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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A5GZW8 | DHSD_PIG | MATLWRLSVLCGARGGGALVLRTSVVRPAHVSAFLQDRHTPGWCGVQHIHLSPSHQASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKVAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL | null | null | mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; protein insertion into mitochondrial inner membrane [GO:0045039]; tricarboxylic acid cycle [GO:0006099] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein transmembrane transporter activity [GO:0008320]; succinate dehydrogenase (quinone) activity [GO:0008177]; ubiquinone binding [GO:0048039] | PF05328; | 1.20.1300.10; | CybS family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. | null | null | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). | Sus scrofa (Pig) |
A5H2P4 | ARO12_LODEL | MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLEGFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPISVDEKIFSKIIGAKKNNLKIDSLIKKMLIDKKNDGSKIRCVLLESIGKCYESKAHQIFKEDIQVVMTDEVFVHPFANRHPESVSITPPGSKSISNRALILAALGEGTTRIKNLLHSDDTKHMLDAVVLMKGATVSFEDSGDTVVVQGHGGKLFACKEEIYLGNAGTASRFLTAVAALVNSTQDEKSVTLTGNARMQERPIAALVDALTTNGSKVDYLNKQGSLPLKIEAGNGFKGGRIELAATTSSQYVSAILMCAPYAEKEVTLSLVGGKPISQLYIDMTIAMMKDFGVDVTKSETEEYTYHIPKAVYQNPQEYVVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCTVEQTSKSTTVTGPPIGTLKALPEIDMEPMTDAFLTASVVAAVSQGTTTISGIANQRVKECNRIKAMVDELAKFGVSADETEDGISIHGVQLKDLKTPGGRGVKTYDDHRVAMSFSLLAGLCKDPVLIQERSTTGKTWPGWWDVLHSKFNAKLEGHEYIRQRSGSLRNGDRSIVIIGMRAAGKTTLSRWLAEHLNFKLLDLDQYLEKKLAVDIKLLVKEKGWDYFREKETEVLNECLEKFGKGHILATGGGIVEGEKPREALKNYTKSGGIVLHLHRDLKETVNFLSKDPTRPAYSDDIEEVWKRREKWYHECSNYHFYSTHCTSEAEFANLKLVFAKFVSKITGDDTFVLPATRSTFVTLTYPDLRKVPSLIKDVSETSNAVELRVDLLANQETAYIAEQIGLLRSVATDLPILYTVRTKSQCGQYPDEDEEGMRKLLMFGLKMGVDIIDLQLISSPSTIAEVISKRGHTKIIASHHDFTGDLKWDNVEWKNKYAQGVSIDADFVKLVGMAKTFDDNLLLENFRRQNTEKPLIGINMGPQGKLSRVLNKVLTPVTHELITDKPIGVGQLSLKEINQALFQIGGLLEKEFWVVGFPVSHSRSPALHNAAYAALGLPYKFDIFETDDAEKVYTQLMQKPTFGGLAVTIPLKLDIKKYCTELSESAKLIGAVNTVTPIADGRKGFLGDNTDWIGIANSFKKADFALASGVTNGLVVGGGGTSRAAIFALHSLGCQKIYLLNRTESKLQDLVDSFPDYDLEILLEKNASSVSIGLVVSCVPGDKALDETLMKKLDGVLSNNKGDKQTRPLLLEAAYKPRVTPIMELAKEKYDWTVIPGVEMLVNQGEAQFKLHTGYTAPYKVIHSAVLNE | 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:0004765] | PF01761;PF01487;PF00275;PF18317;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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
A5H2Q8 | ARO11_LODEL | MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLESFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPISVDEKIFSKIIGAKKNNLKIDSLIKKMLIDKKNDGSKIRCVLLESIGKCYESKAHQIFKEDIQVVMTDEVFVHPFANRHPESVSITPPGSKSISNRALILAALGEGTTRIKNLLHSDDTKHMLDAVVLMKGATVSFEDSGDTVVVQGHGGKLFACKEEIYLGNAGTASRFLTAVAALVNSTQDEKSVTLTGNARMQERPIAALVDALTTNGSKVDYLNKQGSLPLKIEAGNGFKGGRIELAATTSSQYVSAILMCAPYAEKEVTLSLVGGKPISQLYIDMTIAMMKDFGVDVTKSETEEYTYHIPKSVYQNPQEYVVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCTVEQTSKSTTVTGPPIGTLKALPEIDMEPMTDAFLTASVVAAVSQGTTTISGIANQRVKECNRIKAMVDELAKFGVSADETEDGIRIHGVQLRDLKTPGGRGVKTYDDHRVAMSFSLLAGLCKDPVLIQERSTTGKTWPGWWDVLHSKFNAKLEGHEYIRQRSGSLRNGDRSIVIIGMRAAGKTTLSRWLAEHLNFKLLDLDQYLEKKLAVDIKLLVKEKGWDYFREKETEVLNECLEKFGKGHILATGGGIVEGEKPREALKNYTKSGGIVLHLHRDLKETVNFLSKDPTRPAYSDDIEEVWKRREKWYHECSNYHFYSTHCTSEAEFANLKLVFAKFVSKITGDDTFVLPATRSTFVTLTYPDLRKVPSLIKDVSETSNAVELRVDLLANQETAYIAEQIGLLRSVATDLPILYTVRTKSQCGQYPDEDEEGMRKLLMFGLKMGVDIIDLQLISSPSTIAEVISKRGHTKIIASHHDFTGDLKWDNVEWKNKYAQGVSIDADFVKLVGMAKTFDDNLLLENFRRQNTEKPLIGINMGPQGKLSRVLNKVLTPVTHELITDKPIGVGQLSLKEINQALFQIGGLLEKEFWVVGSPVSHSRSPALHNAAYAALGLPYKFDIFETDDAEKVYSQLMQKPTFGGLAVTIPLKLDIKKYCTELSESAKLIGAVNTVTPIADGRKGFLGDNTDWIGIANSFKKADFALASGVSNGLVVGGGGTSRAAIFALHSLGCQKIYLLNRTESKLQDLVDSFPDYDLEILLEKNASSVSIGLVVSCVPGDKPLDETLMKKLDGVLSNNKGDKQTRPLLLEAAYKPRVTPIMELAKEKYDWTVIPGVEMLVNQGEAQFKLHTGYTAPYKVIHSAVLNE | 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:0004765] | PF01761;PF01487;PF00275;PF18317;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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
A5H447 | ZYX_XENLA | MDPAAPATRMTSSFTINISTPSFYNPPKKFAPVVPPKPKINPFKAPEEPQSLVPQENSAGPGLHQAFVGKVGEMPPGVDHDDFVLPPPPPSEESISPPSSSFPPPPPSFGDEGLGSPSGGSFPPPPPPEFSEPFPPPIEEFFPSPPPLEECVSDTQDLPVPVPPPPPPPLPSPPAAPPPKPSAPCEAPKPAPVFPKSSPPPAFPKPEPPSVAPKAASSIFIPKPSAPMAVAPKPLAPPPVAAKPSGPVSFAPPSPAPHTFSPDPSAPAHTFSPKTVTFSPKSAPHTFMPKPSAPVTYPQKTTEPPAEASQSSPKVTPAAKHEAPPPTVPSGGRAPGFSFAQQRERPRVLEKPRANLQGSEPEHEPTVEVQVERTRSLGPQTESGRSPGAQSTGGKDMKPLPEGLRSQKPMSDGIHRTGGQHSGHKVTGQQDQTLGSQGLNMKEVEELEMLTQQLMREMDKPPTAEAHSMELCGFCGRGLSRTETVVRAGEHLYHVACFTCSRCDQQLQGQQYYESAGKPLCDECYQDTLECCAVCDKKITERLLKAIGKSYHPSCFTCAVCKCSLQGEPFIVDDNKLPHCVNDYHRRYAPRCCVCGDPIAPEPGRDETVRVVALEKNFHMMCYKCEDCGCPLSIEADDAGCFPLDGHVLCKKCHTVRARAALG | null | null | cell adhesion [GO:0007155]; integrin-mediated signaling pathway [GO:0007229]; regulation of transcription by RNA polymerase II [GO:0006357]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; stress fiber [GO:0001725] | DNA-binding transcription factor binding [GO:0140297]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cell junction, focal adhesion {ECO:0000250}. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of hesx1. {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. | null | null | null | null | null | FUNCTION: Adhesion plaque protein. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). Suppresses the transcription-repressing activity of hesx1/anf1. {ECO:0000250|UniProtKB:Q04584, ECO:0000269|PubMed:18297730}. | Xenopus laevis (African clawed frog) |
A5H8G4 | PER1_MAIZE | MAKESKLTAGVAAALTVVAACALCLLLPATARAQLRVGFYDTSCPNAEALVRQAVAAAFAKDAGIAAGLIRLHFHDCFVRGCDGSVLLTVNPGGGQTERDALPNNPSLRGFDVIDAAKTAVEQSCPRTVSCADIVAFAARDSISLTGSVSYQVPAGRRDGRVSNATETVDLPPPTSTAQSLTDLFKAKELSVEDMVVLSGAHTVGRSFCASFFKRVWNTSTNPATAIVDAGLSPSYAQLLRALCPSNTTQTTPITTAMDPGTPNVLDNNYYKLLPRGMGLFFSDNQLRVNPQMAALVSSFASNETLWKEKFAAAMVKMGRIQVQTGTCGEVRLNCGVVNPSLYSSSSAVELGSSAPAAVGEEGYAAS | 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]; vacuole [GO:0005773] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Classical plant (class III) peroxidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=61.9 umol/min/mg enzyme with guaiacol as substrate {ECO:0000269|PubMed:18603027}; Note=In the presence of H(2)O(2).; | null | null | null | FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12857829}. | Zea mays (Maize) |
A5HAK0 | RNSL3_DANRE | MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV | 3.1.27.- | null | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; immune system process [GO:0002376] | extracellular region [GO:0005576] | endonuclease activity [GO:0004519]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | PTM: Cleavage between Arg-55 and Arg-56 is catalyzed by a membrane-localized Gram-negative bacterium protease (OmpT in E.coli). The excised fragment is then transported to the bacterium cytosol for cleavage of the disulfide bridge linking Cys-48 and Cys-109, thus separating the N-terminal and LF-ZF3. LF-ZF3 but not the N-terminal peptide possesses bactericidal activity. {ECO:0000269|PubMed:20214681}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P34096}. | null | null | null | null | null | FUNCTION: Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity. {ECO:0000269|PubMed:16861230, ECO:0000269|PubMed:17347156, ECO:0000269|PubMed:18508078, ECO:0000269|PubMed:20214681}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5HBE1 | VP2_POVWU | MGILLAVPEIIAASVAGGAEALSIAGSGAAIATGEGLAALGGLTESAALLGETVEISEAAATVLTKVPELVTVTQGVTAAVQGGAGLVGGIYTALAADRPGDLPASTPTGSPSGLHPPAGYNPQGGGLNIQSIHKPLHAPYPGMALAPIPEYNLETGIPGVPDWVFNFIASHLPELPSLQDVFNRIAYGIWTSYYNTGRTVVNRAVSEELQRLLGDLEYGFRTALATIGESDPVNAIVEQVRSFVSGGRQRELLQIAAGQPVDISEGVSRGTATISNAVEAVRDATQRLSQATYNFVYDASTLPRDGFNALSDGVHRLGQWISMPGATGGTPHYAAPDWILYVLEELNSDISKIPTQGIKRKLQQNGLHSKASLHSKTRKVTKKSTHKSAKPSKTSQKRRGRRAGRRTTVRRNRV | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677] | null | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). {ECO:0000250}. | WU polyomavirus (WUPyV) |
A5HBG1 | LT_POVWU | MDKTLSRNEAKELMQLLGLDMTCWGNLPLMRTKYLSKCKEFHPDKGGNEEKMKKLNSLYLKLQECVSTVHQLNEEEDEVWSSSQIPTYGTPDWDYWWSQFNSYWEEELRCNEEMPKSPGETPTKRTREDDEEPQCSQATPPKKKKDNATDASLSFPKELEEFVSQAVFSNRTLTAFVIHTTKEKAETLYKKLLSKFKCNFASRHSYYNTALVFILTPFRHRVSAVNNFCKGYCTISFLFCKGVNNAYGLYSRMTRDPFTLCEENIPGGLKENDFKAEDLYGEFKDQLNWKALSEFALELGIDDVYLLLGLYLQLSIKVEECEKCNSNEDATHNRLHMEHQKNALLFSDSKSQKNVCQQAIDVVIAKRRVDSLNMSREDLLARRFEKILDKMDKTIKGEQDVLLYMAGVAWYLGLNGKIDELVYRYLKVIVENVPKKRYWVFKGPINSGKTTVAAALLDLCGGKALNINIPADRLNFELGVAIDQFTVVFEDVKGQVGDNKLLPSGNGMSNLDNLRDYLDGSVKVNLEKKHLNKRSQIFPPGIVTMNEYLVPATLAPRFHKTVLFTPKRHLKESLDKTPELMVKRVLQSGMCILLMLIWCRPVSDFHPCIQAKVVYWKELLDKYIGLTEFADMQMNVTNGCNILEKHNA | 3.6.4.- | null | DNA replication [GO:0006260]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity [GO:0039576]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF06431;PF02217; | 3.40.1310.20;1.10.287.110;1.20.1050.70;3.40.50.300;1.10.10.510; | null | PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A. {ECO:0000250|UniProtKB:P03070}.; PTM: O-Glycosylated near the C-terminal region. {ECO:0000250|UniProtKB:P03070}.; PTM: Acetylated by CBP in a TP53-dependent manner. {ECO:0000250|UniProtKB:P03070}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03070}. | null | null | null | null | null | FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. {ECO:0000250|UniProtKB:P03070}. | WU polyomavirus (WUPyV) |
A5HC98 | L_BUNLC | MDYQEYQQFLARINTARDACVAKDIDVDLLMARHDYFGRELCKSLNIEYRNDVPFIDIILDIRPEVDPLTIDAPHITPDNYLYINNVLYIIDYKVSVSNESSVITYDKYYELTRDISDRLSIPIEIVIIRIDPVSRDLHINSDRFKELYPTIVVDINFNQFFDLKQLLYEKFGDDEEFLLKVAHGDFTLTAPWCKTGCPEFWKHPIYKEFKMSMPVPERRLFEESVKFNAYESERWNTNLVKIREYTKKDYSEHISKSAKNIFLASGFYKQPNKNEISEGWTLMVERVQDQREISKSLHDQKPSIHFIWGAHNPGNSNNATFKLILLSKSLQSIKGISTYTEAFKSLGKMMDIGDKAIEYEEFCMSLKSKARSSWKQIMNKKLEPKQINNALVLWEQQFMINNDLIDKSEKLKLFKNFCGIGKHKQFKNKMLEDLEVSKPKILDFDDANMYLASLTMMEQSKKILSKSNGLKPDNFILNEFGSRIKDANKETYDNMHKIFETGYWQCISDFSTLMKNILSVSQYNRHNTFRIAMCANNNVFAIVFPSADIKTKKATVVYSIIVLHKEEENIFNPGCLHGTFKCMNGYISISRAIRLDKERCQRIVSSPGLFLTTCLLFKHDNPTLVMSDIMNFSIYTSLSITKSVLSLTEPARYMIMNSLAISSNVKDYIAEKFSPYTKTLFSVYMTRLIKNACFDAYDQRQRVQLRDIYLSDYDITQKGIKDNRELTSIWFPGSVTLKEYLTQIYLPFYFNAKGLHEKHHVMVDLAKTILEIECEQRENIKEIWSTNCTKQTVNLKILIHSLCKNLLADTSRHNHLRNRIENRNNFRRSITTISTFTSSKSCLKIGDFRKEKELQSVKQKKILEVQSRKMRLANPMFVTDEQVCLEVGHCNYEMLRNAMPNYTDYISTKVFDRLYELLDKKVLTDKPVIEQIMDMMIDHKKFYFTFFNKGQKTSKDREIFVGEYEAKMCMYAVERIAKERCKLNPDEMISEPGDGKLKVLEQKSEQEIRFLVETTRQKNREIDEAIEALATEGYESNLGKIEKLSLGKAKGLKMEINADMSKWSAQDVFYKYFWLIALDPILYPQEKERILYFMCNYMDKELILPDELLFNLLDQKVAYQNDIIATMTNQLNSNTVLIKRNWLQGNFNYTSSYVHSCAMSVYKEILKEAITLLDGSILVNSLVHSDDNQTSITIVQDKMENDKIIDFAMKEFERACLTFGCQANMKKTYVTNCIKEFVSLFNLYGEPFSIYGRFLLTSVGDCAYIGPYEDLASRISSAQTAIKHGCPPSLAWVSIAISHWMTSLTYNMLPGQSNDPIDYFPAENRKDIPIELNGVLDAPLSMISTVGLESGNLYFLIKLLSKYTPVMQKRESVVNQIAEVKNWKVEDLTDNEIFRLKILRYLVLDAEMDPSDIMGETSDMRGRSILTPRKFTTAGSLRKLYSFSKYQDRLSSPGGMVELFTYLLEKPELLVTKGEDMKDYMESVIFRYNSKRFKESLSIQNPAQLFIEQILFSHKPVIDFSGIRDKYINLHDSRALEKEPDILGKVTFTEAYRLLMRDLSSLELTNDDIQVIYSYIILNDPMMITIANTHILSIYGSPQRRMGMSCSTMPEFRNLKLIHHSPALVLRAYSKNNPDIQGADPTEMARDLVHLKEFVENTNLEEKMKVRIAMNEAEKGQRDIVFELKEMTRFYQVCYEYVKSTEHKIKVFILPAKSYTTTDFCSLMQGNLIKDKEWYTVHYLKQILSGGHKAIMQHNATSEQNIAFECFKLITHFADSFIDSLSRSAFLQLIIDEFSYKDVKVSKLYDIIKNGYNRTDFIPLLFRTGDLRQADLDKYDAMKSHERVTWNDWQTSRHLDMGSINLTITGYNRSITIIGEDNKLTYAELCLTRKTPENITISGRKLLGSRHGLKFENMSKIQTYPGNYYITYRKKDRHQFVYQIHSHESITRRNEEHMAIRTRIYNEITPVCVVNVAEVDGDQRILIRSLDYLNNDIFSLSRIKVGLDEFATIKKAHFSKMVSFEGPPIKTGLLDLTELMKSQDLLNLNYDNIRNSNLISFSKLICCEGSDNINDGLEFLSDDPMNFTEGEAIHSTPIFNIYYSKRGERHMTYRNAIKLLIERETKIFEEAFTFSENGFISPENLGCLEAVVSLIKLLKTNEWSTVIDKCIHICLIKNGMDHMYHSFDVPKCFMGNPITRDINWVMFREFINSLPGTDIPPWNVMTENFKKKCIALINSKFETQRDFSEFTKLMKKEGGRSNIEFD | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20862319}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (PubMed:20862319). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000269|PubMed:20862319, ECO:0000269|PubMed:31948728}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A2SZS3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A2SZS3}; Note=For polymerase activity. Initiation activity is stronger in the presence of Mn(2+) than in the presence of Mg(2+). {ECO:0000250|UniProtKB:A2SZS3}; | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF04196;PF15518;PF21561; | 3.40.91.60; | Bunyavirales RNA polymerase family | null | SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion {ECO:0000250|UniProtKB:P20470}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P20470}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (PubMed:20862319). These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (PubMed:26004069). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (PubMed:20862319). {ECO:0000250|UniProtKB:I0DF35, ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:20862319, ECO:0000269|PubMed:26004069}. | Bunyavirus La Crosse |
A5HEH4 | GIF1_MAIZE | MQQQHLMQMNQNMMGGYTSPAAVTTDLIQQYLDENKQLILAILDNQNNGKAEECERHQAKLQHNLMYLAAIADSQPPQTAPLSQYPSNLMMQPGPRYMPPQSGQMMNPQSLMAARSSMMYAHPSLSPLQQQQAAHGQLGMAPGGGGGGTTSGFSILHGEASMGGGGAGAGAGNNMMNAGMFSGFGRSGSGAKEGSTSLSVDVRGGTSSGAQSGDGEYLKVGTEEEGS | null | null | adaxial/abaxial pattern specification [GO:0009955]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; cotyledon development [GO:0048825]; floral meristem determinacy [GO:0010582]; leaf development [GO:0048366]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; root meristem growth [GO:0010449] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | transcription coactivator activity [GO:0003713] | PF05030; | null | SS18 family | null | null | null | null | null | null | null | FUNCTION: Transcription coactivator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences (PubMed:29437990). Regulates shoot architecture and meristem determinacy (PubMed:29437990). Binds to the inflorescence architecture gene UB3 (unbranched3) (PubMed:29437990). Regulates the expression of several genes involved in inflorescence architecture (PubMed:29437990). Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (Probable) (PubMed:26036253). Associates with the core SWI/SNF chromatin-remodeling complex and specific GRFs to tightly regulate the transition between cell division and cell expansion in growing leaves (PubMed:26036253). {ECO:0000269|PubMed:26036253, ECO:0000269|PubMed:29437990, ECO:0000305|PubMed:29437990}. | Zea mays (Maize) |
A5HEI1 | SCC2_ARATH | MSNPSSSGLGSSSGLTHFGIGLANTVQSEVTPYLPLPSLPIFCGAAEPGEFKLFDEVGQGSGYRSLDRSEILAQSSRIANMLHETDVSYLDLRNEARAPDCNSGEHFQLYDLVLRCNPGAFEYVTPGPTCDPLFTNEGPQKIISEPSVPVKMQRQTDTHLARSIEPEPVKRVLRPNHVEDHSWQHETLTNQSPKDVTAYDSRPETITMNELSASKKPKGKKKRKDDLSSVQPDPSVLQESIVQNFCEMLEDFCGRAEVPGDDRDEAEWSSVPVDEVRVLINELMTIRSKMLLHMVPVDILSRLLRTLDHQIHRAEGLSIYSEHSDSDSVLLVLGALESIHASLAVMANSDMPKQLYKEEIIERILEFSRHQMMAVMSAYDPSYRTGSKPAENLAFEGDDDDDNPDHDMGSASKRRRIVKNSKVKKASVNRISGAVNTALQKLCTILGLLKDLLLVERLSDSCILQLLKTSITTFLVENIQILQLKAISLIGGIYNSYSQHRTYVIDEISQLLWKLPSSKRALRAYLLPDEEQRQIQMVTALLIQLVHNSTSLPETSRQAASGNSILETSVDVGYLTKCHEAATETCCLFWTRVLERFTSFKGQDASEIKLIIENLVMDLLTALNLPEYPSVSPILEVLCVILLHNAGLKSKDVSARIMAIELLGTIAARLKRDAVLCSKDRFWTLLESDSEISVDQVCTKDCTFCLGKRAGNLLVCQICQRRFHGDCLGLKELDISSRNWHCPLCVCKRQLLVLQSYCKTDTKGTGKLESEESIENPSMITKTEVVQQMLLNYLQDVGSADDVHTFICWFYLCLWYKDVPKSQNKFKYYIARLKAKSIIRNSGATTSFLTRDAIKQITLALGMNSSFSRGFDKILNMLLASLRENAPNIRAKALRAVSIIVEADPEVLCDKRVQLAVEGRFCDSAISVREAALELVGRHIASHPDVGIKYFEKVAERIKDTGVSVRKRAIKIIRDMCTSNPNFSEFTSACAEILSRISDDESSVQDLVCKTFYEFWFEEPPGHHTQFASDASSIPLELEKKTKQMVGLLSRTPNQQLLVTIIKRALALDFFPQAAKAAGINPVALASVRRRCELMCKCLLEKILQVEEMSREEGEVQVLPYVLVLHAFCLVDPGLCTPASDPTKFVITLQPYLKSQADSRTGAQLLESIIFIIDSVLPLIRKLPLSVTEDLEQDLKHMIVRHSFLTVVHACVRCLCSVSKLAGKGVSIVEHLLQFFFKRLEAQGSDNTQIAGRSLFCLGLLIRHGNSLISTSGGKNFNLSGCLNLFKRHLRTEDIALKVRSLQALGFILIARPEYMLEEDIGKIIETTLADEANGRMKMQALQNMYEYLLDAEKQLGSEKASDNTVNSVEQGGHNVPVAAGAGDTNICGGIVQLFWDKILGRCLDFDDQIRQTSLKIVEVVLRQGLVHPITCVPYLIALETDPQEANQKLAHHLLMNMHEKYPAFFESRLGDGLQMSFIFMQSISQVTSEPNQSLQQKGSTNMLGKNDHASSTLTQARLGVSRIYKLIRGNRVSRNKFMTSIVRKFDNPTWNGSVISFLKYCTETLALLPFTSPDEPLYLVYSINRVMQIRAGAVESNLKALLHKDSAKTQHGNGAYQQDPIPGHMNMMDLNTRIQEEPRHWNSYGHATLIDLNGSVYQDSRDQFTSYQVHNGKADVHKMTSSDPPELSTDDLQKIQVDCLAAIAIQLLLKLKRYLKVTYSLNDDRCQAYSPTEPLKPGDPLSRQSVAFDLSETRTDLPSTYQDLVQRYQEFKNAMREDTVDFTIYSTNVKRKRPTPRKTSRSAKKTVAYNEDDDDDDNDDRGWHGGGGRGAARRLNYSTRSSNRR | null | null | brain development [GO:0007420]; cell division [GO:0051301]; centromere complex assembly [GO:0034508]; chromosome segregation [GO:0007059]; digestive tract development [GO:0048565]; embryo development ending in seed dormancy [GO:0009793]; establishment of protein localization to chromatin [GO:0071169]; heart morphogenesis [GO:0003007]; meiotic cell cycle [GO:0051321]; meiotic sister chromatid cohesion [GO:0051177]; mitotic cohesin loading [GO:0061780]; regulation of gene expression [GO:0010468]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; sister chromatid cohesion [GO:0007062] | chromosome, centromeric region [GO:0000775]; Scc2-Scc4 cohesin loading complex [GO:0090694] | chromatin binding [GO:0003682]; metal ion binding [GO:0046872] | PF12765;PF12830;PF00628; | 1.25.10.10;3.30.40.10; | SCC2/Nipped-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04002}. Chromosome, centromere {ECO:0000250|UniProtKB:Q04002}. Note=Associates with chromatin. {ECO:0000250|UniProtKB:Q04002}. | null | null | null | null | null | FUNCTION: Essential protein required for cell fate determination during embryogenesis (PubMed:15266054, PubMed:19228337, PubMed:28137757). Involved in sister chromatid cohesion during meiosis and mitosis (PubMed:19228337, PubMed:19533160). Forms a complex with SCC4, which is required for the association of the cohesin complex with chromosomes (PubMed:28137757). Plays a structural role in chromatin, especially in centromere organization, chromosomal axis formation, and distribution of the cohesin subunit SCC3 on chromosomes (PubMed:19228337). {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:19228337, ECO:0000269|PubMed:19533160, ECO:0000269|PubMed:28137757}. | Arabidopsis thaliana (Mouse-ear cress) |
A5HNF6 | MYD88_CHICK | MATVPVGAGSAPGPEPADLHSVPMVALNYGVRRRLGLYLNPRAATAADWTALAEKLGHDYLEIRRLEALPDPTAALLEEWQSRCPGGATVGQLLELLRQLGRHDVLLELGGSVEEDCKKYLRRKQQEAEQPLQVPAVDSSVPKTSELMGITTRDDPYGHGTEMFDAFICYCQKDLQFVQEMIRELEQTEFKLKLCVFDRDVLPGTCVWSISGELIERRCRRMVVVISDDYLESDECDFQTKFALSLSPGARLKRLIPVKCKTMKNEFPSILRFITICDYTNPCTKKWFWTRLAKSLLLP | null | null | defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; Toll signaling pathway [GO:0008063]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | TIR domain binding [GO:0070976]; Toll-like receptor binding [GO:0035325] | PF00531;PF13676; | 1.10.533.10;3.40.50.10140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18582498}. Nucleus {ECO:0000269|PubMed:18582498}. Note=Predominantly cytoplasmic, with some expression in the nucleus. | null | null | null | null | null | FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. {ECO:0000250, ECO:0000269|PubMed:18582498}. | Gallus gallus (Chicken) |
A5HNV6 | DCAMP_TRYBB | MSVTRINQQTECPSSVHDLVSCWGGCTQSKTSTDSGLEKRFELNFAQPVDIGTVTVKQLASVMERAGESLRQNSAELGIHTLKFDRSLLVFTAKQIVVRSSVSVMLHEAVHPMLELMRSHNIIVDWASFMRVNYGSPWDMTSETSDIMAHEYAELKSAFPTGHPYLAGPVDRDHCFYFVYDGIDRDPSSCRRENDVQINVYMYNVQADDEYDLDGNTKEQQLLVSHCAGEYETLRVSTYGSTHPFASFETNAVSAASDITKIVNGLLKKFYPERVLLVLLQDRDAQGTTACGVMDRLEGFTVVHRGANHFGGGYVFHQATYARSA | null | null | positive regulation of catalytic activity [GO:0043085]; positive regulation of spermidine biosynthetic process [GO:1901307]; S-adenosylmethionine metabolic process [GO:0046500]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597]; trypanothione biosynthetic process [GO:0019342] | catalytic complex [GO:1902494]; cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; protein heterodimerization activity [GO:0046982] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | null | null | null | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269|PubMed:17485680, ECO:0000269|PubMed:18949025}. | null | null | FUNCTION: Probably has no catalytic activity due to the loss of several residues required for processing and catalysis (PubMed:17485680). Forms a complex with S-adenosylmethionine decarboxylase AdoMetDC which is essential to activate AdoMetDC (PubMed:17485680, PubMed:18949025). Required for the biosynthesis of the polyamine spermidine (PubMed:18949025). Required for growth and survival during the bloodstream life cycle stage (PubMed:18949025). {ECO:0000269|PubMed:17485680, ECO:0000269|PubMed:18949025}. | Trypanosoma brucei brucei |
A5HUI5 | AMPE_GLOBR | MDIEDKSSKMHCMKGKHVAIICGVVIAVGLILGLGLGLGLKPEACNPPEDNGLLSTKPPTTSTPNVTNPSGSSVFCSAKNDENGAWTNFRLPNYVQPVHYDLDLTPEMEAEVYTGMVNISIRLEEQTTRHLWLHLRETKITEMPQLRTSSGQVIEIKRCFGYEPQEYVVIEAEEDLRPGNYFLSMKFKGYLNGSLVGFYSTTYGENGKTKYIAATDHEPTDARKSFPCFDEPNKKATYTISITHEHDYEAISNMPVEKTISLDNKWTKTIFKKSVPMSTYLVAWAVHQFKYEERISSRGIPLRVYAQPQQINTTIYAANVTKVVFDYFENYFNMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDSQESAASNKQRVAAVVAHELVHQWFGNIVTMDWWDDLWLNEGFASFFEFMGVNAKEEKWQMLDQILIDDLLPVLKDDSLVSSHPITVNVSSPDEITSVFDGISYSKGASILRMLEDWISPDHFRAGCQKYLTDHYFKNAKTDDFWKAMEEVSGKPVREVMDTWTRQMGYPVLKVDLNSTVTQQRFLLDPKADPSKPSSQFSYKWNIPVKWKEGNTSSITFYNKSELAGITIMQPSDLPPDSFLKVNKDHVGFYRVNYEPQVWRTLADIMMKDHQNFNLTDRAGFIDDAFALARAGLLKYADALNLTRYLQNETEYIPWQRAVVAVSYIGQMVEDDKALYPKFQRYFGSLVKPIASELKWENDEDHIKSLLRTTVLEFACNMDDPEALGNASLLFKNWTSGISLDVNLRLLVYRFGMQNSGDEQAWNYMFEKYRTATLAQEKEKLLYGLASVKNITLLNRFLNCIKNTTLIRSQDVFTVLRYISFNSYGKTMAWDWVRLNWEYLVKRYTLNDRNLGRLISRISGTFNTELQLWQMENFFERYPDAGAGEASRKQALETTKSNIEWLKQYRDDVATWLENSEQPNFV | 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 | null | 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:17383704}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 (measured only for partially purified enzyme). {ECO:0000269|PubMed:17383704}; | null | FUNCTION: Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium (PubMed:17383704). 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 venom components, and/or processing of other toxins in the venom (By similarity). {ECO:0000250|UniProtKB:D3UW23, ECO:0000250|UniProtKB:P0DQU2, ECO:0000269|PubMed:17383704}. | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
