}. | null | null | null | null | null | FUNCTION: Single-stranded DNA (ssDNA)-binding protein that mediates the recruitment of telomerase to telomeric DNA (PubMed:19941821, PubMed:20363756, PubMed:22143754, PubMed:25225329). Telomerase is an essential ribonucleoprotein (RNP) enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthe... | Tetrahymena thermophila (strain SB210) |
D2EAC2 | ZBED6_MOUSE | MSVCTLSVPVSSISPGRRCSTFGDAGILGCVSINSNTDEDDVVEGKMVAEGANKETKLPAKKKRKKGLRIKGKRRRKKLILAKKFSKDLGSGRPVADAPASLASGAPEQDEESLFEGNIEKQIYLPSTRAKTSIVWHFFHVDPQYTWRAICNLCEKSVSRGKPGSHLGTSTLQRHLQARHSPHWTRANKFGVTNGEEDFTLDLSLSPPSPGSNGSFEYIPTDSVDENRMGKKRDKSASDALRAKRGRFLIKSNIVKHALIPGTRAKTSAVWNFFYTDPQHISRAVCNICKRSVSRGRPGSHLGTSTLQRHLQATHPIHWA... | null | null | blastocyst hatching [GO:0001835]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of insulin secretion involved in cellular response to glucose stimulus [G... | centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976] | PF05699;PF02892; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:32557799}. Nucleus, nucleolus {ECO:0000269|PubMed:20016685}. Cytoplasm {ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:32557799}. Note=Located predominan... | null | null | null | null | null | FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3', transcription regulation may be tissue-specific (PubMed:20016685, PubMed:20134481, PubMed:24043816, PubMed:29440408, PubMed:32557799). Regulates the expression of target genes such as: IGF2, PGAP6/TMEM8, ENHO, and PIANP (PubMed:2001... | Mus musculus (Mouse) |
D2GXM8 | CBPC5_AILME | MELRCGGLLFSSRFDSGNLAHVEKVDSVSGDGEGGAAGASAPFSSIASSPDYEFNVWTRPDCAETEFENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPTRPRWERIRDRPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLNQLDQRFLENHPTHSSPLDTIYYHREILCYSLDGLRVDLLTITSCHGLREDREPRLQQLFPDTGTPRPFCFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDA... | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; intercellular bridge [GO:0045171]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed. Colocalizes with alpha-tubuli... | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=le... | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tu... | Ailuropoda melanoleuca (Giant panda) |
D2GZV9 | ENTP5_AILME | MATTWGAAFFMLVASCVCSTVFHRDQQTWFEGVFLSSMCPINVSASTLYGIMFDAGSTGTRIHIYTFVQKIPGQLPILEGEIFESVKPGLSAFVDQPKQGAETVEELLEVAKDSVPRSHWKRTPVVLKATAGLRLLPEQKAEALLFEVREIFRKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHSQKTVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGIDGHTFRSACLPRWLEAEWIFGGVKYQYGGNKEGNEGSGEVGFEPCYAEVLRVVQGKL... | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-su... | Ailuropoda melanoleuca (Giant panda) |
D2H526 | CDK12_AILME | MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAAPLGTIIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGTDRSDRLHKHRHHQHRRSRDLLKTKQTEKEKNQEVSSKSGSMKDRISGSSKRSNEENEDYGKAQISKSSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSY... | 2.7.11.22; 2.7.11.23 | null | mRNA processing [GO:0006397]; negative regulation of stem cell differentiation [GO:2000737]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of MAP kinase activity [GO:0043... | cyclin K-CDK12 complex [GO:0002944]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-894 increases kinase activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferen... | Ailuropoda melanoleuca (Giant panda) |
D2HBJ8 | UBP44_AILME | MLTMDKCKHIGQLRLAQDHSILNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNATGDLKLLRSMLSAIKSQNYQCTTRSGRVLRSMGTSDDTYYLHDGTQSLLQNEDQMYTALWHRRRILMSKIFRTWFEQSPTGRKRQEEQFQEKIAKREVKKRRQELEYQVKAELETIHPRKSLRLQGLAQSTTVEIVPVQVPLQTPASPAKDKVVSTSEDVRLKKASDSSGKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVTASDKTRSP... | 3.4.19.12 | null | antiviral innate immune response [GO:0140374]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; proteasome-mediated ubiquitin-dependent protein catabolic proc... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family, USP44 subfamily | PTM: Dephosphorylated by CTDP1. {ECO:0000250}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H0E7}. Cytoplasm {ECO:0000250|UniProtKB:Q9H0E7}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. {ECO:0000250}. | 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:0000250|UniProtKB:Q9H0E7}; | null | null | null | null | FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads t... | Ailuropoda melanoleuca (Giant panda) |
D2HEW7 | KLH22_AILME | MAEEQEFTQLCKLPVQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYTLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVANALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTVLSDQAKY... | null | null | cell division [GO:0051301]; cellular response to leucine [GO:0071233]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of autophagy [GO:0010507]; negative regulation of type I interferon production [GO:0032480]; positive regulation of ce... | centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; lysosome [GO:0005764]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; polar microtubule [GO:0005827] | 14-3-3 protein binding [GO:0071889]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344;PF13415;PF13964; | 1.25.40.420;2.120.10.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}. Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome {ECO:0000250|UniProtKB:Q53GT1}. No... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent re... | Ailuropoda melanoleuca (Giant panda) |
D2HHP1 | WEE2_AILME | MDDSSINKELKQKLNFSYCEEESESEGQEAWETRDAHSQIPDRAEGQESEAKFTPPGPPLSSVHEVGTFQEKTKKSPEQVLMTPVSGFRNYPETPAQPDSRSKLLDCESPFTPKGLLSQSVISSTEKIPSRGSKHLRFTPVPFVDEMTSSALVNINPFTPESYRKQFLKSNGKRKTRGDFEEAGPGEGNVEQGLPAKRCVLQETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPFAGLSNENLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQTAISENTKSGNHFQEPKLKD... | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; female pronucleus assembly [GO:0035038]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of oocyte maturation [GO:1900194]; phosphorylation [GO:0016310]; positive regulation of phosphorylation ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylation leads to increase its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: 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: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphoryl... | Ailuropoda melanoleuca (Giant panda) |
D2HKB0 | UBIA1_AILME | MAASQVPGEINIQAGETAKSGDRDLLGNDCRDQDRLPQRSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSQGVLDPRLLVGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVLFGVFLYTLGCVCAACLYCLSPLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLVILITFGPLAVMFAYAVQVGSLAVFPLVYAIPLALSTEAVLHSNNTRDMESDREAGIVTLAILIGPTLSYVLYNTLLFLPYLIFSILATHCSISLALPLLTVPMAFSLERQFRSQTFNKLPQRTAKLNLLLGL... | 2.5.1.-; 2.5.1.39 | null | circulatory system development [GO:0072359]; endothelial cell development [GO:0001885]; menaquinone biosynthetic process [GO:0009234]; phylloquinone biosynthetic process [GO:0042372]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate [GO:0032194]; vitam... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; antioxidant activity [GO:0016209]; prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000... | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; Evidence={EC... | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}. | null | null | FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquin... | Ailuropoda melanoleuca (Giant panda) |
D2HNY3 | FAN1_AILME | MSEGKSPAKKRARRSLSISKTKKNECNSIISFFNNVPPAKLACPICSKMVPRYDLNWHLDEKCANNDNITPVDLRHVGFTDSSGSTVNLTNTVLENVTPGKLSPSKASLTPDPSDSAKMGIKQQTSPYFKNNKDLVFKNQDKLRHHNVKVITLGSLSSKLSRRYTEARRSICKKNEEFASKSPQSPSSTVVRSPVDNCSEIEDKDQILENSSQKENVFTCDSLNEQRTEHSVEDTKVLEAESQEATQECGRSPLTPAFSDNAFVLFSPDLTRGNPLRSTSEDSLEWETITGIDGKDVEKCEAGSCEEVKVTVASEAKTQL... | 3.1.21.-; 3.1.4.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:Q9I2N0, ECO:0000250|UniProtKB:Q9Y2M0}; | DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; nucleotide-excision repair [GO:0006289] | nucleus [GO:0005634] | 5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; flap-structured DNA binding [GO:0070336]; metal ion binding [GO:0046872]; phosphodiesterase I activity [GO:0004528]; ubiquitin-dependent protein binding [GO:0140036] | PF21315;PF21169;PF21170;PF08774; | 3.40.1350.10; | FAN1 family | PTM: Ubiquitinated and degraded during mitotic exit by the APC/C-Cdh1 complex. {ECO:0000250|UniProtKB:Q9Y2M0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}. Note=Localizes at sites of DNA damage following recruitment by monoubiquitinated FANCD2. Localizes to stalled replication forks via its UBZ4-type zinc finger. {ECO:0000250|UniProtKB:Q9Y2M0}. | CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; | null | null | null | null | FUNCTION: Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination interme... | Ailuropoda melanoleuca (Giant panda) |
D2HS90 | STPAP_AILME | MAAVDLDVQSLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSAQLTQYFQAFGPVASVVMDKDKGVFAIVEMGDVGTREAVLSQPQHTLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLTKALAEAPDVGAQMVKLVGLRELSEAERQLRNLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEESQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPSPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLQEDRGEGDLG... | 2.7.7.19; 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Note=Binds 1 divalent cation per subunit. {ECO:0000250|UniProtKB:Q9H6E5}; | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; snRNA processing [GO:0016180]; U6 snRNA 3'-end processing [GO:0034477] | mitochondrion [GO:0005739]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; enzyme-substrate adaptor activity [GO:0140767]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265]; U6 snRNA binding [GO:0017070] | PF03828;PF00076;PF12874; | 1.10.1410.10;3.30.70.330;3.30.460.10; | DNA polymerase type-B-like family | PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region. {ECO:0000250|UniProtKB:Q9H6E5}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; CATALYTIC ACTIVITY: Reaction=A... | null | null | null | null | FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of t... | Ailuropoda melanoleuca (Giant panda) |
