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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
E3YBA4 | MBCTN_METTR | MTVKIAQKKVLPVIGRAAALCGSCYPCSCM | 1.11.1.-; 1.15.1.1 | null | copper ion transport [GO:0006825] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]; superoxide dismutase activity [GO:0004784] | null | null | null | null | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Secreted as apo-mb, uptake into the cytoplasm in complex with copper as Cu-mb. In the cytoplasm, Cu-mb is associated with the cell membrane. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:18372044}; | null | null | null | null | FUNCTION: Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated lev... | Methylosinus trichosporium |
E4MYY0 | HCS_KITSK | MAEFEIPDFYVPFPLECNPHLEEASRAMWEWIDANGLAPTERARDRMRRTGADLSGAYVWPRADLDTLTIGLKWIALTFRIDDQIDEDDTAERLPARMTAIDELRGTLHGLPVSGRSPTARALGALWQETALGRPATWCDAFIGHFEAFLQTYTTEAGLNAHGAGLRLDDYLDRRMYSVGMPWLWDLDELRLPIFLPGSVRTCGPMNKLRRAGALHIALVNDVFSVERETLVGYQHNAVTIIREAQGCSLQEAVDQVAVLVEAQLHTVLQARQELLEELDRQALPSRAREAAVDYAANVAANLSGQLVWHSSVERYAVDD... | 4.2.3.187 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:B5HDJ6}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6}; | terpenoid biosynthetic process [GO:0016114] | null | metal ion binding [GO:0046872]; terpene synthase activity [GO:0010333] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2Z,6E)-hedycaryol + diphosphate; Xref=Rhea:RHEA:54060, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:138044, ChEBI:CHEBI:175763; EC=4.2.3.187; Evidence={ECO:0000269|PubMed:24399794}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization. {ECO:0000269|PubMed:24399794}. | Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae) |
E4NKF8 | PUB1_MEDTR | MNDPRSKMMISPGLLPTESLLDSLILISNEVSSMQKFPLVQIKNVSSMIRRIKLLSSLFEEIQESDSPLPPSSILCFIEIFSVITRVKVLIQECTDGSSLWSLIQLDFISNQFFVLVKEMGRALDILPLNLLNVAQDIKEQVDLLHKQSKRVELELFIDPREVQRRENLFEVMSKNCLQNKKTNNNKGFIDFVKVEEIMCSIGLRTLSDYVEEISKLEVEAQNQAGTGGLIVVSNINNLMSLVSYTKSMVFRNDGESEECKPISMFLYNKSKIHDNDSSSSSSFSQSMMTVNIPDEFRCPISLDLMRDPVIVSSGHTYDR... | 2.3.2.27 | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877]; protein ubiquitination [GO:0016567]; response to molecule of bacterial origin [GO:0002237]; response to symbiotic bacterium [GO:0009609]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ubiquitin protein ligase activity [GO:0061630] | PF00514;PF04564; | 1.25.10.10;3.30.40.10; | null | PTM: Phosphorylated by LYK3 in vitro (PubMed:20971894). Phosphorylated by NORK/DMI2 (PubMed:26839127). {ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:26839127}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20971894}. | 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:0000269|PubMed:20971894}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:20971894}. | null | null | FUNCTION: Exhibits U-box-dependent E3 ubiquitin ligase activity in vitro (PubMed:20971894, PubMed:26839127). Negatively modulates successive stages of infection and development of rhizobial (e.g. Sinorhizobium meliloti) and arbuscular mycorrhizal fungi (AM, e.g. Rhizophagus irregularis) symbioses, in an ubiquitin ligas... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
E4Q361 | GH1A_CALOW | MSFPKGFLWGAATASYQIEGAWNEDGKGESIWDRFTHQKGNILYGHNGDVACDHYHRHEEDVSLMKELGIKAYRFSTAWARIFPDGFGNINQKGLEFYDKLINELVENGIEPVVTLYHWDLPQKLQDIGGWANPEIVNYYFEYAMLIINRYKDKVKKWITFNEPYCIAFLGHWHGIHAPGIKNFKVAMDVVHNIMLSHFKVVKAVKENNIDVEIGITLNLTPVYLQTERLGYKVSEIEREMVNLSSQLDNELFLDPVLKGSYPQKLLDYLVQKDLLDSQKVNNMQQEVKENFIFPDFLGINYYTRSVRLYDENSGWIFPI... | 3.2.1.21; 3.2.1.23; 3.2.1.37; 3.2.1.74; 3.2.1.91 | null | cellulose catabolic process [GO:0030245]; glucan catabolic process [GO:0009251]; lactose catabolic process [GO:0005990]; protein homotrimerization [GO:0070207]; xylan catabolic process [GO:0045493] | cytosol [GO:0005829] | beta-galactosidase activity [GO:0004565]; beta-glucosidase activity [GO:0008422]; cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; glucan 1,4-beta-glucosidase activity [GO:0031217]; scopolin beta-glucosidase activity [GO:0102483]; xylan 1,4-beta-xylosidase activity [GO:0009044] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:27141233}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.61 mM for p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; KM=1.52 mM for p-nitrophenyl beta-D-glucopyranoside (pNPGlu) (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; KM=0.87 mM f... | PATHWAY: Glycan metabolism; beta-D-glucan degradation. {ECO:0000269|PubMed:27141233}.; PATHWAY: Glycan metabolism; cellulose degradation. {ECO:0000269|PubMed:27141233}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 using p-nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Retains 80% of its maximal activity at pH 5.0 and 6.0, and 20% at pH 4.5 and 7.0. {ECO:0000269|PubMed:27141233}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75-85 degrees Celsius using p-nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Retains 100% of its maximal activity after incubation at 75 or 65 degrees Celsius at pH 5.5 for 12 hours. Retains more than 80% of its maximal activity... | FUNCTION: Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p-nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu),... | Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL) |
E4QP00 | HMFO_METS6 | MTDTIFDYVIVGGGTAGSVLANRLSARPENRVLLIEAGIDTPENNIPPEIHDGLRPWLPRLSGDKFFWPNLTIHRAAEHPGITREPQFYEQGRLLGGGSSVNMVVSNRGLPRDYDEWQALGADGWDWQGVLPYFIKTERDADYGDDPLHGNAGPIPIGRVDSRHWSDFTVAATQALEAAGLPNIHDQNARFDDGYFPPAFTLKGEERFSAARGYLDASVRVRPNLSLWTESRVLKLLTTGNAITGVSVLRGRETLQVQAREVILTAGALQSPAILLRTGIGPAADLHALGIPVLADRPGVGRNLWEHSSIGVVAPLTEQA... | 1.1.3.47; 1.8.3.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24271187, ECO:0000305|Ref.5}; | glycine betaine biosynthetic process from choline [GO:0019285] | null | choline dehydrogenase activity [GO:0008812]; FAD binding [GO:0071949]; oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor [GO:0016670]; oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor [GO:0016899] | PF05199;PF00732; | 3.30.410.40;3.50.50.60; | GMC oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=5-hydroxymethylfurfural + 2 H2O + 3 O2 = 2,5-dicarboxyfuran + 2 H(+) + 3 H2O2; Xref=Rhea:RHEA:32683, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:83389, ChEBI:CHEBI:412516; EC=1.1.3.47; Evidence={ECO:0000269|PubMed:24271187, ECO:0000269|PubMed:2480... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for 5-(hydroxymethyl)furfural {ECO:0000269|PubMed:24271187}; KM=1.5 mM for 1,4-benzenedimethanol {ECO:0000269|PubMed:24271187}; KM=1.4 mM for 1,3-benzenedimethanol {ECO:0000269|PubMed:24271187}; KM=1.3 mM for benzyl alcohol {ECO:0000269|PubMed:24271187}; KM=... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:24271187}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:24271187}; | FUNCTION: Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups... | Methylovorus sp. (strain MP688) |