A5IQA5 | HCHA_STAA9 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Staphylococcus aureus (strain JH9) |
A5JTM5 | CBADH_PSEUC | MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV | 3.8.1.7 | null | coenzyme A metabolic process [GO:0015936] | null | 4-chlorobenzoyl-CoA dehalogenase activity [GO:0018787] | PF00378; | 1.10.12.10; | Enoyl-CoA hydratase/isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride + H(+); Xref=Rhea:RHEA:14853, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57354, ChEBI:CHEBI:57356; EC=3.8.1.7; Evidence={ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=4.2 uM for 4-bromobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=6.5 uM for 4-iodobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=10.4 uM for 2,4-dichlorobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=42 uM for 3,4-dichlorobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=30 uM for 4-chloro-2-nitrobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; KM=5.5 uM for 4-chloro-3-nitrobenzoyl-CoA {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; Vmax=2.2 umol/min/mg enzyme with 4-chlorobenzoyl-CoA as substrate {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; | PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. {ECO:0000269|PubMed:1610806}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5. Stable from pH 6.5 to 11.0, activity is lost following 10 minutes incubation at pH 4.5 or 12.0. {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. Retains 60% of maximum activity at 30 degrees Celsius and 65 degrees Celsius. After 15 minutes preincubation at 60 degrees Celsius 70% of the initial activity remains, 15 minutes preincubation at 65 degrees Celsius results in a total loss of activity. {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883}; | FUNCTION: Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA. {ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}. | Pseudomonas sp. (strain CBS-3) |
A5JTM6 | CBACL_PSEUC | MQTVHEMLRRAVSRVPHRWAIVDAARSTFDICRTGETSRNEGSATARLWPQPARPLAVVSGNSVEAVIAVLALHRLQAVPALMNPRLKPAEISELVARGEMARAVVANDAGVMEAIRTRVPSVCVLALDDLVSGSRVPEVAGKSLPPPPCEPEQAGFVFYTSGTTGLPKGAVIPQRAAESRVLFMATQAGLRHGSHNVVLGLMPLYHTIGFFAVLVAAMAFDGTYVVVEEFDAGNVLKLIERERVTAMFATPTHLDALTTAVEQAGARLESLEHVTFAGATMPDTVLERVNRFIPGEKVNIYGTTEAMNSLYMRAVRIAGTVMRPGFFSEVRIVRVGGDVDDGCPTVKRASWRWRRRMRPFQATLTNLRLLQKSFRKAGTGRAICVRDGSGNIVVLGRVDDMIISGGENIHPSEVERILAAAPGVAEVVVIGVKDERWGQSVVACVVLQPGASASAERLDAFCRASALADFKRPRRYVFLDELPKSAMNKVLRRQLMQHVSATSSAAVVPAPAVKQRTYAPSGRAIAR | 6.2.1.33 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806}; | fatty acid metabolic process [GO:0006631] | null | 4-chlorobenzoate-CoA ligase activity [GO:0018861]; ATP binding [GO:0005524]; medium-chain fatty acid-CoA ligase activity [GO:0031956] | PF00501;PF13193; | 3.30.300.30;3.40.50.980; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=4-chlorobenzoate + ATP + CoA = 4-chlorobenzoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23220, ChEBI:CHEBI:17861, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57354, ChEBI:CHEBI:456215; EC=6.2.1.33; Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.5 uM for 4-chlorobenzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=70 uM for CoA {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=104 uM for ATP (with magnesium as cofactor) {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=43 uM for ATP (with manganese as cofactor) {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=59 uM for ATP (with cobalt as cofactor) {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=15 uM for 4-bromobenzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=17 uM for 4-iodobenzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=700 uM for benzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; KM=130 uM for 4-methylbenzoate {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. {ECO:0000269|PubMed:1610806}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of activity remains at pH 7.0. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}; | FUNCTION: Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids palmate, caproate, laurate and butyrate. Negligible activity is detected when ATP is replaced by UTP, CTP or GTP as cosubstrate. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293}. | Pseudomonas sp. (strain CBS-3) |
A5JUY8 | PERL_BUBBU | MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGQTRTAIRNGQVWEESFKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLTRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKFSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248}; | antibacterial humoral response [GO:0019731]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; peroxidase activity [GO:0004601]; thiocyanate peroxidase activity [GO:0036393] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12071645, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:12071645, ECO:0000305|PubMed:19339248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137; Evidence={ECO:0000305|PubMed:12071645, ECO:0000305|PubMed:19339248}; CATALYTIC ACTIVITY: [Lactoperoxidase]: Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid; Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907; Evidence={ECO:0000305|PubMed:19339248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417; Evidence={ECO:0000305|PubMed:19339248}; CATALYTIC ACTIVITY: Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:29232; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421; Evidence={ECO:0000250|UniProtKB:P80025}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 60 degrees Celsius) {ECO:0000269|PubMed:12071645}; KM=0.77 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12071645}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:12071645}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:12071645}; | FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (PubMed:12071645). Shows antibacterial properties against E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis and S.dysenteriae (PubMed:12071645). May protect the udder from infection and may promote growth in newborns (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity). {ECO:0000250|UniProtKB:A0A452E9Y6, ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:P80025, ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:12071645, ECO:0000305|PubMed:12071645, ECO:0000305|PubMed:19339248}. | Bubalus bubalis (Domestic water buffalo) |
A5JYS0 | PCS1_CAEEL | MSQRRHFKMSVTAKNFYRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESMLDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSPDFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSPLAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGLVELELKKGTRPLIMYGLKAYVNINDSDFATSVISWNQFLLCDPLEDDEEEFQLCCRKFGQCFAPHAMCCTQKTFDADQKNSCTECSTDQNEACKMICSEIRRTRFAEVFSSSAVAALLIAWPFEKGYSERSDRIGNLAEKYKNEFSAETMNEMNQLTTQIRTLISCSKPPVVININKPDATSNKCCKNKIGQSCACANDVNL | 2.3.2.15 | null | cellular detoxification of cadmium ion [GO:0098849]; detoxification of cadmium ion [GO:0071585]; detoxification of copper ion [GO:0010273]; detoxification of mercury ion [GO:0050787]; detoxification of zinc ion [GO:0010312]; phytochelatin biosynthetic process [GO:0046938] | null | glutathione gamma-glutamylcysteinyltransferase activity [GO:0016756]; metal ion binding [GO:0046872] | PF05023; | 3.90.70.30; | Phytochelatin synthase family | null | null | CATALYTIC ACTIVITY: Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA-COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:131728; EC=2.3.2.15; Evidence={ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:20221439}; | null | null | null | null | FUNCTION: Involved in the synthesis of phytochelatins, which are heavy metal binding proteins required for the detoxification of heavy metals such as cadmium, arsenic and copper. {ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:20221439, ECO:0000269|PubMed:26907254}. | Caenorhabditis elegans |
A5JYW9 | SIN3_CAEEL | MYNPPPGGGGGNNGGDQSQQQPTNNATLFLLQMIQQSQHQQQHQNQQQQQLELQIRDQERILIEQQRMQHQQQQNQLLQGLNQFPFNPLGLFQVQAAVQAAQAQFAQNAQGSPIPFHIGSPLQPSHSPAASALQQQYLLPSHSPAITPFARNSEAARNIEQFIAQEEAANVPRANSQQQSPLIRPIPQQQALNIQNLTSTQQAQQILAHHRQVPVQQVQHQQHIPTPPLALPIAQQGPISNEVPSVPPVVPATSAGCPQREPRQQQGGRRQNRPGRRKKPEGPPRVDEALAYLRVIKSTFSSDVPVYHRFLEIMKDFRAQRIETPDVIEQVAELLYDSPELVLGFNTFLPTGYRITLTPDRKYVFSSPQMQPRVLLSPDERRARAIEAGAQAVGAIELGSQEGISKDEDRTIEDEDMDKSKEKDDVDGIDDEDDEESGIEDKNNEEMMEEDNHLIEEIICDDRKKDDCEDSQQEIEMSSELAAHTLNIIELLKKSFLARPTKLVDFMTFIDFFMSDQQYKKDMEKLRKDDEDDEIEENEKIEVDDVPGPSNAPQEIKKPDDIEKKDSSKNLQIEESCSDYLVSMLANCCIGEPDLLAATIDFLPYLGKLLVNGSDAIALKIKTILHFSATNDRNDIPPVNRVNPSDVDMDLVKQMEKCKMGTKKNEKLKLKVAGQGDEGATVELMILKKSYRILYERLKSRTTPNQLSHLMVLINAYANLDITREQLISELPKIMGTSGSDLEMIILQLLGAEKEPKNRPENDMDAVMRKDLPAIQPKRGLRDQKMLQQVKNVEAATVCTLGPSYRFMKDTKATDCSGRVELDDDLKGVLNDTWTSIPSWSSEDTGSQAIKKSNLEEFHFKTEDERYELDIIVDSNRTVIEQLSKTLRDYEAMSDEDKKSFKLDKWLNASSRSTTIRVLAKVFTNSAQDFIDAAQKNPLVGLRRILESLKEKDLLWSRFQQDTNRTWRDALDKQMSAATTILNNQHKNYDQKAFKSKPLVNQIEQICEERRKNNSTDTSPHLILEYTPERKVYRDVNDVTGHFFHDLSGTKCDRDRTKIVLFSYRILMEWLCQEGQQVQIDLDNGEIFKFQGDLNEDENLMTLLNMDGRRICGDRVVPVSTSLESNESSIDHFSENLHQKRTRRTFYGDDSVYMIIRYHHMIQERFAKILSTQAIYAQEHFDNQKKNKRWEDGIGADMHGRKALQENIKQRRAAVNDIRNVRSCPSSSYETTLRELKQLGNAQMDIVAFEEAVKNLFPGDIVLFNNIDKLFSSLAKNIHHATCAEERENPIKLYLKYRQRIMNAERDEDMESVIQEYGQTAEEVLRGKNTYRFEFVEEQNKPFIKIWVIPREEKDDDDDDDEEGNEGGKDEDNVKDEDDGGDGEGRDGPDDDQPPPSNDDGDDEEDEDDEEDGPSGADEPESTSGSGNVPMDHLNIGENFLWSPPEEKVCTGKMTTNEKEQRNSVDYMKVTTTPRLRIHKRMLKEHKGCNVELMTGFQQLSAIVPLM | null | null | cell fate specification [GO:0001708]; chromatin remodeling [GO:0006338]; defense response to other organism [GO:0098542]; locomotion [GO:0040011]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail mating organ morphogenesis [GO:0090597]; response to endoplasmic reticulum stress [GO:0034976]; vulval development [GO:0040025] | chromatin [GO:0000785]; histone deacetylase complex [GO:0000118]; Sin3-type complex [GO:0070822] | transcription corepressor activity [GO:0003714] | PF02671;PF08295;PF16879; | 1.20.1160.11; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}. | null | null | null | null | null | FUNCTION: Probable transcriptional repressor required for the deposition of dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed chromosome pairs (both autosomes and sex chromosomes) during meiosis, but this does not seem to solely affect the transcriptional status (PubMed:21909284). Plays a role in ray fusion and patterning in the male tail, and this may be through activity of the histone deacetylase complex (HDAC) (PubMed:17506990). {ECO:0000269|PubMed:17506990, ECO:0000269|PubMed:21909284, ECO:0000305|PubMed:21909284}. | Caenorhabditis elegans |
A5JYX5 | DHS3_CAEEL | MPYVFLLSPQLEIASQWDGYYEKTFEVSDHVHKEIILKVSGQTVLITGSGSGLGRLMAFEFGKLGARLVLWDINEQGNKETLKELEAMGVEAKAYTVDLSEYKEINRTADLVKSEVGKVDILVNNAGIVTGKKLLQCPDELMVKTVSVNTNALFFTTKNFLPGMLESNKGHIVTIASMAGKCGVAGLVDYCASKHGAVGFNDSLASELYALKKDVKTTVVCPIYINTGMFDGIATKWPTLLPILSPEYVVDCIMEAVLTDRAFLAIPKFSYIFIALAGLLPTEVLNLYGDHFGITHSMDHFKGRQSRQA | 1.1.1.1 | null | response to oxidative stress [GO:0006979] | lipid droplet [GO:0005811] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26025681, ECO:0000269|PubMed:26121959}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10001}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10001}; | null | null | null | null | FUNCTION: May play a role in lipid droplet formation. May modulate triglyceride levels. {ECO:0000269|PubMed:26025681}. | Caenorhabditis elegans |
A5JYX8 | NCLN_CAEEL | MQDEIIDFFRSPALLFYMTLMLTICVVNGSQQVGEVVETEFHAYRLHQYEISGNIYGCKNYRVSYEAVSLGARTLRRTMVTTWRDLLTTDVDDMWALSTGAVLIFIPDNLDELNDIDRKAFIDLEAKLLSAKTDLAVYVAPFNDDAVSILHDVNTRSEKAPTALQHLLQSLSGNTISITSSDQSPELPPSYKPLNIVGRLSSGDRAAPTIAFVAHYDTQSAVPGVSPGADSNGSGIVALLELLAVLSKFYDSPSTRPPYNILFIWTAAGKLNYQGTRHWIDEYQKGFDSADYAKSGLSRKGFSDDRVDLAICIEAIGRKTGGFFMHAGKTPSENSVAAQLLRRLKYFSSISPKKNIELVTKKISLTTVSAWEHEKFNIKRMPAITLSTLPSPSDPARNSILDLPSALDEDELIDNIRLIGEAVLGYILDLPESGPSSDSRVKSEATMLSKDAVDKQRVHHFIRQFASRPRPVGDQRATESITSNLASVAAGYGNVFKSAVTITDAKAFGVTQNRLVAERVKPAVFELVIAAGVFTYLSAFYYIATHSQNTIEGTVAAIRKSIF | null | null | protein-containing complex assembly [GO:0065003]; regulation of protein targeting to membrane [GO:0090313]; regulation of signal transduction [GO:0009966] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | null | PF05450; | 3.40.630.10; | Nicastrin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19609303}; Single-pass type I membrane protein {ECO:0000255}. Note=During the assembly of acetylcholine receptor in muscles, colocalizes with L-AChR component unc-29 in the ER. {ECO:0000269|PubMed:19609303}. | null | null | null | null | null | FUNCTION: Involved in the recognition and selection of protein complexes to exit the endoplasmic reticulum (ER) (PubMed:19609303, PubMed:24567339). In muscles, regulates levamisole-sensitive nicotinic acetylcholine receptor (L-AChR) subunit composition, possibly by allowing only specific L-AChR subunit combinations to exit the ER (PubMed:19609303). Specifically, may promote the inclusion of alpha subunits unc-38 and unc-29 into L-AChR (PubMed:19609303). Regulates L-AChR sensitivity to agonists such as nicotine and levamisole at neuro-muscular junctions (PubMed:15990870, PubMed:19609303). In touch neurons, may prevent ER exit of incorrectly folded mec-4-mec-10 ion channel (PubMed:24567339). {ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:19609303, ECO:0000269|PubMed:24567339}. | Caenorhabditis elegans |
A5K302 | PLM5_PLAVS | MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTHIPEDLYNKLNYFFDILCIQDMNNAYDVNKRLKMTNESFNNPLVQFDDFRKSLKSIIAKENMCVKIVDGVQCWKYLEGLPDLFVTLSNNYKMKWQPHSYLYKKESFWCKGIEKQVNNKPILGLTFFKNRQVIFDIQKNRIGFVDANCPSHPTHTRPRTYNEYKRKDNIFLKIPFFYLYSLFVVFALSVLLSLVFYVRRLYHMEYSPLPSEGKAPADA | 3.4.23.- | null | proteolysis [GO:0006508] | endoplasmic reticulum membrane [GO:0005789] | aspartic-type endopeptidase activity [GO:0004190] | PF00026;PF14543; | 2.40.70.10; | Peptidase A1 family | PTM: It is not clear if the zymogen has a cleavable propeptide (By similarity). Cleavage of the putative propeptide is dispensable for catalytic activity (By similarity). {ECO:0000250|UniProtKB:Q8I6Z5}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24983235}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8I6Z5}. | null | null | null | null | null | FUNCTION: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:24983235). Specifically, cleaves after the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including EMP1 (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity). {ECO:0000250|UniProtKB:Q8I6Z5, ECO:0000250|UniProtKB:W7JPD9, ECO:0000269|PubMed:24983235}. | Plasmodium vivax (strain Salvador I) |
A5K3U9 | AMPL_PLAVS | MPLLRSSQHIKNTYWNIPKKSFRTGVPQFAESKKTRILHLHPLCKSASGVESPPFFDSQTFSSISNRKEFRKMATTVPQVVSLDPTTIPIDYHTPIDDLSIEVKDISAEACPADEGLIVFLLNSAPKHSSSGGSGGNGGSAGSSGNGEGGAQIKINSSVKDNTINEFLKEGNMENFTGKLGTSKSFYIANDQKKYVSLAYVGCGPANEETELEIRKVAYALVTLLHDSKHKKVSIIFEIKIEEALFRFFLEHLFYEYVTDERFKSADKSTETDFIKNLSLHIANADAYKGQIDKARVYFYGTYYAAQLIAAPSNYCNPVSLSNAAVELAQKVNLECKILDVKELEELKMGAYLSVGKGSMYPNKFIHLTYKGAQTGASQNEKKKIALIGKGITFDSGGYNLKAAPGSMIDLMKFDMSGCAAVLGCAYCIGTIKPDNVEVHFLSAVCENMVSKNSYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAMLYSLGTSYAGVFGNNDQLINKILSSSKTSNEPVWWLPIINEYRSSLNSKYADLNNISSSVKASSVVASLFLKEFIENTPWAHIDIAGVSWNFKARKPKGFGVRLLTEFVLNDAV | 3.4.11.1; 3.4.13.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633}; Note=Binds 2 Zn(2+) ions per subunit (PubMed:33303633). Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals (PubMed:33303633). Site 1 binds metal with low affinity and can be occupied by Zn(2+), Mn(2+), Co(2+) or Mg(2+) (By similarity). While Zn(2+) has the highest affinity for site 1, catalytic activity is the highest with Mn(2+) or Co(2+) and less with Mg(2+) (PubMed:33303633). Site 2 binds tightly to the metal ion and can be occupied only by Zn(2+) or Co(2+) (By similarity). A third metal binding site is also present in an inactive conformation of the hexamer; in this conformation only the metal binding sites 1 and 3 are occupied (By similarity). {ECO:0000250|UniProtKB:Q8IL11, ECO:0000269|PubMed:33303633}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; metallodipeptidase activity [GO:0070573]; zinc ion binding [GO:0008270] | PF00883; | 3.40.220.10;3.40.630.10; | Peptidase M17 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19931315}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633, ECO:0000269|PubMed:34133730}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence={ECO:0000269|PubMed:33303633}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.95 uM for H-Leu-NHMec {ECO:0000269|PubMed:19931315}; KM=31 uM for H-Leu-NHMec (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:34133730}; KM=20.1 uM for H-Leu-NHMec (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) {ECO:0000269|PubMed:33303633}; KM=34.2 uM for H-Leu-NHMec (at pH 8, at 37 degrees Celsius and in the presence of Mn(2+)) {ECO:0000269|PubMed:33303633}; Vmax=476.2 umol/min/ug enzyme towards H-Leu-NHMec {ECO:0000269|PubMed:19931315}; Note=kcat is 0.04 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:34133730). kcat is 0.98 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:33303633). kcat is 13.8 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Mn(2+)) (PubMed:33303633). {ECO:0000269|PubMed:33303633, ECO:0000269|PubMed:34133730}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (PubMed:19931315). Optimum pH is 7-8 for the cleavage of the Cys-Gly dipeptide (PubMed:33303633). {ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633}; | null | FUNCTION: Aminopeptidase which preferentially cleaves leucine residues from the N-terminus of peptides (PubMed:19931315, PubMed:34133730). Also, has some activity towards tryptophan and methionine and has very low activity towards alanine, arginine, asparagine, phenylalanine and tyrosine (PubMed:19931315, PubMed:34133730). No activity towards histidine, serine, valine, isoleucine, glycine, aspartic acid and glutamic acid (PubMed:34133730). In addition, cleaves the Cys-Gly dipeptide, probably as part of the glutathione regulation pathway; cleavage only occurs in the presence of Mn(2+) (PubMed:33303633). Plays a role in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides providing a source of amino acids for the parasite protein synthesis and for the maintenance of osmotic homeostasis (PubMed:34133730). {ECO:0000269|PubMed:19931315, ECO:0000269|PubMed:33303633, ECO:0000269|PubMed:34133730}. | Plasmodium vivax (strain Salvador I) |
A5K464 | SYFB_PLAVS | MPTISVHEEDLIEKLGEKIEEEKLNDICFEFGIEIDDVEYKGEKKIYKIEVPANRYDLVCVEGLCRALKSFIGKYENVSYALLTNSEEACVKEKHFMRVDESVDERRSYVVSAVLKNVKMNENVYNNIIELQEKLHHNLGKKRILLAIGIHDYDKINFPVAYKFEEKEKINFIPLNETQNVNGNNFINFYQDNINLKSYLKIISDFEKFPVIVDAGGQILSLPPIINCDYTKITYDTRNLFIECTAIDRNKAEIAVNIICSMLSEYCTPKYSIHSFFVQYDKNHKAEKGNGYLYPVFKNKTLTCHMDYVRKLSGILNLSVKDVEPLLKKMMITSKVIDSSTFTVDVPFYRSDIMHFCDIVEDIAIAYGYGNIVSEKIEIAKKNSLSACTELFRNVLAECTYTEVMTNALLSKRENYDCMLRKHRSYDDRKINLDEYNPLAPPVQIMNSKTSEYEIVRTSLIVNMLKFVSANKHRELPLRFFEIGDVSYTTYDRTDTNAVNKRYLSVIFADKFTAGLEEAHGMLETVLKEFQLFSDYKIEEKSKENVAIRSDVFYKLVPKEDPSFLNERVVDIVLCPHNLKFGIMGIIHPKVLENFSIDIPVSVIEINIETIMDVLMM | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33436639}; | phenylalanyl-tRNA aminoacylation [GO:0006432]; protein heterotetramerization [GO:0051290] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; RNA binding [GO:0003723] | PF03483;PF03484;PF18262;PF17759; | 3.30.56.10;3.50.40.10; | Phenylalanyl-tRNA synthetase beta subunit family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NSD9}. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; Evidence={ECO:0000269|PubMed:33436639}; | null | null | null | null | null | Plasmodium vivax (strain Salvador I) |
A5K9M4 | PNPH_PLAVS | MEGEMQRHIKLTKAQTTPVVLVVGDPGRVDKVKVLCDSYVDLAYNREYKSVECTYKGQKFLCVSHGVGSAGCAICFEELMNNGAKVIIRAGSCGSLQPTQMKRGDICICNAAVREDRVSHLMIYSDFPAVADYEVYATLNQVAEELKVPVFNGISLSSDMYYPHKIIPTRLEDYSKANVAVVEMEVATLMVMGTLRKVKTGGIFIVDGCPLKWDEGDFDNNLVPERLENMIKISLETCARLAKKY | 2.4.2.1 | null | inosine catabolic process [GO:0006148]; purine nucleotide catabolic process [GO:0006195]; purine ribonucleoside salvage [GO:0006166]; uridine catabolic process [GO:0006218] | cytosol [GO:0005829] | purine-nucleoside phosphorylase activity [GO:0004731]; uridine phosphorylase activity [GO:0004850] | PF01048; | 3.40.50.1580; | PNP/MTAP phosphorylase family | null | null | CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:19575810}; CATALYTIC ACTIVITY: Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:19575810}; CATALYTIC ACTIVITY: Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:19575810}; CATALYTIC ACTIVITY: Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:19575810}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for inosine {ECO:0000269|PubMed:19575810}; KM=11.2 uM for guanosine {ECO:0000269|PubMed:19575810}; KM=61.4 uM for 2'-deoxyinosine {ECO:0000269|PubMed:19575810}; KM=35.1 uM for 2'-deoxyguanosine {ECO:0000269|PubMed:19575810}; Note=kcat is 1.2 sec(-1) with inosine as substrate (PubMed:19575810). kcat is 0.7 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 5.6 sec(-1) with 2'-deoxyinosine as substrate (PubMed:19575810). kcat is 0.7 sec(-1) with 2'-deoxyguanosine as substrate (PubMed:19575810). {ECO:0000269|PubMed:19575810}; | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:19575810}. | null | null | FUNCTION: As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:19575810). Preferentially acts on inosine and guanosine, and to a lesser extent on 2'-deoxyinosine and 2'-deoxyguanosine (PubMed:19575810). {ECO:0000269|PubMed:19575810}. | Plasmodium vivax (strain Salvador I) |