D2HWM5 | RFWD3_AILME | MAQEAMEYNVDEQLEHRVAEQPVPAEVVSTQGGPPPLQPLPTEVVSSQGAPPLLQPAPAEGTSSQVGPHLLQPAAQLSVDLTEEVELLGEDRVENINPGASEEHRQPSRVNRPIPVSSLDSMNSFISGLQRLHGMLEFLRPPSDHNVGPVRSRRRRGSASRRSRTVGSQRTDSARSRAPLDAYFQVSRTQPHLPSMSQDSETRNPVSEDLQVSSSSSSDSESSAEYEEVVVQAEDTRAVVSEEQGGTAAEQEVTCVGGGETLPKQSPQKTNPLLPSVSKDDEEGDTCTICFEHWTNAGDHRLSALRCGHLFGYKCISKWL... | 2.3.2.27 | null | DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; protein ubiquitination [GO:0016567]; regulation of DNA damage checkpoint [GO:2000001]; replication fork processing ... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PML body [GO:0016605]; site of DNA damage [GO:0090734]; site of double-strand break [GO:0035861] | MDM2/MDM4 family protein binding [GO:0097371]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; ubiquitin protein ligase activity [GO:0061630] | PF13639; | 2.130.10.10;3.30.40.10; | null | PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence. {ECO:0000250|UniProtK... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PCD5}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6PCD5}. Cytoplasm {ECO:0000250|UniProtKB:Q6PCD5}. Note=In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies. In response to replication block, such as that ... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q6PCD5}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q6PCD5}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leadi... | Ailuropoda melanoleuca (Giant panda) |
D2HXI8 | GWL_AILME | MEPTAGSEKESEGDTVTGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFFTPVAEKNKDSANILSTHVSETSQLSQGLVCPMSVDHRDTTPYSSKLLNSCLETVAPNPGMPVKCLTSHLLQSRRRLATSSASSQSHTFVSSVESECHSS... | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; female meiosis II [GO:0007147]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:... | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-744 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | 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: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and E... | Ailuropoda melanoleuca (Giant panda) |
D2IYS2 | TORSO_BOMMO | MYSEGKLLKVFLIFAGFIIFSLCGEVVSQRYPPAPGLLKYLEQDVCYSLYYYLNWTSLADCKTNFEETGISDVPSTVKVRCQSKNSIRFETEPSEHWQLFILMEHDNFDPIPFTLIEPNNVFGELITTANKEYQIWSTYLDEYGTLQDWMEGPIVLKFDQRNQQPDDIKYNVTQEFKYIILGNDSYTINGKFVWNTTGDRDLCFDIANICQNTNMKHAKIWPTAHPSFDVENLVLNDECEIHVKGIHGTTKHKYKTPSCFELPECFLNNMEPEIPQDVAIAADQDLRGWWNINVAWAKPHFQPEIYNVTVRANMIRSIIL... | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | phosphorylation [GO:0016310]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF21468; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: May be auto-phosphorylated on tyrosine residues. {ECO:0000269|PubMed:26928300}.; PTM: At least one of the 3 cysteine residues Cys-381, Cys-393 or Cys-394 is involved in the formation of interchain disulfide bonds. The disulfide bond sites in the extracellular region are not involved in homodimer formation. {ECO:00... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19965758}; Single-pass type I membrane protein {ECO:0000305}. | 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: Probable receptor tyrosine kinase. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone (PTTH) (By similarity). Binding to PTTH stimulates activation of canonical MAPK signaling leading to ERK ph... | Bombyx mori (Silk moth) |
D2J0Y4 | CJ090_MOUSE | MISPVVISRLIDEKKSMENGAILPQAIAQPQLCPTKPALARRDGVSMHRRFALSPDRLGILTPSDDQGLETEPLSTGDNLGKGSHSGFSSITITARRVGPPASSLVWDTFRDPLCPKCKAKDALFQEPPVLAGDAHLCQHNRPFTCTESPSNGSVEGMKVFQAHSRLSARQDYWVTHTNDNEDSFSSDNSPSRKVPLVFSSCVHFRVSQQCPNAIYYLDKSLSVPLERPQIASPKMHRSVLSLSLRCSSHQLTADGVDSSANGEPISTALSQELSEGKQDLLGPQWGQPQGGHWKESPALVPVHLGSGTCPRTGSPPLEN... | 2.3.2.- | null | DNA damage response [GO:0006974]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of cell growth [GO:0030308]; protein polyubiquitination [GO:0000209]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of centriole replication [GO:0046599]; response to ioni... | centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829] | histone deacetylase binding [GO:0042826]; microtubule binding [GO:0008017]; ubiquitin protein ligase activity [GO:0061630] | PF15309;PF17730; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96M02}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96M02}. Note=Localizes to the actin cytoskeleton in a proportion of cells. Colocalizes with centriolar acetylated tubulin (By similarity). {ECO:0000250, ECO:0000250|... | null | null | null | null | null | FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage (PubMed:20154723, PubMed:20843368, PubMed:24240685). Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits ubiquitin ligase (E3) activity and ass... | Mus musculus (Mouse) |
D2KC46 | PKHA8_CANLF | MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTRMDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSELRLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSELLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELNSCENGSLHMEINDGEEILMKNKSSLYLKPEIDCSISSEENTDDNITVQGEIMKEEGEDNLGNHDSSLAQPASDSSSSPPESHWEEGQEIIPTFFSTMNTSFS... | null | null | ceramide transport [GO:0035627]; ER to Golgi ceramide transport [GO:0035621]; intermembrane lipid transfer [GO:0120009]; lipid transport [GO:0006869]; protein transport [GO:0015031] | cytosol [GO:0005829]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | ceramide 1-phosphate binding [GO:1902387]; ceramide 1-phosphate transfer activity [GO:1902388]; ceramide binding [GO:0097001]; glycolipid binding [GO:0051861]; glycolipid transfer activity [GO:0017089]; identical protein binding [GO:0042802]; phosphatidylinositol-4-phosphate binding [GO:0070273] | PF08718;PF00169; | 1.10.3520.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q96JA3}. Membrane {ECO:0000250|UniProtKB:Q96JA3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JA3}. Note=Binds through its PH domain to PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites. {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: Cargo transport protein that is required for apical transport from the trans-Golgi network (TGN). Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and... | Canis lupus familiaris (Dog) (Canis familiaris) |
D2KX21 | PLAT1_RAT | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS | 2.3.1.-; 3.1.1.32; 3.1.1.4 | null | ether lipid metabolic process [GO:0046485]; lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008]; peroxisome organization [GO:0007031]; phosphatidylcholine metabolic process [GO:0046470] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope lumen [GO:0005641]; nucleus [GO:0005634]; peroxisome [GO:0005777] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; N-acyltransferase activity [GO:0016410]; O-acyltransferase activity [GO:0008374]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]; phospholipase activity [GO:0004... | PF04970; | 3.90.1720.10; | H-rev107 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9QZU4}. Nucleus {ECO:0000250|UniProtKB:Q9QZU4}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9QZU4}; Physiologica... | null | null | null | null | FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing ... | Rattus norvegicus (Rat) |
D2W6T1 | TET1_NAEGR | MTTFKQQTIKEKETKRKYCIKGTTANLTQTHPNGPVCVNRGEEVANTTTLLDSGGGINKKSLLQNLLSKCKTTFQQSFTNANITLKDEKWLKNVRTAYFVCDHDGSVELAYLPNVLPKELVEEFTEKFESIQTGRKKDTGYSGILDNSMPFNYVTADLSQELGQYLSEIVNPQINYYISKLLTCVSSRTINYLVSLNDSYYALNNCLYPSTAFNSLKPSNDGHRIRKPHKDNLDITPSSLFYFGNFQNTEGYLELTDKNCKVFVQPGDVLFFKGNEYKHVVANITSGWRIGLVYFAHKGSKTKPYYEDTQKNSLKIHKET... | 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; | null | null | 5-methylcytosine dioxygenase activity [GO:0070579]; double-stranded methylated DNA binding [GO:0010385]; iron ion binding [GO:0005506] | null | 3.60.130.30; | null | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEB... | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), and thereby plays a role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). ... | Naegleria gruberi (Amoeba) |
D2WL32 | GLGB3_ARATH | MVSLSNQTRFSFHPNNLVVSEKRRLGISGVNFPRKIKLKITCFAAERPRQEKQKKKSQSQSTSDAEAGVDPVGFLTRLGIADRIFAQFLRERHKALKDLKDEIFKRHFDFRDFASGFELLGMHRHMEHRVDFMDWGPGSRYGAIIGDFNGWSPTENAAREGLFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDYDKGDSGVSAEEIFQKANDEYWEPGEDRFIKNRFEVPAKLYEQMFGPNSPQTLEELGDIPDAETRYKQWKEEHKDDPPSNLPPCDIIDKGQGKPYDIFNVVTSPEWTKKFYEKEPPIPYWLE... | 2.4.1.18 | null | carbohydrate metabolic process [GO:0005975]; glycogen biosynthetic process [GO:0005978]; post-embryonic development [GO:0009791]; starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; plastid [GO:0009536] | 1,4-alpha-glucan branching enzyme activity [GO:0003844]; 1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) [GO:0102752]; cation binding [GO:0043169] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family, GlgB subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20377688}. Plastid, amyloplast {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Essential during embryogenesis. {ECO:0000269|PubMed:17028209, ECO:000026... | Arabidopsis thaliana (Mouse-ear cress) |
D2X8K2 | PA2_CONGI | GVWQFAYMIAKYTGRNPLDYWGYGCWCGLGGKGNPVDAVDRCCYVHDVCYNSITQGPRPTCSRIAPYHKNYYFTGKKCSTGWLTSKCGRAICACDIAAVKCFRRNHFNKKYRLYKKNIC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:20562011}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:20562011}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in induction of edema in another organism [GO:0044398]; envenomation resulting in myocyte killing in another organism [GO:0044522]; hemostasis [GO:0007599]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; suppression of b... | extracellular region [GO:0005576]; nematocyst [GO:0042151] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Sea anemone phospholipase A2 (PLA2). When incubated with plasma, this protein shows a moderate anticoagulant activity (0.15 ug of enzyme/200 uL of plasma), inhibiting clotting induced by thrombin. This enzyme also induces myotoxicity, and edema. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl gr... | Condylactis gigantea (Giant Caribbean anemone) (Condylactis passiflora) |