E4TN31 | TM175_MARTH | MRKVFETVVGLNPNFSFRGKQQTRIETFSDAVFALAITLLVLSSTIPETFEDLWASMRDVIPFAICVALIIVIWYQHYIFFLKYGLQDKVTILLNTILLFVLLVYVYPLKFLARFLSEIYGGIFGIIETDLSRFGEYSHQNLKLLMVNYGLGAFAIFLVFSLMYWRAYKMKSLLDLNSYEIFDTKSSIIANLLMCSVPLLSLIITLIDPWGNFRTTILSGFLYFLYVPIMIVFGRITSKKSRRLLQD | null | null | potassium ion transmembrane transport [GO:0071805]; protein homotetramerization [GO:0051289] | plasma membrane [GO:0005886] | potassium ion leak channel activity [GO:0022841]; proton channel activity [GO:0015252] | PF06736; | null | TMEM175 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32267231}; Multi-pass membrane protein {ECO:0000269|PubMed:32267231}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:32267231}; | null | null | null | null | FUNCTION: Potassium channel; forms a potassium-permeable leak-like channel with weak selectivity for potassium (PubMed:32267231). The channel is permeable for K(+), Rb(+) and Cs(+) (PubMed:32267231). {ECO:0000269|PubMed:32267231}. | Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus) |
E5D3Z8 | A31_LOXLA | MYVHLALILGCWTVVLQGAETDVGERADNRRPIWNLAHMVNAVKQIPTFLDLGANALEADVTFKGSVPTYTYHGTPCDFGRDCIRWEYFNVFLKTLREYTTPGNAKYRDGFILFVLDLKTGSLSNDQVRPAGENVAKELLQNYWNNGNNGGRAYVVLSLPDIGHYEFVRGFKEVLKKEGHEDLLEKVGYDFSGPYLPSLPTLDATHEAYKKAGVDGHIWLSDGLTNFSPLGDMARLKEAIKSRDSANGFINKIYYWSVDKYSTTRTALDVGVDGIMTNYPNVLIDVLNEDGYKDNYRLATYDDNPWETYKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | null | 3.20.20.190; | Arthropod phospholipase D family, Class I subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21692149}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:24472346}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (PubMed:24472346). It may also act on ce... | Loxosceles laeta (South American recluse spider) (Scytodes laeta) |
E5D8F2 | POLG_HRV15 | MGAQVSRQNNGTHENGVTASNGSVIKYFNINYYKDSASSGLSRQDFSQDPSKFTQPLVDTLTNPALMSPSVEACGYSDRLKQITIGNSTITTQDSLHTVLAYGEWPTYLSDIDATSVDKPTHPETSADRFYTLDSVEWQVGSHGWWWKLPDALKDMGVFGQNMYYHSMGRSGFIIHTQCNATKFHSGALIVAVIPEHQLAYVGGVKVNVGYDHTHPGQSGHQIRGPSQSNDRSGGKPDEDPLFNCNGTLLGNITIFPHQIINLRTNNSSTIVVPYINCVPMDNMLKHNNLSLVIIPLVPLRPGSSGINSVPITVTIAPYK... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; 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 [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;3.40.50.300;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000269|PubMed:27511920}. Host cytoplasm {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000269|PubMed:27511920}. Note=The internal surface of the capsid is lined by the 60 copies of VP4. {ECO:0000303|PubMed:29633974}.; SU... | CATALYTIC ACTIVITY: [Protein 2C]: 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:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:27511920, PubMed:32152109). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:27511920, PubMed:321521... | Human rhinovirus C (strain C15) (HRV-C15) |
E5KGE0 | BRIZ1_ARATH | MFILRVHSVDSERPISVEEEESGFTYASKRAQPPLKLIQPSLKLTDRKGLIHLYRKSSHSSLPNPSSRSTTLFIVAVPNYLSSLDFIRFCDSRISQVSDILFIRNDGMEDRYSVLITFSDQSEADGFYNNLNGKKFAPSEAEVCHILYVMSVEHTEFDEVAAEAPTGFTELPTCPICLERLDPDTSGIVSTLCDHSFQCSCTSKWTYLSCQVCRLCQQQDEILNCSICGKTENVWACLVCGFVGCGRYKEGHSIRHWKETHHCYSLDLRTQQIWDYVGDSYVHRLNHSKIDGKSVEMSTSCLSHQGDCGLCECSEDTGIS... | 2.3.2.27 | null | protein ubiquitination [GO:0016567]; Ras protein signal transduction [GO:0007265]; regulation of seed germination [GO:0010029] | cytoplasm [GO:0005737]; ubiquitin ligase complex [GO:0000151] | hydrolase activity [GO:0016787]; protein heterodimerization activity [GO:0046982]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF07576;PF02148; | 3.30.40.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20810661}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:20810661}. | null | null | FUNCTION: RING-type ubiquitin E3 ligase required for seed germination and post-germination growth. {ECO:0000269|PubMed:20810661}. | Arabidopsis thaliana (Mouse-ear cress) |
E5KIB6 | CYPA_STRSQ | MRSEMTLTSTNSAEALAAQDFANTVLSAAAPGFHADCETPAMATPATPTVAQFVIQGSTICLVC | null | null | defense response to Gram-positive bacterium [GO:0050830] | extraorganismal space [GO:0043245] | null | null | null | Linaridin family | PTM: Maturation involves the enzymatic conversion of Cys-61 into 2,3-didehydroalanine followed by formation of a thioether bond with Cys-64. The C-terminal meso-lanthionine then undergoes decarboxylation. {ECO:0000269|Ref.3}.; PTM: Dimethylated at the N-terminus. Dimethylation is required for antibiotic activity. {ECO:... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7802859}. | null | null | null | null | null | FUNCTION: Antibiotic peptide structurally related to lantibiotics. Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against mouse P388 leukemia cells (IC(50)=1.3 ug/ml). {ECO:0000269|PubMed:20805503, ECO:0000269|PubMed:7802859}. | Streptomyces sp |
E5RQA1 | GHD7_ORYSJ | MSMGPAAGEGCGLCGADGGGCCSRHRHDDDGFPFVFPPSACQGIGAPAPPVHEFQFFGNDGGGDDGESVAWLFDDYPPPSPVAAAAGMHHRQPPYDGVVAPPSLFRRNTGAGGLTFDVSLGERPDLDAGLGLGGGGGRHAEAAASATIMSYCGSTFTDAASSMPKEMVAAMADDGESLNPNTVVGAMVEREAKLMRYKEKRKKRCYEKQIRYASRKAYAEMRPRVRGRFAKEPDQEAVAPPSTYVDPSRLELGQWFR | null | null | flower development [GO:0009908]; negative regulation of long-day photoperiodism, flowering [GO:0048579]; regulation of flower development [GO:0009909]; regulation of photoperiodism, flowering [GO:2000028] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF06203; | null | null | PTM: Phosphorylated at Ser-68 by HD16/EL1, a casein kinase 1. {ECO:0000305|PubMed:23789941}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18454147}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in the regulation of flowering time under long day (LD) conditions. Plays a major role as repressor of flowering. Controls flowering time by negatively regulating the expression of EHD1 and HD3A. {ECO:0000269|PubMed:18454147, ECO:0000269|PubMed:23789941}. | Oryza sativa subsp. japonica (Rice) |