A5K9S0 | SYFA_PLAVS | MQAKAQEEQKGEELSQFLQALEEEFALCQEGGGDKREADGPSLENAEAEELANRRAYYLQLKEERNVLVEESKHVTSLHMSSKHNIEHAKVLGMAKKLETLYYVVNHVRSFNTYQLTEEGKEYLRDGSPEHVTLRYVMEQEGCTLEDLKKLFGKKGEIGLNINLKKKKIELRKSDKRLFPHVEGSAHSLVDETRCYLQKVEAHGNDEGALVSHLKGILPPEKGEKKEEDEANNLIKELKKRKLIEAKKISYIYIIRTNLFTKEIKKQITDLTYLLIKNEEYKKYQVKKYNFFSSGKKMNKGNIHLLIRQMRTFKDVFVSLGFEEMNTHNYVESSFWCFDALYIPQQHPSRDLQDTFFIKVPEMCQEEFTDQSYIENVKRVHSVGDYGSFGWNYQWELKSTKKNVLRTHTTANSCRALFQLAKEYQKTGSIIPKKFFSIDRVFRNENLDSTHLAEFHQVEGLIIDRNLGLSHLIGTLSAFYKYIGISKLRFKPTFNPYTEPSMEVYGYHEENKKWLEVGNSGIFRPEMLRAMGFPPEVSVIAWGLSLERPTMIKYSIRNIRDLFGYRSVI | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33436639}; | phenylalanyl-tRNA aminoacylation [GO:0006432]; protein heterotetramerization [GO:0051290] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF01409; | 1.10.10.2320;1.10.10.2330;3.30.1370.240; | Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q505J8}. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; Evidence={ECO:0000269|PubMed:33436639}; | null | null | null | null | null | Plasmodium vivax (strain Salvador I) |
A5KE01 | ADA_PLAVS | MNILQEPIDFLKKEELKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFVSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIKVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYNLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHKADFVGFDHGGHEVDLKEYKEIFDYVRESGVPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVAESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKIKNLYF | 3.5.4.31; 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:18602399, ECO:0000305|PubMed:19728741}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741}; | adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | 2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:19728741}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=9.5 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 1.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.13 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741). {ECO:0000269|PubMed:19728741}; | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:19728741}. | null | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (PubMed:19728741). {ECO:0000269|PubMed:19728741}. | Plasmodium vivax (strain Salvador I) |
A5LGW7 | POLG_HAVJ8 | MNMSRQGIFQTVGSGLDHILSLADVEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGAHQSEPLKTSVDKPGSKRTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDASQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPEQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVSHITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSSHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTKQNVPDPQVGITTVRDLKGKANQGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNTNAMMSSETMLDRIALGDLESSVDDPRSEEDRKFESHIEKRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKIKGVFSQAKISLFYTEDHEIMKFSWKGITADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLVRVNDEKWTEMKDDKIVSLVEKFTSNKHWSKINFPHGMLDLEEIAANSKEFPNMSETDLCFLLHWLNPKKINLADRMLGMSGIQEIKEKGVGLIGECRAFLDSITTTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQEEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSISNWLRDICSGITIFKSFKDAIYWLYTRIREYYDVNYGNKKDVLNILKDNQQKIERAIEEADNFCVLQIQDVEKFEQYQKGVDLIQKLRTVHSMAQVDPGLTVHLAPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLVMDSHNISLSELLSSLVMTVEIRKQNMSEFMELWSQGMSDDDNDSAVAEFFQSFPSGEPSGSKLSRFFQSVTNHKWVAVGAAVGVLGVLVGGWYVYKHFTKKKEEPIPSEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGIKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITEHFIKKSDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTIDLTVDQAWRGKGEGLPGMCGGALISSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIVESQRIMKVEFTQCSMNVVSKTLFKKSPIHHHIDKNMINFPAVMPFSRAEIDPMAVMLSKYSLPIVDEPEDYKDVSVFFQNKILGKSPLVDDFLDIEMAITGAPGIDAINMDSSPGYPYVQEKLTKRDLIWLDDNGMFLGVHPRLAQRILFNTTMMENCSDLDVVFTTCPKDELRPLDKVLESKTRAIDSCPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDQLFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRILTEMSGAPNHFGEALINTIIYSKHLLYNCCYHVYGSMPSGSPCTALLNSIINNVNLYYVFSKIFKKSPVFFCDAIRILCYGDDVLIVFSRQVQFDNLDSIGQRIVDEFRKLGMTATSADKSVPQLKPVSELTFLKRSFNLVDDRIRPAIAEKTIWSLVAWQRSNAEFEQNLENAQWFAFMHGYEFYQDFYHFVQSCLEKEMIEYRLKSYDWWRMKFNDQCFVCDLS | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03303}.; PTM: [Protein VP1-2A]: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Viral protein genome-linked]: VPg is uridylylated prior to priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Unlike other picornaviruses, does not seem to be myristoylated. {ECO:0000250|UniProtKB:P08617}. | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2B]: Host membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2C]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. May associate with membranes through a N-terminal amphipathic helix. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3ABC]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion outer membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3AB]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3A]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}; Cytoplasmic side {ECO:0000250|UniProtKB:P08617}. Note=Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P08617}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P08617}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of the immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2BC]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3ABC]: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3AB]: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3A]: May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3CD]: Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. {ECO:0000250|UniProtKB:P08617}. | Human hepatitis A virus genotype IIIB (isolate HAJ85-1) (HHAV) (Human hepatitis A virus (isolate Human/Japan/HAJ85-1/1985)) |
A5LHG2 | ADM5_PIG | MTAHILLLWLFASSILGDPDSAGRLTRHQVSLKSGRLCSLGTCQTHRLPEIIYWLRSASTKELSGKAGRKPQDPYSYGRRRRRRRRRREARLLRRLQDPSLRRAQLAG | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; positive regulation of heart rate [GO:0010460]; regulation of systemic arterial blood pressure [GO:0003073]; regulation of urine volume [GO:0035809] | extracellular region [GO:0005576] | hormone activity [GO:0005179] | null | null | Adrenomedullin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Seems to have a peripheral vasodepressor effect and a central vasopressor effect. {ECO:0000269|PubMed:18434369}. | Sus scrofa (Pig) |
A5LHX3 | PSB11_HUMAN | MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV | 3.4.25.1 | null | CD8-positive, alpha-beta T cell differentiation [GO:0043374]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; proteolysis [GO:0006508]; T cell differentiation in thymus [GO:0033077] | cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome core complex, beta-subunit complex [GO:0019774] | endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; threonine-type endopeptidase activity [GO:0004298] | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; | null | null | null | null | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome (By similarity). Plays a pivotal role in development of CD8-positive T cells (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A5PF10 | NEUR1_PIG | MTAERPGAVPLGRPGRPPMLGLGEAYRAQVFASIFLLLLSPAGVGARAKNDFNLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSASDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCRVASTMLVWSKDDGISWSSPRNLSLDIGTEMFAPGPGSGIQKQWAPQKGRLIVCGHGTLERDGVFCLLSDDHGASWRYGSGISGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGAVATSSGIIFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQIWPGPSGYSSLATLEGSVGGEDQAPQLYVLYEKGRNRYTESISLAKVSVYGTL | 3.2.1.18 | null | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308] | PF13088; | 2.120.10.10; | Glycosyl hydrolase 33 family | PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). {ECO:0000250}. | Sus scrofa (Pig) |
A5PHD6 | PKS1_SARSH | MAAHGQTSKRGNNTLLLFGALVQSHDVSTLRSMRESIVVQHGEHSWLVDSIKALPQDFEAALPHLPFFDQATTTTIHQLLVDAVSSFLTGSFETLVSPLPAALLIPLAVATQLAHYVEYSRQSPTGLAEGKEALGFCTGILSAFAVASSHDVCDLAKYGAAAMRLGMLVGLVVDCEDAAAGQGRYRSVSAGWDSEEKHAAMLKIVQSFEEAYVSVHFDKNRATITTSPGTISNLTRQLQKEGLVASDMGLLGRFHFAGSTKPREVTVDQLVSFCNSPAGALFRLPDADSLRLATRINDRDGGLITQGSLHEHALQSILVKLAAWFETFSSATTTQANTGAQNGRARPQIVDFGPQNSVPHSLASTVDINSGNGKTRRVKPADAQSSANSTHTRPWLDTDIAIVGMSCKVPGAENLEEFWDLLVSGKSQHQEISGQEGGRFDFGDTAFRTAADQRRRWFANLVSNHDQFDHRFFKKSARESASMDPQQRHILQVAYQAVEGSGYFNKSSSSTPTNANIGCYVGLCLGDYESNVASHPATAFTATGNLQGFVSGKVSHYFGWTGPAVTVNTACSSSLVAVHLACQAILSGECEAALAGGSHIMTSATWFQNLAGGSFLSPTGACKPFDSKADGYCRGEGVGAVFLKRMSQAMADGDMVLGVVAATGVQQNQNCTPIFVPNAPSLENLFSRVMTKARVKPADISVVEGHGTGTAVGDPAEYDAIRKALGGTTHRSADKPLMLSSVKGLVGHMECTSGVIGMIKLLLMMNKGALPPQASFQSINPALGATPADHMFIPTRPQPWVVPAGGFRAALLNNYGASGSNASAVLVQSPSMSFRPEITVGSRPAAGIKFPFWLAAFDKKSLSRYVKALRKWLCRLDGDQSLASLSFNLARQSNRTMQANLVLTARSIEALDQSLADFENGNDGSFIERTPASSQPTVILCFGGQVSCFVGLDKQVYQDMALVRYYLDRVDAVIQCQGGRSIFPGIFNRSPPSKVDIVHLHTMLFAMQYASARCWIDSGVKPAALVGHSFGTLTALCISGILSLEDTIKAIMCRAKLLNEAWGPDQGGMIAVEGDIDVIEELLDEANKNHDDKPATIACYNGPTSFTLAGSTTAMDAVAAQLKNGAKYSKGMKSKRIYVTHAFHSVLVDPLLEELTQRVADSGVRFRKPIIPVELSTEQHMSESELTSEFMANHMRQPVYFHHAVERLARRYAGGSSPCVFLEAGTNSSVCNMASRALGSTEFVTKSSSLSFHGVNIANCDAGWNKLTDTTVNLWETGVRVHHWAHHGVQQMHQTDIKPLLVPPYQFDPDSRHWIDLKVPRKALMETDEADAGGKKQSDAEKLPETILTFHSSDAVGAQKQARFRVNTMLEEYKQLLRGHMTLETAPILSATLQINLVIEAISSTQPEYKSSKSQPQIQDVVYQSPVCFNSANTLWVEVTNVSGQWMFQVFSTTTQELSPKSTRMVHTKGTVAFKNPGDAEIRRQLMSYERLFSHGRATDLLQNSNASTAPIDEMLGNQSIYRIFSEIVSYGPEFRGLQKMVSRGNETAGHVVHLKHQDSASTEAEPWFDPHLADTFCQLGGLWVNCMMPERERGNGHVYLANGIDQWIRGYPAASTDRPEAFNVFAVNKQASEQLTLTDVFVFNAADGALVEVILGIAYVKIARPSMEKLLARLTEPSWVAGGKTTPQTATKPAAAPVVADHTPRTTESASTVNGVNLDDRKPEGTALPQEMLSDTEELRPKAQGQELQDMIARVKAVMADISGLDISEIKDDSNLADLGIDSLVGMEMTHEIESTLKVELPESEIMSVVDMEGLLQCVAGALGLSMTGASSDTLTASSDSGINSAKSSILSGTSTSTSTGTTDTGSDVGQSMKEPSLMLDTVKKAFAQTKEATDARIKAASNQVSYCSTSLPQQNELSVLLTITALEALGAGFSTARPGSQLTRISHAPGHEQFVTHLYKEIETATQIIKIDGHGAQAVITRTAVPLPDVESRQVALCEQMLRGDPEQVGTMELIKHAGENLHRVLSGETDGAKVIFGSKTGSKLVSQWYAQWPLNRSLIAQMGDFLTAVVAGIQADEDMPFSEINPLRIMETGAGTGGTTKQIVPLLARLGLPVVYTFTDLAPSFVAAARKTWGKEYPWMQFRTLDMEKTPPSVEDGLPLQHFIVSANAVHATKSISATTGNLRKALRTDGFLLMMEMTRTPFWVDLIFGLFEGWWLFEDGRKHALTHEALWDQELSKVGFGYVDWTEGMTAESEIQKIILASADANTRLERVRLPASHTDYHLNQVGVENEARELMVADYVSTLTKEFNKTMTQYTDAGLSLSSRTSQTPMSSQKRCILITGGTGGLGAHLVAEAALLPDVNMVICLNRPNRKQEARERQLVSLEKKGLILSPEALAKITVFETDLSQPGSLGLSDDKYNLLRGNVTHIIHNAWLMHSKWPVRRFEPQLRIMAHMLNLAADIATCQRTQGQRQPGPPVSFVFVSSIATVGYHPVVTNPGNPAVPETRIPISSVLPTGYGEAKYICERMLDATLHQYPAQFRASAVRLGQIAGSEINGHWNSAEHISFLVKSSQSIGALPALPGPMGWTPADYVARGLVEIATQPDNIELYPIYHIENPVRQPWDEALAVLADEMGISSEALPFQEWVQTVRDWPRQGDNTAAGANPAYLLVDFLEDHFLRMSCGGLLLGTAKAREHSPSLAGMGPVSDELLRLFVRSWKEVGFLL | 2.3.1.- | null | fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550]; terpenoid biosynthetic process [GO:0016114] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00698;PF18558;PF00109;PF02801;PF08242;PF07993;PF00550;PF16073; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17912413, ECO:0000269|PubMed:20552126, ECO:0000269|PubMed:29773797}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:17912413, PubMed:20552126, PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:20552126, PubMed:29773797). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). {ECO:0000269|PubMed:17912413, ECO:0000269|PubMed:20552126, ECO:0000269|PubMed:29773797}. | Sarocladium schorii (Acremonium strictum (strain IMI 501407)) |
A5PJM4 | FSP1_BOVIN | MGSQVSMDAGAVHVVIVGGGFGGIAAASQLQALNIPFVLVDMKDSFHHNVAALRASVESGFAKKTFISYSVTFKENFRQGLVVEIDLKNQTVLLEDGQALPFSHLILATGSTGLFPGKFNQVSSQQMAIQAYEDMVTQVQRSQSIVVVGGGSAGVEMAAEIKTEYPEKEVTLIHSKMALADTELLPCVRQEVKEILLRKGVQLLLSERVSNLEALPVNERRECIKVQTDKGTEVDANLVIVCNGIKINSAAYRSAFGDRLASNGALRVNEYLQVEGYSHIYAIGDCADVREPKMAYHASLHANVAVANIVNSMKQRPLKTYKPGSLTFLLAMGRNDGVGQISGFYVGRLMVRLAKSRDLLVSTSWKTMKQSPP | 1.6.5.- | COFACTOR: Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; Note=Binds 6-hydroxy-FAD non-covalently. {ECO:0000250|UniProtKB:Q9BRQ8}; | apoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]; regulation of cellular response to oxidative stress [GO:1900407]; vitamin K metabolic process [GO:0042373] | cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655] | PF07992; | 3.50.50.100; | FAD-dependent oxidoreductase family | PTM: N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane. {ECO:0000250|UniProtKB:Q9BRQ8}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9BRQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BRQ8}. Nucleus {ECO:0000250|UniProtKB:Q9BRQ8}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + phylloquinone = NAD(+) + phylloquinol; Xref=Rhea:RHEA:74075, ChEBI:CHEBI:15378, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74076; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menaquinone-4 + NADH = menaquinol-4 + NAD(+); Xref=Rhea:RHEA:74079, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78277, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74080; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADH = menadiol + NAD(+); Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378, ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; | null | null | null | null | FUNCTION: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death. {ECO:0000250|UniProtKB:Q9BRQ8}. | Bos taurus (Bovine) |
A5PJN2 | ERO1A_BOVIN | MGRRWGFLIGFLVAVGLLGLGHGEQQPSETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGKSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVVPFFERPDFQLFTGNKDQDAENKMLLLEILHEIKSFPLHFDENSFFAGNKKEANKLKEDFRLHFRNISRIMDCVGCLKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH | 1.8.4.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q96HE7}; | cell redox homeostasis [GO:0045454]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; release of sequestered calcium ion into cytosol [GO:0051209]; response to endoplasmic reticulum stress [GO:0034976] | dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; protein-disulfide reductase activity [GO:0015035]; thiol oxidase activity [GO:0016972] | PF04137; | null | EROs family | PTM: The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on Ser-145 by FAM20C in the Golgi which increases its enzymatic activity (By similarity). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (By similarity). {ECO:0000250|UniProtKB:Q8R180, ECO:0000250|UniProtKB:Q96HE7}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q96HE7}. Secreted {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000250|UniProtKB:Q96HE7}. | null | null | null | null | null | FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000250|UniProtKB:Q96HE7}. | Bos taurus (Bovine) |
A5PJP6 | BRCC3_BOVIN | MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDLRNDPKFTYTGTEMRTVAEKVDTVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESPRGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHVQELQQEKEELLQELSSLE | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7, ECO:0000250|UniProtKB:P46736}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; response to ionizing radiation [GO:0010212] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity). {ECO:0000250|UniProtKB:P46736, ECO:0000250|UniProtKB:P46737}. | Bos taurus (Bovine) |
A5PJS6 | UBP10_BOVIN | MALRSPQYIFGDFSPDEFNQFFVTPRASVELPPYGGTVLCGAQAADDLPDGHDYQRIEFGVNEVIEPSDTLPRTPNYSISSTLNPQAPEFILSCTTSKKLPDDIDKEVNYSSANCQYPGPALALDGGSPAEAEALENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGEGGPSAEALVNGHAGPAVSNSVGAEDTDLMGDVPTAGTPRTWGSPQDATDFVSDAGPAGAFPGALDGGARTAGQLEGCPGADSEASCLPAEAGRDTLLRTAVAQPSVGTDTTENLGVTNGQILESLGEGTAANGVELHTVESSDSDPAKAESAPPPADAPASAAGTVPASQPAKSWASLFHDSKPSSSSLPVVSVETKYSPPATSPLVSEKQAEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKLIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVIKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPNNDKLTISNGPKSHSVNEDEQEEPGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTRQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGSSATGGHYTTDVFQIGLNGWLRIDDQTVKVVSQQQVVRPAAERTAYLLYYRRVDLL | 3.4.19.12 | null | autophagy [GO:0006914]; cellular response to interleukin-1 [GO:0071347]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA repair [GO:0006281]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of stress granule assembly [GO:0062030]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; rescue of stalled ribosome [GO:0072344] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; p53 binding [GO:0002039]; transmembrane transporter binding [GO:0044325] | PF07145;PF00443; | 3.90.70.10; | Peptidase C19 family, USP10 subfamily | PTM: Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. {ECO:0000250}.; PTM: Ubiquitinated. Deubiquitinated by USP13 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus {ECO:0000250|UniProtKB:Q14694}. Early endosome {ECO:0000250|UniProtKB:Q14694}. Note=Cytoplasmic in normal conditions (By similarity). After DNA damage, translocates to the nucleus following phosphorylation by ATM (By similarity). {ECO:0000250|UniProtKB:Q14694}. | 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:Q14694}; | null | null | null | null | FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits. Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid-liquid phase separation (LLPS) and assembly of stress granules. Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome. Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization. Plays a negative role in the RLR signaling pathway upon RNA virus infection by blocking the RIGI-mediated MAVS activation. Mechanistically, removes the unanchored 'Lys-63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, essential for its activation. {ECO:0000250|UniProtKB:Q14694}. | Bos taurus (Bovine) |
A5PJW8 | RPB2_BOVIN | MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVEDAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETKKAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQKFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLSHLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSEVSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASGVVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIVAIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGMRHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELEGTNRRYTKRDCSTFLRTSETGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEGITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGYHLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSRDGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGCRNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P30876}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P30876}; | null | chromosome, telomeric region [GO:0000781]; RNA polymerase II, core complex [GO:0005665] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; hydrolase activity [GO:0016787]; ribonucleoside binding [GO:0032549]; RNA polymerase II activity [GO:0001055]; RNA-dependent RNA polymerase activity [GO:0003968]; zinc ion binding [GO:0008270] | PF04563;PF04561;PF04565;PF04566;PF04567;PF00562;PF04560; | 2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10; | RNA polymerase beta chain family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30876}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21250; Evidence={ECO:0000250|UniProtKB:P30876}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P30876}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:P30876}; CATALYTIC ACTIVITY: Reaction=a 3'-end ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end ribonucleotide-RNA + a ribonucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:77763, Rhea:RHEA-COMP:17428, Rhea:RHEA-COMP:18982, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58043, ChEBI:CHEBI:74896, ChEBI:CHEBI:197502; Evidence={ECO:0000250|UniProtKB:P30876}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77764; Evidence={ECO:0000250|UniProtKB:P30876}; | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (PubMed:16769904, PubMed:26789250). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:16769904, PubMed:26789250). Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:16769904, PubMed:26789250). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:9604937). {ECO:0000250|UniProtKB:P30876, ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250, ECO:0000269|PubMed:9604937}.; FUNCTION: RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription. {ECO:0000250|UniProtKB:P30876}. | Bos taurus (Bovine) |
A5PJZ1 | SCMC1_BOVIN | MLRWLRGFVLPTAACQDVEPPTRYETLFQKLDRNGDGVVDISELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQILGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSAKMNIYGGFQQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFVSGSMAGATAQTFIYPMEVLKTRLAVGKTGQYSGMFDCAKKILKYEGMGAFYKGYVPNLLGIIPYAGIDLAVYELLKSHWLDNFAKDSVNPGVMVLLGCGALSSTCGQLASYPLALVRTRMQAQAMIEKSPQLNMVGLFRRILSKEGLPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK | null | null | adenine nucleotide transport [GO:0051503]; ADP transport [GO:0015866]; ATP transport [GO:0015867] | mitochondrial inner membrane [GO:0005743] | adenine nucleotide transmembrane transporter activity [GO:0000295]; ADP:inorganic phosphate antiporter activity [GO:0140988]; ATP transmembrane transporter activity [GO:0005347]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509] | PF13499;PF00153; | 1.10.238.10;1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6NUK1}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) + phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out); Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in) + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out); Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) + ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out); Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) + H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) + H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out); Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out); Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) + phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57667; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; | null | null | null | null | FUNCTION: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates. {ECO:0000250|UniProtKB:Q6NUK1}. | Bos taurus (Bovine) |