D2XV59 | GTPB1_RAT | MAAERSRSPVDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQESGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQE... | null | null | cytoplasmic translation [GO:0002181]; GTP metabolic process [GO:0046039]; positive regulation of mRNA catabolic process [GO:0061014]; translational elongation [GO:0006414] | cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829] | alpha-aminoacyl-tRNA binding [GO:1904678]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049] | PF00009;PF03144; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, GTPBP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21515746}. | null | null | null | null | null | FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity. {ECO:0000269|PubMed:21515746}. | Rattus norvegicus (Rat) |
D2Y1X6 | H1A01_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X7 | H1A02_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFTVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X8 | H1A03_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEVRECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X9 | H3A01_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y0 | H3A02_CYRHA | MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y1 | H3A03_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFALDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y2 | H3A04_CYRHA | MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGKERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y3 | H3A05_CYRHA | MKASRFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z4 | H3A06_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKESPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z7 | H3A07_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKVFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z8 | H3A08_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFTGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y232 | H4A01_CYRHA | MKASMFLALAGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin that selectively inhibits neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) (IC(50)=44.6 nM) (PubMed:12518233, PubMed:14512091). It is active on Nav1.2/SCN2A (IC(50)=22.4 nM), Nav1.6/SCN8A (IC(50)=50.1 nM) and Nav1.7/SCN9A (IC(50)=48.9 nM) (PubMed:29703751). It shows low affinity ... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y233 | H4A02_CYRHA | MKASMFLALAGLDLLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels. {ECO:0000269|PubMed:12518233, ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D1 | H3A09_CYRHA | MKASMFLALAGLALLFVVCYASESEEKEFPIELLSKIFAVDVFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D2 | H3A10_CYRHA | MKASMFLALAGLVRLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D3 | H3A11_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKDFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D7 | H4A03_CYRHA | MKASMFLALTGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels. {ECO:0000269|PubMed:12518233, ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2I3 | H3A12_CYRHA | MKASMFLALAGLVLLFVVGYASGSEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and... | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Z026 | DCSC_STRLA | MIRMRTPSTLPFTKMHGAGNDFVVLDLRDGPDPSPELCRALADRHKGVGCDLVLGIREPRSARAVAAFDIWTADGSRSAQCGNGARCVAAWAVRAGLARGPRFALDSPSGTHEVDVLDADTFRVALAVPRFAPESIPLFGHDGEQDLYEADLGDGTRVRFAAVSMGNPHAVIEVDDTATAPVARVGRAVQASGLFLPTVNVGFARVESRDRVHLRVHEYGAGETLACGSGACAAAAVLMRRGRVDRNVSVVLPGGELRISWPDDAADVLMTGPAAFVYEGTFLHASV | 5.1.1.19 | null | antibiotic biosynthetic process [GO:0017000]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | diaminopimelate epimerase activity [GO:0008837]; racemase and epimerase activity, acting on amino acids and derivatives [GO:0016855] | PF01678; | null | Diaminopimelate epimerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=O-ureido-L-serine = O-ureido-D-serine; Xref=Rhea:RHEA:36707, ChEBI:CHEBI:73389, ChEBI:CHEBI:74158; EC=5.1.1.19; Evidence={ECO:0000269|PubMed:22307920, ECO:0000269|PubMed:23529730}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 mM for O-ureido-D-serine (at 30 degrees Celsius) {ECO:0000269|PubMed:22307920}; KM=110 mM for O-ureido-L-serine (at 30 degrees Celsius) {ECO:0000269|PubMed:22307920}; Note=kcat is 158 sec(-1) and 29 sec(-1) for O-ureido-L-serine and O-ureido-D-serine, respective... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:22307920}; | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the stereoinversion of O-ureido-L-serine to O-ureido-D-serine. {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:22307920, ECO:0000269|PubMed:23529730}. | Streptomyces lavendulae |
D2Z027 | DCSD_STRLA | MPLFNSILDTIGRTPIVRLQRMAPEHTSVYVKVESFNPGGSVKDRLALSVVLDAEAKGLLKPGDTIVECTSGNVGIALAMVAAARGYRFVAVMGDTYSVERRKLIRAYGGKLVLFPGHLGSKGGNLIADELAEKYGWFRARQFDNPANPSYHRETTASEILADFAGKRLDHFVTGFGTTGTLTGVGQMLRVARPEVRVVALEPSNAAMLARGEWSPHQIQGLAPNFVPGVLDRSVIDDLVTMDEVTARDTSRRLAAEEGIFAGISAGATVATALSIAEHAPEGTVLLAMLPDTGERYLSTFLFDGVDEGSDDAWLASLDT... | 2.5.1.47; 2.6.99.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937, ECO:0007744|PDB:3X43}; | antibiotic biosynthetic process [GO:0017000]; cysteine biosynthetic process from serine [GO:0006535] | cytoplasm [GO:0005737] | cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146] | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydroxyurea + O-acetyl-L-serine = acetate + H(+) + O-ureido-L-serine; Xref=Rhea:RHEA:36263, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44423, ChEBI:CHEBI:58340, ChEBI:CHEBI:73389; EC=2.6.99.3; Evidence={ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937}; CATALYTIC ACTIVITY: Re... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 mM for OAS {ECO:0000269|PubMed:23529730}; KM=190 mM for OAS {ECO:0000269|PubMed:26207937}; KM=0.12 mM for hydrogen sulfide {ECO:0000269|PubMed:26207937}; | null | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent (PubMed:20086163). Catalyzes the addition of hydroxyurea on O-acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as the second substrate, followed by h... | Streptomyces lavendulae |
D2Z028 | DCSE_STRLA | MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDI... | 2.3.1.30; 2.3.1.31 | null | cysteine biosynthetic process from serine [GO:0006535]; homoserine metabolic process [GO:0009092]; methionine biosynthetic process [GO:0009086] | cytoplasm [GO:0005737] | homoserine O-acetyltransferase activity [GO:0004414]; O-succinyltransferase activity [GO:0016750]; serine O-acetyltransferase activity [GO:0009001] | PF00561; | 1.10.1740.110;3.40.50.1820; | AB hydrolase superfamily, MetX family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine; Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30; Evidence={ECO:0000269|PubMed:20086163}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.9 mM for L-serine (at 30 degrees Celsius and pH 8) {ECO:0000269|PubMed:23396912}; KM=98 mM for L-homoserine (at 30 degrees Celsius and pH 8) {ECO:0000269|PubMed:23396912}; Note=kcat is 95 min(-1) and 88 min(-1) for L-serine and L-homoserine, respectively (at 30 d... | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:20086163}. | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over ... | Streptomyces lavendulae |
D2Z030 | DCSG_STRLA | MGILALVTDAVSLPIDYDMPPLLEACRTVGITAEVCDWEDGTVDWSRFEAVVFRSPWTWAERQAEFLAFCERVSHVTRLITPMPLVRWALDKRYLADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLKP | 6.3.3.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31793174}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:31793174}; | antibiotic biosynthetic process [GO:0017000] | null | ATP binding [GO:0005524]; cyclo-ligase activity [GO:0016882]; metal ion binding [GO:0046872] | null | 3.40.50.20;3.30.1490.20;3.30.470.20; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H(+) + H2O + O-ureido-D-serine = ADP + CO2 + D-cycloserine + NH4(+) + phosphate; Xref=Rhea:RHEA:36711, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:74158, ChEBI:CHEBI:75929, ChEBI:CHEBI:456216; EC=6.3.3.5... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for O-ureido-D-serine (D-OUS) in the presence of 5 mM ATP {ECO:0000269|PubMed:31793174}; KM=10 mM for D-OUS in the presence of 5 mM ATP {ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26578703}; KM=19 mM for D-homocysteine {ECO:0000269|PubMed:23529730, ECO:... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:23529730}; | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the synthesis of D-cycloserine from O-ureido-D-serine (D-OUS). It reacts with D-OUS, D-homocysteine and beta-aminooxy-D-alanine. {ECO:0000269|PubMed:20086163,... | Streptomyces lavendulae |