E5XP76 | CAR_SEGRC | MTESQSYETRQARPAGQSLAERVARLVAIDPQAAAAVPDKAVAERATQQGLRLAQRIEAFLSGYGDRPALAQRAFEITKDPITGRAVATLLPKFETVSYRELLERSHAIASELANHAEAPVKAGEFIATIGFTSTDYTSLDIAGVLLGLTSVPLQTGATTDTLKAIAEETAPAVFGASVEHLDNAVTTALATPSVRRLLVFDYRQGVDEDREAVEAARSRLAEAGSAVLVDTLDEVIARGRALPRVALPPATDAGDDSLSLLIYTSGSTGTPKGAMYPERNVAQFWGGIWHNAFDDGDSAPDVPDIMVNFMPLSHVAGRI... | 1.2.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588}; | organonitrogen compound biosynthetic process [GO:1901566] | membrane [GO:0016020] | ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor [GO:0016620]; phosphopantetheine binding [GO:0031177] | PF00501;PF07993;PF00550; | 1.10.1200.10;3.40.50.12780;3.40.50.720; | ATP-dependent AMP-binding enzyme family, Carboxylic acid reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde + diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_... | null | null | null | null | FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (PubMed:28719588). Catalyzes the reduction of a very wide range of carboxylic acids, including benzoic acids, heterocyclic, phenylacetic, phenylpropanoic and fatty acid substrates (PubMed:28719588). {ECO:000026... | Segniliparus rugosus (strain ATCC BAA-974 / DSM 45345 / CCUG 50838 / CIP 108380 / JCM 13579 / CDC 945) |
E6LHV7 | CAS10_ENTI1 | MNKKLELMYGSLLHDIGKIVYRSNSVDFAKGTHSKIGSQFLNKFKPFQLSGIVDSVSYHHYKELASSSLLDDSVAYITYIADNIASGTDRRASEGDYEGEGNRQRFDKRAPLASIFNVVNSETKGLANYTYSFEKEQVYRYPTDAKKEYTSSQYAALVNKMTDDLSNKLKVGPDSFSSLLQWTESLWSYIPSSTDTNQVMDVSLYDHSKITCAIASCIYDYLTEMNCVNYRKELFSPYEKTKQFYQEDVFLLVSLDMSGIQDFIYNISGSKALKSLRSRSFYLETMLESLVDDLLSDLELSRANLLYTGGGHAYLLLPNT... | 2.7.7.-; 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28722012}; Note=Synthesis of cA6 requires Mg(2+). {ECO:0000269|PubMed:28722012}; | defense response to virus [GO:0051607] | null | ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; RNA binding [GO:0003723]; transferase activity [GO:0016740] | PF20824;PF18211; | 3.30.70.270;1.10.3210.10; | CRISPR-associated Cas10/Csm1 family | null | null | CATALYTIC ACTIVITY: Reaction=6 ATP = cyclic hexaadenylate + 6 diphosphate; Xref=Rhea:RHEA:58276, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:142456; Evidence={ECO:0000269|PubMed:28722012}; | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5) |
E6MVD9 | NALP_NEIMH | MRTTPTFPTKTFKPTAMALAVATTLSACLGGGGGGTSAPDFNAGGTGIGSNSRATTAKSAAVSYAGIKNEMCKDRSMLCAGRDDVAVTDRDAKINRPPPPNLHTGDFPNPNDAYKNLINLKPAIEAGYTGRGVEVGIVDTGESVGSISFPELYGRKEHGYNENYKNYTAYMRKEAPEDGGGKDIEASFDDEAVIETEAKPTDIRHVKEIGHIDLVSHIIGGRSVDGRPAGGIAPDATLHIMNTNDGTKNEMMVAAIRNAWVKLGERGVRIVNNSFGTTSRAGTADLFQIANSEEQYRQALLDYSGGDKTDEGIRLMQQSD... | 3.4.21.- | null | peptide hormone processing [GO:0016486] | cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular space [GO:0005615]; neuron projection [GO:0043005] | serine-type endopeptidase activity [GO:0004252] | PF03797;PF12951;PF00082; | 2.40.128.130;3.40.50.200; | Peptidase S8 family | PTM: A fusion protein of the first 44 residues with beta-lactamase is lipidated in E.coli, strongly suggesting this is a lipoprotein in situ (PubMed:14617158). The lipidated form is briefly retained on the cell surface which allows it to process its endogenous substrates on the cell surface before the passenger domain ... | SUBCELLULAR LOCATION: [Neisserial autotransporter lipoprotein NalP]: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:15014442, ECO:0000305|PubMed:23258267}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:14617158, ECO:0000305|PubMed:23258267}. Cell surface {ECO:0000... | null | null | null | null | null | FUNCTION: Major human immunogenic protein. Autotransporter with a secreted protease domain involved in processing other autotransporter proteins including App and IgA. Probably autoprocesses to release the about 70 kDa passenger domain (PubMed:14617158). Processes the lactoferrin receptor lipoprotein subunit (LbpB) ext... | Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) |
E6Y2X0 | PILR2_LINUS | MAAGFLFHMGSLPAIATVGHKSKVLVIGGTGYLGKRLVTASLAAGHETYVLQRPEIGVDIEKIQLLLSFKKAGASLVSGSFNDYRSLVDAVKLVDVVICAVSGVHIRSHQILLQLKLVDAIKEAGNVKRFLPSEFGTDPATMENAMEPGRVTFDDKMVVRKAIEEAGIPFTYISANCFAGYFLGGLCQPGFILPSREQVTLLGDGNQKAVYVDEDDIARYTIKMIDDPRTLNKTVYIKPPKNVLSQREVVGIWEKYIGKELKKTTLSVEEFLAMMKEQDYAEQVGLTHYYHVCYEGCLTNFEIGDEAGEATKLYPEVGYT... | 1.23.1.1; 1.23.1.2 | null | (+)-lariciresinol biosynthetic process [GO:1902132]; (+)-lariciresinol catabolic process [GO:1902131]; (+)-pinoresinol catabolic process [GO:1902125]; (-)-secoisolariciresinol biosynthetic process [GO:1902138]; lignan biosynthetic process [GO:0009807] | null | lariciresinol reductase activity [GO:0010284]; pinoresinol reductase activity [GO:0010283] | PF05368; | 3.40.50.720;3.90.25.10; | NmrA-type oxidoreductase family, Isoflavone reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH; Xref=Rhea:RHEA:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1; Evidence={ECO:0000269|PubMed:20514607}; CATALYTIC ACTIVITY: Reaction=(-)-secoisolariciresinol + NADP(+... | null | null | null | null | FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. {ECO:0000269|PubMed:20514607}. | Linum usitatissimum (Flax) (Linum humile) |
E6Y5X0 | UREA2_CANEN | MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKV... | 3.5.1.5 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000255|PROSITE-ProRule:PRU00700}; Note=Binds 2 nickel ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00700}; | urea catabolic process [GO:0043419] | urease complex [GO:0035550] | lipid binding [GO:0008289]; nickel cation binding [GO:0016151]; urease activity [GO:0009039] | PF01979;PF00449;PF00699;PF00547;PF18473; | 3.20.20.140;2.10.150.10;3.30.280.10;2.30.40.10; | Metallo-dependent hydrolases superfamily, Urease alpha subunit family | PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000250|UniProtKB:P07374}. | null | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000269|PubMed:21893219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20558; Evidence={ECO:0000269|Pu... | null | PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000305}. | null | null | FUNCTION: Urea hydrolase involved in recycling metabolically derived urea generated internally or externally (By similarity). Is able to impair growth of the phytopathogenic fungus Penicillium herguei, and shows entomotoxic activity by inhibiting diuresis in Malpighian tubules isolated from Rhodnius prolixus (PubMed:21... | Canavalia ensiformis (Jack bean) (Dolichos ensiformis) |
E6Z0R3 | VBHT_BARSR | MRKYEGSNDPYTDPETGVMYNLLGIKDQARLERVESAFAYIRSFELGRTSISGKFDLDHMKKIHKKLFGDVYEWAGKTRLVDIVKDNSKFAHYTQIESYAPQITQQLAREQHLRGLDANEFSQRAGYYMGELNALHPFREGNGRTLREFIWQLAREAGYHIDWDRVERQEMTRASIESYYGNSDLMSALIRRNLTEFTVNRRVDVSQGINERVLSHIDIDKEWPQKGFNIAIQTTQQAPYLSSYTDTSNLEEKAQNALRNEQSYVDTFKELNDHLKTIYKDPQAAALKIEQTILAGKGDKLPDILAKAPNKVGELRGSDR... | 2.7.7.108 | null | protein adenylylation [GO:0018117]; regulation of cell division [GO:0051302] | null | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803] | PF17841;PF02661; | 1.10.3290.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000269|PubMed:22266942, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Toxic component of type II toxin-antitoxin (TA) system VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. | Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1) |