A5PK42 | ODAD4_BOVIN | MADPENEVLRSTFPSYMAEGERLYLCGEFAKAAHSFSNALHLQSGDKNCLVARSKCFLKMGELEKSLEDAEASLQGDPTFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFKVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAESMRAQQKPHPVRQLIHHPKRESKRKGSLKSEKIVRQLLGELYVDKEYLEKLLLDEDLIKGTIKHGLTVEDLIMTGINYLETRSDFWRQQKPIYARERDRKLMQEKWLRDRKRRPSQTARYILKSLEDIDMLLTSGSAEGSLQKAEKVLKKVLEWNKEEVPNKDELVGNLYSCIGNAQIELGQMVAALQSHRKDLEIAKEYDLPDAKSRALDNIGRVFARVGKFQQAIDTWEEKIPLAKTTLEKTWLFHEIGRCYLELDQAWEAQSYGEKSQQCAEEEGDMEWQLNASVLVAQAQVKLRDFESAVNNFEKALERAKLVHNNEAQQAIINALDDANKGIIEELKKTNYREILKEKKEKENATMLDGQTRTAKEKETRKTKDEPEKVMKQWVQEQTEKQLEGVLSKETLGVTARQPEQRQREDPEKASWRKELGAKERGPGDTAKGQFGEAGRTEQNREETREIYRRPSELDQNLSDESSPRESEGLEKRLSKTDGGELEALGKTESGEIKEMEITENSEKIEKDEKEDEPIE | null | null | brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart development [GO:0007507]; lung development [GO:0030324]; mucociliary clearance [GO:0120197]; outer dynein arm assembly [GO:0036158]; protein localization to motile cilium [GO:0120229] | 9+0 motile cilium [GO:0097728]; 9+2 motile cilium [GO:0097729]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; outer dynein arm docking complex [GO:0120228] | null | PF13181; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. | null | null | null | null | null | FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme. {ECO:0000269|PubMed:34715025}. | Bos taurus (Bovine) |
A5PK46 | LIPR2_BOVIN | MLPSWTIGLLLLATVRGKEICYEPFGCFSDEKPWTGILQRPLKLFPWSPEDIDAHFLLYTNENPNNYQRINITDLATVRASNFQLDRKTRFVIHGFIDDGDSGWPTDLCKKMFKVEKVNCICVDWEHGAWTKYTQAVHNTRVVGAEIAFFIQGLSTELGYGPENVHLIGHSLGAQLAAEAGRRLGGQVGRITGLDPAQPCFEGTPEEVRLDPSDAMFVDVIHTDSASIIPFLSLGIRQKVGHLDFYPNGGKEMPGCQKNILSTIIDINGIWQGIQDFVACSHLRSYKYYSSSILNPDGFLGYPCASYEEFQEGGCFPCPAGGCPKMGHYADQFQGKTSAVGQTFFLNTGSSGNFTSWRYRVSVTLAGTKKVRGSIRIALYGSNGNSKQYQIFKGSLQPNASHTHDIDVDLNVGKVQKVKFLWNNNVINLFWPKLGASRVTVQGGEDRTEYNFCSNDTMRENALQTLYPC | 3.1.1.26; 3.1.1.3 | null | cellular defense response [GO:0006968]; galactolipid catabolic process [GO:0019376]; intestinal lipid catabolic process [GO:0044258]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; response to bacterium [GO:0009617]; triglyceride catabolic process [GO:0019433] | extracellular space [GO:0005615]; neuron projection [GO:0043005]; zymogen granule membrane [GO:0042589] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; acylglycerol lipase activity [GO:0047372]; calcium ion binding [GO:0005509]; galactolipase activity [GO:0047714]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+); Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+) + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153, ChEBI:CHEBI:88155; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) + octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:88066; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol + H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol; Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+); Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+); Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396, ChEBI:CHEBI:28868, ChEBI:CHEBI:90310; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + a monoacyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665; Evidence={ECO:0000250|UniProtKB:P54317}; | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000250|UniProtKB:P54317}.; PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}. | null | null | FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols. When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids. Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides. Hydrolyzes long-chain monoglycerides with high efficiency (By similarity). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54317, ECO:0000250|UniProtKB:P54318}. | Bos taurus (Bovine) |
A5PK74 | RIOX1_BOVIN | MDGLRASAGLLRRGRLRRRRQQQPHSGSVLALPLRPRKIRRQLRRSVSSRMAALRAQTLQSEDSEDSRVESTVGEPGDPLAGGTAALSDATGREPHGQLGPVELLEASPASRSLQTPRALVEAQTPAARLVEAQTPAARLVEAHTPAARLVEAHTPPARLVEASALPARLVETSALLCSTQHLAAVPPSVAPAMLSGPQGESTGEELPWDSPLQRILAELNRIPSSRRRAARLFEWLISPMPPDHFYRRLWEREAVLVRRQDHSYYQGLFSTAVLDSILRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYRAGCSLRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTFQRNTWGDFLEAVLPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGLPIRWEAGEPVNVGAQLTTETEVHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLRSYPEFVRVGDLPCDTVEDQLSLATMLYDKGLLLTKMPLT | 1.14.11.27; 1.14.11.79 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9JJF3}; | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of osteoblast differentiation [GO:0045668] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506]; peptidyl-histidine dioxygenase activity [GO:0036139]; protein demethylase activity [GO:0140457] | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6W3}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6W3}. Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. {ECO:0000250|UniProtKB:Q9H6W3}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.27; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl-[protein] + O2 = CO2 + formaldehyde + L-lysyl-[protein] + succinate; Xref=Rhea:RHEA:60924, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60925; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L-histidyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:54256, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:13840, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29979, ChEBI:CHEBI:30031, ChEBI:CHEBI:138021; EC=1.14.11.79; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54257; Evidence={ECO:0000250|UniProtKB:Q9H6W3}; | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis. Participates in MYC-induced transcriptional activation (By similarity). {ECO:0000250|UniProtKB:Q9H6W3, ECO:0000250|UniProtKB:Q9JJF3}. | Bos taurus (Bovine) |
A5PKJ4 | MK07_BOVIN | MAEPLKEDDGEDGSGEPPGPVKAEPAGTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMTVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARVSAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPLPCPGPAPDTIDLTLQPPPPASEPAPPKKEGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGVSGGPSADPLAGLVLSDNDRSLLERWTRMAQPPAPAPATARPPSPPAGPATQPTGPLPQPACPPPAPAAGPAAPQTTAASGLLAPQPLVPPPGLPGPSALSVLPYFPSGPPPPDPGGAPQPSTSESPDVTLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQEP | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | calcineurin-NFAT signaling cascade [GO:0033173]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to transforming growth factor beta stimulus [GO:0071560]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of response to cytokine stimulus [GO:0060761]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; phosphorylation [GO:0016310]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of angiogenesis [GO:0045765] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}. Note=Translocates to the nucleus upon activation. {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=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; | null | null | null | null | FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via interaction with STUB1/CHIP and promotion of STUB1-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression (By similarity). Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P0C865}. | Bos taurus (Bovine) |
A5PKP9 | UB2D4_XENLA | MALKRIQKELMDLQRDPPAQCSAGPVGEDLFHWQATIMGPNDSPFQGGVFFLTIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPEIAHTYKADREKYNRLAREWTQKYAM | 2.3.2.23 | null | pronephric nephron tubule development [GO:0039020]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567] | nucleus [GO:0005634] | ATP binding [GO:0005524]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:Q9Y2X8, ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9Y2X8, ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Regulates pronephros development, possibly by promoting ubiquitination and thus inactivation or degradation of map3k10/mlk2. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18021256}. | Xenopus laevis (African clawed frog) |
A5PKW4 | PSD1_HUMAN | MAQGAMRFCSEGDCAISPPRCPRRWLPEGPVPQSPPASMYGSTGSLLRRVAGPGPRGRELGRVTAPCTPLRGPPSPRVAPSPWAPSSPTGQPPPGAQSSVVIFRFVEKASVRPLNGLPAPGGLSRSWDLGGVSPPRPTPALGPGSNRKLRLEASTSDPLPARGGSALPGSRNLVHGPPAPPQVGADGLYSSLPNGLGGPPERLATLFGGPADTGFLNQGDTWSSPREVSSHAQRIARAKWEFFYGSLDPPSSGAKPPEQAPPSPPGVGSRQGSGVAVGRAAKYSETDLDTVPLRCYRETDIDEVLAEREEADSAIESQPSSEGPPGTAYPPAPRPGPLPGPHPSLGSGNEDEDDDEAGGEEDVDDEVFEASEGARPGSRMPLKSPVPFLPGTSPSADGPDSFSCVFEAILESHRAKGTSYTSLASLEALASPGPTQSPFFTFELPPQPPAPRPDPPAPAPLAPLEPDSGTSSAADGPWTQRGEEEEAEARAKLAPGREPPSPCHSEDSLGLGAAPLGSEPPLSQLVSDSDSELDSTERLALGSTDTLSNGQKADLEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQRYFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSIKNEKLQWAIDEEELRRSLSELADPNPKVIKRISGGSGSGSSPFLDLTPEPGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYKPGKALSETELKNAISIHHALATRASDYSKRPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFPAAVSSQKKFSRPLLPSAATRLSQEEQVRTHEAKLKAMASELREHRAAQLGKKGRGKEAEEQRQKEAYLEFEKSRYSTYAALLRVKLKAGSEELDAVEAALAQAGSTEDGLPPSHSSPSLQPKPSSQPRAQRHSSEPRPGAGSGRRKP | null | null | neuron projection development [GO:0031175]; regulation of ARF protein signal transduction [GO:0032012]; signal transduction [GO:0007165] | cleavage furrow [GO:0032154]; dendritic spine [GO:0043197]; postsynaptic density, intracellular component [GO:0099092]; ruffle membrane [GO:0032587] | guanyl-nucleotide exchange factor activity [GO:0005085]; phospholipid binding [GO:0005543] | PF15410;PF01369; | 1.10.1000.11;2.30.29.30; | PSD family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Cleavage furrow {ECO:0000269|PubMed:23603394}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In later cytokinesis phases, fades away from the cleavage furrow and becomes uniformly distributed throughout the plasma membrane. {ECO:0000269|PubMed:23603394}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for ARF6 (PubMed:23603394). Induces cytoskeletal remodeling (By similarity). {ECO:0000250|UniProtKB:Q5DTT2, ECO:0000269|PubMed:23603394}. | Homo sapiens (Human) |
A5PLL7 | PDES1_HUMAN | MAGAENWPGQQLELDEDEASCCRWGAQHAGARELAALYSPGKRLQEWCSVILCFSLIAHNLVHLLLLARWEDTPLVILGVVAGALIADFLSGLVHWGADTWGSVELPIVGKAFIRPFREHHIDPTAITRHDFIETNGDNCLVTLLPLLNMAYKFRTHSPEALEQLYPWECFVFCLIIFGTFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVSPHETYFCITTGWLNYPLEKIGFWRRLEDLIQGLTGEKPRADDMKWAQKIK | 1.14.19.77 | null | ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | plasmanylethanolamine desaturase activity [GO:0050207] | PF10520; | null | Fatty acid desaturase CarF family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11076860, ECO:0000269|PubMed:31604315}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:22956, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:75028, ChEBI:CHEBI:77290; EC=1.14.19.77; Evidence={ECO:0000269|PubMed:31604315, ECO:0000269|PubMed:32209662}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22957; Evidence={ECO:0000269|PubMed:31604315}; CATALYTIC ACTIVITY: Reaction=a 1-O-hexadecyl-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z-hexadecenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:61960, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145181, ChEBI:CHEBI:145186; Evidence={ECO:0000269|PubMed:31604315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61961; Evidence={ECO:0000269|PubMed:31604315}; CATALYTIC ACTIVITY: Reaction=a 1-O-octadecyl-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z-octadecenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:61964, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145182, ChEBI:CHEBI:145187; Evidence={ECO:0000269|PubMed:31604315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61965; Evidence={ECO:0000269|PubMed:31604315}; CATALYTIC ACTIVITY: Reaction=a 1-O-(9Z-octadecenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-O-(1Z,9Z-octadecadienyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:61968, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145183, ChEBI:CHEBI:145188; Evidence={ECO:0000269|PubMed:31604315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61969; Evidence={ECO:0000269|PubMed:31604315}; | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:31604315}. | null | null | FUNCTION: Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the endoplasmic reticulum membrane (PubMed:31604315, PubMed:32209662, PubMed:33859415). Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxidative and signaling mechanisms (PubMed:31604315). {ECO:0000269|PubMed:31604315, ECO:0000269|PubMed:32209662, ECO:0000269|PubMed:33859415, ECO:0000303|PubMed:31604315}. | Homo sapiens (Human) |
A5PN09 | UBP20_DANRE | MTDSGDLCPHLDSIGEVTKEELIQKSKGTCQSCGVGGPNLWACLQCDCPYVGCGESYSDHSTIHAQAKKHNLTVNLTTFRVWCYVCEREVFLEPKPVTPVSSAHRCKPHDQDPVSQTTCYPLKAVPIAVADEEGSESEEDELKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFQDCSGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPTTLFHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPLFDCSGGISEVEPDLSLDSCNLVDGDRSPSEDEFLSCDSGSGSERGDGERAGGEAELLIQDECVAVRGTGGISEKERLKERRGEERTREMDEDADVDTAAQDGQAERETETATPATAVPAPGNTEPDNEASMHCPSSRPCSPAHSVQELHSRLSSNPPRSSPLRTGPTYTFKKAQMLLSTKKKKQSRFRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSSIHQSAPVKAGVCTDGYAAQGWISYIMDSIRRFVVSCIPSWFWGPMVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLKPFLAKESPSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEESVRERQRVVALANLKEPSLLQFYISREWLNKFNTFTEPGPITNHTFLCQHGGIPPTKYHYVDDLVVILPQNVWEYLYNRFGGGPAVNHLYVCAICQVEIETLAKRRKLEIDTFIKLNKEFQAEEAPTVILCISMQWFREWENFVKGKDNEPPGPIDNSKIAVMKGGHIQLKQGADYGQISEETWQYLLSIYGGGPEIAVRQTISPPDTDTHGERKIEAETRAL | 3.4.19.12 | null | central nervous system morphogenesis [GO:0021551]; cranial skeletal system development [GO:1904888]; endocytosis [GO:0006897]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of G protein-coupled receptor signaling pathway [GO:0008277] | centrosome [GO:0005813]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; zinc ion binding [GO:0008270] | PF06337;PF00443;PF02148; | 3.90.70.10;3.30.2230.10;3.30.40.10; | Peptidase C19 family, USP20/USP33 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {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; | null | null | null | null | FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5PN28 | OTO1A_DANRE | MPNILHPFIIIMTLLVVATGNQASIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLKGARGIRGFKGFKGEPAVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATKD | null | null | extracellular matrix organization [GO:0030198]; otolith development [GO:0048840]; otolith mineralization [GO:0045299]; protein complex oligomerization [GO:0051259] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF00386;PF01391; | 2.60.120.40; | OTOL1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000250|UniProtKB:Q4ZJM7}. | null | null | null | null | null | FUNCTION: Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear (PubMed:15905077, PubMed:29076638). Acts as a scaffold for biomineralization by sequestering calcium (PubMed:29076638). {ECO:0000269|PubMed:15905077, ECO:0000269|PubMed:29076638}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5TY85 | PKNA_MYCTA | MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTFSSGQRALLWAAGVLGALAIIIAVLLVIKAPGDNSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTPHSRASLARYEIAQ | 2.7.11.1 | null | phosphorylation [GO:0016310]; regulation of primary metabolic process [GO:0080090] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {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; Evidence={ECO:0000269|PubMed:11856348, ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11856348, ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}; | null | null | null | null | FUNCTION: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ and MurD. Shows a strong preference for Thr versus Ser as the phosphoacceptor. {ECO:0000269|PubMed:11856348, ECO:0000269|PubMed:17068335, ECO:0000269|PubMed:18557704}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U1U6 | KGD_MYCTA | MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHELLLSDGFWDEVFRELSIPYLPVRWSTDNPDSIVDKNARVMNLIAAYRNRGHLMADTDPLRLDKARFRSHPDLEVLTHGLTLWDLDRVFKVDGFAGAQYKKLRDVLGLLRDAYCRHIGVEYAHILDPEQKEWLEQRVETKHVKPTVAQQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGATGLYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLDHGSIDSDGQRAFSVVPLMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVARLAVDFRQRFKKDVVIDMLCYRRRGHNEGDDPSMTNPYVYDVVDTKRGARKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHGVQPSESVESDQMIPAGLATAVDKSLLARIGDAFLALPNGFTAHPRVQPVLEKRREMAYEGKIDWAFGELLALGSLVAEGKLVRLSGQDSRRGTFSQRHSVLIDRHTGEEFTPLQLLATNSDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSARIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRHKAAVSEIKDFTEIKFRSVLEEPTYEDGIGDRNKVSRILLTSGKLYYELAARKAKDNRNDLAIVRLEQLAPLPRRRLRETLDRYENVKEFFWVQEEPANQGAWPRFGLELPELLPDKLAGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFG | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity). {ECO:0000250}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U2Z7 | LYSX_MYCTA | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAADFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHADYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U493 | BLAC_MYCTA | MRNRGFGRRELLVAMAMLVSVTGCARHASGARPASTTLPAGADLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPREALLAEAATCVAGVLA | 3.5.2.6 | null | beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | beta-lactamase activity [GO:0008800] | PF13354; | 3.40.710.10; | Class-A beta-lactamase family | PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000250|UniProtKB:P9WKD3}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WKD3}. Secreted {ECO:0000269|PubMed:9624479}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:9624479}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for benzylpenicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=38 uM for phenoxymethylpenicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=94 uM for amoxicillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=185 uM for azlocillin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=81 uM for nitrocefin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=798 uM for cephaloridine (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=490 uM for cefazolin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=308 uM for cephalothin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=680 uM for cephapirin (at pH 6.0) {ECO:0000269|PubMed:9624479}; KM=645 uM for cefamandole (at pH 6.0) {ECO:0000269|PubMed:9624479}; Note=kcat is 21 sec(-1) with benzylpenicillin as substrate. kcat is 20 sec(-1) with phenoxymethylpenicillin as substrate. kcat is 2 sec(-1) with amoxicillin as substrate. kcat is 55 sec(-1) with azlocillin as substrate. kcat is 31 sec(-1) with nitrocefin as substrate. kcat is 8 sec(-1) with cephaloridine as substrate. kcat is 8 sec(-1) with cefazolin as substrate. kcat is 8 sec(-1) with cephalothin as substrate. kcat is 3 sec(-1) with cephapirin as substrate. kcat is 22 sec(-1) with cefamandole as substrate. Assays performed at pH 6.0. {ECO:0000269|PubMed:9624479}; | null | null | null | FUNCTION: Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics. {ECO:0000250|UniProtKB:P9WKD3, ECO:0000269|PubMed:9624479}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U4N0 | ADOK_MYCTA | MTIAVTGSIATDHLMRFPGRFSEQLLPEHLHKVSLSFLVDDLVMHRGGVAGNMAFAIGVLGGEVALVGAAGADFADYRDWLKARGVNCDHVLISETAHTARFTCTTDVDMAQIASFYPGAMSEARNIKLADVVSAIGKPELVIIGANDPEAMFLHTEECRKLGLAFAADPSQQLARLSGEEIRRLVNGAAYLFTNDYEWDLLLSKTGWSEADVMAQIDLRVTTLGPKGVDLVEPDGTTIHVGVVPETSQTDPTGVGDAFRAGFLTGRSAGLGLERSAQLGSLVAVLVLESTGTQEWQWDYEAAASRLAGAYGEHAAAEIVAVLA | 2.7.