D3DJG4 | SOXA1_HYDTT | MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:O33434}; Note=Binds 2 heme c groups covalently per subunit. {ECO:0000250|UniProtKB:O33434}; | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; transferase activity [GO:0016740] | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-214. {ECO:0000250|UniProtKB:O33434}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:O33434}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:2... | null | null | null | null | FUNCTION: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. ... | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3DJG5 | SOXA2_HYDTT | MRKLWFLPILLGAVGGVSLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDTFGGQRIRLQTLAKVKEDKVATHWPAYRFSNDQLWTMEDRIRGCYNQIRVTPPPHFSWPQIALSLYMAYESKGGTIETPGFVR | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:O33434}; Note=Binds 2 heme c groups covalently per subunit. {ECO:0000250|UniProtKB:O33434}; | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; transferase activity [GO:0016740] | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-220. {ECO:0000250|UniProtKB:O33434}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:O33434}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:2... | null | null | null | null | FUNCTION: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. ... | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3DKC4 | GLYA_HYDTT | MRHLFNTDAEIYEAIVKEYERQFYHLELIASENFTSLAVMEAQGSVMTNKYAEGLPHKRYYGGCEFVDIAEDLAIERAKALFDAEHANVQPHSGTQANMAVYMAVLKPGDTIMGMDLSHGGHLTHGAKVNFSGKIYNAVYYGVHPETHLIDYDQLYRLAKEHKPKLIVGGASAYPRVIDWAKLREIADSVGAYLMVDMAHYAGLIAGGVYPNPVPYAHFVTSTTHKTLRGPRSGFILCKKEFAKDIDKSVFPGIQGGPLMHVIAAKAVAFKEAMSQEFKEYARQVVANARVLAEEFIKEGFKVVSGGTDSHIVLLDLRDT... | 2.1.2.1; 4.1.2.48 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; L-allo-threonine aldolase activity [GO:0008732]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; CATALYTIC ACTIVITY: Reaction=L-threonine = acetaldehyde +... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 mM for L-serine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=0.78 mM for glycine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=7.64 mM for L-threonine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:2214134... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}.; PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 for the THF-independent L-allothreonine aldolase activity. More than 95% of full activity remains at pH 8.4, although the activities are reduced to about 90% at pH 6.9 and about 75% at pH 5.9. {ECO:0000269|PubMed:22141341}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Retains almost complete THF-independent L-allo-threonine aldolase activity after being incubated at 75 degrees Celsius for 10 minutes, and retains about 77% residual activity after being treated at 87 degrees Celsius for the same time. {ECO:00... | FUNCTION: Its primary function is to catalyze the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecu... | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3GDK4 | GUN_CRYAT | MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810] | PF02015; | 2.40.40.10; | Glycosyl hydrolase 45 (cellulase K) family | PTM: N- and O-glycosylated. Contains hybrid- and complex-type N-glycans. {ECO:0000269|PubMed:24848382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24848382}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10069, ECO:0000269|PubMed:22333528, ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 (PubMed:24848382, PubMed:28156112). More than 90% of the maximal activity is maintained between pH range 3-5 (PubMed:24848382). More than 60% of the maximal activity is maintained between pH range 2-8 (PubMed:24848382, PubMed:28156112). About 80% of the m... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 40-50 degrees Celsius (PubMed:24848382, PubMed:28156112). Has more than 50% of the maximal activity between 10-70 degrees Celsius, and more than 30% of activity at 0 degrees Celsius. Stable at 50 degrees Celsius for 30 minutes (PubMed... | FUNCTION: Hydrolyzes carboxymethylcellulose (CMC) (PubMed:24848382, PubMed:28156112). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is compl... | Cryptopygus antarcticus (Antarctic springtail) |
D3GE74 | STR1_MEDTR | MARLERDGTNKSLESLMDSHKPGGTTTNLNQLRTQKSIPGYGLEFTNLSYSIIKKQKKDGVWINKETYLLHDISGQAIKGEIMAIMGPSGAGKSTFLDALAGRIAKGSLQGSVRIDGKPVTTSYMKMVSSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRDEKKKRVHELLNKLGLQSATHTYIGDEGRRGVSGGERRRVSIGIEIIHKPSLLFLDEPTSGLDSTSAYSVVEKIKDIAQGGSIVLMTIHQPSFRIQMLLDKITILARGRLIYMGRPDALHTHLSGFGRPVPDGENNIEYLLDVITEYDQATVGLDPLV... | 7.6.2.- | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF01061;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Stunted arbuscule (STR) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20453115}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000269|PubMed:20453115}. | null | null | null | null | null | FUNCTION: Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis. {ECO:0000269|PubMed:20453115}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
D3J162 | VPY_MEDTR | MDRLIKLDPSNIVLIRVEEGQKCLGKITLNNVMYTMPVAFRIQPLIKTRYTIKPQSGIISPLASLVIEITYHPPQQQGSNNLPHSFPFSDDSFLLHSVLAPGAAIKEPSSMFDSVPSDWFTTKKKQVFIDSAIKVMFVGSQILTQLVEDGNSMDDIREVLEKSDPLWESVNSKDSQGQTLLHLAISKTRPDLVQLILEFKPDIEAINSVGSTPLEAASSSGESLIVELLLAHKANTEGSESSVFRPIHHASREGHMEILRLLLLKGARVDSLTKDGNTSLHLAVEEKRRDCARLLLANGARTDVRNMREGDTPLHIAAAN... | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877]; response to molecule of bacterial origin [GO:0002237]; response to symbiotic bacterium [GO:0009609]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | null | PF12796;PF00635; | 1.25.40.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:21223389}. Nucleus {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:21223389}. Cell membrane {ECO:0000269|PubMed:26234213}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=In cells containing arbuscular myco... | null | null | null | null | null | FUNCTION: Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme and Gigaspora gigantea) both during fungal passage across root epidermis and for arbuscule formation in cortical cells; this symbiosis promotes phosphorus (P) and copper (Cu) uptake (PubMed:19912567, PubMed:21223389). Ess... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
D3K0R6 | AT2B4_BOVIN | MTNPTEHTLPSNSILESREGEFGCTVMDLRKLMELRSSDAIDQINVHYGGVMNLCSRLKTNPVEGLSGNPADLEKRKQVFGQNLIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGGENEQCGLAVTSPEDEGEAEAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQNRIEKEQKFSVIRNGHIIQLPVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLERDPMLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGASEGEEEEKKKKGKKQGVPENRNKAKTQDGVA... | 7.2.2.10 | null | cellular response to acetylcholine [GO:1905145]; flagellated sperm motility [GO:0030317]; intracellular calcium ion homeostasis [GO:0006874]; regulation of cytosolic calcium ion concentration [GO:0051480]; urinary bladder smooth muscle contraction [GO:0014832] | intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165] | PF12424;PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21187283}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P23634}; | null | null | null | null | FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cells calcium homeostasis, may play a role in sperm motility (By similarity). {ECO:0000250|UniProtKB:P23634, ECO:0000250|U... | Bos taurus (Bovine) |
D3K5I7 | NCAP_RVFV | MDNYQELAIQFAAQAVDRNEIEQWVREFAYQGFDARRVIELLKQYGGADWEKDAKKMIVLALTRGNKPRRMMMKMSKEGKATVEALINKYKLKEGNPSRDELTLSRVAAALAGRTCQALVVLSEWLPVTGTTMDGLSPAYPRHMMHPSFAGMVDPSLPGDYLRAILDAHSLYLLQFSRVINPNLRGRTKEEVAATFTQPMNAAVNSNFISHEKRREFLKAFGLVDSNGKPSAAVMAAAQAYKTAA | null | null | null | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF05733; | null | Phlebovirus nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:34960686}. Host cytoplasm {ECO:0000269|PubMed:34960686}. Host nucleus {ECO:0000269|PubMed:34960686}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi apparatus {ECO:0000250|UniProtKB:I6WJ72}. | null | null | null | null | null | FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases (Probable) (PubMed:20547879). Displays high affinity for single-stranded nucleic acid (PubMed:23129612). The encapsidated genomic RNA is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:20547879). The ribonucleoprotein has a non-helical struc... | Rift valley fever virus (RVFV) |
D3KCC4 | CRNS1_CHICK | MISVDRLSEEQALGMKEQEWAGPEALCPGWQEEEVSDGEGPEDSGHPDPTAHAYEVLQHTLRLEGMPLTIDRTGQPRTGSGPLDMTVCVLGSPTAFLPVLLEGGTRYPGAMVLCLAPAWASRVPSETSPGSWSLLLSRGVSFEAGGCTALEEFVPPRRATYVTGTFGSEGSWEGELARDLDCPTGGSALLTRWLEDPLLSRWLLSARAGLPVPPTLAFITGLWETLPEEPEPPGVHLVRLQDPQGQESLVRDEVGAFLEGSSMQPYDQVAVRLSGWRWRGTDPHSTHRKVEGEAVAQAVAALLKGLREEESILLEALVPT... | 6.3.2.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | carnosine biosynthetic process [GO:0035499] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; carnosine synthase activity [GO:0047730]; homocarnosine synthase activity [GO:0102102]; metal ion binding [GO:0046872] | PF18130;PF15632; | 3.40.50.20;3.30.470.20; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + L-histidine = ADP + carnosine + H(+) + phosphate; Xref=Rhea:RHEA:19297, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57485, ChEBI:CHEBI:57595, ChEBI:CHEBI:57966, ChEBI:CHEBI:456216; EC=6.3.2.11; Evidence={ECO:0000269|PubMed:20097752}; Physiologic... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.033 mM for beta-alanine {ECO:0000269|PubMed:20097752}; KM=0.35 mM for 4-aminobutanoate {ECO:0000269|PubMed:20097752}; KM=0.1 mM for L-histidine {ECO:0000269|PubMed:20097752}; KM=1.42 mM for L-lysine {ECO:0000269|PubMed:20097752}; KM=1.62 mM for L-ornithine {ECO:0... | null | null | null | FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}. | Gallus gallus (Chicken) |
D3KU66 | ASMT_MOUSE | MHRGRSASARQERDFRALMDLAHGFMASQVLFAGCALRVFDAAALGPVDAAALARSSGLSPRGTRLLLDACAGLGLLRRRRGAGPRGPAYTNSPLASTFLVAGSPLSQRSLLLYLAGTTYLCWGHLADGVREGRSQYARAVGVDADDPFTAIYRSEAERLLFMRGLQETWSLCGGRVLTAFDLSPFRVICDLGGGSGALARMAARLYPGSEVTVFETPDVVAAARAHFPPPADEDGAEPRVRFLSGDFFRSPLPPADLYVLARVLHDWADAACVELLRRVRGALRPGGAVLLVESVLSPGGAGPTRTLLLSLTMLLQARG... | 2.1.1.4 | null | lipid metabolic process [GO:0006629]; male gonad development [GO:0008584]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; negative regulation of male gonad development [GO:2000019] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF16864;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378, ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.4; Evidence={ECO:0000269|PubMed:20308563}; PhysiologicalDirection=left-to... | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. {ECO:0000269|PubMed:20308563}. | null | null | FUNCTION: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). {ECO:0000269|PubMed:20308563}. | Mus musculus (Mouse) |