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14594827}; | AMP salvage [GO:0044209]; fructose metabolic process [GO:0006000]; purine ribonucleoside salvage [GO:0006166]; regulation of glycogen metabolic process [GO:0070873]; response to fructose [GO:0009750]; response to glucose [GO:0009749]; response to insulin [GO:0032868]; response to sucrose [GO:0009744]; response to zinc ion [GO:0010043] | null | adenosine kinase activity [GO:0004001]; ATP binding [GO:0005524]; ketohexokinase activity [GO:0004454] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20; Evidence={ECO:0000269|PubMed:14594827}; CATALYTIC ACTIVITY: Reaction=adenosine + GTP = AMP + GDP + H(+); Xref=Rhea:RHEA:52532, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:14594827}; CATALYTIC ACTIVITY: Reaction=adenosine + dGTP = AMP + dGDP + H(+); Xref=Rhea:RHEA:52536, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:14594827}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for adenosine (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; KM=3.4 uM for adenosine (in the absence of KCl) {ECO:0000269|PubMed:14594827}; KM=79 uM for methyl-adenosine (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; KM=709 uM for methyl-adenosine (in the absence of KCl) {ECO:0000269|PubMed:14594827}; KM=1100 uM for ATP (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; Vmax=180 nmol/min/mg enzyme with adenosine as substrate (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; Vmax=60 nmol/min/mg enzyme with adenosine as substrate (in the absence of KCl) {ECO:0000269|PubMed:14594827}; Vmax=72 nmol/min/mg enzyme with methyl-adenosine as substrate (in the presence of 10 mM KCl) {ECO:0000269|PubMed:14594827}; Vmax=2.3 nmol/min/mg enzyme with methyl-adenosine as substrate (in the absence of KCl) {ECO:0000269|PubMed:14594827}; Note=GTP and dGTP are the best phosphate donors, with 2.5 and 4.7 times the activity observed with ATP, respectively. UTP, dATP, and dTTP exhibit about 33% of the activity observed with ATP, while CTP and dCTP are the worst phosphate donors, with 1.7 and 0.2% of the activity observed with ATP, respectively. Since K(+) exists at millimolar levels within cells, stimulation by K(+) is physiologically relevant, and kinetic values obtained in the presence of K(+) more closely reflect the true physiological state of the enzyme than values obtained in the absence of K(+). {ECO:0000269|PubMed:14594827}; | PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1. {ECO:0000305|PubMed:14594827}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-11. Activity decreases rapidly at values above pH 11 and below pH 8. Is inactive at pH 4.3. {ECO:0000269|PubMed:14594827}; | null | FUNCTION: Catalyzes the phosphorylation of adenosine to adenosine monophosphate (AMP). Can also catalyze the phosphorylation of the adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the first step in the metabolism of this compound to an active form that displays antitubercular activity. Is not active on guanosine, inosine, deoxyadenosine, cytidine, uridine, or thymidine. Prefers dGTP and GTP to ATP as phosphate donors in vitro. {ECO:0000269|PubMed:14594827}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U654 | PPGK_MYCTA | MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH | 2.7.1.2; 2.7.1.63 | null | null | null | ATP binding [GO:0005524]; glucokinase activity [GO:0004340]; polyphosphate-glucose phosphotransferase activity [GO:0047330] | PF00480; | 3.30.420.40; | ROK (NagC/XylR) family | null | null | CATALYTIC ACTIVITY: Reaction=[phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:22036, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:61548; EC=2.7.1.63; Evidence={ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2; Evidence={ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.4 uM for (Phosphate)(32) (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=13.9 uM for polyphosphate type 35 (Sigma) (at pH 7.5) {ECO:0000269|PubMed:8703950}; KM=6.1 uM for polyphosphate type 35 (Sigma) (at pH 8.6) {ECO:0000269|PubMed:8703950}; KM=0.28 mM for D-glucose (at pH 7.5, in the polyphosphate-dependent glucokinase reaction) {ECO:0000269|PubMed:8703950}; KM=0.37 mM for D-glucose (at pH 8.6, in the polyphosphate-dependent glucokinase reaction) {ECO:0000269|PubMed:8703950}; KM=0.06 mM for D-glucose (at pH 7.5, in the ATP-dependent glucokinase reaction) {ECO:0000269|PubMed:8703950}; KM=0.22 mM for D-glucose (at pH 8.6, in the ATP-dependent glucokinase reaction) {ECO:0000269|PubMed:8703950}; KM=0.88 mM for ATP (at pH 7.5) {ECO:0000269|PubMed:8703950}; KM=1.4 mM for ATP (at pH 8.6) {ECO:0000269|PubMed:8703950}; KM=1.46 mM for ATP (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=0.29 mM for GTP (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=1.43 mM for dATP (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=2.19 mM for UTP (at pH 8.6) {ECO:0000269|PubMed:8381043}; KM=8.32 mM for CTP (at pH 8.6) {ECO:0000269|PubMed:8381043}; Note=kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as substrate at pH 7.5. kcat is 116 sec(-1) with ATP as substrate at pH 8.6 (PubMed:8703950). kcat is 149 sec(-1) with poly(P)(32) as substrate at pH 8.6. kcat is 60 sec(-1) with ATP as substrate at pH 8.6. kcat is 60 sec(-1) with GTP as substrate at pH 8.6. kcat is 61 sec(-1) with dATP as substrate at pH 8.6. kcat is 37 sec(-1) with UTP as substrate at pH 8.6. kcat is 19 sec(-1) with CTP as substrate at pH 8.6 (PubMed:8381043). {ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5 and 9.6-9.5 with poly(P)(32) and ATP as the phosphoryl donors, respectively. {ECO:0000269|PubMed:8381043}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius for both activities. {ECO:0000269|PubMed:8381043}; | FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor (PubMed:8381043, PubMed:8703950). Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis (PubMed:8703950). GTP, UTP and CTP can replace ATP as phosphoryl donor (PubMed:8381043). {ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U6Z7 | DBH_MYCTA | MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK | 1.16.3.1 | null | chromosome condensation [GO:0030261]; intracellular iron ion homeostasis [GO:0006879] | cytosol [GO:0005829]; nucleoid [GO:0009295] | DNA binding [GO:0003677]; oxidoreductase activity [GO:0016491]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family, Long actinobacterial subfamily | PTM: Phosphorylated in vivo on Ser and Thr-residues; the protein is degraded during purification so most sites were not identified, but at least one of Thr-43 and/or Thr-45 are modified in vivo. In vitro at least PknE, PknF and PknB phosphorylate HupB; PknE is the most active and phosphorylates many sites in vitro including Thr-43 and Thr-45 (PubMed:24816602). {ECO:0000269|PubMed:24816602}.; PTM: Acetylated on 8 Lys residues in vivo (probably by Eis) (Probable) (PubMed:26817737). In vitro acetylated by Eis on 28 residues (strains H37Rv and H37Ra), many more than those identified in vivo (PubMed:26817737). Also acetylated by MRA_0812 (PubMed:34224344). Deacetylated in vitro by NAD-dependent protein deacylase NPD (MRA_1161) (PubMed:28935371). {ECO:0000269|PubMed:26817737, ECO:0000269|PubMed:28935371, ECO:0000269|PubMed:34224344, ECO:0000305|PubMed:26817737}.; PTM: Succinylated in vivo and in vitro by MRA_0812 and by Eis; only 3 residues are found to be succinylated in vivo, while 27 are modifed in vitro by MRA_0812 and 32 are succinylated by Eis. NAD-dependent protein deacylase (MRA_1161) desuccinylates this protein. {ECO:0000269|PubMed:34224344}. | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:24916461}. | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:Q9XB18}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149; Evidence={ECO:0000250|UniProtKB:Q9XB18}; | null | null | null | null | FUNCTION: A nucleoid-associated protein (NAP) that plays a role in local chromosome architecture (Probable) (PubMed:24916461). Binds DNA non-sequence specifically; in vitro phosphorylation of an N-terminal fragment decreases DNA-binding (PubMed:24816602). Stimulates supercoiling relaxation by topoisomerase 1 (Top1, topA), at higher than 80 uM inhibits relaxation, has no effect on DNA gyrase; the effect is independent of DNA-binding. Increases the intervening strand passage activity of Top1 that occurs between the two catalytic trans-esterification reactions (PubMed:25200077). Does not bind ssDNA, probably helps condense chromosomes (PubMed:24916461). Binds dsDNA; in vitro acetylated protein binds 10-fold less well to DNA (note in vitro acetylated protein is more heavily modified than in vivo modified protein). In vitro acetylated protein compacts DNA less well than unmodified protein (PubMed:26817737, PubMed:28935371). In vitro succinylated DNA bind dsDNA less well than unmodified protein (note in vitro succinylated protein is more heavily modified than in vivo modified protein) (PubMed:34224344). {ECO:0000269|PubMed:24816602, ECO:0000269|PubMed:24916461, ECO:0000269|PubMed:25200077, ECO:0000269|PubMed:26817737, ECO:0000269|PubMed:28935371, ECO:0000269|PubMed:34224344, ECO:0000305|PubMed:24916461}.; FUNCTION: Has ferroxidase activity, converts Fe(2+) into Fe(3+). Binds Fe(3+) but not Fe(2+); prevents the generation of hydroxyl radicals by the Fenton reaction and thus protects DNA from damage. May function in iron storage. {ECO:0000250|UniProtKB:Q9XB18}.; FUNCTION: Required for biofilm formation; trimethylation by recombinant human SUV39H1 (a histone methyltransferase) inhibits biofilm formation (By similarity). Probably influences transcription (By similarity). RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host (By similarity). {ECO:0000250|UniProtKB:P9WMK7, ECO:0000250|UniProtKB:Q9ZHC5}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5U8S6 | PAND_MYCTA | MLRTMLKSKIHRATVTCADLHYVGSVTIDADLMDAADLLEGEQVTIVDIDNGARLVTYAITGERGSGVIGINGAAAHLVHPGDLVILIAYATMDDARARTYQPRIVFVDAYNKPIDMGHDPAFVPENAGELLDPRLGVG | 4.1.1.11 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_00446}; | alanine biosynthetic process [GO:0006523]; pantothenate biosynthetic process [GO:0015940]; response to antibiotic [GO:0046677] | cytosol [GO:0005829] | aspartate 1-decarboxylase activity [GO:0004068] | PF02261; | 2.40.40.20; | PanD family | PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. {ECO:0000255|HAMAP-Rule:MF_00446}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; | null | PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00446}. | null | null | FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446}.; FUNCTION: Overexpression of wild-type or mutant proteins confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA), when grown on agar plates. {ECO:0000269|PubMed:26038753}. | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) |
A5W059 | HMGA_PSEP1 | MNTLIGKTGIVVRNIQRAELDSIDALGRLGVATVHEAQNRKGLLSSKMRPIQQGTSLAGSAVTVLVAPGDNWMFHVAVEQCRPGDVLVVSPSSPCTDGYFGDLLATSLQARGVRALIVDAGVRDTQTLRDMGFAVWARAINAQGTVKETLGSVNLPVICGGQLINPGDIVVADDDGVVVVRRDECESTLVAAAERAGLEEEKRLRLAAGELGLDIYKMRERLEAKGLRYVDNIEDLEG | 4.1.1.112; 4.1.3.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20843800}; | null | null | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity [GO:0047443]; metal ion binding [GO:0046872]; oxaloacetate decarboxylase activity [GO:0008948] | PF03737; | 3.50.30.40; | LigK/PcmE family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate; Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:20843800, ECO:0000269|PubMed:24359411}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate; Xref=Rhea:RHEA:28935, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:58075; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:20843800}; CATALYTIC ACTIVITY: Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=4.1.1.112; Evidence={ECO:0000269|PubMed:20843800}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for oxaloacetate (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=0.036 mM for oxaloacetate (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; KM=0.26 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=0.022 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; KM=0.066 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-hydroxy-4-oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=0.03 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-hydroxy-4-oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; KM=0.15 mM for alpha-keto-gamma-hydroxyglutarate (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=0.071 mM for alpha-keto-gamma-hydroxyglutarate (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; KM=25 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of magnesium) {ECO:0000269|PubMed:20843800}; KM=8.8 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of manganese) {ECO:0000269|PubMed:20843800}; | null | null | null | FUNCTION: Catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway. The preferred substrates of the enzyme are 2-keto-4-hydroxy acids with a 4-carboxylate substitution. Catalyzes the conversion of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) to pyruvate. Also catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA) to pyruvate and oxaloacetate. {ECO:0000269|PubMed:20843800, ECO:0000269|PubMed:24359411}. | Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) |
A5WMW1 | LYSX_MYCTF | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAADFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHADYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}. | Mycobacterium tuberculosis (strain F11) |
A5WVX9 | ZDH17_DANRE | MADALVGYEKEAGCVPILHPEEIKPQSHYNHGYNESRKSHVDDYSTWDIVKATQYGIFERCRELVEAGYDVRQPDKENVTLLHWAAINNRVDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCVHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEANANVDAQNIKGETPLDLAKQRKNVWMINHLQEARQAKGYDSPSYLKRLKMDKEFRQKVMLGTPFLVIWLVGFIADLDIDSWLIKGVMYAVMWLVVQFLSKSFFDHSMHSALPLGIYLATKFWMYITWFYWFWNDLPFVTIHLPFLLNSLALFYNFGKSWKSDPGIIKASEEQKKKTIVELAETGSLDLSIFCSTCLIRKPIRSKHCAVCNRCIAKFDHHCPWVGNCVGSGNHRYFMGYLFFLLCMICWMMYGCICYWRIHCATSYTKDGFWIYITQIATCSPWMFWMFLNSVFHFMWVAVLIMCQLYQIAVLGITTNERMNARRYKHFKVTATSIESPFNHGCMRNLIDFFELRCCGLLRPVPIDWTSQYTIEYDQTSGSGYQLV | 2.3.1.-; 2.3.1.225 | null | axonogenesis [GO:0007409]; habituation [GO:0046959]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386] | cell projection [GO:0042995]; cytoplasmic vesicle membrane [GO:0030659]; Golgi membrane [GO:0000139]; presynaptic membrane [GO:0042734] | palmitoyltransferase activity [GO:0016409]; protein-cysteine S-myristoyltransferase activity [GO:0019705]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; protein-cysteine S-stearoyltransferase activity [GO:0140439] | PF12796;PF01529; | 1.25.40.20; | DHHC palmitoyltransferase family, AKR/ZDHHC17 subfamily | PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8IUH5}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q8IUH5}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; Evidence={ECO:0000250|UniProtKB:Q80TN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; Evidence={ECO:0000250|UniProtKB:Q80TN5}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; Evidence={ECO:0000250|UniProtKB:Q80TN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; Evidence={ECO:0000250|UniProtKB:Q80TN5}; | null | null | null | null | FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Plays a role in axonogenesis (PubMed:26232532). {ECO:0000250|UniProtKB:Q80TN5, ECO:0000250|UniProtKB:Q8IUH5, ECO:0000269|PubMed:26232532}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5X5Y0 | 5HT3E_HUMAN | MEGSWFHRKRFSFYLLLGFLLQGRGVTFTINCSGFGQHGADPTALNSVFNRKPFRPVTNISVPTQVNISFAMSAILDVNEQLHLLSSFLWLEMVWDNPFISWNPEECEGITKMSMAAKNLWLPDIFIIELMDVDKTPKGLTAYVSNEGRIRYKKPMKVDSICNLDIFYFPFDQQNCTLTFSSFLYTVDSMLLDMEKEVWEITDASRNILQTHGEWELLGLSKATAKLSRGGNLYDQIVFYVAIRRRPSLYVINLLVPSGFLVAIDALSFYLPVKSGNRVPFKITLLLGYNVFLLMMSDLLPTSGTPLIGVYFALCLSLMVGSLLETIFITHLLHVATTQPPPLPRWLHSLLLHCNSPGRCCPTAPQKENKGPGLTPTHLPGVKEPEVSAGQMPGPAEAELTGGSEWTRAQREHEAQKQHSVELWLQFSHAMDAMLFRLYLLFMASSIITVICLWNT | null | null | inorganic cation transmembrane transport [GO:0098662]; serotonin receptor signaling pathway [GO:0007210] | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; serotonin-activated cation-selective channel complex [GO:1904602]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; serotonin-gated monoatomic cation channel activity [GO:0022850]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily, HTR3E sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:17392525}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:19012743}; Multi-pass membrane protein {ECO:0000255}. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000269|PubMed:17392525}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17392525}; | null | null | null | null | FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons. {ECO:0000269|PubMed:17392525}. | Homo sapiens (Human) |
A5Y5L5 | CIN_NICSU | MNHHLIITPIFHLQIMLPVATLKRPPPPAATCSIYSFSRGTPSLVSKARLSTAAVGGMKNEPSPNHYSDISSSDLNLTRRSGNYGPTMWDFEYIQSIHNDYTEKKYMNRLNKLKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLFREYGFHISQEIFGGLSETHTEDTKGMLYLYEASFLATEGESELEKARNWTEKHLREYLENKNDDQNVAELVHHALELPLHWRMLRIEARWFINFYKKKQDMIPLLLELAILDFNIVQAAHIEDLKYVARWWKETCLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTMDELQCFTHAFQRWNIDELDNLPDNMKMCYFALDNFINEVAGDAFEEHRVPILSYLRNAWTDLCKAYLREAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLVANPVNKEVLHYLENYHDIIRWSALILRLANDLGTSSEELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKCAMNLARMAQCMYQHGDGHGHGDLNSETTNHIMALLFESIPPA | 4.2.3.-; 4.2.3.106; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17611797}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17611797}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000269|PubMed:17611797}; | alpha-pinene biosynthetic process [GO:0046248]; circadian rhythm [GO:0007623]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; limonene biosynthetic process [GO:0046250]; monoterpene biosynthetic process [GO:0043693] | chloroplast [GO:0009507] | (E)-beta-ocimene synthase activity [GO:0034768]; 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate; Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663; Evidence={ECO:0000269|PubMed:17611797}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:17611797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:17611797}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:17611797}; Note=kcat is 0.33 sec(-1) with (2E)-geranyl diphosphate as substrate. {ECO:0000269|PubMed:17611797}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17611797}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:17611797}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:17611797}; | FUNCTION: Monoterpene synthase involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent (PubMed:17611797). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole and, as minor products, limonene, sabinene, (E)-beta-ocimene, beta-myrcene, alpha-pinene and alpha-terpineol (PubMed:17611797). {ECO:0000269|PubMed:17611797}. | Nicotiana suaveolens (Australian tobacco) |
A5YKK6 | CNOT1_HUMAN | MNLDSLSLALSQISYLVDNLTKKNYRASQQEIQHIVNRHGPEADRHLLRCLFSHVDFSGDGKSSGKDFHQTQFLIQECALLITKPNFISTLSYAIDNPLHYQKSLKPAPHLFAQLSKVLKLSKVQEVIFGLALLNSSSSDLRGFAAQFIKQKLPDLLRSYIDADVSGNQEGGFQDIAIEVLHLLLSHLLFGQKGAFGVGQEQIDAFLKTLRRDFPQERCPVVLAPLLYPEKRDILMDRILPDSGGVAKTMMESSLADFMQEVGYGFCASIEECRNIIVQFGVREVTAAQVARVLGMMARTHSGLTDGIPLQSISAPGSGIWSDGKDKSDGAQAHTWNVEVLIDVLKELNPSLNFKEVTYELDHPGFQIRDSKGLHNVVYGIQRGLGMEVFPVDLIYRPWKHAEGQLSFIQHSLINPEIFCFADYPCHTVATDILKAPPEDDNREIATWKSLDLIESLLRLAEVGQYEQVKQLFSFPIKHCPDMLVLALLQINTSWHTLRHELISTLMPIFLGNHPNSAIILHYAWHGQGQSPSIRQLIMHAMAEWYMRGEQYDQAKLSRILDVAQDLKALSMLLNGTPFAFVIDLAALASRREYLKLDKWLTDKIREHGEPFIQACMTFLKRRCPSILGGLAPEKDQPKSAQLPPETLATMLACLQACAGSVSQELSETILTMVANCSNVMNKARQPPPGVMPKGRPPSASSLDAISPVQIDPLAGMTSLSIGGSAAPHTQSMQGFPPNLGSAFSTPQSPAKAFPPLSTPNQTTAFSGIGGLSSQLPVGGLGTGSLTGIGTGALGLPAVNNDPFVQRKLGTSGLNQPTFQQSKMKPSDLSQVWPEANQHFSKEIDDEANSYFQRIYNHPPHPTMSVDEVLEMLQRFKDSTIKREREVFNCMLRNLFEEYRFFPQYPDKELHITACLFGGIIEKGLVTYMALGLALRYVLEALRKPFGSKMYYFGIAALDRFKNRLKDYPQYCQHLASISHFMQFPHHLQEYIEYGQQSRDPPVKMQGSITTPGSIALAQAQAQAQVPAKAPLAGQVSTMVTTSTTTTVAKTVTVTRPTGVSFKKDVPPSINTTNIDTLLVATDQTERIVEPPENIQEKIAFIFNNLSQSNMTQKVEELKETVKEEFMPWVSQYLVMKRVSIEPNFHSLYSNFLDTLKNPEFNKMVLNETYRNIKVLLTSDKAAANFSDRSLLKNLGHWLGMITLAKNKPILHTDLDVKSLLLEAYVKGQQELLYVVPFVAKVLESSIRSVVFRPPNPWTMAIMNVLAELHQEHDLKLNLKFEIEVLCKNLALDINELKPGNLLKDKDRLKNLDEQLSAPKKDVKQPEELPPITTTTTSTTPATNTTCTATVPPQPQYSYHDINVYSLAGLAPHITLNPTIPLFQAHPQLKQCVRQAIERAVQELVHPVVDRSIKIAMTTCEQIVRKDFALDSEESRMRIAAHHMMRNLTAGMAMITCREPLLMSISTNLKNSFASALRTASPQQREMMDQAAAQLAQDNCELACCFIQKTAVEKAGPEMDKRLATEFELRKHARQEGRRYCDPVVLTYQAERMPEQIRLKVGGVDPKQLAVYEEFARNVPGFLPTNDLSQPTGFLAQPMKQAWATDDVAQIYDKCITELEQHLHAIPPTLAMNPQAQALRSLLEVVVLSRNSRDAIAALGLLQKAVEGLLDATSGADADLLLRYRECHLLVLKALQDGRAYGSPWCNKQITRCLIECRDEYKYNVEAVELLIRNHLVNMQQYDLHLAQSMENGLNYMAVAFAMQLVKILLVDERSVAHVTEADLFHTIETLMRINAHSRGNAPEGLPQLMEVVRSNYEAMIDRAHGGPNFMMHSGISQASEYDDPPGLREKAEYLLREWVNLYHSAAAGRDSTKAFSAFVGQMHQQGILKTDDLITRFFRLCTEMCVEISYRAQAEQQHNPAANPTMIRAKCYHNLDAFVRLIALLVKHSGEATNTVTKINLLNKVLGIVVGVLLQDHDVRQSEFQQLPYHRIFIMLLLELNAPEHVLETINFQTLTAFCNTFHILRPTKAPGFVYAWLELISHRIFIARMLAHTPQQKGWPMYAQLLIDLFKYLAPFLRNVELTKPMQILYKGTLRVLLVLLHDFPEFLCDYHYGFCDVIPPNCIQLRNLILSAFPRNMRLPDPFTPNLKVDMLSEINIAPRILTNFTGVMPPQFKKDLDSYLKTRSPVTFLSDLRSNLQVSNEPGNRYNLQLINALVLYVGTQAIAHIHNKGSTPSMSTITHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCTMLYLFAEANTEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPAFKFWNHEFVHCAPEIEKLFQSVAQCCMGQKQAQQVMEGTGAS | null | null | miRNA-mediated post-transcriptional gene silencing [GO:0035195]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; regulation of stem cell population maintenance [GO:2000036]; trophectodermal cell differentiation [GO:0001829] | CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]; P-body [GO:0000932]; peroxisomal membrane [GO:0005778] | armadillo repeat domain binding [GO:0070016]; molecular adaptor activity [GO:0060090]; nuclear estrogen receptor binding [GO:0030331]; nuclear retinoic acid receptor binding [GO:0042974]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723] | PF16415;PF16418;PF16417;PF12842;PF04054; | 1.25.40.180;1.25.40.790;1.25.40.800;1.25.40.840; | CNOT1 family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:21976065}. Nucleus {ECO:0000305|PubMed:21976065}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250|UniProtKB:Q6ZQ08}. | null | null | null | null | null | FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:16778766, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:21976065, ECO:0000269|PubMed:21984185, ECO:0000269|PubMed:22367759, ECO:0000269|PubMed:23644599, ECO:0000269|PubMed:27558897, ECO:0000269|PubMed:32354837}. | Homo sapiens (Human) |
A5YM72 | CRNS1_HUMAN | MLLCLSPAWLMKVPAPGQPGEAALLVSKAVSFHPGGLTFLDDFVPPRRATYFLAGLGLGPGRGREAAELARDLTCPTGASAELARLLEDRLLTRQLLAQQGGVAVPATLAFTYKPPGLLRGGDASLGLRLVELSGKEGQETLVKEEVEAFLRSEALGDILQVAVKLSGWRWRGRQAWRLHPRAELGAVVDTVLALLEKLEEEESVLVEAVYPPAQLPCSDGPSPGPGLAVRICAVVCRTQGDRPLLSKVVCGVGRGDRPLRHHNSLPRTLEVALAQCGLGEEAQVAAVRQRVKAAAEAALAAVLALEAGLSAEQRGGRRAHTDFLGVDFALTAAGGVLTPVALELNGGLCLEACGALEGLWAAPRLGPAADEAVAAPLVETMLRRSARCLMEGKQLLVVGAGGVSKKFVWEAARDYGLQLHLVESDPNHFASQLVQTFIHFDMTEHRRDEENARLLAELVRARGLKLDGCFSYWDDCLVLTALLCQELGLPCSSPAAMRLAKQKSLTQLHLLHHHGPPWPAPSLHAVPCCPLESEADVERAVHQVPLPGVMKLEFGAGAVGVRLVEDAPQCHEHFSRITRDLQGEADHPGIGLGWGNAMLLMEFVEGTEHDVDLVLFGGRLLAAFVSDNGPTRLPGFTETAACMPTGLAPEQEAQMVQAAFRCCLGCGLLDGVFNVELKLTGAGPRLIEINPRMGGFYLRDWILELYGVDLLLAAVMVACGLRPALPTRPRARGHLVGVMCLVSQHLQALSSTASRETLQALHDRGLLRLNLLEEALVPGEYEEPYCSVACAGPSPTEARLRLLGLCQGLGIDGPSYPVAHFLSHFK | 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]; histidine catabolic process [GO:0006548] | cytosol [GO:0005829] | 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; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19298; Evidence={ECO:0000305|PubMed:20097752}; CATALYTIC ACTIVITY: Reaction=4-aminobutanoate + ATP + L-histidine = ADP + H(+) + L-homocarnosine + phosphate; Xref=Rhea:RHEA:59568, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57595, ChEBI:CHEBI:59888, ChEBI:CHEBI:143075, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:20097752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59569; Evidence={ECO:0000305|PubMed:20097752}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for beta-alanine {ECO:0000269|PubMed:20097752}; KM=1.84 mM for 4-aminobutanoate {ECO:0000269|PubMed:20097752}; KM=0.37 mM for L-histidine {ECO:0000269|PubMed:20097752}; KM=4.67 mM for L-lysine {ECO:0000269|PubMed:20097752}; KM=7.66 mM for L-ornithine {ECO:0000269|PubMed:20097752}; KM=24.7 mM for N-methylhistidine {ECO:0000269|PubMed:20097752}; Vmax=65.3 nmol/min/mg enzyme toward beta-alanine {ECO:0000269|PubMed:20097752}; Vmax=54.7 nmol/min/mg enzyme toward gamma-aminobutyrate {ECO:0000269|PubMed:20097752}; Vmax=0.76 nmol/min/mg enzyme toward L-histidine {ECO:0000269|PubMed:20097752}; Vmax=0.61 nmol/min/mg enzyme toward L-lysine {ECO:0000269|PubMed:20097752}; Vmax=0.28 nmol/min/mg enzyme toward L-ornithine {ECO:0000269|PubMed:20097752}; Vmax=0.62 nmol/min/mg enzyme toward N-methylhistidine {ECO:0000269|PubMed:20097752}; | null | null | null | FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}. | Homo sapiens (Human) |