D3KZG3 | TMC1_CAEEL | MQEAARRASLRKEHTPTNEKFGDLSKQDSLGERASSKLTLDDELYDILYAFGETDAFINKGDKQRETDEDGNPLTRQALLERIRQKKEVIGKLRCQAWSMTRKRRTLKLAQKYLEQHESKVSRSHLYMEEMRKRARLMKRSFSNFKTYLIPWESKIKRIESHFGSVVSSYFTFLRWIVFVNIMITLIALVFVVLPETLADSVANEGRFNRTKTRKQIPANERVHADELAVVWHYDGYLRYSPLFYGYYSDDPFLGNKIKYALPLAYFMVTLTIFAYSFFAILRKMAANARMSKLSGSKAEQYIFNWKLFTGWDYTIGNSE... | null | null | detection of stimulus involved in sensory perception [GO:0050906]; monoatomic ion transmembrane transport [GO:0034220]; sensory perception of chemical stimulus [GO:0007606] | neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic ion channel activity [GO:0005216]; sodium channel activity [GO:0005272] | PF07810; | null | TMC family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23364694}; Multi-pass membrane protein {ECO:0000269|PubMed:23364694}. | null | null | null | null | null | FUNCTION: Sodium-sensor ion channel that acts specifically in salt taste chemosensation. Required for salt-evoked neuronal activity and behavioral avoidance of high concentrations of NaCl. {ECO:0000269|PubMed:23364694}. | Caenorhabditis elegans |
D3RVD4 | TSDA_ALLVD | MRGDVRVHTASPIAAAWLLAVGLVAHAEEPPTVALTVPAAALLPDGALGESIVRGRRYLSDTPAQLPDFVGNGLACRHCHPGRDGEVGTEANAAPFVGVVGRFPQYSARHGRLITLEQRIGDCFERSLNGRALALDHPALIDMLAYMSWLSQGVPVGAVVAGHGIPTLTLEREPDGVHGEALYQARCLACHGADGSGTLDADGRYLFPPLWGPRSFNTGAGMNRQATAAGFIKHKMPLGADDSLSDEEAWDVAGFVLTHPRPLFQEPTGD | 1.8.2.2 | null | null | periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; thiosulfate dehydrogenase activity [GO:0050338] | PF13442;PF21342; | 1.10.760.10; | null | PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000269|PubMed:22779704}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16995898}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + 2 thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + tetrathionate; Xref=Rhea:RHEA:20549, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15226, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542; EC=1.8.2.2; Evidence={ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=30000 umol/min/mg enzyme (with 1 mM ferricyanide) {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.2. {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}; | null | FUNCTION: Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate. {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}. | Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum) |
D3TTC1 | VM3KL_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQFTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNE... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF01562;PF01421; | 3.40.1620.60;3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that cleaves the membrane-bound precursor of TNF-alpha (TNF) into its mature soluble form showing the same digestion pattern than ADAM17. {ECO:0000269|PubMed:19932752}. | Naja atra (Chinese cobra) |
D3TTC2 | VM3H_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQAKKYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKKLLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKT... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that seems to inhibit cell migration. This activity is dominated by the local structure of the hyper-variable region. {ECO:0000269|PubMed:19932752}. | Naja atra (Chinese cobra) |
D3UW23 | AMPE_BITRH | MDIEDKTSKMHCMKGKHVVIICGVVIAVGLILGLGLGLGLDTKACNPPEVNGQVSTKSPISNTPDVTSPSGSSVFCSAKNDENGPWTHFRLPNYVHPVHYDLHLTPEMEAEVYTGMVNISIRLEEQTTKHLWLHLRETKITEMPQLWTSSGQVIEIKRCFGYEPQEYVVIEAEEDLRPSNYFLSMRFKGYLNGSLVGFYSTTYGENGKIKYIAATDHEPTDARKSFPCFDEPNKKATYTISITHEHDYEAISNMPVEKTISLDNKWTKTIFKKSVPMSTYLVAWAVHQFKYEERISSRGIPLRIYAQPQQINTAIYAANV... | 3.4.11.7 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q07075}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q07075}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: N-glycosylated. Glycosylation counts for an increased mass of about 32% of the protein mass (about 48 kDa). {ECO:0000269|PubMed:20706583}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein {ECO:0000255}. Note=Found in the venom as transmembrane proteins in exosome-like vesicles. {ECO:0000250|UniProtKB:P0DQU2}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.; EC=3.4.11.7; Evidence={ECO:0000269|PubMed:20706583}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=703 uM for Glu-AMC (in presence of 1.2 mM Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=2478 uM for Asp-AMC (in presence of 1.2 mM Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=2235 uM for Glu-AMC (in absence of Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=4119 uM for Asp-AMC... | null | null | null | FUNCTION: Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium (PubMed:20706583). It may have several roles in venom including alteration of blood pressure by cleaving circulating angiotensin-2, general degradation of host tissue, increase of permeability to other... | Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) |
D3UW26 | IF4EA_SOLTU | MAAAEMERTTSFDAAEKLKAADAGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDSPIAKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVMGADFHCFKHKIEPKWEDPVCANGGTWKMSFLKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRSKGEKIALWTKNAANETAQVSIGKQWKQFLDHSDSVGFIFHDDAKRLDRSAKNRYTV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Solanum tuberosum (Potato) |
D3VML5 | PZNA_BACVZ | MTQIKVPTALIASVHGEGQHLFEPMAARCTCTTIISSSSTF | null | null | cytolysis by symbiont of host cells [GO:0001897]; defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275] | null | null | null | null | PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogen... | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:20971906, ECO:0000269|PubMed:21950656}. | null | null | null | null | null | FUNCTION: Peptide antibiotic inhibiting growth of Gram-positive bacteria in the dimethylated form plantazolicin A. The desmethyl form plantazolicin B has no antibiotic activity. The mode of action appears to be disruption of cell walls and lysis of cells. Inhibits B.subtilis strain HB0042, B.megaterium strain 7A1 and B... | Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) |
D3W0D1 | KLRF2_HUMAN | MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV | null | null | natural killer cell degranulation [GO:0043320]; positive regulation of cytokine production [GO:0001819] | plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; protein homodimerization activity [GO:0042803] | PF00059; | 3.10.100.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:20194751}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20194751}; Single-pass type II membrane protein {ECO:0000269|PubMed:20194751}. | null | null | null | null | null | FUNCTION: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A. {ECO:0000269|PubMed:20194751}. | Homo sapiens (Human) |
D3WYW0 | LSC_LACGS | MLENKKHKKMSLSGKSLLMGTLSTAAIVLSASTVNAATNTDTVDNANASQVTTVKASASVNKNDNSGLKENATNDKVAGTETNLNSSLNSGKETSSQVNDSKEDSSSTQVGSTPISSAIINNGKASSDLNQDSDNISDHFKDNNSQGQSSTSSEKTELKGKIKEIVNNSGIDVTKLTNDQINNLNKVNFDNDPQDGTKLTLNDLDAIGQALIRRDPKYAVPYFNAKEIKNMDAAETKDAQTGKTETLEIWDSWPVQDPITGYVSNYKGYQLVIAMMGMPKKNDNHIYLLYNKYNDNEFSHWRNAGSIFGYNETPDLQEWS... | 2.4.1.10 | null | carbohydrate utilization [GO:0009758] | cell surface [GO:0009986]; extracellular region [GO:0005576] | levansucrase activity [GO:0050053]; metal ion binding [GO:0046872] | PF02435;PF00746; | null | Glycosyl hydrolase 68 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:20075040}. | CATALYTIC ACTIVITY: Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; Evidence... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5-4.5. {ECO:0000269|PubMed:20075040}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Activity drastically decreases at 60 degrees Celsius. {ECO:0000269|PubMed:20075040}; | FUNCTION: Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce levan polymer and the fructo-oligosaccharide (FOS) 1-kestose. Is also able to convert raffinose into a fructan polymer and a single oligosaccharide (most likely Gal-Glc-Frc-Frc) in vitro; however, L.gasseri str... | Lactobacillus gasseri |
D3XDS2 | UL97_MUHVS | MSVELTPPRSDGSVGFAPVVVPPAPRKPLRRRAVSDLEKLYKVKRRLVFGADDGAVDNDTSNNNSGSSSTTSRSRRKTAADVVSDSPKRTDDSSTAGEDGYTHCVHSCACTPGERHLLCCELVSIGDSVSVARCPLCSLGISTTYLSRGCCRGRSKVTGGDEDEEDEDEEENSQDEDRDEEEAASASSSGGLEWSDDSNSALSWSDENIIISPFPGLKCYVTTFEDIRQPVLLETGSAYLPVYVPYDESFCRNRCLERGGDDDDERDATLIGKGSFGQVWRLSDKKTALKAAASESINETLLTVWISGVVRSRAQDAGYR... | 2.7.11.1 | null | phosphorylation [GO:0016310]; viral process [GO:0016032] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674] | PF06734; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, HCMV ganciclovir subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P16788}. Host nucleus {ECO:0000269|PubMed:32973148}. Host cytoplasm {ECO:0000269|PubMed:32973148}. Note=Present in host nucleus at early times but redistributes to a predominantly cytoplasmic localization pattern at 24 hours post infection. {ECO:0000269|PubMed:3297314... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P16788}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that plays important roles in several processes including viral morphogenesis, nuclear viral egress, viral replication or regulation of host cell cycle progression (PubMed:17910700, PubMed:32973148). Participates in the acquisition of tegument during virion morphogenesis in the... | Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus) |
D3YN49 | GEMC1_XENLA | MNTILTCQDEYFAGGLGYDCPYFSSTSASTVDVSKETWVSLWASGLLDNRSSNHGPHTQGQLYNMGNSLQEDYLFGDQLSSQISANKQLQDTLLQKEEELSRLHEENNKLKEFLNSAFVKTLAEKTKKLLHQNGQSSFCTNPNSRVPFSSNSTPGSKAKRARRNLYGELTACEAQSSPVVEKWVLQTLGLKDVDTIDDSALANYSAMSLQPKQDSPSSGYSSAHLTPGHSQAATSCSLSPSQCSSASLPESETASPLSSPTYHTPDVAPNKTEVAFSTSLHPHCNVKTHSFPQGQAFVRRDTQGGWKFTWVPKQSE | null | null | cell cycle [GO:0007049]; DNA replication initiation [GO:0006270]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156] | nucleus [GO:0005634] | chromatin binding [GO:0003682] | null | null | GEMC1 family | PTM: Highly phosphorylated by cdk2; stimulates initiation of DNA replication. {ECO:0000269|PubMed:20383140}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20383140}. Note=Associates with chromatin during pre-replication complex (pre-RC) formation following interaction with topbp1. | null | null | null | null | null | FUNCTION: Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating topbp1- and cdk2-dependent recruitment of cdc45l onto replication origins. {ECO:0000269|PubMed:20383140}. | Xenopus laevis (African clawed frog) |