A5YVK8 | ERVA_TABDI | AVIPLKNQGKCGSCWAFSTVTTVESINQIRTGNLISLSEQQLVDCSKKNHGCKGGYFDRAYQYIIANGGIDTEANYPYKAFQGPCRAAKKVVRIDGCKGVPQCNENALKNAVASQPSVVAIDASSKQFQHYKSGIFTGPCGTKLNHGVVIVGYGKDYWIVRNSWGRHWGEQGYTRMKRVGGCGL | 3.4.22.- | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83654}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.071 mM for N-benzoyl-Phe-Val-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.75 mM for D-Val-Leu-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=1.666 mM for D-Ile-Phe-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=0.501 mM for Ala-Ala-Val-Ala-pNA {ECO:0000269|PubMed:18167146}; KM=0.683 mM for D-Ile-Pro-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.55 mM for N(a)-benzoyl-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=2.36 mM for D-Leu-Ser-Thr-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=1.888 mM for N-benzoyl-Val-Gly-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=76.25 mM for E64 {ECO:0000269|PubMed:18167146}; Note=kcat is 35.330 sec(-1) with N-benzoyl-Phe-Val-Arg-pNA as substrate (PubMed:18167146). kcat is 4.276 sec(-1) with D-Val-Leu-Lys-pNA as substrate (PubMed:18167146). kcat is 5.474 sec(-1) with D-Ile-Phe-Lys-pNA as substrate (PubMed:18167146). kcat is 0.333 sec(-1) with Ala-Ala-Val-Ala-pNA as substrate (PubMed:18167146). kcat is 0.017 sec(-1) with D-Ile-Pro-Arg-pNA as substrate (PubMed:18167146). kcat is 0.07 sec(-1) with N(a)-benzoyl-Arg-pNA as substrate (PubMed:18167146). kcat is 0.198 sec(-1) with D-Leu-Ser-Thr-Arg-pNA as substrate (PubMed:18167146). kcat is 0.117 sec(-1) with N-benzoyl-Val-Gly-Arg-pNA as substrate (PubMed:18167146). {ECO:0000269|PubMed:18167146}; | null | null | null | FUNCTION: Cysteine proteinase. {ECO:0000269|PubMed:18167146}. | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
A5Z1X6 | ITB1_CAMBA | MNLQLIFWIGLISSVCCVFGQADEDRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDTENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLKNDVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENSKLPEGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPDKNSETIKIKPLGFTEEVEIILQFICECECQGEGIPGSPKCHDGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTTSCMAVNGQICNGRGVCECGACKCTDPKFQGPTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNITKVENRDKLPQPGQVDPLSHCKEKDVDDCWFYFTYSVNGNNEATVHVVETPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKERMNAKWDTGENPIYKSAVTTVVNPKYEGK | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]; negative regulation of vasoconstriction [GO:0045906]; positive regulation of cell migration [GO:0030335]; positive regulation of protein localization to plasma membrane [GO:1903078]; receptor internalization [GO:0031623]; regulation of collagen catabolic process [GO:0010710] | cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin alpha9-beta1 complex [GO:0034679]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; recycling endosome [GO:0055037]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:P05556}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner. {ECO:0000250|UniProtKB:P05556}. | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (By similarity). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (By similarity). {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055}. | Camelus bactrianus (Bactrian camel) |
A6BM07 | I7GT1_SOYBN | MKDTIVLYPNLGRGHLVSMVELGKLILTHHPSLSITILILTPPTTPSTTTTTLACDSNAQYIATVTATTPSITFHRVPLAALPFNTPFLPPHLLSLELTRHSTQNIAVALQTLAKASNLKAIVIDFMNFNDPKALTENLNNNVPTYFYYTSGASTLALLLYYPTIHPTLIEKKDTDQPLQIQIPGLSTITADDFPNECKDPLSYACQVFLQIAETMMGGAGIIVNTFEAIEEEAIRALSEDATVPPPLFCVGPVISAPYGEEDKGCLSWLNLQPSQSVVLLCFGSMGRFSRAQLKEIAIGLEKSEQRFLWVVRTELGGADDSAEELSLDELLPEGFLERTKEKGMVVRDWAPQAAILSHDSVGGFVTHCGWNSVLEAVCEGVPMVAWPLYAEQKMNRMVMVKEMKVALAVNENKDGFVSSTELGDRVRELMESDKGKEIRQRIFKMKMSAAEAMAEGGTSRASLDKLAKLWKQS | 2.4.1.170 | null | null | null | isoflavone 7-O-glucosyltransferase activity [GO:0050004] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56344, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140301; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:17565994}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for genistein {ECO:0000269|PubMed:17565994}; KM=190 uM for UDP-glucose {ECO:0000269|PubMed:17565994}; Note=kcat is 0.74 sec(-1)for genistein (at pH 8.5 and 30 degrees Celsius).; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:17565994}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:17565994}; | FUNCTION: Involved in the biosynthesis of isoflavonoids. Specific for UDP-glucose. Can use genistein > daidzein > formononetin > quercetin > kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin > esculetin > naringenin as substrates, but not cyanidin, trans-p-coumaric acid, caffeic acid, benzoic acid, m- and p-hydroxybenzoic acids, salicylic acid, salicyl alcohol, and hydroquinone. {ECO:0000269|PubMed:17565994}. | Glycine max (Soybean) (Glycine hispida) |
A6BM72 | MEG11_HUMAN | MVLSLTGLIAFSFLQATLALNPEDPNVCSHWESYAVTVQESYAHPFDQIYYTRCTDILNWFKCTRHRISYKTAYRRGLRTMYRRRSQCCPGYYESGDFCIPLCTEECVHGRCVSPDTCHCEPGWGGPDCSSGCDSDHWGPHCSNRCQCQNGALCNPITGACVCAAGFRGWRCEELCAPGTHGKGCQLPCQCRHGASCDPRAGECLCAPGYTGVYCEELCPPGSHGAHCELRCPCQNGGTCHHITGECACPPGWTGAVCAQPCPPGTFGQNCSQDCPCHHGGQCDHVTGQCHCTAGYMGDRCQEECPFGSFGFQCSQHCDCHNGGQCSPTTGACECEPGYKGPRCQERLCPEGLHGPGCTLPCPCDADNTISCHPVTGACTCQPGWSGHHCNESCPVGYYGDGCQLPCTCQNGADCHSITGGCTCAPGFMGEVCAVSCAAGTYGPNCSSICSCNNGGTCSPVDGSCTCKEGWQGLDCTLPCPSGTWGLNCNESCTCANGAACSPIDGSCSCTPGWLGDTCELPCPDGTFGLNCSEHCDCSHADGCDPVTGHCCCLAGWTGIRCDSTCPPGRWGPNCSVSCSCENGGSCSPEDGSCECAPGFRGPLCQRICPPGFYGHGCAQPCPLCVHSSRPCHHISGICECLPGFSGALCNQVCAGGYFGQDCAQLCSCANNGTCSPIDGSCQCFPGWIGKDCSQACPPGFWGPACFHACSCHNGASCSAEDGACHCTPGWTGLFCTQRCPAAFFGKDCGRVCQCQNGASCDHISGKCTCRTGFTGQHCEQRCAPGTFGYGCQQLCECMNNSTCDHVTGTCYCSPGFKGIRCDQAALMMEELNPYTKISPALGAERHSVGAVTGIMLLLFLIVVLLGLFAWHRRRQKEKGRDLAPRVSYTPAMRMTSTDYSLSGACGMDRRQNTYIMDKGFKDYMKESVCSSSTCSLNSSENPYATIKDPPILTCKLPESSYVEMKSPVHMGSPYTDVPSLSTSNKNIYEVEPTVSVVQEGCGHNSSYIQNAYDLPRNSHIPGHYDLLPVRQSPANGPSQDKQS | null | null | homotypic cell-cell adhesion [GO:0034109]; retina layer formation [GO:0010842] | basolateral plasma membrane [GO:0016323] | null | PF12661;PF00053; | 2.10.25.10;2.170.300.10; | MEGF family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Basolateral cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Note=Forms an irregular, mosaic-like adhesion pattern in region of the cell that becomes firmely fixed to the substrate. Localized to protruding lamellipodia. Does not localize with MEGF10. | null | null | null | null | null | FUNCTION: May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A6BMK7 | NEUR1_BOVIN | MTEEGPGIVSLGKLRRPRMLRLWGICRVQIFSAIFMLMSPAGVGAGAKDDFSLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSTSDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVSWSSPRNLSLDIGTEMFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGVSWRYGGGVSGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIILRSYDACDTLRPRDVTFDTELVDPVVAAGAVATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQLWPGPSGYSSLTTLEGNVDGKDEAPQLYVLYEKGRNQYMESISLVKVSVYGTL | 3.2.1.18 | null | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308] | PF13088; | 2.120.10.10; | Glycosyl hydrolase 33 family | PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A6H5Y3 | METH_MOUSE | MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENYAPPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPRVPPASVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTHGTGGKKVIQTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARLNGEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREEARLINGSVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLRDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAEGVVPQAAEPIATFYGLRQQAEKDSSSTDPYHCLSDFIAPLHSGVCDYLGLFAVACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLTESLAMAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKNMPVAEVEKWLGPILGYDTD | 2.1.1.13 | COFACTOR: Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; Evidence={ECO:0000250|UniProtKB:P13009}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P13009}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P13009}; | axon regeneration [GO:0031103]; cellular response to nitric oxide [GO:0071732]; cobalamin metabolic process [GO:0009235]; homocysteine metabolic process [GO:0050667]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; methylation [GO:0032259]; response to axon injury [GO:0048678]; tetrahydrofolate metabolic process [GO:0046653] | cytosol [GO:0005829] | amino acid binding [GO:0016597]; cobalamin binding [GO:0031419]; folic acid binding [GO:0005542]; methionine synthase activity [GO:0008705]; methyltransferase activity [GO:0008168]; zinc ion binding [GO:0008270] | PF02310;PF02607;PF02965;PF00809;PF02574; | 3.40.50.280;1.10.288.10;3.20.20.20;3.20.20.330;1.10.1240.10;3.10.196.10; | Vitamin-B12 dependent methionine synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99707}. | CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000250|UniProtKB:Q9Z2Q4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11173; Evidence={ECO:0000250|UniProtKB:Q9Z2Q4}; | null | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. {ECO:0000250|UniProtKB:Q9Z2Q4}. | null | null | FUNCTION: Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. {ECO:0000250|UniProtKB:Q99707}. | Mus musculus (Mouse) |
A6H630 | ARMT1_MOUSE | MAESPAFLSAKDEGSFAYLTIKDRTPQILTKVIDTLHRHKSEFFEKHGEEGIEAEKKAISLLSKLRNELQTDKPITPLVDKCVDTHIWNQYLEYQRSLLNEGDGEPRWFFSPWLFVECYMYRRIHEAIMQSPPIHDFDVFKESKEENFFESQGSIDALCSHLLQLKPVKGLREEQIQDEFFKLLQISLWGNKCDLSLSGGESSSQKANIINCLQDLKPFILINDTESLWALLSKLKKTVETPVVRVDIVLDNSGFELITDLVLADFLFSSELATEIHFHGKSIPWFVSDVTEHDFNWIVEHMKSSNLESMSTCGACWEAYARMGRWAYHDHAFWTLPHPYCVMPQVAPDLYAELQKAHLILFKGDLNYRKLMGDRKWKFTFPFHQALSGFHPAPLCSIRTLKCELQVGLQPGQAEQLTASDPHWLTTGRYGILQFDGPL | 2.1.1.-; 3.1.3.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q04371}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250|UniProtKB:Q04371}; | DNA damage response [GO:0006974]; methylation [GO:0032259] | nucleus [GO:0005634] | enzyme binding [GO:0019899]; fructose 6-phosphate aldolase activity [GO:0097023]; fructose-1-phosphatase activity [GO:0103026]; metal ion binding [GO:0046872]; phosphatase activity [GO:0016791]; protein carboxyl O-methyltransferase activity [GO:0051998]; protein-glutamate O-methyltransferase activity [GO:0008983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF01937; | 1.20.930.60;3.40.50.10880; | Damage-control phosphatase family, Sugar phosphate phosphatase III subfamily | PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}. | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate; Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721, ChEBI:CHEBI:43474, ChEBI:CHEBI:138881; Evidence={ECO:0000250|UniProtKB:Q04371}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; Evidence={ECO:0000250|UniProtKB:Q04371}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:82795; Evidence={ECO:0000250|UniProtKB:Q9H993}; | null | null | null | null | FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity). {ECO:0000250|UniProtKB:Q04371, ECO:0000250|UniProtKB:Q9H993}. | Mus musculus (Mouse) |
A6H639 | DRC5_MOUSE | MQETPSVPSNSSSHSQSVLTIQRQVSALGSSSTGPTSLKTSSTPTPGQLKTKVPNVRRMRRIISEDAEWSLAIVPLLTELCIQHIVKNFQNNPILKQLPLEHQKKVLSNLPPELPLTVTANLIDDENYWHRCCIKRWSVCHVSRHGGSWKRMFFERHLENLLKLFIPGTTDPNVILDLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQLQTLVGGLKHLEELDLVYGVKDCGMNFEWNLFLFTYRDCYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREAARQRTLNPGHFSSPTNNCTENSVV | null | null | flagellated sperm motility [GO:0030317]; microtubule-based movement [GO:0007018] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; sperm flagellum [GO:0036126] | null | PF13516; | 3.80.10.10; | DRC5 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HMZ4}. Note=Detected along the length of the sperm flagellum. {ECO:0000269|Ref.2}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC (By similarity). Required for sperm motility (PubMed:28630322). {ECO:0000250|UniProtKB:A8HMZ4, ECO:0000269|PubMed:28630322}. | Mus musculus (Mouse) |
A6H687 | SAC31_MOUSE | MGRFKGENRSQARWIMGGVSKGRGSGKSRKPRQAAFGQTGARVCPSSPQQDAVPRFRWPGDAECASSTHTPTMSGCKLPMGLCPDMCPAAERARRERERRLHRLEVEPGGRGNAPRADPKRTVKEYSRPAAGKPRPPPSLLRPPPVLLATVRYLAGEVAGRGDVSCAEVASFVADRLRAVRLDLSLQGVDDADAATVLEAALATLLAVVARVRPEETRGAADPVLLQTQVQEGFGSLRRCYARGKGPYPRQAAFQGLFLLYNLGSVEALQEVLQLPAALRACPPLQAALAVDAAFREDNHARLFRLLRTLPYLQSCAVQEHIGYARRKALARLSRALSTPKGQTLPLDFIEHFLALDGLQEARDLCQAHGLTLDKDRVVFLRGQYSEEGLPPPGAYHILVGNKLQGHTLEDVVMAEEGDIHRPGSAA | null | null | cell division [GO:0051301]; centrosome duplication [GO:0051298]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; regulation of immune response [GO:0050776]; spindle assembly [GO:0051225] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; spindle [GO:0005819] | null | PF03399; | 1.25.40.990; | SAC3 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15322101}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15322101}. Note=Localizes on centrosomes in interphase cells and at spindles in mitosis. | null | null | null | null | null | FUNCTION: Involved in centrosome duplication and mitotic progression. {ECO:0000269|PubMed:15322101}. | Mus musculus (Mouse) |
A6H6A9 | RBG1L_MOUSE | MEVRASFQKVSGSSDSVATLNSEEFVLVSQHTDATSIKDDGKPQLKIASNGDEQLEKAMEEILRDSEKGQSGLPVDCQGSSEISDCPFGDVPASQTTKPPLQLILDPSNTEISTPRPSSPSRFPEEDSVLFNKLTYLGCMKVSSPRSEVEALRAMATMRASSQYPFAVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDGTAESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQVSDVKDSVIPTPDSDVFTFSVSLEVKEDDGKGNFSPVPKDRDKFYFKIKQGIEKKVVITVQQLSNKELAIERCFGMLLSPGRNVKNSDMHLLDMESMGKSYDGRAYVITGMWNPNAPIFLALNEETPKDKRVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANERFWYFSRKTFTETFFMRLKQSEGKGHSSAGDAIYEVVSLQRESDKEEPITPTSAGGPMSPQEDEAEEESDNELSSGTGDVSKDCPEKILYSWGELLGRWHNNLGGRPKGLFTLVKSGVPEALRAEVWQLLAGCHDNQEMLDKYRILITKDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICKAYSVFDEDIGYCQGQSFLAAVLLLHMPEEQAFCVLVTIMYGYKLRDLYRNNFEDLHCKFYQLEKLMQEQLPDLYSHFCDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLLQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIKVPTKKLKKYEKEYQAMRENQLQQEDPMDRYKFVYL | null | null | endocytosis [GO:0006897]; megakaryocyte development [GO:0035855]; protein transport [GO:0015031]; regulation of protein localization [GO:0032880] | early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267] | PF12473;PF00566; | 2.30.29.30;1.10.8.270;1.10.10.750;1.10.472.80; | null | null | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:27718357}. Golgi apparatus {ECO:0000250|UniProtKB:Q5R372}. Note=Colocalizes on endosomes partially with EEA1 (By similarity). Colocalizes and cotransports on motile vesicles with ANK2 (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}. | null | null | null | null | null | FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP (By similarity). Plays a role in endocytosis and intracellular protein transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes, where it inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}. | Mus musculus (Mouse) |
A6H6E2 | MMRN2_MOUSE | MIPTLLLGFGVYLSWGLLGSWAQDPGTKFSHLNRPGMPEGWRLGAEDTSRDPIRRNWCPYQKSRLVTFVAACKTEKFLVHSQQPCPQGAPDCQGVRVMYRVAQKPVYQVQQKVLISVDWRCCPGFQGPDCQDHNPTANPEPTEPSGKLQETWDSMDGFELGHPVPEFNEIKVPQEQQENLLQNLQNDAQSVEDGFPGSWEAPPSNLTDEMTEANLTEFEFPGRTSEHLLQPHIDAFLKAHFSPIWKNFNDSLHSLSQAIRNLSLDVEANHQAIKMIQEGTVARADFQELGAKFEAKVQQNSQRLGQLWQDVEDQLHAQRRSVHHALSDVQAEVSTKLKQLVKAQELPGANGSLVMASAAAAARPEPESLQARLGQLQRNLSALHMVTSQREEELQSTLKNMDSVLKQHAEEIKELYSESDETFDQISKVERQVEELLVNHTGLRELRVILMEKSLIMEENKEEIERQLLELNLTLQHLHAGHADLIKYVKDCNCQRVNSDVDVAPEGHRDVMHTLEETQVSLDEQHQLDGSSLQALQSTVDAMSSAMDAYRGEGERARAERARIRSQLRALDHAVEALKTAANGTRKEIRLLHGSFTALLEDALRHQAVLAALFGEEMIDEMSEEAPRPLPLDYEQIRLALQDAASGLQEQAIGWEDLATRVEALEKAAGGFVEQHPQLAEGLEPSHDSGREEEAMTLAELEQEIRRLSSDVKQIGQCCEASWAASLNSSLEDLHSMLLDTQHGLRQHRQLFHNLFQNFQGLVASNISLDLGKLQAMLSKKDKKQPRGPGESRKRDKKQVVMSTDAHAKGLELWETGSPVAFYAGSSEGATALQMVKFNTTSINVGSSYFPEHGYFRAPKRGVYLFAVSITFGPGPGMGQLVFEGHHRVPVYSTEQRGGSTATTFAMVELQKGERAWFELIQGSATKGSQPGTAFGGFLMFKT | null | null | cell adhesion [GO:0007155]; cell migration involved in sprouting angiogenesis [GO:0002042]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration [GO:0030336]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of defense response to bacterium [GO:1900426]; positive regulation of epithelial tube formation [GO:1905278]; positive regulation of morphogenesis of an epithelium [GO:1905332] | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; multimerin complex [GO:1990972] | null | PF00386;PF07546; | 2.60.120.40; | null | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9H8L6}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H8L6}. | null | null | null | null | null | FUNCTION: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it down-regulates KDR activation by binding VEGFA. {ECO:0000250}. | Mus musculus (Mouse) |
A6H730 | PPAP_BOVIN | MRNAALLMTRATSLRLSLLLLLSFLPDLDGGVRAKELRFVTLVFRHGDRSPIETFPNDPIKESSWPQGFGQLTQLGMAQHYELGQYIRKRYENFLNESYKREQVHVRSTDIDRTLMSAMTNLAALFPPEGISIWNPSLPWQPIPVHTVPVSEDQLLYLPFRNCPRFQELQSETLISEEFQKRLQPYKDFIEVLPKLTGYHDQDLLGIWSKVYDPLFCEGVHNFTLPSWATEDTMTKLKEISELSLLSLYGIHKQKEKSRLQGGVLINEILNHMKSATQPSNRRKLIMYSAHDTTVSGLQMALDVYNGILPPYASCHMMELYFQDGEYFVEMYYRNETRYEPHPLTLPGCTPSCPLAKFVELVAPVISQDWSMECAIRNHKGTEDIIN | 3.1.3.2; 3.1.3.48 | null | adenosine metabolic process [GO:0046085]; dephosphorylation [GO:0016311]; lipid metabolic process [GO:0006629]; lysosome organization [GO:0007040]; positive regulation of adenosine receptor signaling pathway [GO:0060168]; regulation of sensory perception of pain [GO:0051930]; thiamine metabolic process [GO:0006772] | extracellular space [GO:0005615]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506] | 5'-nucleotidase activity [GO:0008253]; acid phosphatase activity [GO:0003993]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725]; thiamine phosphate phosphatase activity [GO:0042131] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15309}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000250|UniProtKB:P15309}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:P15309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000250|UniProtKB:P15309}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:P15309}; | null | null | null | null | FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity). {ECO:0000250|UniProtKB:P15309}. | Bos taurus (Bovine) |
A6H737 | LOXL2_BOVIN | MERRGSSCLCRCLALLALLPTLSLAQYESWRHYPEYFQEPAPEYHRPEVPSDVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFTIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNVYCTGSEATLAACSSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLINSIENMNIQVEDIRIRAILSAFRKRTPVTEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGEKTYNTKVYKMFAARKKQRYWPYSMDCTGTEAHISSCKLGPQVSLDPVKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGANVGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAITGSRLGQGIGPIHLNEIECTGNEKSIIDCKFNAESQGCNHEEDAAVRCNIPAMGFQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGENWGIVEAMVVCRQLGLGFASNAFQETWYWHGNINANKVVMSGVKCSGTELSLAHCRHDGEDVACPEGGVRYGAGVACSETAPDLVLNAEIVQQSTYLEDRPMFMLQCAMEENCLSASAAQTNPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNYEVAESDYTNNIMKCRTRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLINNQVSKR | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein modification process [GO:0036211]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040] | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.; PTM: N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0}. | Bos taurus (Bovine) |
A6H772 | PP4C_BOVIN | MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | double-strand break repair via homologous recombination [GO:0000724]; protein phosphorylation [GO:0006468]; regulation of double-strand break repair via homologous recombination [GO:0010569] | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase 4 complex [GO:0030289] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-4 (PP-X) subfamily | PTM: Methylation at the C-terminal Leu-307 is critical for interactions with regulatory subunits and functions in DNA repair. {ECO:0000250|UniProtKB:P60510}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on Ser-140 (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin. {ECO:0000250}. | Bos taurus (Bovine) |