D3YUJ3 | CCYL1_MOUSE | METRIRAAQLKGRGGAFPKLGRRAGPAEPDYESEVYEAAAGDAVAVAPAPAAAVEPAELDFGAGEGHHLQHISDREMPEDLALESNPSDHPRASTIFLSKSQTDVREKRKSNHLNHVSPGQLTKKYSSCSTIFLDDSTVSQPNLRTTIKCVTLAIYYHIKNRDANRSLDIFDERSHPLTREKVPEEYFKHDPEHKFIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPTNWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNEMERHFLELLQFNINVPASVYAKYYFDLRSLADDNNLNFLFAPL... | null | null | flagellated sperm motility [GO:0030317]; neurogenesis [GO:0022008]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of protein phosphorylation [GO:0001932]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; plasma membrane [GO:0005886] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; protein kinase binding [GO:0019901] | PF00134; | 1.10.472.10; | Cyclin family, Cyclin Y subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26305884, ECO:0000269|PubMed:26590424}. | null | null | null | null | null | FUNCTION: Key regulator of Wnt signaling implicated in various biological processes including male fertility, embryonic neurogenesis and cortex development (PubMed:26305884, PubMed:26590424, PubMed:34431536). Activates the cyclin-dependent kinase CDK16, and promotes sperm maturation (PubMed:26305884, PubMed:26590424). ... | Mus musculus (Mouse) |
D3YVF0 | AKAP5_MOUSE | METSVSEIQVETKDEKGPVAASPQKERQERKTATLCFKRRKKANKTKPKAGSRTAEETKKHTPEAGGSGQRQPAGAWASIKGLVTHRKRSEPAKKQKPPEAEVQPEDGALPKKKAKSRLKFPCLRFSRGAKRSRHSKLTEDSGYVRVQGEADDLEIKAQTQPDDQAIQAGSTQGLQEGVLVRDGKKSQESHISNSVTSGENVIAIELELENKSSAIQMGTPELEKETKVITEKPSVQTQRASLLESSAAGSPRSVTSAAPPSPATTHQHSLEEPSNGIRESAPSGKDDRRKTAAEEKKSGETALGQAEEAAVGQADKRAL... | null | null | amylase secretion [GO:0036394]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; clustering of voltage-gated calcium channels [GO:0070073]; clustering of voltage-gated potassium channels [GO:0045163]; establishment of localization in cell [GO:0051649]; gene expressio... | asymmetric synapse [GO:0032279]; basolateral plasma membrane [GO:0016323]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; dendritic spine membrane [GO:0032591]; excitatory synapse [GO:0060076]; filopodiu... | actin binding [GO:0003779]; adenylate cyclase binding [GO:0008179]; beta-2 adrenergic receptor binding [GO:0031698]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; G protein-coupled receptor binding [GO:0001664]; GABA receptor binding [GO:0050811]; glutamate receptor binding [GO:0035254]; kinase bindin... | PF03832; | null | null | PTM: Palmitoylated. Palmitoylation at Cys-36 and Cys-123 play a key role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis. {ECO:0000250|UniProtKB:P24588}. | SUBCELLULAR LOCATION: Postsynaptic recycling endosome membrane {ECO:0000250|UniProtKB:P24588}; Lipid-anchor {ECO:0000250|UniProtKB:P24588}. Note=Associates with lipid rafts. {ECO:0000250|UniProtKB:P24588}. | null | null | null | null | null | FUNCTION: Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathwa... | Mus musculus (Mouse) |
D3YVL2 | CFA70_MOUSE | MDQTSSTTKIVHITVTNGYDLKGFKGDTPVTFVRAEFNQTVLGDSSKVTVSPEGTAKYNFTSNIDLSPDGGGALDDLAHKPLFLTVTEVLPKEKKQKDEKTLILGQAVVDLLPLLEGEESFETTVPLHPVPGSPLETPLPGSKQCSLDVKVFVAEPLLTPAQVSASNLLKVTLEAAYSVPESFIPVGPQQNYMVGLQVPSVGEKDYTMIFKNGNLKLGGEKEPVPRPKKWPIANILAPGASNIPDEFIVGGPYEEEEGELNHPEDREFRNQAECTKKRIVWDLESRCFLHPFAVASFQKRIADCRLWPVEITRVPLVVMP... | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341] | axoneme [GO:0005930]; extracellular exosome [GO:0070062]; motile cilium [GO:0031514]; outer dynein arm [GO:0036157]; sperm flagellum [GO:0036126] | null | PF13181; | 1.25.40.10; | CFAP70 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:30158508}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q5T0N1}. Cell projection, cilium {ECO:0000269|PubMed:30158508}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30158508}. Note=Present all along the f... | null | null | null | null | null | FUNCTION: Axoneme-binding protein that plays a role in the regulation of ciliary motility and cilium length. {ECO:0000269|PubMed:30158508}. | Mus musculus (Mouse) |
D3YWP0 | EFMT3_MOUSE | MASSRTDPETEPESVFPREIRLFTDSYSESSRFCFCGHELSITQNFGSRLGVAARVWDAALSLCDYFESQNVDFRGKKVIELGAGTGIVGILAALQGGDVTITDLPVALEQIQDNVHANVPPGGRARVCALSWGIDQHVFPGNYDLVLGADIVYLEPTFPLLLGTLRHLCGPHGTIYLASKMRAEHGAETFFRRLLPQHFHLELAQRDEDVNVNIYRARHREVAPAGQHPFC | 2.1.1.- | null | peptidyl-lysine methylation [GO:0018022] | centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991] | heat shock protein binding [GO:0031072]; histone methyltransferase activity [GO:0042054]; methyltransferase activity [GO:0008168]; protein-lysine N-methyltransferase activity [GO:0016279] | PF10294; | 3.40.50.150; | Methyltransferase superfamily, METTL21 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AZ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96AZ1}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; ... | null | null | null | null | FUNCTION: Protein-lysine methyltransferase that selectively mono-, di- and trimethylates 'Lys-165' of the translation elongation factors EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner (By similarity). EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stres... | Mus musculus (Mouse) |
D3YWQ0 | DGKI_MOUSE | MDAAGRGCHLLPLPAARGPARAPAASSALSPTGLCSGTTSASFAAAGAVAMNPSSSAGEERGATGGSSSSGSGAGSCCLGAEGGADPRGAGAAAAAALEEPAAAGQKEKEEALEEKLRDLTFRKQVSYRKAISRTGLQHLAPAHPLGLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWII... | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; excitatory postsynaptic potential [GO:0060079]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; neurotransmitter secretion [GO:0007269]; phosphatidic acid biosynthetic process [GO:0006654]; positive regulation o... | axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; extrinsic component of postsynaptic density membrane [GO:0099147]; extrinsic component of presynaptic active zone membrane [GO:0098891]; glutamatergic synapse [GO:0098978]; guanyl-nuc... | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; GTPase inhibitor activity [GO:0005095]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF12796;PF00130;PF00609;PF00781; | 2.60.200.40;3.30.60.20;1.25.40.20; | Eukaryotic diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:F1MAB7}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1MAB7}. Presynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynaptic density {ECO:0000250|UniProtKB:F1MAB7}. Synaptic cell membrane {ECO:0000250|UniProtKB:... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000250|UniProtKB:O75912}; PhysiologicalDirection=left-to-righ... | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000250|UniProtKB:O75912}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite e... | Mus musculus (Mouse) |
D3YXG0 | HMCN1_MOUSE | MIAQEVVHTVFLVALFRSSLAGDGTPQSESRAEEIPEGASTLAFVFDVTGSMYDDLVQVIEGASKILETSLKRPKRPLYNFALVPFHDPEIGPVTITTDPKKFQYELRELYVQGGGDCPEMSIGAIKIALEISLPGSFIYVFTDARSKDYRLTHEVLQLIQQKQSQVVFVLTGDCDDRNHIGYKVYEEIASTSSGQVFHLDKKQVNEVLKWVEEAVQASKVHLLSTDHLEHAVNTWKIPFDPSLKEVTVSLSGPSPVIEIRNPFGKLIKKGFGLNELLNIHNSAKVVNVKEPEAGMWTVKTSSSGRHSVRITGLSTIDFR... | null | null | actin cytoskeleton organization [GO:0030036]; basement membrane organization [GO:0071711]; cell cycle [GO:0007049]; cell division [GO:0051301]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; response... | adherens junction [GO:0005912]; axon [GO:0030424]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cleavage furrow [GO:0032154]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; muscle tendon junction [GO:0005927]; ne... | axon guidance receptor activity [GO:0008046]; calcium ion binding [GO:0005509] | PF12662;PF07645;PF07474;PF07679;PF13927;PF00090; | 2.40.155.10;2.60.40.10;2.10.25.10;2.20.100.10;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:29488390, ECO:0000269|PubMed:32035013, ECO:0000269|PubMed:34504132}. Cytoplasm {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:29488390}. Cell junct... | null | null | null | null | null | FUNCTION: Involved in transforming growth factor beta-mediated rearrangement of the podocyte cytoskeleton which includes reduction of F-actin fibers and broadening, flattening and elongation of podocytes (By similarity). Plays a role in basement membrane organization (PubMed:34504132). May promote cleavage furrow matur... | Mus musculus (Mouse) |
D3YXJ0 | DGKH_MOUSE | MAGAGSQHHPQGVAGGAVAGASAVSPTAAGPGEDSSDSEAEQEGPQKLIRKVSTSGQMRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEASTKNANNSFTIITPFRRLMLCAENRKEMEVWISSLKSVQSREPYEVAQFNVEHFSGMHNWYACSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDEDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDVYHPVCPLGQCKVSIIPPIALNSTDSDGFCR... | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endosome [GO:0005768]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF00130;PF00609;PF00781;PF00169;PF07647; | 2.60.200.40;3.30.60.20;2.30.29.30;1.10.150.50; | Eukaryotic diacylglycerol kinase family | PTM: Phosphorylated. Phosphorylation does not inhibit catalytic activity. {ECO:0000250|UniProtKB:Q86XP1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27643686}. Cell membrane {ECO:0000269|PubMed:27643686}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27643686}. Note=Translocated from the cytoplasm to endosomes in response to stress stimuli. Isoform 2 is rapidly relocated back to the cytoplasm upon removal of stress ... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:27643686}; PhysiologicalDirection=left-to-right... | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000305|PubMed:27643686}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:27643686). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targ... | Mus musculus (Mouse) |
D3YXK1 | SAMD1_MOUSE | MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRVPRGGPAAPPPTPAPPPAPVAAPTRAPRAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAAAPPAGPRRAPPPAVAAREPPAPPQQQQPPPPQPQPPPEGGAARAGGPARPVSLREVVRYLGGSGGASGRLTRGRVQGLLEEEAARGRLERTRLGALALPRGDRPGRAPPAASARAARSKRGGEERVFEKEEEDEDEDEEEE... | null | null | chromatin organization [GO:0006325]; foam cell differentiation [GO:0090077]; lipoprotein lipid oxidation [GO:0034439]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein homooligomerization [GO:0051260]; regulation of DNA methylation-dependent heterochromatin formation [GO:0090308] | chromosome [GO:0005694]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; low-density lipoprotein particle binding [GO:0030169] | PF00536;PF21524; | 1.10.150.50; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33980486}. Chromosome {ECO:0000269|PubMed:33980486}. Secreted {ECO:0000269|PubMed:34006929}. Note=In atherosclerotic lesions, it is found in the extracellular compartment and in foam cells cytoplasm. {ECO:0000269|PubMed:34006929}. | null | null | null | null | null | FUNCTION: Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor (PubMed:33980486, PubMed:34006929). Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs (PubM... | Mus musculus (Mouse) |
D3YXK2 | SAFB1_MOUSE | MAETLSGLGDASAAGAAAVSSAASETGTRRLSDLRVIDLRAELKKRNLDSSGNKSVLMERLKKAIEDEGGNPDEIEVTSECNKKMPKRPSKGRKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLADSTELVEGDLKGLPEQLQEHAIDDKDTVNNVDTSSSDFTMLQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKREPA... | null | null | hormone metabolic process [GO:0042445]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of growth [GO:0040008]; regulation of mRNA processing [GO:0050684]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00076;PF02037; | 3.30.70.330;1.10.720.30; | null | PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity. {ECO:0000250|UniProtKB:Q15424}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15424}. | null | null | null | null | null | FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Functions as an estrogen receptor corepressor and can ... | Mus musculus (Mouse) |
D3YYI7 | RN217_MOUSE | MGEEQSTVSGSGGARASGGGSAGQPESPRPRGDRVRTAGPRAAASSSRPNGGGGGRDPGCVDASVQEPASNRAPAGQPARLPLSGPLDPQSLELQLEREAEGAGPREAPPGQQPPDGLLLDVLAQRHPPPAKPQVLCSVYCVESDLPEAPSAESPSPSESPPQAPLGPIPASPPPSFPSSPLSLPADPLSPDGGSIELEFYLAPEPFSVPGLLGAPPYSGLGGVGDPYAPLMVLMCRVCLEDKPIKPLPCCKKAVCEECLKIYLSSQVQLGQVEIKCPVTECFEFLEETTVVYNLTHEDSIKYKYFLELGRIDSSTKPCP... | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; membrane [GO:0016020]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01485; | 1.20.120.1750;3.30.40.10; | RBR family, RNF217 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8TC41}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:33895792}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of the iron exporter ferroportin/SLC40A1 and thus regulates iron homeostasis. {ECO:0000269|PubMed:3389... | Mus musculus (Mouse) |
D3YZU1 | SHAN1_MOUSE | MTHSPATSEDEERHSASECPEGGSESDSSPDGPGRGPQGTRGRGSGAPGNLASTRGLQGRSMSVPDDAHFSMMVFRIGIPDLHQTKCLRFNPDATIWTAKQQVLCALSESLQDVLNYGLFQPATSGRDANFLEEERLLREYPQSFEKGVPYLEFRYKTRVYKQTNLDEKQLAKLHTKTGLKKFLEYVQLGTSDKVARLLDKGLDPNYHDSDSGETPLTLAAQTEGSVEVIRTLCLGGAHIDFRARDGMTALHKAACARHCLALTALLDLGGSPNYKDRRGLTPLFHTAMVGGDPRCCELLLYNRAQLGIADENGWQEIHQ... | null | null | adult behavior [GO:0030534]; associative learning [GO:0008306]; dendritic spine morphogenesis [GO:0060997]; determination of affect [GO:0050894]; habituation [GO:0046959]; long-term memory [GO:0007616]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of actin filament bundle assembly [GO:... | cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Schaffer collateral - CA1 synapse [GO:009... | ankyrin repeat binding [GO:0071532]; G protein-coupled receptor binding [GO:0001664]; identical protein binding [GO:0042802]; ionotropic glutamate receptor binding [GO:0035255]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; SH3 domain binding [GO:0017124]; signaling receptor co... | PF12796;PF17820;PF00536;PF07653; | 2.30.42.10;1.25.40.20;2.30.30.40;1.10.150.50; | SHANK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Colocalizes with alpha-latrotoxin receptor 1. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendri... | Mus musculus (Mouse) |
D3YZZ2 | TGR3L_MOUSE | MVGTALLLLALLPGTSSKHGTPRAPLLPGAPGPWLRRPLFSLELSDAEDAFPRRAGPLEVPADSHVFVQAALARPSPRWGLALHRCSVTPSSRPTLGPALVLLRGGCPADDSVSFSPPPRPDAASVSRFSFRLRPVFNASVQFLHCQISRCRRRSSHHRRAVRLTPVPLTPPAPLRCLPQDEACAGSSLSLGTDSPHLHMLTQPIVVTIPRPSPRPSKSLPGRSVHPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPPPPGPPPRASLSGPQLQRPPVGRDGTTQ | null | null | cell migration [GO:0016477]; epithelial to mesenchymal transition [GO:0001837]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glycosaminoglycan binding [GO:0005539]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; type II transforming growth factor beta receptor binding [GO:0005114] | PF00100; | 2.60.40.4100; | null | PTM: Glycosylated. {ECO:0000269|PubMed:34910520}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34910520}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. {ECO:0000269|PubMed:34910520}. | Mus musculus (Mouse) |
D3Z120 | FOXI3_MOUSE | MALYCGDNFVYSQPAAAPGAPPTSRAPYGLSDYAAPPAAAANPYLWLNGPGVGGPASAASYLGAPPPPPGAAPGPFLQPPAAPGTFAGAQRGFAQPSASAPASPAGSAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADNFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRRRRAEASSNLTVPSGTSKSEGQSSRLRVSGKLEGDSPSSILRPSQSPEPPEGTKSTASSPGASTLTSTPCLNTFLSTFNTLNVNSSSSMGNQRTLPGS... | null | null | anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; epidermal cell fate specification [GO:0009957]; hair follicle development [GO:0001942]; odontogenesis of dentin-containing tooth [GO:0042475]; otic placode development [GO:1905040]; parathyroid gland development [GO:0060017]; pharyngeal... | 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] | PF00250; | 1.10.10.10; | null | PTM: Phosphorylation promotes the transcription factor activity (PubMed:30467319). Dephosphorylation by protein phosphatase 2A (PP2A) reduces its activity (PubMed:30467319). {ECO:0000269|PubMed:30467319}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:30467319, ECO:0000269|PubMed:37041148}. | null | null | null | null | null | FUNCTION: Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development (PubMed:24650709, PubMed:26550799, PubMed:26992132, PubMed:30467319). May act as a pioneer transcription factor during pharyngeal arch development (PubMed:26550799, PubMed:26992132). Requi... | Mus musculus (Mouse) |
D3Z1Q2 | MRAP2_MOUSE | MEMSAQRLASNRTSPQSPSNSDYTWEYEYYEIGPVSFEGLKAHKYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHQDNAESSERRFRMNSFVSDFGKPLESDKVFSRQGNEESRSLFHCYINEVEHLDRVKVCHQTTAIDSDVHLQEASRSSGRPEEELARFMKFDIPNFVNTEQSSFGEDDLLISEAPVLLENKPVSQTSRIDLD | null | null | energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; feeding behavior [GO:0007631]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; negative regulation of protein localization to plasma membrane [GO:1903077]; positive regulation o... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | corticotropin hormone receptor binding [GO:0031780]; identical protein binding [GO:0042802]; signaling receptor regulator activity [GO:0030545]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]; type 5 melanocortin re... | PF15183; | null | MRAP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extra... | null | null | null | null | null | FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP. May also act as a negative regulator of MC2R: competes wit... | Mus musculus (Mouse) |
D3Z291 | CAHM1_MOUSE | MDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNVVYSLGILLTPPLVLFLLGLVMNNNISMLAEEWKRPAGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVATLGNGSLVPGLPAPELARLLARVPCPEIYDGNWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQVAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGVLATATATATATEAVQSPSDRTEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQ... | null | null | ATP transport [GO:0015867]; monoatomic cation transport [GO:0006812]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; regulation of monoatomic ion transmembrane transport [GO:0034765]; response to stimulus [GO:0050896]; sensory perception of bitter taste [GO:0050913]; sensory perce... | basolateral plasma membrane [GO:0016323]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | calcium-activated cation channel activity [GO:0005227]; identical protein binding [GO:0042802]; monoatomic cation channel activity [GO:0005261]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated monoatomic ion channel activity [GO:0005244] | PF14798; | null | CALHM family | PTM: N-glycosylated. Assembly with CALHM3 is associated with N-glycan remodeling and formation of hybrid complex- and high mannose-type glycochains. This N-glycan processing regulates channel trafficking and gating kinetics. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3, ZDHHC20 and possibly ZDHHC7. Palm... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Basolateral cell membrane {ECO:0000269|PubMed:30804437}; Multi-pass m... | CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:23467090, ECO:0000269|PubMed:28734079, ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidenc... | null | null | null | null | FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes (PubMed:23467090). With CALHM3 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gusta... | Mus musculus (Mouse) |
D3Z2R5 | SELN_MOUSE | MGQARPAARRPHSPDPGAQPAPPRRRARALALLGALLAAAAAVAAARACALLADAQAAARQESALKVLGTDGLFLFSSLDTDQDMYISPEEFKPIAEKLTGSVPVANYEEEELPHDPSEETLTIEARFQPLLMETMTKSKDGFLGVSRLALSGLRNWTTAASPSAAFAARHFRPFLPPPGQELGQPWWIIPGELSVFTGYLSNNRFYPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGTVACLTAISDSYYTVMFRIHAEFQLSEPPDFPFWFSPGQFTGHIILSKDATHIRDFRLFVPNHRSLNVDMEWLYGASETSN... | null | null | calcium ion homeostasis [GO:0055074]; cellular response to caffeine [GO:0071313]; cellular response to oxidative stress [GO:0034599]; lung alveolus development [GO:0048286]; mitochondrion organization [GO:0007005]; multicellular organismal response to stress [GO:0033555]; positive regulation of response to oxidative st... | endoplasmic reticulum membrane [GO:0005789] | calcium ion binding [GO:0005509]; oxidoreductase activity [GO:0016491] | null | null | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NZV5}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZV5}. | null | null | null | null | null | FUNCTION: Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the co... | Mus musculus (Mouse) |