A6H782 | TEKT3_BOVIN | MELLGSTLTATYAHPRPTPTNFLPAISTMASTYRDRFPHYNLTHSLSLPWRPSTYYKAASNWPTLDPYCTRSQRVSESTMLPFVSNRTTLFTRYTPDDWYRSNLTNFQESNTSRHNSERLRVDTSRLIQDKYQQTRKTQADSTQNLGERVNDIGFWKSEIIHELDAMIGETNELTDIKKRLERALMETEAPLQVARECLFHREKRMGIDLVHDEVEKELLTEVDTILCCQERMKLYLDKAIAQLAANRAAQHELEKDLSDKQSAYRIDDKCHHLRNTSDGVSYFHGVERVDATVSVPESWAKFTDDNILRSQSERAASAKLRDDIQNVLVVTANEMWNQFNKVNLAFTNRIAETADAKNKIQTHLAKTLQEIFQTEMTIESIKKAIVEKSAFLKVAQTRLDERTRRPNIELCRDMAQLRLVNEVYEVDDTIQTLQQRLRDAEDTLQSLAHTKATLEHDLAVKANSLYIDQDKCMSMRRSFPSTLRLVGFC | null | null | cilium assembly [GO:0060271]; cilium movement involved in cell motility [GO:0060294]; flagellated sperm motility [GO:0030317]; regulation of brood size [GO:0060378] | acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; axonemal microtubule [GO:0005879]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; outer acrosomal membrane [GO:0002081]; sperm flagellum [GO:0036126] | null | PF03148; | null | Tektin family | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26268136}.; PTM: May be proteolytically processed during the epididymal transit of spermatozoa. {ECO:0000269|PubMed:26268136}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27883267}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000269|PubMed:19478333, ECO:0000269|PubMed:26268136, ECO:0000269|PubMed:27883267}; Peripheral membrane protein {ECO:0000305}. Note=In spermatozoa, preferentially localizes to the flagella, but also found in the head (By similarity). In the sperm flagellum, localizes to the periaxonemal region where it associates with the mitochondrial sheath and outer dense fibers (By similarity). Not detected in the central axonemal region of the flagellum (By similarity). Associates with the acrosome membrane in the equatorial segment of the sperm head (PubMed:27883267). Also detected just below the plasma membrane in the post-acrosomal region where it might localize to the postacrosomal dense lamina (PubMed:27883267). However, other studies report little or no expression in the postacrosomal region (By similarity). Translocates from the postacrosomal region to the equatorial segment after sperm activation (PubMed:27883267). Retained in the postacromal region, but not the equatorial segment, following the acrosome reaction (PubMed:27883267). Some studies report strong expression in the anterior acrosomal cap region (PubMed:19478333, PubMed:26268136). However, other studies report little or no expression in the acrosomal cap (PubMed:27883267). {ECO:0000250|UniProtKB:Q4V8G8, ECO:0000250|UniProtKB:Q9BXF9, ECO:0000269|PubMed:19478333, ECO:0000269|PubMed:26268136, ECO:0000269|PubMed:27883267}. | null | null | null | null | null | FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (PubMed:34715025). Required for normal sperm mobility (By similarity). {ECO:0000250|UniProtKB:Q6X6Z7, ECO:0000269|PubMed:34715025}. | Bos taurus (Bovine) |
A6H7G2 | DBNL_BOVIN | MAVNLSRNGPALLEAYQQVVNEKSSTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMAGFLKGAHVTINARAEEDVEPECIMQKVARASGANYTFHKESSRFQDTGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEERQQLEQERRERELREAALREQRYQEQGGEAGLQRKYEQHEVLSRNREEQPAHPREIFKQKERAMSTTSISSPQPGKLKSPFLQKQLTQPDTPISRESPHATSRPRADLREEPVPSIPPCSVQVEEEAVYEEPPEQETFYEEPPAVQQQDASSEPIDHYPGLSGKGLCARALYDYQAADETEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE | null | null | adaptive immune response [GO:0002250]; endocytosis [GO:0006897]; neuron projection morphogenesis [GO:0048812]; podosome assembly [GO:0071800]; positive regulation of axon extension [GO:0045773]; positive regulation of dendritic spine morphogenesis [GO:0061003]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of actin filament polymerization [GO:0030833]; synapse assembly [GO:0007416] | actin filament [GO:0005884]; anchoring junction [GO:0070161]; clathrin-coated vesicle membrane [GO:0030665]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; perikaryon [GO:0043204]; podosome [GO:0002102]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; ruffle [GO:0001726]; site of polarized growth [GO:0030427] | actin filament binding [GO:0051015] | PF00241;PF14604; | 3.40.20.10;2.30.30.40; | ABP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000250|UniProtKB:Q62418}. Perikaryon {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62418}. Cell membrane {ECO:0000250|UniProtKB:Q9JHL4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Cell projection, podosome {ECO:0000250|UniProtKB:Q62418}. Early endosome {ECO:0000250|UniProtKB:Q9UJU6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density {ECO:0000250|UniProtKB:Q9JHL4}. Note=Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q62418, ECO:0000250|UniProtKB:Q9JHL4}. | null | null | null | null | null | FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A6H7I5 | DYN2_BOVIN | MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAVPNQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHYELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD | 3.6.5.5 | null | actin filament bundle organization [GO:0061572]; autophagy [GO:0006914]; centrosome cycle [GO:0007098]; membrane tubulation [GO:0097749]; neuron projection morphogenesis [GO:0048812]; phagocytosis [GO:0006909]; protein polymerization [GO:0051258]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of axon extension [GO:0030516]; stress fiber assembly [GO:0043149]; synaptic vesicle budding from presynaptic endocytic zone membrane [GO:0016185]; vesicle scission [GO:0099050] | anchoring junction [GO:0070161]; cell junction [GO:0030054]; centriole [GO:0005814]; centrosome [GO:0005813]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; endosome [GO:0005768]; microtubule [GO:0005874]; midbody [GO:0030496]; neuron projection [GO:0043005]; phagocytic cup [GO:0001891]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; podosome [GO:0002102]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; recycling endosome [GO:0055037]; synapse [GO:0045202]; uropod [GO:0001931] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein self-association [GO:0043621] | PF01031;PF00350;PF02212;PF00169; | 1.20.120.1240;3.40.50.300;2.30.29.30; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Phosphorylation at Ser-844 by GSK3-alpha relieves the inhibition of BIN1 and promotes endocytosis. Phosphorylation at Ser-760 by CDK1 is greatly increased upon mitotic entry (By similarity). It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis (By similarity). Dephosphorylated by calcineurin/PP2 during cytokinesis in a Ca(2+)- and calmodulin-dependent manner (By similarity). Phosphorylated on tyrosine residues by EGFR and after activation of SRC (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P50570}. Cell projection, uropodium {ECO:0000250|UniProtKB:P50570}. Endosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P50570}. Recycling endosome {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P39054}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P39054}; Peripheral membrane protein {ECO:0000250|UniProtKB:P39054}. Cell projection, podosome {ECO:0000250|UniProtKB:P39054}. Cytoplasm {ECO:0000250|UniProtKB:P39052}. Cell junction {ECO:0000250|UniProtKB:P39052}. Postsynaptic density {ECO:0000250|UniProtKB:P39052}. Synapse, synaptosome {ECO:0000250|UniProtKB:P39052}. Midbody {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P39052}. Note=Localized in recycling endosomes fragment to release nascent autophagosomes (By similarity). Co-localizes with PIK3C3 and RAB5A to the nascent phagosome. Localized at focal ahesion site upon induction of focal adhesions and stress-fiber formation, when interacts with SDC4 (By similarity). Exists as a dynamic component of the centrosome. Associates with clathrin-coated vesicles at both the plasma membrane and the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:P50570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton. Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocytosis (CME), exocytic and clathrin-coated vesicle from the trans-Golgi network, and PDGF stimulated macropinocytosis. During vesicular trafficking process, associates to the membrane, through lipid binding, and self-assembles into ring-like structure through oligomerization to form a helical polymer around the vesicle membrane and leading to vesicle scission (By similarity). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes. During organization of the actin cytoskeleton, self-assembles into ring-like structure that directly bundles actin filaments to form typical membrane tubules decorated with dynamin spiral polymers (By similarity). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (By similarity). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (By similarity). The interaction with CTTN stabilizes the interaction of DNM2 and actin filaments and stimulates the intrinsic GTPase activity that results in actin filament-barbed ends and increases the sensitivity of filaments in bundles to the actin depolymerizing factor, CFL1 (By similarity). Plays a role in the autophagy process, by participating in the formation of ATG9A vesicles destined for the autophagosomes through its interaction with SNX18, by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (By similarity). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). Also plays a role in cytokinesis (By similarity). May participate in centrosome cohesion through its interaction with TUBG1. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Involved in membrane tubulation (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570}. | Bos taurus (Bovine) |
A6H7J1 | INSM1_BOVIN | MPRGFLVKRSKKSTPVSYRIRGGEDGDRALLLLPGCGGARASPPAPGPGPVPGPLQPPPPTERAHAALAAALACAPGPPPPPPGLRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLVGGGGGGGGGGANGAGGGGTCSGDPLLFAPAELKMGTAFSAAAEAARGPGPGPPLPPAAALRPPGKRPSPPASAAAAAEPPAKVAKAPGSKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGAARPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPAPAAARACEPETPARAEAREATGGGGSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPPPAPPAEDLLALYPGPDEKVPQEAAGDGEAAGVLGLSASAECHLCPVCGETFPSKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC | null | null | adrenal chromaffin cell differentiation [GO:0061104]; cell cycle [GO:0007049]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; noradrenergic neuron development [GO:0003358]; norepinephrine biosynthetic process [GO:0042421]; pancreatic A cell differentiation [GO:0003310]; positive regulation of cell differentiation [GO:0045597]; positive regulation of neural precursor cell proliferation [GO:2000179]; regulation of cell cycle [GO:0051726]; regulation of cell cycle process [GO:0010564]; regulation of gene expression [GO:0010468]; regulation of protein-containing complex assembly [GO:0043254]; sympathetic ganglion development [GO:0061549]; transdifferentiation [GO:0060290]; type B pancreatic cell differentiation [GO:0003309] | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | INSM1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4'. Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation. {ECO:0000250|UniProtKB:Q01101}. | Bos taurus (Bovine) |
A6H8H2 | DEN4C_MOUSE | MIEDKGPRVTDYFVVAGLTDTSTLLDQEINRTDTNSIGPKAPITDIAVIIKSAGETVPEGYTCVEATPSALQANLNYGSLKSPELFLCYRRGRDKPPLTDIGVLYEGKERLMPGCEVIQATPYGRCANVNNSSTTSQRIFITYRRAPPVRSQNSLAVTDICVIITSKGETPPHTFCKVDKNLNCGMWGSNVFLCYKKSVPASNAIAYKAGLIFRYPEEDYESFPLSPSVPLFCLPMGATIECWDPQIKYPLPVFSTFVLTGSSAEKVYGAAIQFYEPYSQERLTEKQLTQLGLLTLVEKRVVSKPINSNKCICLLSHWPFFEAFKNFLMFIYKVSVSGPHPLPIEKHISHFMQNIPFPSPQRPRILIQLSVHDAFILSQPVSTPLPLSGANFSSLLMNLGPENCATLLLLVLLESKILLHSLRPAVLTGVAEAVVAMIFPFQWQCPYIPLCPLSLAGVLSAPLPFIVGVDSRYFDLHDPPQDVVCIDLDTNTLYVADERKNINWKQLPKRPCKSLLGTLRRLYQQLCSVHRKPQESSAIEMTPIEADYSWQKKMTQLEMEIQETFLRFMASILKGYRSYLRPITEAPSNKATAADSLFDRQGFLKSRDRAYTKFYTLLSKTQIFIRFIEECSFVSDKDTGLAFFDDCIEKLFPDKGVERTEKVDLDSAEDTRLIELDDSQRSEHTVFIMPPEPPPDDGNNLSPQYSYTYFPRLDLKLFDSPQKLKLCFNRHPPGSSITNSPALMAKRTKQEIKTAHKLAKRCYTNPPQWAKYLFSHCYSLWFICLPAYVRVSHPKVRALQQAHDVLVKMRKTDVDPLDEVCYRVVMQLCGLWVNPVLAVRVLFEMKTARIKPNAITYGYYNKVVLESPWPSSTRSGIFLWTKVRNVVHGLAQFRQPLKKTGQKSQVFSISGGQSDQGYGSKDELVKEGADGHAPEEHTPPELTTTELHIEEECDISAIVSKHLQPTPEPQSPTEPPAWGSSIVKVPSGLFDTNNRTSTGSTSTVLFSTQAPVEDAVFSEVTNFKKNGDRGEKKQKHFPERSCSFSSESRAGMLLKKSSLDLNSSEMAIMMGADAKILTAALTCPKTSPPHVTRTHSFENVNCHLADSRTRMSEGTRDSEHRSSPVLEMLEESQELLEPVVGDNVAETAAEMTCNSLQSNSHSDQSRDTQAGAQDPVNKRSSSYATRKAIEREDVETGLDPLSLLATECVEKTSDSEDKLFSPVISRNLADEIESYMNLKSPLGSKSCSMELHGEGNQEPGSPAVFAHPLERSSSLPSDRGPPARDSTETEKSSPAVSSSKTLTGRFKPQSPYRAYKDRSTSLSALVRSSPNSSLGSVVNSLSGLKLDNILSGPKIDVLKSSMKQAATVASKMWVAVASAYSYSDDEEETNKDYSFPAGLEDHHIVGETLSPNTSVSGLVPSELTQSNTSLGSSSSSGDVGKLQCPAGEVPFSRNIKGQDFEKSDHGSSQNTSMSSIYQNCAMEVLMSSCSQCRACGALVYDEEIMAGWTADDSNLNTTCPFCKSNFLPLLNVEFKDLRGSASFFLKPSTSGDSLQSGSIPSASEPSEHKPTSSSAEPDLISFMDFSKHSETITEEASYTVESSDEIKKTNGDVQSVKMSSVPNSLSKRNVSLTRSHSVGGPLQNIDFSQRPFHGVSTVSLPSSLQEDVDHLGKRPSPPPVSVPYLSPLVLRKELESLLENEGDQVIHTSSFINQHPIIFWNLVWYFRRLDLPSNLPGLILTSEHCNGGVQLPLSSLSQDSKLVYIQLLWDNINLHQEPGEPLYVSWRNLNSEKKPSLLSEQQQAASALVETIRQSIQQNDVLKPINLLSQQMKPGTKRQRSLYREILFLSLVSLGRENIDIEAFDNEYGLAYRSLPSESLERLQRIDAPPSISVEWCRKCFGAPLI | null | null | cellular response to insulin stimulus [GO:0032869]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; regulation of Rab protein signal transduction [GO:0032483] | cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; insulin-responsive compartment [GO:0032593]; plasma membrane [GO:0005886]; retromer complex [GO:0030904] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF03455;PF02141;PF03456; | 2.100.10.50;3.40.50.11500;1.25.40.10; | null | PTM: Phosphorylated in response to insulin. {ECO:0000269|PubMed:21454697}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21454697}. Cell membrane {ECO:0000269|PubMed:21454697}. Cytoplasm, cytosol {ECO:0000269|PubMed:21454697}. Note=Associates with SLC2A4/GLUT4 storage vesicles. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed:21454697}. | Mus musculus (Mouse) |
A6H8H5 | KCNB2_MOUSE | MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQNDSHEHLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEQPERPCVYEEEIEMEEVICPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTDEHQRARAPPFLTLSRDKGPAAREAAVDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRASAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEEALPQGQPPLLEADDSAHCQGPSKGFSPRFPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRSRPDKQADPSPNCLADKPGDARDSLREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGHCPTRETSM | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; protein localization to plasma membrane [GO:0072659] | dendrite [GO:0030425]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; protein heterodimerization activity [GO:0046982]; transmembrane transporter binding [GO:0044325] | PF02214;PF00520;PF03521; | 1.10.287.70;1.20.120.350; | Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.2/KCNB2 sub-subfamily | PTM: Phosphorylated (By similarity). Phosphorylation at Ser-608 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB (By similarity). {ECO:0000250|UniProtKB:Q63099, ECO:0000250|UniProtKB:Q92953}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63099}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q63099}. Perikaryon {ECO:0000250|UniProtKB:Q63099}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63099}. Note=Localized uniformly throughout cell bodies and dendrites. Colocalizes with KCNB1 to high-density somatodendritic clusters on cortical pyramidal neurons. {ECO:0000250|UniProtKB:Q63099}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of about 20 msec. After that, inactivate very slowly. Their activation requires low threshold potentials of about -20 to -30 mV, with a midpoint activation at about 10 mV. For inactivation, the voltage at half-maximal amplitude is about -30 mV. Channels have an unitary conductance of about 14 pS. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system and post-translational modifications. {ECO:0000305|PubMed:10414301}; | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. {ECO:0000250|UniProtKB:Q63099}. | Mus musculus (Mouse) |
A6H8Y1 | BDP1_HUMAN | MFRRARLSVKPNVRPGVGARGSTASNPQRGRESPRPPDPATDSASKPAEPTDVPTVDFGGAEPQEKAPRSSTEKTGGDNDVEESSRSSSTVSQRRKRISSTSSLVKSSVSVPSESHPLSTINQEAPQPTATSTKEKQPCSDRYRIYKAQKLREMLKEELRKEKKQWKNKYAINESQRPPDRSKMTMRDFIYYLPDNNPMTSSLEQEKKTEKPSTPVQTREQEGKSTPNAEDNEMEEETDDGPLLVPRVKVAEDGSIILDEESLTVEVLRTKGPCVVEENDPIFERGSTTTYSSFRKNYYSKPWSNKETDMFFLAISMVGTDFSMIGQLFPHRARIEIKNKFKREEKTNGWRIDKAFQEKRPFDFDFFAHLLQKVLAEEEKRKQKSVKNHSLKEKKSTKPRKNVKVKKVACEGVNNDPDESMSSRISDTERSQKDAQTVEEESLTLSREDAEQVALEVDLNQKKRRRKKQDGANELGVNNLLENATVQAGPSKGEKHKNKCQAIRPELKEGECSKEQMLSCTQNIDGIVGFASTEKVEKRTDPILSLSNQQDATSVATESSESSTSDLPSFEVGIRALCEVNNAEGSCIEERNVDLKNNSLEIDQTENVKPMLRGRFQRPKPNLSRAGKKSVLSQGKTESESKNSHSKTSVEKNHVEKDKMNTLDILRMETTERENPEAETVSVLGEKNCLQEGSQLKALRPVQVRGRLQKPKPNAGKAAERKEILISQEEIGANVEKNENESCADRDTPQHMEDQSRKDFEEEDVILQPEKNDSFQNVQPDEPKVLNECLSVQENNKANKLNQVPILRTRFQKPKPNIGRGTGRREISSKEEVLEKILVSGEMAAALRETVRLDTSPKEMVPAEINTKEMQSDLKETGRRAISPREKILDVIDDTIEMETGLKAMGREICLREKTPEVIDATEEIDKDLEEAGRREISPQKNGPEEVKPLGEVETDLKATGNESSPREKTPEVTDATEEIDKNLEETGRRKISPRENGPEEVKPVDEMETDLNATGRESSPREKTPEVIDATEEIDLEETEREVSPQENGLEEVKPLGEMETDLKATGRDSFPRGKTPEVIDAIEEIEIDLEETEREISPQENGLEEVKPLGEMQTDLKATGREISPREKTPEVIDATEEIDKDLEETGRREISPEENGPEEVKPVDEMETDLKTTGREGSSREKTREVIDAAEVIETDLEETEREISPQENGPEEVKPVGKMETDLKEIREEISQREKVLAEFSAIREKEIDLKETGKRDIPIMEKVSGKMAVVEEMEADLKETGKENFRERGSEEICVTEEKVAELKQTGKTDISPRENELEETSTSRQTDTHLMQSGSNDFSAVPSLDIQNISSEVLSMMHTPVEEKRNSEKEVSSHFSHFKISSQTHESDKTEVQGIQSPDVPEQFSDINLSKSLPQEQKPLEIKPAPFVRSRFKRPKPNLARAALKRETTESEKYIYEKKSETKKMETIVMQENNEQTDTLPSQHDEASLMISREKDTLGHRNEEAVILPCTQTERNLSPSNSCEPKEESQSAPVQKNDSVVSVGTNNVNTFQQEMKESVIQTARQVRGRLQRPRPNIRKTGQRQIVDKGEAKGIIKEGRTILPKDETEKKVLTVSNSQIETEIEVPSSAVPEHRMYENQSQVVLVENLHVNKTNETIRHENKPYVPSSAQMTRRKFQKAKPNLGRAHSKKEEPVLEKVTTDQSKEGKPEDHLLQKGASNTQLLLKEKAELLTSLEVSARKDCVGSKESALAKIDAELEEVGPSRRVGEETVGDNSPSSVVEEQYLNKLTSCPQPLNETSYSKIALDGKTTISSTSEYERNRGERRSHKKFKPNVTRGRGSKRVRGKTSKKEPRASKAMLVTLRASQEEDDDADDFESDYEEESYHLAPEEVNKAPVFVPVGLRSPEPVSAQIEETMEELEITVNVPDVGCIAVVEHELPNTDVTTEEMKQEENLSVPFEMTTSEHIQDEPGTNDGSTEAAITLLTMGDLVLQSEISSEQGDVGVCIIPHVHSKDKSHIPSSLDNVNHKIVHECQELSSPVITTSPASFEENKIVLEEQSSREEISLMEKVKENATPTRNTISKVTSNLRIRSRLAKPKPNLEKTLGTNRLDDYQEVSSLCVTKGAEMETQRETEKNASKATELENKNLGPVTTAENKDQSKLACVHGIKGTSISSEVNLTERNENQEESSQEVHMLSVAPVASSETGPCTLGLDRGLGENSVEEPQIKDSKGDSVLTLPVPEYTPTSIPEVQQENIINPQDLTVNLVANVPQDGEDEQAFILTLVEIPANAVEEFTDATAQFMPNPLLPAPILVKSVNTEERGDMSICLPATSVGQDAMGLSISGRDNSKKPPDNLDLVSRKRFQCRLDKNDHIPPAKKRSLTLRDDCQEYTTEVHSKELTNVFEETGESHKGQDIFLTSGSTLTTPEPQRQQVEAAFQSRGSRSPDACMDKNVPQLPQDEMIVSDKEERTDAAPKSQQMDSRTSSSKASLSRPGRRPLGFLSLICSKNSLESDEPMQVHSKKRLKPLIPGLRKKLKRSNPFNESQEKNRESSDLLPSPSVITTQSENISSSATQVSCDQPLLKEGYKSAQKRAPQGEATTVSEYFFNDIFIEVDETE | null | null | RNA polymerase III preinitiation complex assembly [GO:0070898] | nucleoplasm [GO:0005654]; transcription factor TFIIIB complex [GO:0000126] | TFIIIC-class transcription factor complex binding [GO:0001156] | PF15963; | null | null | PTM: Phosphorylated by CSNK2A1 during mitosis, resulting in its release from chromatin and suppression of polymerase III transcription. {ECO:0000269|PubMed:15469824}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11161782}. | null | null | null | null | null | FUNCTION: General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site. {ECO:0000269|PubMed:11040218}. | Homo sapiens (Human) |
A6H8Z2 | F221B_HUMAN | MEAHEIIEEPHITMDAEKHPPSKDPSAEDLQENHISESFLKPSTSETPLEPHTSESPLVPSPSQIPLEAHSPETHQEPSISETPSETPTYEASLDSPISVVPEKHLTLPPQSRDYVCLSSSDTLKEDLSSESSSNEVPWTRRSTHLSESESLPEHCLSGPSSQVQVDTTEKQEEEAGEVEKGVDASDSTAHTAQPGHQLGNTARPVFPARQTELVEVAKAMHREEFGAQVNNLFQWEKDAALNAIQTGLYIGWRCPHYLWDCFRIGDESRCFCGHLLREHRIISDISVPCKVSQCRCFMFCFIPSRPEEVGEFWLKRRATFDPKAWRAQCRCKHSHEEHAATGPHPCRHHGCCCGCFESNFLCAACDRRWEEHETFFDTQKTRQRGGRPRGTDTVSNWHRPL | null | null | null | null | null | PF14753; | null | FAM221 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A6HD62 | CHIP_RAT | MKGKEEKEGGARLGTGGGGSPDKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGDEDDGHIRAQQACIEAKHDKYMADMNELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY | 2.3.2.27 | null | cellular response to misfolded protein [GO:0071218]; DNA repair [GO:0006281]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of vascular associated smooth muscle contraction [GO:1904694]; positive regulation of chaperone-mediated protein complex assembly [GO:0090035]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of mitophagy [GO:1901526]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of proteolysis [GO:0045862]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of glucocorticoid metabolic process [GO:0031943]; regulation of protein stability [GO:0031647]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear inclusion body [GO:0042405]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; ubiquitin ligase complex [GO:0000151]; Z disc [GO:0030018] | enzyme binding [GO:0019899]; G protein-coupled receptor binding [GO:0001664]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; kinase binding [GO:0019900]; misfolded protein binding [GO:0051787]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; R-SMAD binding [GO:0070412]; SMAD binding [GO:0046332]; TPR domain binding [GO:0030911]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-ubiquitin ligase activity [GO:0034450] | PF12895;PF18391;PF04564; | 6.10.140.2020;1.25.40.10;3.30.40.10; | null | PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2 and enhanced in the presence of MAP2K5 (By similarity). Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000250|UniProtKB:Q9WUD1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19237536, ECO:0000269|PubMed:19483080, ECO:0000269|PubMed:30980393}. Nucleus {ECO:0000269|PubMed:19237536, ECO:0000269|PubMed:30980393}. Mitochondrion {ECO:0000269|PubMed:29934347}. Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg) (By similarity). Localizes to mitochondria following oxygen and glucose deprivation-induced cellular stress (PubMed:29934347). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000269|PubMed:29934347}. | 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:Q9WUD1}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9WUD1}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:26265139). Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress (PubMed:29934347). Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction (PubMed:19237536). Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1-mediated transcription of pro-apoptotic genes (PubMed:19483080). Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes (PubMed:20724525). Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3 (PubMed:30980393). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (By similarity). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (By similarity). Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex (PubMed:26265139). Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (PubMed:21808025). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (By similarity). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (By similarity). Mediates polyubiquitination of CYP3A4 (By similarity). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (By similarity). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (By similarity). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (By similarity). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (By similarity). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (By similarity). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (By similarity). Plays a role in the degradation of TP53 (By similarity). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (By similarity). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000250|UniProtKB:Q9WUD1, ECO:0000269|PubMed:19237536, ECO:0000269|PubMed:19483080, ECO:0000269|PubMed:20724525, ECO:0000269|PubMed:21808025, ECO:0000269|PubMed:26265139, ECO:0000269|PubMed:29934347, ECO:0000269|PubMed:30980393}. | Rattus norvegicus (Rat) |