D3Z3K2 | CIP1_MOUSE | MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEVVLDISSRALAFWTYQVHQERLYQEYNFSKAENHLKQMEKMYMQQIQSKNIELTSMKGEVISMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIASQEGSLEPGMIPQSGVFGFPPGNNSKFSLDHIPVGNQGGGDEDVQFRPFFVCSPTAPEPINNFFSFASPSHEAEQQVCSRAFKAKRI | 2.3.2.27 | null | blastocyst formation [GO:0001825]; chiasma assembly [GO:0051026]; protein ubiquitination [GO:0016567]; reciprocal meiotic recombination [GO:0007131]; spermatid development [GO:0007286] | condensed nuclear chromosome [GO:0000794]; synaptonemal complex [GO:0000795] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF14634; | null | null | PTM: Ubiquitinated; autoubiquitinated. {ECO:0000250}.; PTM: Phosphorylated by CDK1 on serine or threonine residues (in vitro). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24390283}. Chromosome {ECO:0000269|PubMed:24390283}. Note=Associates to the synaptonemal complex. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9NPC3}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gam... | Mus musculus (Mouse) |
D3Z4I3 | RBM24_MOUSE | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | null | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cell differentiation [GO:0030154]; DNA damage response [GO:0006974]; endocardial cushion development [GO:0003197]; mRNA destabilization [GO:0061157]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; negative regulation of cytoplasmic translation [GO:20007... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; pre-mRNA intronic binding [GO:0097157]; sequence-specific mRNA binding [GO:1990825] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000269|PubMed:25217815}. | null | null | null | null | null | FUNCTION: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation (PubMed:25313962, PubMed:26844700). Plays a major role in pre-mRNA alternative splicing regulation (PubMed:25313962, PubMed:26844700). M... | Mus musculus (Mouse) |
D3Z5L6 | S18B1_MOUSE | MDEAGSPAPAGTGGGDDPGGSTRETSRRLSREQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTMIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLYILPSYAQESDPGKQSFWKLVTLPKMGLLAFVIISLSSCFGFLDPTLSLFVMEKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPTLRKWLLVFGNLITAGCYM... | null | null | serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; spermine transport [GO:0000296] | secretory granule membrane [GO:0030667]; synaptic vesicle membrane [GO:0030672] | monoamine:proton antiporter activity [GO:0015311]; polyamine:proton antiporter activity [GO:0015312]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:28082679}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D4A9K4}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with VAMP3 and VAM... | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + spermine(in) = n H(+)(in) + spermine(out); Xref=Rhea:RHEA:74263, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725; Evidence={ECO:0000250|UniProtKB:Q6NT16}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74264; Evidence={ECO:0000250|UniProtKB:Q6NT16}; CATALYTIC ACTIVITY: Reaction=n H... | null | null | null | null | FUNCTION: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecu... | Mus musculus (Mouse) |
D3Z5S8 | TET5A_MOUSE | MHQRYFWTDQGQVAFGGHYMAEGEGYFAMAEDELTGGPYIPLGGDFGGGGSSFGDRCSDYCESPTAHCNVLNWEQVQRLDGILSETIPIHGRGNFPTLELQPSLIVKVVRRRLEEKGIGVRDVRLNGSAASHVLHQDSGLGYKDLDLIFCADLRGEEEFQTVKDVVLDCLLDFLPEGVNKEKITPLTLKEAYVQKMVKVCNDSDRWSLISLSNNSGKNVELKFVDSLRRQFEFSVDSFQIKLDSLLLFYECSENPMTETFHPTIIGESVYGDFHEAFDHLCNKIIATRNPEEIRGGGLLKYCNLLVRGFRPASEEIKTLQ... | 2.7.7.19 | null | mRNA stabilization [GO:0048255]; positive regulation of bone mineralization [GO:0030501]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of ossification [GO:0030278]; response to bacterium [GO:0009617] | cytoplasm [GO:0005737] | poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723] | PF07984; | null | TENT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33882302}. | 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:33882302}; PhysiologicalDirection=left-to-... | null | null | null | null | FUNCTION: Cytoplasmic non-canonical poly(A) RNA polymerase that catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and participates in the cytoplasmic polyadenylation (PubMed:33882302). Polyadenylates mRNA encoding extracellular matrix constituents and ot... | Mus musculus (Mouse) |
D3Z6P0 | PDIA2_MOUSE | MDKQLLPVLLLLLGVSGSWGQGEEPGGPSEVLPEEPTGEEVPKEDGILVLNHRTLSLALQEHSALMVEFYAPWCGHCKELAPEYSKAAALLAAESAVVTLAKVDGPAEPELTKEFEVVGYPTLKFFQNGNRTNPEEYAGPKTAEGIAEWLRRRVGPSATHLEDEEGVQALMAKWDMVVIGFFQDLQGKDMATFLALAKDALDMTFGFTDQPQLFEKFGLTKDTVVLFKKFDEGRADFPVDKETGLDLGDLSRFLVIHSMHLVTEFNSQTSPKIFAAKILNHLLLFVNQTLAQHRELLTDFREAAPPFRGQVLFVMVDVAA... | 5.3.4.1 | null | platelet aggregation [GO:0070527]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788] | protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]; steroid binding [GO:0005496] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Glycosylated. {ECO:0000269|PubMed:9115635}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q13087, ECO:0000255|PROSITE-ProRule:PRU10138}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity). {ECO:0000250|UniProtKB:Q13087}. | Mus musculus (Mouse) |
D3Z752 | SPXN_MOUSE | MKGPSVLAVTAVVLLLVLSALENSSGAPQRLSEKRNWTPQAMLYLKGAQGRRFLSDQSRRKELADRPPPERRNPDLELLTLPEAAALFLASLEKSQKDEGGNFDKSELLEDRLFNW | null | null | long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; negative regulation of heart rate [GO:0010459]; negative regulation of renal sodium excretion [GO:0035814]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of sy... | cytoplasm [GO:0005737]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; transport vesicle [GO:0030133] | neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF15171; | null | Spexin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24550067}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not a... | null | null | null | null | null | FUNCTION: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity). {ECO:0000250}.; FUNCTION: [Spexin-1]: Acts as a ligand for ... | Mus musculus (Mouse) |
D3Z7A5 | DAW1_MOUSE | MKLKSLLLRYYPPGIMLEYEKGGELKTKSIDLLELSPSTDVNTLVGEIQQAEPLITASRTKQVRLLVQRLQEKLRQHSDHNFYLFKVLRAHILPLTNVALNKAGSCFITGSYDRTCKVWDTASGEELHTLEGHKNVVYAIAFNNPYGDKIATGSFDKTCKLWSAETGKCYHTFRGHTAEIVCLSFNPQSTVVATGSMDTTAKLWDIQNGEEVVTLTGHLAEIISLSFDTSGDRIITGSFDHTVVVWDASTGRKVHTLIGHCAEISSALFNWDCSLILTGSMDKTCMLWDATSGKYVATLTGHDDEILDSCFDYTGKLIAT... | null | null | cerebrospinal fluid circulation [GO:0090660]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; heart development [GO:0007507]; intraciliary transport [GO:0042073]; outer dynein arm ass... | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; motile cilium [GO:0031514]; SCF ubiquitin ligase complex [GO:0019005]; Set1C/COMPASS complex [GO:0048188] | histone binding [GO:0042393]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF00400; | 2.130.10.10; | WD repeat WDR69 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q3Y8L7}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q3Y8L7}. Note=Expression is concentrated at the flagellum basal body but is also detected along the length of the flagellum. {ECO:0000250|UniProtKB:Q3Y8L7... | null | null | null | null | null | FUNCTION: Required for axonemal dynein assembly and ciliary motility in ciliated organs, including Kupffer's vesicle, during embryogenesis (By similarity). Facilitates the onset of robust cilia motility during development (By similarity). {ECO:0000250|UniProtKB:Q8N136}. | Mus musculus (Mouse) |
D3Z7P3 | GLSK_MOUSE | MMRLRGSAMLRELLLRPPAAVGAVLRRAQPLGTLCRRPRGGSRPTAGLVAAARLHPWWGGGGRAKGPGAGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSG... | 3.5.1.2 | null | chemical synaptic transmission [GO:0007268]; glutamate biosynthetic process [GO:0006537]; glutamine catabolic process [GO:0006543]; intracellular glutamate homeostasis [GO:0090461]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; suckling beha... | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; synapse [GO:0045202] | glutaminase activity [GO:0004359]; identical protein binding [GO:0042802] | PF12796;PF17959;PF04960; | 1.10.238.210;1.25.40.20;3.40.710.10; | Glutaminase family | PTM: Synthesized as a 74-kDa cytosolic precursor which is proteolytically processed by the mitochondrial-processing peptidase (MPP) via a 72-kDa intermediate to yield the mature mitochondrial 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}. | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P13264}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264... | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106, ECO:0000269|PubMed:27542409}; | null | null | null | null | FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain. {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:22228304, EC... | Mus musculus (Mouse) |
D3Z8D9 | MD2L2_RAT | MTTLTRQDLNFGQVVADVLSEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSINSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKNS | null | null | actin filament organization [GO:0007015]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response, signal transduction resulting in transcription [GO:0042772]; double-strand break repair [GO:0006302]; error-prone translesion synthesis [GO:0042276]; negative regulation of canonical Wnt signaling pathway... | anaphase-promoting complex [GO:0005680]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; zeta DNA polymerase complex [GO:0016035] | JUN kinase binding [GO:0008432]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF02301; | 3.30.900.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis... | Rattus norvegicus (Rat) |
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