A6K136 | PPM1K_RAT | MLSTAFITLVRSGRNQVKKRVLLSSILLQDHRQMTPACYCSISEPRCSRFDPDGSGQPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASLIGKRKENEDRFGFAQLTEEVLYFAVYDGHGGPAAADFCHTHMEKCVTDLLPREKDLETVLTLAFLEIDKAFSSYAHLSADASLLTSGTTATVALLRDGVELVVASVGDSRALLCRKGKPMKLTTDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKASGVIAEPETTRIKLYHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPKEAAHAVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA | 3.1.3.16; 3.1.3.52 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8N3J5}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8N3J5}; | branched-chain amino acid catabolic process [GO:0009083]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | manganese ion binding [GO:0030145]; protein serine/threonine phosphatase activity [GO:0004722] | PF00481; | 3.60.40.10; | PP2C family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000305|PubMed:29779826}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000269|PubMed:29779826}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] + phosphate; Xref=Rhea:RHEA:77247, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.52; Evidence={ECO:0000250|UniProtKB:Q8N3J5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77248; Evidence={ECO:0000250|UniProtKB:Q8N3J5}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:29779826}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000269|PubMed:29779826}; | null | PATHWAY: Protein modification. {ECO:0000269|PubMed:29779826}. | null | null | FUNCTION: Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle (By similarity) (PubMed:29779826). At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction (By similarity). Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis (By similarity) (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (By similarity). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (By similarity). {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000269|PubMed:29779826}. | Rattus norvegicus (Rat) |
A6M931 | IF4A3_PIG | MAATATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI | 3.6.4.13 | null | embryonic cranial skeleton morphogenesis [GO:0048701]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of translation [GO:0006417]; rRNA processing [GO:0006364] | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; U2-type catalytic step 1 spliceosome [GO:0071006] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, eIF4A subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites. {ECO:0000250|UniProtKB:Q3B8Q2}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P38919}; | null | null | null | null | FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development. {ECO:0000250|UniProtKB:P38919}. | Sus scrofa (Pig) |
A6M9B7 | GLCT_ECOLX | MKIAYVVSSKKKCGPNIVILNIVKELANKHEMEIFFLDESDDDVFECVNVKSTQIKKASDLKEHLKRFDIIHSSGIRPDALVVLCKVIYRVKCKIITTIHNYVFQDLYYSYGLVKSLIGGLLWCSIWLFFDKLVILSKNADNYYWFLPSAKKNIIYNGIDDNDCLQNKKCNYRKEFNIPDDGILAGSCANLTKRKGIDLVIQTLTKEHKIYYIVAGNGIEKHNLINLVKARKLHERVYFIDFLDEPESFMSQLDVFLMPSRSEGFGLTVLESTKLGIPVITSNIPIFMELFDQMCLTFDIKNPSTLIDVITYAKKNRLHLSQKFHAIFQDRFTSSKMATKYENVYNNLFREVL | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243]; sulfolipid biosynthetic process [GO:0046506] | Gram-negative-bacterium-type cell wall [GO:0009276]; membrane [GO:0016020] | glucosyltransferase activity [GO:0046527]; glycogen (starch) synthase activity [GO:0004373]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF13439;PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.345 mM for Gal-beta1-3GalNAc-PP-PhU {ECO:0000269|PubMed:32421169}; Vmax=152 nmol/h/mg enzyme with Gal-beta1-3GalNAc-PP-PhU as substrate {ECO:0000269|PubMed:32421169}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:21968437, ECO:0000269|PubMed:32421169}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. Retains 24% of maximal activity at pH 5 and 14% of activity at pH 9. {ECO:0000269|PubMed:32421169}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 50% of the activity in elution buffer/20% glycerol for four days at 4 degrees Celsius. Retains 60% of the activity in several days storage at -20 degrees Celsius with 20% glycerol.; | FUNCTION: Involved in the assembly of the O-repeating unit during O-antigen biosynthesis. Glucosyltransferase accountable for the alpha-D-Glc-1,4-beta-D-Gal linkage within the O-antigen (PubMed:21968437, PubMed:32421169). Transfers alpha-1,4-Glc to the Gal moiety of a specific Gal-beta1-3GalNAc-alpha-OPO3-PO3-phenoxyundecyl (Gal-beta1-3GalNAc-PP-PhU) synthetic natural acceptor substrate analog. Requires both Gal-beta1-3GalNAc-alpha and the diphosphate moiety in the acceptor. Not active with GalNAc-PP-PhU, GlcNAc-PP-PhU, Gal-beta1-3GalNAc-alpha-O-benzyl, D-Rha-alpha1-3GlcNAc-alpha-PP-PhU or D-Man-alpha1-3Man-alpha-5-benzamidopentyl (BAP), nor with glycopeptides TTTVTP (Gal-beta1-3GalNAc-alpha-)TPTG or TT (Gal-beta1-3GalNAc-alpha-)TVTPTPTG as acceptor substrates. Has a broad nucleotide sugar donor substrate specificity with ADP-Glc, TDP-Glc and UDP-Glc as superior donors. Gal, GlcNAc, and GalNAc residues are transferred from UDP-sugars, but with low activity. UDP-Xyl, UDP-GlcA, GDP-Fuc or GDP-K-Rha do not act as donors (PubMed:32421169). {ECO:0000269|PubMed:21968437, ECO:0000269|PubMed:32421169}. | Escherichia coli |
A6MEY4 | PA2B_BUNFA | MNPAHLLVLLAVCVSLLGAANIPPQSLNLYQFKNMIQCAGTQLCVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKTYEYTCNKPDLTCTDAKGSCARNVCDCDRAAAICFAAAPYNLANFGINKETHCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | 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, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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:0000255|PROSITE-ProRule:PRU10036}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits blood coagulation and shows bactericidal activities against both Gram-negative and -positive bacteria (E.coli, MIC=0.4 uM and S.aureus, MIC=0.1 uM). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17383773}. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
A6MFK7 | FAXD1_DEMVE | MAPQLLLCLIQTFLWSLPEAESNVFLKSNVANRFLQRTKRANSGFEEIYPANFERECVEERCSKEEAREVFEDDEKTEAFWTVYVDGDQCLSNPCHYGGTCKDGIGSYTCTCLAGYEGKNCEHDLLKSCRVDNGNCWHFCKPVQNDTQCSCAEGYRLGDNGFSCIAEGEFSCGRNIKSRNKREASLPDFQTDFSDDYDAIDENNLIETVQSQSATLLKKSDNPNPDIRIVNGLDCKLGECPWQAVLIDEKGTAFGGGTILSPYFVLTAAHCINKTKSIAVVVGQVDISRKETRRLLSVDKVYTHPKYVHVTNDYDIAIIQLKTPIQFSENVVPACLPTADFANHVLMKQDFGIVSGFGRIEEKGPTSNILKVVMVPYVDRHTCILSTKIPITRNMFCAGYGNQPEDACEGDSGGPHITAYKDTHFLTGIVSWGEGCGRDGKYGIYTKVSNFLPWIKTIMRRKQPSTESSTGRL | 3.4.21.6 | null | blood coagulation [GO:0007596]; envenomation resulting in positive regulation of blood coagulation in another organism [GO:0044469]; induction of blood coagulation in another organism [GO:0035807]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; peptidase activator activity [GO:0016504]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity). {ECO:0000250}. | Demansia vestigiata (Lesser black whip snake) (Demansia atra) |
A6MFK8 | FAXD2_DEMVE | MAPQLLLCLILTFLWSLPEAESNVFLKSNVANRFLQRTKRANSIFEEIRPGNIERECVEEKCSKEEAREVFQDNEKTEAFWTVYVDGDQCLSNPCHYRGTCKDGIGSYTCTCLPGYEGKNCEHVVVKSCRLFNGNCWHFCKTVQNDTQCSCAEGYRLGVDGFSCIAEGDFSCGRIIKSRNKREASLPDFHFSDDYDAIDENNLVETVQSQSATLLKKSDNPSPDIRIVSGLDCKLGECPWQAVLIDEHGKAFGGGTILSPYFVLTAAHCLNQTKSIAVVVGQVDISRKETRHLLHVDKAYMHSKYVRATYDHDIAILRLRTPIQFSENVVPACLPTADFADEVLMKQDFGIVSGFGRLHERGSTSDILKVIRVPYVDRYTCMLSSNYRITPSMFCAGYGNQPQDACQGDSGGPHITAYGDTHFITGIISWGEGCGRKGKYGIYTKVSNFIPWIKTIMRRNQPSTESSTGRL | 3.4.21.6 | null | blood coagulation [GO:0007596]; envenomation resulting in positive regulation of blood coagulation in another organism [GO:0044469]; induction of blood coagulation in another organism [GO:0035807]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; peptidase activator activity [GO:0016504]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity). {ECO:0000250}. | Demansia vestigiata (Lesser black whip snake) (Demansia atra) |
A6N3Q4 | CC14C_SYMSY | MKRKSEGRSSWAAATCSPCCSLTSPSVKKIRSPTQQDPRHRDPQDDVYLDITDRLRLAILYSRPKSASNVHYFSIDNELEYENFSEDFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEEAYRTLIFGDTSYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNRNVTTIIRLNKKMYDAKCFTDAGFDHHDLFFADGSSPTDAIVKGFLDICENAEGAIAVHCKAGLGRTGTLIACYIMKHYRMTAAETIAWVRICRPGLVIGPQQQFLVMKQTSLWLEGDYFCQKLKGQENGQHRAAFPKLHSGVDDISINGVENQDQQEPEPYSDDDEINGGTQGDRLRALKSRRQSKTNAILLTCPLAVLTSALCSVVIWWIVCDYILPILLFCLDGFGT | 3.1.3.16; 3.1.3.48 | null | cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | myosin phosphatase activity [GO:0017018]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138] | PF00782;PF14671; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus, nucleolus. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18547142}. Note=Nucleolar during interphase (By similarity). Microtubular association (PubMed:18547142). {ECO:0000250, ECO:0000269|PubMed:18547142}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity). {ECO:0000250}. | Symphalangus syndactylus (Siamang) (Hylobates syndactylus) |
A6N6J5 | WDR35_RAT | MFFYLSKKIAVPNNVKLKCISWNKDQGFIACGGEDGLLKVLRLETQTDDSKLRGLAAPSNLSMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVWMLYKGSWYEEMINNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQLCHVTWSADSKILLFGMANGEIHIYDNQGNFIMKMKLNCLVNVTGAISIAGIHWYHGTEGYVEPDCPCLAICFDNGRCQIMRHENDQNPVLIDTGMYVVGIQWNHIGSVLAVAGSQKVVTQDKDVNIVQFYTPFGEHLGTLKVPGKQMCSLSWEGGGLKIALAVDSFIYFANIRPDYKWGYCSNTVVYAYTRPDRPEYCVVFWDTKNNEKYVKYVKSLISITTCGDFCILATKADENHPQFVLVLCNSIGTPLDPKYIDLVPLFVAMTKTHVIAASKEALYTWQYRVAKKLTALEINQITRSRKEGRERIYHVDDVPSGSVDGVFDYSKAIQGTRDPICAITASDKTLIVGRESGVIQRYSFPNVALIQKYSLDCRACQLSLNCNSSRLAIIDIAGVLTFFDLDTRVTDSTGQQVVGELLKLERKDVWDMKWAKDNPDLFAMMEKTRMYVFRNLDPEEPIQTSGYICNFEDLEIKSVLLDEILKNPEHPSKDYIMNFEIRSLRDSRALIEKVGIEDASQFIEDNPHPRLWRLLAEAALQKLDLYTAQQAFVRCKDYQGIKFVKRLGNLQSESMKQAEVIAYFGRFEEAERMYLDMDRRDLAIGLRLKLGDWFRVLQLLKTGSGDADDSLLEQAHNAIGDYFADRQKWMNAVQYYVKGRNQERLAECYYMLEDYEGLENLANSLPENHKLLPEIAQMFVRVGMCEQAVSAFLKCNQPKAAVDTCVHLNQWNKAVELAKSHSMKEIGSLLARYASHLLEKNKTLDAIELYRKASYFFDAAKLMYKIADEEAKKRTKPLRVKKLYVLSALLIEQYHEQMKNAQRGKVKGKNSEATSALAGLLEEEVLSTTSRFTDNAWRGAEAYHFFILAQRQLYEGYVDTALKTALHLRDYEDIIPSVEIYSLLALCACASRAFGTCSKAFIKLESLETLSAEQKQQYEDLALEIFTKHTPKDNRKSELNSLLEGGEGKLPTCIATGSPIIEYQFWVCKVCKHYVLAQEISNYNFCPLCHSSVE | null | null | cellular response to glucose stimulus [GO:0071333]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to xenobiotic stimulus [GO:0071466]; cilium assembly [GO:0060271]; intraciliary retrograde transport [GO:0035721]; intraciliary transport [GO:0042073]; liver regeneration [GO:0097421]; negative regulation of gene expression [GO:0010629]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; non-motile cilium assembly [GO:1905515]; positive regulation of apoptotic process [GO:0043065]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of vasoconstriction [GO:0045907]; protein localization to cilium [GO:0061512]; response to lipopolysaccharide [GO:0032496]; response to toxic substance [GO:0009636] | axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; intraciliary transport particle A [GO:0030991]; non-motile cilium [GO:0097730] | null | PF12894;PF00400; | 1.25.40.470;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BND3}. | null | null | null | null | null | FUNCTION: As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking (By similarity). May promote CASP3 activation and TNF-stimulated apoptosis (PubMed:20193664). {ECO:0000250|UniProtKB:Q9P2L0, ECO:0000269|PubMed:20193664}. | Rattus norvegicus (Rat) |
A6NC98 | CC88B_HUMAN | MEGGKGPRLRDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEGREAPQGELVPEAWGLRQEGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGALEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRLMRPRREGGPPGGLRLGADGAGSTESLGGPPETELPEGREADGTGSPSPAPMRRAQSSLCLRDETLAGGQRRKLSSRFPVGRSSESFSPGDTPRQRFRQRHPGPLGAPVSHSKGPGVGWENSAETLQEHETDANREGPEVQEPEKRPLTPSLSQ | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton-dependent intracellular transport [GO:0030705]; defense response to protozoan [GO:0042832]; positive regulation of cytokine production [GO:0001819]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell proliferation [GO:0042102] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | dynein light intermediate chain binding [GO:0051959]; microtubule binding [GO:0008017] | PF19047; | 1.10.418.10; | CCDC88 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q4QRL3}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:25762780}. Endoplasmic reticulum {ECO:0000269|PubMed:21289099}. Golgi apparatus {ECO:0000269|PubMed:21289099}. Cytoplasm {ECO:0000269|PubMed:21289099}. | null | null | null | null | null | FUNCTION: Acts as a positive regulator of T-cell maturation and inflammatory function. Required for several functions of T-cells, in both the CD4(+) and the CD8(+) compartments and this includes expression of cell surface markers of activation, proliferation, and cytokine production in response to specific or non-specific stimulation (By similarity). Enhances NK cell cytotoxicity by positively regulating polarization of microtubule-organizing center (MTOC) to cytotoxic synapse, lytic granule transport along microtubules, and dynein-mediated clustering to MTOC (PubMed:25762780). Interacts with HSPA5 and stabilizes the interaction between HSPA5 and ERN1, leading to suppression of ERN1-induced JNK activation and endoplasmic reticulum stress-induced apoptosis (PubMed:21289099). {ECO:0000250|UniProtKB:Q4QRL3, ECO:0000269|PubMed:21289099, ECO:0000269|PubMed:25762780}. | Homo sapiens (Human) |
A6NCS4 | NKX26_HUMAN | MLLSPVTSTPFSVKDILRLERERSCPAASPHPRVRKSPENFQYLRMDAEPRGSEVHNAGGGGGDRKLDGSEPPGGPCEAVLEMDAERMGEPQPGLNAASPLGGGTRVPERGVGNSGDSVRGGRSEQPKARQRRKPRVLFSQAQVLALERRFKQQRYLSAPEREHLASALQLTSTQVKIWFQNRRYKCKRQRQDKSLELAGHPLTPRRVAVPVLVRDGKPCLGPGPGAPAFPSPYSAAVSPYSCYGGYSGAPYGAGYGTCYAGAPSGPAPHTPLASAGFGHGGQNATPQGHLAATLQGVRAW | null | null | atrial cardiac muscle cell development [GO:0055014]; cell differentiation [GO:0030154]; digestive tract development [GO:0048565]; embryonic heart tube development [GO:0035050]; epithelial cell apoptotic process [GO:1904019]; epithelial cell differentiation [GO:0030855]; epithelial cell proliferation [GO:0050673]; hypothalamus development [GO:0021854]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell apoptotic process [GO:1904036]; pericardium development [GO:0060039]; pharyngeal system development [GO:0060037]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; tongue development [GO:0043586]; ventricular cardiac muscle cell development [GO:0055015] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | NK-2 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator (PubMed:15649947). In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development. {ECO:0000250|UniProtKB:P43688, ECO:0000269|PubMed:15649947}. | Homo sapiens (Human) |
A6ND01 | JUNO_HUMAN | MACWWPLLLELWTVMPTWAGDELLNICMNAKHHKRVPSPEDKLYEECIPWKDNACCTLTTSWEAHLDVSPLYNFSLFHCGLLMPGCRKHFIQAICFYECSPNLGPWIQPVGSLGWEVAPSGQGERVVNVPLCQEDCEEWWEDCRMSYTCKSNWRGGWDWSQGKNRCPKGAQCLPFSHYFPTPADLCEKTWSNSFKASPERRNSGRCLQKWFEPAQGNPNVAVARLFASSAPSWELSYTIMVCSLFLPFLS | null | null | cell adhesion [GO:0007155]; fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; single fertilization [GO:0007338]; sperm-egg recognition [GO:0035036] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102] | PF03024; | null | Folate receptor family | PTM: The protein is rapidly cleaved following fertilization, being only weakly detectable in zona-intact fertilized eggs at telophase II and undetectable at the pronuclear stage. Sheding is probably required to block to polyspermy and ensuring egg fusion with a single sperm. {ECO:0000250|UniProtKB:Q9EQF4}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9EQF4}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9EQF4}. Cell projection, microvillus membrane {ECO:0000269|PubMed:36070373}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9EQF4}. Note=GPI-anchored at the oolemma microvilli. {ECO:0000250|UniProtKB:Q9EQF4}. | null | null | null | null | null | FUNCTION: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate. {ECO:0000250|UniProtKB:Q9EQF4}. | Homo sapiens (Human) |
A6ND36 | FA83G_HUMAN | MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLSELELKRILETIEVYDPGSEDPRGTGPSQGPEDNGVGDGEEASGADGVPIEAEPLPSLEYWPQKSDRSIPQLDLGWPDTIAYRGVTRASVYMQPPIDGQAHIKEVVRKMISQAQKVIAVVMDMFTDVDIFKDLLDAGFKRKVAVYIIVDESNVKYFLHMCERACMHLGHLKNLRVRSSGGTEFFTRSATKFKGALAQKFMFVDGDRAVCGSYSFTWSAARTDRNVISVLSGQVVEMFDRQFQELYLMSHSVSLKGIPMEKEPEPEPIVLPSVVPLVPAGTVAKKLVNPKYALVKAKSVDEIAKISSEKQEAKKPLGLKGPALAEHPGELPELLPPIHPGLLHLERANMFEYLPTWVEPDPEPGSDILGYINIIDPNIWNPQPSQMNRIKIRDTSQASAQHQLWKQSQDSRPRPEPCPPPEPSAPQDGVPAENGLPQGDPEPLPPVPKPRTVPVADVLARDSSDIGWVLELPKEEAPQNGTDHRLPRMAGPGHAPLQRQLSVTQDDPESLGVGLPNGLDGVEEEDDDDYVTLSDQDSHSGSSGRGPGPRRPSVASSVSEEYFEVREHSVPLRRRHSEQVANGPTPPPRRQLSAPHITRGTFVGPQGGSPWAQSRGREEADALKRMQAQRSTDKEAQGQQFHHHRVPASGTRDKDGFPGPPRYRSAADSVQSSTRNAGPAMAGPHHWQAKGGQVPRLLPDPGSPRLAQNARPMTDGRATEEHPSPFGIPYSKLSQSKHLKARTGGSQWASSDSKRRAQAPRDRKDP | null | null | BMP signaling pathway [GO:0030509]; epidermal growth factor receptor signaling pathway [GO:0007173]; intermediate filament cytoskeleton organization [GO:0045104]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of cell migration [GO:0030335]; protein localization to mitotic spindle [GO:1902480]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of TOR signaling [GO:0032006] | cytosol [GO:0005829]; keratin filament [GO:0045095]; membrane [GO:0016020]; mitotic spindle pole [GO:0097431]; nucleus [GO:0005634] | keratin filament binding [GO:1990254]; protein kinase binding [GO:0019901] | PF07894; | 3.30.870.10; | FAM83 family | PTM: BMP signaling induces the phosphorylation by BMPR1A at Ser-610, Ser-614 and Ser-616. Phosphorylation at Ser-610 is necessary for the activation of SMAD4-independent BMP target genes such as NEDD9 and ASNS. {ECO:0000269|PubMed:24554596}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24554596}. Nucleus {ECO:0000269|PubMed:24554596}. Note=Detected predominantly in the cytosol. Upon BMP stimulation, a small portion localizes the nucleus. {ECO:0000269|PubMed:24554596}. | null | null | null | null | null | FUNCTION: Substrate for type I BMP receptor kinase involved in regulation of some target genes of the BMP signaling pathway. Also regulates the expression of several non-BMP target genes, suggesting a role in other signaling pathways. {ECO:0000269|PubMed:24554596}. | Homo sapiens (Human) |
A6NDB9 | PALM3_HUMAN | MAESSLYRQRLEVIAEKRRLQEEIRAARREVEEEKLRVERLKRKSLRERWLMDGAAAVPEPSEDPTSKDPQSPEGQAQARIRNLEDSLFTLQSQLQLLQSASTGAQHKPSGRPSWRRQGHRPLSQSIVEAGSVGQTDLNKRASLPAGLVGTPPESPSEPREDVLGFLPGPRQVPGAAGDSSEANGPCPSPIPTPEQGLSQRAVPSEGRVGEAKGGGVVSVVWEGLRATEDCATGATGPELEAKVEEVVLEAIGDRKGAGSLELPAWVKEDRGIVEVVWEGVGGSDAEAMGEIGRVPEVVQTSSPRLQERLEAAASIEGEDVPQGSPEGDGQGGSGGEEGSFIWVERVTLSEEWEELLVEGLEGPEVAGRERGDESPLGAEGAKTGGGEETWEAEKRKAEESMGIGSEEKPGTGRDEAEMSPVVERKGGEKKLELESRGSAEKLGTEREGGEEPLGIERKVEGHLRAEKEGDEEKRGAEEEEVEEPLGVEKKGGEEEPEATKEPLEAERKGGEETLEAEKRGGEESLETEKTQGTEGDLNLEQGSREGSESQAEEMNEAGPPLEANTETRPEKEGPQPQEKPVGALEEEGVKPQTAAEGQGPLGDATPLLAETPAPEQPAECQPLLQGEGPSANPSAHPVPTYAPARQPEPSAPTEGEEASGPKQKTCQCCAVM | null | null | negative regulation of cytokine-mediated signaling pathway [GO:0001960]; regulation of cell shape [GO:0008360]; response to lipopolysaccharide [GO:0032496]; Toll signaling pathway [GO:0008063] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524] | PF03285; | null | Paralemmin family | PTM: Palmitoylated on Cys-667 and Cys-669 and prenylated on Cys-670; which is required for membrane association. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. | null | null | null | null | null | FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}. | Homo sapiens (Human) |
A6NDE4 | RBY1B_HUMAN | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSQEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREAYGSSSYVASIVDGGESRSEKGDSSRY | null | null | male gonad development [GO:0008584]; mRNA processing [GO:0006397]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; RNA splicing [GO:0008380]; spermatogenesis [GO:0007283] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | RNA binding [GO:0003723] | PF08081;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. | Homo sapiens (Human) |
Subsets and Splits