E7CLP2 | SX12F_RHOJU | MKILIFIIASFMLIGVECKEGYPMGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTNLPEDAQVWDSSTNKCGG | null | null | defense response [GO:0006952]; modulation of voltage-gated potassium channel activity in another organism [GO:0044360]; modulation of voltage-gated sodium channel activity in another organism [GO:0044488] | extracellular region [GO:0005576] | potassium channel regulator activity [GO:0015459]; sodium channel inhibitor activity [GO:0019871]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:21605585}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21605585}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to insects (A.domestica). It is not toxic to mice and ... | Rhopalurus junceus (Caribbean blue scorpion) |
E7EAU8 | GCY9_CAEEL | MRLYLFFISSLLLAESRRSISKISHDEINQHVKTTLSSEGIVRIGHLHPTNPIIAHEPDVLKMCADDLKMRNILPQNYTLTVFTMESCNKYSGVEHAAFLHYLKNASVYFGPGCNNEMLVIGRLAPRWNVPIIAHMSGDDALSDRVQFPTLGSVALTSASEMAKATVTYLNLNNWDQIGIVRPSVGYERLSVYSLQHQIKKRDINLNVILDIEPFSSPEEIISTGKLTTLKSMARIIVVELGMDIHSVTNFMLAIHRSEIKNEEFVFVIPWLAHQNDHYPWEAANVDKQEVKLAFENTIIITAHGYDKKFFDDFQMKFSA... | 4.6.1.2 | null | calcium-mediated signaling [GO:0019722]; cellular response to acidic pH [GO:0071468]; cGMP biosynthetic process [GO:0006182]; detection of carbon dioxide [GO:0003031]; detection of chemical stimulus involved in sensory perception [GO:0050907]; positive regulation of exocytosis [GO:0045921]; positive regulation of neuro... | neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07701;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:21173231}. Note=Localizes in cilium of sensory neurons. {ECO:0000269|PubMed:21173231}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187}; | null | null | null | null | FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Involved in the sensing of CO2 levels and acidity by the BAG neurons. May act as a direct receptor for CO2 and H+ (PubMed:21173231, PubMed:24240097). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:21173231, ECO:00002... | Caenorhabditis elegans |
E7EM37 | DOPR2_CAEEL | MEAGETWNVSLEWPPPSLDLSTITQTPSTIVGSGIPLNYAGLSLIVIPLITLLGNLLVIISVLRYRALQSAINFLILGLAVADLLVAIIVMPYAVYVYVTNGDWYLGNLMCDIYMASDVCCSTASILLLAVISFDRYRAVSLPIQYSRQSQNVKRVWTLIAVIWLVSLTLASPMVFGVNVRPPDANPYECRFYNAEFSILSSMISFVIPCFLVLFVYIRIIIALKKREKAAKMRREKNTIAHGLTMRPDTGEEQVDEEAAGRIVAGPVVNVMMAALPSMTRRMRQFERHRRAIELAGDEEWEEDELDVMDECCGGDDAGD... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; cellular response to amphetamine [GO:0071419]; cellular response to nicotine [GO:0071316]; chemical synaptic transmission [GO:0007268]; dopamine receptor signal... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; synapse [GO:0045202] | dopamine neurotransmitter receptor activity, coupled via Gi/Go [GO:0001591]; G protein-coupled serotonin receptor activity [GO:0004993]; neurotransmitter receptor activity [GO:0030594] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12887685}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor which binds to the neurotransmitter dopamine with high affinity leading to the activation of an associated G-protein and downstream signaling pathways (PubMed:12887685). Couples to G-proteins to inhibit adenylate cyclase (AC) activity and cAMP production (PubMed:12887685). Inhibits ... | Caenorhabditis elegans |
E7EZF3 | UHRF1_DANRE | MWIQVRTMDGKETHRVDSLSKLTKVDELRVKIAELFNVEPERQRLFYRGKQMEDGHTIFDYNVGLNDIVQLLVRQAVAATVLPKDKEAELSDSDSGCGSAQSESDKGSTHGESDVQSAGASGQTDTADLIDPGFGFYKINEFVDARDLNMGAWFEAQIVKVTKTPAEDGGAEDIVYHVKYEDYPENGVVQLRGKDVRPRARTVYQWHQLEPGMIVMVNYNPDDPKERGYWYDAEIQRKRETRTQREVFGKILLGDAGDSLNDCRIMFVTEIYKIEEPGSAEGPGASSDSPLKKGSNGPECKVCKDDPKKNCRVCNCHVCG... | 2.3.2.27 | null | animal organ regeneration [GO:0031100]; cell cycle [GO:0007049]; heterochromatin formation [GO:0031507]; inflammatory response [GO:0006954]; intestinal epithelial structure maintenance [GO:0060729]; lens development in camera-type eye [GO:0002088]; liver development [GO:0001889]; negative regulation of gene expression ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; replication fork [GO:0005657] | hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00628;PF02182;PF12148;PF00240; | 2.30.30.1150;2.30.30.140;2.30.280.10;3.30.40.10; | null | PTM: Phosphorylation at Ser-649 is required for gastrulation. {ECO:0000269|PubMed:22072796}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Cytoplasm {ECO:0000269|PubMed:22072796}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions (By similarity). {ECO:0000250}. | 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; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits dnmt1 methyltransferase to ensure faithful propagation of the DNA methylation patterns t... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7EZG2 | MY9AA_DANRE | MSVHDVGGRRRFEDSELTLRIYPGIIAEGTIYCPVAARKITSAAEVIEQVIDRLQLDRTKCYVLAEVKEFGGEEWILNPTDYPVQRMMLWPRMALENRFSSEDYRFLLREKNLDGSIHYGNLQMWLQVTEERRRMVERGFLPQPLPKDFDDLCNLPDLNEKTLLDNLRSRFKQEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQSRQNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEKYL... | null | null | axon development [GO:0061564]; axon extension [GO:0048675]; establishment of epithelial cell apical/basal polarity [GO:0045198]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; neuromuscular junction development, skeletal muscle fiber [GO:0098529]; swimming behavior [GO:0036269] | actin filament [GO:0005884]; axonal growth cone [GO:0044295]; cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin complex [GO:0016459]; synapse [GO:0045202] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; microfilament motor activity [GO:0000146] | PF00130;PF00612;PF00063;PF00788;PF00620; | 1.10.10.820;1.20.5.190;1.20.58.530;3.30.60.20;6.20.240.20;3.40.850.10;1.20.120.720;1.10.555.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}. Synapse {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell bodies, dendrites and axons with occasional hin... | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons (By similarity). Required for the regulation of neurite branching and motor neuron axon guidance (PubMed:27259756). {ECO:0000250|U... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F1H9 | YTHD2_DANRE | MSASSLLEQRPKGQANKVQNGAVTQKDTLNDDEFEPYLNAQPRQSNAYTAMSDSYMPSYYSPSIGFTYSLNEAAWSTGGDPPMPYLASYGQLSNGEHHFLPDAMFGQSGALGNNPFLGQHGFNFFPSGIDFPAWGNSSSQGQSTQSSGYSSSYAYAPSTLGGAMIDGQSPFAANEPLNKAVGMNSLDQGMAGLKIGAGDMAPKVVGSGLPGGPLSQVSTAPTMPPASMAPAKTASWADIASKPAKPQPKLKTKGGLGGTNLPPPPIKHNMDIGTWDNKGNMPKPAAPQQTSLPTNGQPPNQSSPQPGATAGGVPQLPLSN... | null | null | embryonic morphogenesis [GO:0048598]; endothelial to hematopoietic transition [GO:0098508]; gamete generation [GO:0007276]; hematopoietic stem cell proliferation [GO:0071425]; mRNA catabolic process [GO:0006402]; mRNA destabilization [GO:0061157]; negative regulation of Notch signaling pathway [GO:0045746]; negative re... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932] | C5-methylcytidine-containing RNA reader activity [GO:0062153]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247] | PF04146; | 3.10.590.10; | YTHDF family, YTHDF2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y5A9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9Y5A9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9Y5A9}. Nucleus {ECO:0000250|UniProtKB:Q9Y5A9}. Note=Localizes to the cytosol and relocates to the nucleus following heat shock stress. Can partiti... | null | null | null | null | null | FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:28192787). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (By similarity). Acts as a regulator of mRNA stabilit... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F3F0 | MY9AB_DANRE | IMSCHDVGGRRRFEDSEFTLRVYPGSLSESTIYCPVSARKVTTAAEVIERVIERLQLDRTRLYVLAEVKEFGGEEWILNPSDCPAQRMMLWPRMALENRLLGEDYRFLLREKNLDGSIHYGSLQMWLRVTEERRRMVERGLLPQPPAAQFVADLCSLPDLNEHTMLENLRGRFRQENIYTYVGSILIAVNPFKFLPIYNPKYVKMYDKHRLGQLEPHIFAVADAAYHAMLQRHRNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEK... | null | null | animal organ development [GO:0048513]; cell development [GO:0048468]; establishment of epithelial cell apical/basal polarity [GO:0045198]; intracellular signal transduction [GO:0035556]; system development [GO:0048731] | actin filament [GO:0005884]; axonal growth cone [GO:0044295]; cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin complex [GO:0016459]; synapse [GO:0045202] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; microfilament motor activity [GO:0000146] | PF00612;PF00063;PF00788;PF00620; | 1.10.10.820;1.20.5.190;1.20.5.4820;1.20.58.530;3.30.60.20;3.40.850.10;1.20.120.720;1.10.555.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}. Synapse {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell bodies, dendrites and axons with occasional hin... | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons (By similarity). Required for the regulation of neurite branching and motor neuron axon guidance (PubMed:27259756). {ECO:0000250|U... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F3I6 | CLP1_DANRE | MTAEAAEKSVEEGLSSSGSAGSSGTRFDLDKETELRFEVEAGERVQLELLSGLAEIFGSELNRNKKYTFGPGSKIAVFTWQGCGVALSGKTEVAYVSKDTPMLLYLNTHAALEQMRRQAEKDNERGPRVMVVGPTDVGKSTVCRMLLNYAVRLGRRPTLVELDVGQSSVSVPGTMSALCIERPADVEEGFSVQAPLVFHFGSTTPGTNIKLYNKLTSSLADAFSQRCEVNRRASVGGCIINTCGWVKGSGYQALVHCASAFQVDVVLVLDQERLYNELKRDLPHFVRVVLLPKSGGVVERSKDCRRETRDEKIREYFYGF... | 2.7.1.78 | null | brain development [GO:0007420]; cerebellar cortex development [GO:0021695]; mRNA polyadenylation [GO:0006378]; phosphorylation [GO:0016310]; RISC complex assembly [GO:0070922]; spinal cord motor neuron differentiation [GO:0021522]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388] | mRNA cleavage factor complex [GO:0005849]; nucleus [GO:0005634]; tRNA-intron endonuclease complex [GO:0000214] | ATP binding [GO:0005524]; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity [GO:0046404]; ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity [GO:0051736]; polynucleotide 5'-hydroxyl-kinase activity [GO:0051731] | PF06807;PF16573;PF16575; | 2.60.120.1030;3.40.50.300;2.40.30.330; | Clp1 family, Clp1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + ADP + H(+); Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412, ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;... | null | null | null | null | FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated mor... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F4N7 | STING_DANRE | MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRMSEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSFYIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKITHNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSREL... | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of defense response... | autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO... | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta. Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by tbk1, leading to recruitment of the transcription factor irf3 to induce type-I interferons and ot... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23091644}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:23091644). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivere... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F4V8 | PEX2_DANRE | MAGAGGDKPFAKAGPSPLSRVLRISQLDAFELDGALEQLVWSQFTQCFQHFKPGILTPVEPELKALLQLLLWRFTIYSNSATVGQSLLNIRYKNALIPGQKYRPMSRPQKFWFALLTVGEKWFRERSHSLFLNHPAESNARKARKVLSILLGLTKAASLVNFLLFLQRGTFPTLTERLLGVQPVFSRPQGPRDINFQYLNRELLWHGFAEFLIFLLPLINVWKLKAGVSALFSPLSDLTGTQSSEETHLTECAICGEWPTMPHSIGCKHVFCYYCVKSNVIADIYFTCPKCGAETGQIEPVRLQVGTELLQS | 2.3.2.27; 2.3.2.36 | null | fatty acid beta-oxidation [GO:0006635]; peroxisome organization [GO:0007031]; pexophagy [GO:0000425]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein ubiquitination [GO:0016567]; response to amino acid starvation [GO:1990928]; very long-chain fatty acid metabolic process [GO:0000038] | Cdc73/Paf1 complex [GO:0016593]; peroxisomal membrane [GO:0005778] | ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF04757;PF00097; | 3.30.40.10; | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P28328}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; Evidence={ECO:0000250|UniProtKB:P32800}; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiq... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P28328}. | null | null | FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subun... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F568 | COBL_DANRE | MNLGDATTRPPVGRRMKAQAPPPPRPPQPAPRRIFRNAVPDGGGSSGGDCKENMLRSYVDLHISLPTGYQTTINVDGRKALMDLLVDLCSQYHLNPAYHTLELLSPDAQPVSFKPNALLGALDVSCALIKERVLEDRVIRKPPPKVPEKTVRLVVNYHRSQKAVVRVNPLAPLQTLVPVICQKCEFDPAHVLLFKDNINHQQLDLDKSLSDLGIRELYVLDQTLVLQPKMASTPALNYSAESLRSNSLSGSEKKGLLGFLKFNRRKSKGMSVVASGPCVEARPSTLGQSQSVMNISKMSPKVELKKRRAPAPPPAPTQTL... | null | null | auditory receptor cell stereocilium organization [GO:0060088]; cilium assembly [GO:0060271]; heart jogging [GO:0003146]; heart looping [GO:0001947] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; ruffle [GO:0001726] | actin monomer binding [GO:0003785] | PF09469;PF02205; | null | null | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle {ECO:0000250}. Cytoplasm. Cytoplasm, cytosol. Note=Detected throughout the neuron cell body, as well as in axons and dendrites (By similarity). Colocalizes with the actin cytoskeleton. Re... | null | null | null | null | null | FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin de... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F590 | VPS41_DANRE | MAEVEEQGRKLSEESTDESEEEDTEEEPKLKYERLTNGVTEILQKDAASCMTVHDKFLALGTHFGKVFLLDIQGNVTQKFEISSVKINQISLDESGDHVGICSEDGKVQVFGLYTREGFHENFDCPIKVVALHPQFSKSNNKQFVTGGNKLLLYERNWLNRWKTSVLHEGEGNITSVKWRGNLIAWANNVGVKIYDIGSKQRITNVLRDNTSLRPDMYPCSLCWKDNTTLIIGWGCSVKICAVKERDPTEMRDLPSRYVEIVSAFETEFFISGLAPLADQLVTLYYVKENSDHMEEEFRTRPRLDIIQPLPEGCEEISSD... | null | null | cellular response to starvation [GO:0009267]; endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; macroautophagy [GO:0016236]; protein targeting to vacuole [GO:0006623] | clathrin-coated vesicle [GO:0030136]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; Golgi apparatus [GO:0005794]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765] | metal ion binding [GO:0046872] | PF00637; | 1.25.40.10;2.130.10.10; | VPS41 family | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Late endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Early endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membra... | null | null | null | null | null | FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes. {ECO:0000269|PubMed:33764426}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F594 | G137B_DANRE | MQKDSLPTLSPAVPPYVMLGLTVAYTIFYCLLFVFVYVQLWLVLRYRHKRFSYQTVFLFLCLLWAALRALLFSFYFKNCVTANTLGPFCFWLLYCFPVCLQFFTLSLMNLYFAQVIFKAKSKYSPELQKYRLPLYLLFLSISLLFLLVNLTCALLVKINRANTETVVLVRVTVNDSLFVLCAVSLSLCLYRIAKMSLANIYLEAKGTSVCQVTLIGVTVVLLYSSRACYNLVVLALTKIKSINSFDYDWYNVSDQADLKSTLGDAGYVVFGVILFVWELLPTSLVVYFFRVRKPTLDRSASVIPGHMFSSRAYFFDNPRR... | null | null | autophagy [GO:0006914]; bone remodeling [GO:0046849]; negative regulation of bone resorption [GO:0045779]; negative regulation of osteoclast differentiation [GO:0045671]; positive regulation of protein localization to lysosome [GO:0150032]; positive regulation of TORC1 signaling [GO:1904263]; regulation of autophagy [G... | lysosomal membrane [GO:0005765] | null | null | null | GPR137 family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O60478}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Lysosomal integral membrane protein that regulates the localization and activity of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (By similarity). Interacts with Rag GTPases and increases the lysosomial localization and activity of Rag GTPases ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F654 | NOL9_DANRE | MTMKVHKVHSRSQQRQRNASKQHGKNKWNKKVRSLDSTLLNTSSGTAKLEQEIAKKEKPAIKRLKKLYAKPVTLLSDNNCADEDKVKPTSVTFAHVHTNGGTELDDSSRSVDSQEWSEYANSVLQNGMETSTLPDSDQAEDGLQFHAHLDHTKNRAVLVMKQSQVLCFRGKCLLTCLYGHVEVLGFTIEEGQQPYPVFSPPTHCPLTITALGNNQSSSKNKKEGQLEAKAIVRKYFTTEPSKKLMNEVDSDSCVVLLESLDTPLTRFLSSFSELTELFGLNSKELKSQAAIYSPVLSAVGVTALRGPCAQGLVMSRSYKE... | 2.7.1.78 | null | cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; definitive hemopoiesis [GO:0060216]; digestive tract development [GO:0048565]; exocrine pancreas development [GO:0031017]; liver development [GO:0001889]; pancreas morphogenesis [GO:0061113]; ph... | nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; polynucleotide 5'-hydroxyl-kinase activity [GO:0051731]; RNA binding [GO:0003723] | PF16575; | 3.40.50.300; | Clp1 family, NOL9/GRC3 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TZX8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5SY16}. Note=Colocalizes with pre-60S rRNP particles. {ECO:0000250|UniProtKB:Q5SY16}. | CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + ADP + H(+); Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412, ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;... | null | null | null | null | FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates (By similarity). Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2) (PubMed:26624285). Essential for definitive hematopoiesis and pancreas morph... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F6F7 | ABCB7_DANRE | MAPLLVPLKCGFHMQRRKLSLLLQRSSAVQAWTFHDHRAANKRKERNTYLLSDPSRESSTWANNRGQNSQQILEAVKHLHLQERQCWHGNAGGGLSADPKNVLKEVNSSKILGAMFTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMLNLSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEA... | null | null | cellular detoxification [GO:1990748]; detoxification of zinc ion [GO:0010312]; intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; pos... | mitochondrial inner membrane [GO:0005743] | ABC-type iron-sulfur cluster transporter activity [GO:0140481]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}. | CATALYTIC ACTIVITY: Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O = (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:... | null | null | null | null | FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). May play a role in cad... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F7X0 | LMOD3_DANRE | MSERTEQESYTDKIDEDEILAGLSAEELKQLQSEMDDIAPDERVPVGLRQKDASHEMTVRDCTEPESEEEIDEDEILAGLSAEELKQLQSEMEEIAPDERVPVGMRQRDQTDKPPTGSFDHRSLVEYLYWEKESKRMLEEERVPTTLLPSQKTNEEHEAKNEDKVEELELVYEEIVEEVEGGQGDAVVDEVIEEVIMEVEEEDKVCDKPVKTDLDATDPTVTSEDGLQRPSESADANVEAKTDQSGLDTETKVNEEKKEDSTEPAPSSYENWVPEKEERVISKLKIPKLALGGNTFVKKTARPSGNETNLESTLDKIRNN... | null | null | actin filament organization [GO:0007015]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; skeletal muscle fiber development [GO:0048741]; skeletal muscle thin filament assembly [GO:0030240] | cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865] | tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:E9QA62}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VAK6}. | null | null | null | null | null | FUNCTION: Essential for the organization of sarcomeric thin filaments in skeletal muscle. {ECO:0000269|PubMed:25250574}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F9L8 | MYO1D_DANRE | MAEHESLEFGKADFVLLDNVSLEEFMANLKLRFEKGRIYSYIGEVVVSVNPYRAMNIYGRDVIEQYKGRELYERPPHLFAIADAAYKAMKRRNKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIFQQEGERSFHSFYQLVKGAPDAQLRSLHIQRDPTAYNYIKVGGQLKSSINDSAEFKAVADAMKVIGFTTEEIQTVYKILATILHLGNLKFGTDGDVTLIENSKLVSVLGDLLSTKEENVEKAMLYRTV... | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; determination of liver left/right asymmetry [GO:0071910]; determination of pancreatic left/right asymmetry [GO:0035469]; endocytosis [GO:0006897]; epithelial cilium movement involved in determination of left/right asymmetry [GO:006028... | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; extracellular region [GO:0005576]; microvillus [GO:0005902]; myosin complex [GO:0016459]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF06017; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63357}. Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63357}. Early endosome {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q63357}. Note=Colocalizes with the actin cytoskeleton in the c... | null | null | null | null | null | FUNCTION: Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in the formation of Kupffer's vesicle, an organ that functions as a left-right organizer during embryogenesis (PubMed:29769531, PubMed:30139971). Plays a role in vesicular trafficking events th... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FAG6 | AMR1A_DANRE | MKLGQRNSVCILSSRERGAPGLASYRVLQQLVEEKTQRMKWQSQKVELPDSPRSTFLLAFSPDRSLMASTHVNHNIYITEVKSGKCVHSLVGHRRTPWCLTFHPIIPGLIASGCLDGEVRIWDLHGGSESWLTESNSAIASLAFHPTAQLLLIATNNEVHLWDWSRKEPFTVVKTASETERVRLVRFDPLGHYLLTAIVNPSNQPNDDDPEIPMDSVEMPHLRQRSFLQSQPARRTPILHNFLHILTSRNSVPQAGGAHSASTDGSSDSSGPYTLMCVQPLGMVCFCSRCSAARVPSPPDEDPSDSASLEAQAHTFSSAR... | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cell cycle [GO:0007049]; chordate embryonic development [GO:0043009]; locomotory behavior [GO:0007626]; mitophagy [GO:0000423]; positive regulation of free ubiquitin chain polymerization [GO:1904544]; positive regulation of mitophagy [GO:1901526]; positive re... | autophagosome [GO:0005776]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleus [... | ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF00400; | 2.130.10.10; | WD repeat AMBRA1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:A2AH22}. Mitochondrion {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:A2AH22}. Nucleus {ECO:0000250|Uni... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9C0C7}. | null | null | FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy (PubMed:23348054). The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins (By similarity). Acts as an upstream master regulator of the tr... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FAM5 | LIN41_DANRE | MCEVILWSSAQMASFPDSDLQTCPLCKELCGCSAPISSNSSTSSSSSQTSNSSSTSSTRRLHVLPCLHAFCRQCLEGQRSPGDPLKLRCPTCDQKVSLSESGVDALPSSNFLFSNLLDVVVSAEEQGKNGRSSAVVHHGGLLRPQHLSDPQCSSCDEGNPATSHCLDCQEYLCDNCVRAHQRVRLTKDHFIEGLLESLHLANRTNNSNTPVSISQSFHNSFSMLNVFQERMDFCQHHDDAVLRFFCDSCTVPICRECSLGRHAGHSFTYLQDALQDSRALTIQLLADAQQGRQAIQLSIEKAQAIAEQVELKAKVVQSEV... | 2.3.2.27 | null | fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; neural tube development [GO:0021915]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein aut... | P-body [GO:0000932] | miRNA binding [GO:0035198]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00630;PF01436;PF00643; | 4.10.830.40;3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10; | TRIM/RBCC family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}. | 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; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and participates in post-transcriptional repression of transcripts. Required to maintain proliferation and prevent premature differentiation of neu... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FB98 | UBIA1_DANRE | MQEMKPAALSGSNGLNGASGSSVRVPCSRLSRAGRMALDLQSKCAAYVLALRPWSFSASLTPVALGSALAYKLEGSVDLLLLLVCAVAVLLVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILKPQDVVMFGAVLYSAGCLCATLLYFLSSLKLEHLALIYFGGLSSSFLYTGGIGLKYVALGDVVILITFGPLAVMFAHAVQVGYLSVLPLVYAVPLALNTEAILHSNNTRDMDSDKQAGIVTLAILLGPTLSYVIYNLLLFVPYLLFCILATRYTISMALPLLTLPMAFPLERQFRCRCYAKIPQKTAKLNLLMGLF... | 2.5.1.-; 2.5.1.39 | null | cellular response to fluid shear stress [GO:0071498]; circulatory system development [GO:0072359]; endothelial cell development [GO:0001885]; menaquinone biosynthetic process [GO:0009234]; phylloquinone biosynthetic process [GO:0042372]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process via ... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; antioxidant activity [GO:0016209]; nitric-oxide synthase activity [GO:0004517]; prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:23374346}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:00002... | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; Evidence={EC... | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}. | null | null | FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10 (PubMed:23374346). MK-4 is a vitamin K2 isoform required for endothelial cell development (By similarity). Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) t... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FBF7 | FCHO1_DANRE | MIHFFHTLQGEKNAGFDVLYHNMKHGQIATKELAEFVRERAAIEETYSKSMSKLAKMASNGSPLGTFAPMWDVFRVSSDKLALCHLELMRKMNDLIRDINKYSDEQVKIHRKTKEEAIGTLESVQSLQVQNGHLQKTREGYHSKCVELERLRKEGVPQKELEKAELKCKKAAESFAGSIEKFNRAGGDFEQKMSESAQKFQDIEEAHLRQMKLLIKGYSHSIEDTHVQVGQVHEEFKQNVENIGIENLIQKFTEQKGTGKERPEGPVGFEEYLSSLASENSKKSRAKAFRIPGLGKRDKEPDSTVHVYFLQNNSPLEVDD... | null | null | BMP signaling pathway [GO:0030509]; clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; convergent extension involved in axis elongation [GO:0060028]; dorsal/ventral pattern formation [GO:0009953] | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | null | PF00611;PF10291; | 1.20.1270.60; | FCHO family | null | SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: May function in an early step of clathrin-mediated endocytosis. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. {ECO:0000269|PubMed:22484487}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FBY6 | AGRA2_DANRE | MSGPCVRIPFWVRVFLLLLLYRIAAGCPELFSSGCSCTEDRSKAHPTPGTRRKVSCGGKELTETPEVSLLPNRTVSLNLSNNRIRMLKNGSFAGLSSLEKLDLRNNLISTIMPGAFLGLTALRKLDLSSNRIGCLTPEMFQGLTNLTKLNISGNIFSSLDPNVFMELHSLKLVNFHSEFLSCDCGLRWVPSFFRSGSARLGDETLCAYPRRLQNKPLRLLRESDLSCEGPLELHTLSLLPSQRQVVFKGDRLPFHCTASLVDKITALHWRQNGQPVTSDPTKGIHLEESVQHDCTFITSELILSNVHVEASGEWECVVST... | null | null | canonical Wnt signaling pathway [GO:0060070]; central nervous system development [GO:0007417]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; sprouting angiogenesis [GO:0002040] | plasma membrane [GO:0005886]; Wnt signalosome [GO:1990909] | G protein-coupled receptor activity [GO:0004930] | PF00002;PF01825;PF13895;PF00560;PF13855;PF01463; | 2.60.220.50;4.10.1240.10;2.60.40.10;1.20.1070.10;3.80.10.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Proteolytically cleaved into two subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:Q96PE1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:27979830}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with reck at the plasma membrane. {ECO:0000269|PubMed:26051822}. | null | null | null | null | null | FUNCTION: Endothelial receptor which functions together with reck to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b) (PubMed:26051822, PubMed:30026314). Plays a key role in Wnt7-specific responses: Required for normal central nervous system (CNS) vascularization where it functions... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FCP8 | NAGS_DANRE | MAKVNSGSSGCRAMVMAGQFWTKPFALSSQRSGPHRRSAAEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTLIYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGS... | 2.3.1.1 | null | arginine biosynthetic process [GO:0006526]; glutamate metabolic process [GO:0006536]; urea cycle [GO:0000050] | mitochondrial matrix [GO:0005759] | acetyl-CoA:L-glutamate N-acetyltransferase activity [GO:0004042]; acetylglutamate kinase activity [GO:0003991]; arginine binding [GO:0034618]; methione N-acyltransferase activity [GO:0103045]; N-acetyl-gamma-glutamyl-phosphate reductase activity [GO:0003942] | PF04768; | 3.40.630.30;3.40.1160.10; | Acetyltransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N159}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000269|PubMed:24465614}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for acetyl-CoA {ECO:0000269|PubMed:24465614}; KM=1.13 mM for L-glutamate {ECO:0000269|PubMed:24465614}; | null | null | null | FUNCTION: Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (cps1) activity. {ECO:0000305|PubMed:24465614}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FDV5 | IYD_DANRE | MAVFSSLTPVFVAVLCVIIGFLFKNSQRKESRSKQKPSDQTARPWVDEDLQDDTEISTKDNEENNEDWMDTTDEENLPHVPYSPVQYSVSEMLDRSERFYTLMNLRRSVRFISPEPVPKEVIDNVIRTAGTAPSGAHTEPWTFVVVSDTDVKHRIREIIEEEEEINYKQRMGNKWVQDLKRLRTNWVKEYLDVAPYLILVFKQAYGILPSGKKKTHYYNEISVSISCGILLAALQNAGLVTVTTTPLNCGPQLRSLLQRPANEKLLMLLPVGFPASDAKVPDLKRKDLNDIMVLV | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:24153409}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | membrane [GO:0016020] | FMN binding [GO:0010181]; iodotyrosine deiodinase activity [GO:0140616]; oxidoreductase activity [GO:0016491] | PF00881; | 3.40.109.10; | Nitroreductase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:24153409}; PhysiologicalDirection=rig... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for diiodotyrosine (L-DIT) {ECO:0000269|PubMed:24153409}; Note=kcat 4.1 min(-1) for the deiodination of diiodotyrosine (L-DIT). {ECO:0000269|PubMed:24153409}; | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine (PubMed:24153409). Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). {ECO:0000250|UniProtKB:Q6PHW0, ECO:0000269|PubMed:24153409}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FE13 | LGR4_DANRE | MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTG... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; hormone-mediated signaling pathway [GO:0009755]; hypothalamus gonadotrophin-releasing hormone neuron development [GO:0021888]; negative regulation of cytokine productio... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF13855; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BXB1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BXB1}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering t... | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FHC4 | HYD2A_PYRFU | MIIELDEFTRVEGNGKAEIVIENGEVKDARVKIVEGPRFFEILTLGRDYWDVPDLEARICAICYIAHSVASVRAIEKALGIDVPESVEKLRELALWGEIIESHALHLYLLALPDVFGYPDAISMIPRHGELVKEGLTIKAFGNAIRELIGGREIHGINIKPGGFGRYPSEEELEKIAEHSKSLIKFARRIVGIFASQEAGGAVGEVLMATSDYLWGDELIINGERVQYYEVDEVPVGYSFAKHSYYKGNPVFVGALPRLLLKGESIEGEAARMLEEYRDKLESKYVIYNNLAQAIELLYALERVPQLVEEILSEGIERGN... | 1.12.1.5 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10714990}; Note=Binds 1 nickel ion per subunit. {ECO:0000269|PubMed:10714990}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; | null | cytoplasm [GO:0005737] | ferredoxin hydrogenase activity [GO:0008901]; hydrogen dehydrogenase (NADP+) activity [GO:0050583]; hydrogen dehydrogenase activity [GO:0047985]; nickel cation binding [GO:0016151] | PF00374; | 1.10.645.10; | [NiFe]/[NiFeSe] hydrogenase large subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10714990}. | CATALYTIC ACTIVITY: Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.12.1.5; Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463}; CATALYTIC ACTIVITY: Reaction=H2 + NAD(+) = H(+) + NADH; Xref=Rhea:RHEA:24636, ChEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.25 mM for methyl viologen (sodium dithionate and H(+) as cosubstrates) {ECO:0000269|PubMed:10714990}; KM=1 mM for methyl viologen (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.13 mM for H(2) (methyl viologen as cosubstrate) {ECO:0000269|PubMed:1071499... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for hydrogenase activity at >95 degrees Celsius. {ECO:0000269|PubMed:10714990}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is greater than 90 degrees Celsius. Activity increases with increasing temperature from 30 degrees Celsius to 90 degrees Celsius. Has a half-life of 6 hours at 95 degrees Celsius. {ECO:0000269|PubMed:10714990}; | FUNCTION: Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes th... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FHF8 | HYD2D_PYRFU | MKLGVFELTDCGGCALNLLFLYDKLLDLLEFYEIAEFHMATSKKSREKIDVALVTGTVSTQRDLEVLRDARNRSEYLIALGTCATHGSVQGVIENSKEAYRRVYGNGKPPVKLLNPKPVTDYVPVDFAIPGCPYDKEEVFQVLIDIAKGIEPVAKDYPVCLECKLNEYECVLLKKRIPCLGPVTAGGCNAKCPSYGLGCIGCRGPSLDNNVPGMFEVLKEILPDEEIARKLRTFARW | 1.12.1.5 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10714990}; Note=Binds 1 nickel ion per subunit. {ECO:0000269|PubMed:10714990}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:10714990}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:10714990}; COFAC... | null | cytoplasm [GO:0005737] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; hydrogen dehydrogenase (NADP+) activity [GO:0050583]; hydrogen dehydrogenase activity [GO:0047985]; metal ion binding [GO:0046872] | PF01058; | 3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10714990}. | CATALYTIC ACTIVITY: Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.12.1.5; Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463}; CATALYTIC ACTIVITY: Reaction=H2 + NAD(+) = H(+) + NADH; Xref=Rhea:RHEA:24636, ChEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.25 mM for methyl viologen (sodium dithionate and H(+) as cosubstrates) {ECO:0000269|PubMed:10714990}; KM=1 mM for methyl viologen (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.13 mM for H(2) (methyl viologen as cosubstrate) {ECO:0000269|PubMed:1071499... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for hydrogenase activity at >95 degrees Celsius. {ECO:0000269|PubMed:10714990}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is greater than 90 degrees Celsius. Activity increases with increasing temperature from 30 degrees Celsius to 90 degrees Celsius. Has a half-life of 6 hours at 95 degrees Celsius. {ECO:0000269|PubMed:10714990}; | FUNCTION: Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes th... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FHP1 | ACDB1_PYRFU | MDRVAKAREIIEKAKAENRPLVEPEAKEILKLYGIPVPEFKVARNEEEAVKFSGEIGYPVVMKIVSPQIIHKSDAGGVKINIKNDEEAREAFRTIMQNARNYKPDADLWGVIIYRMLPLGREVIVGMIRDPQFGPAVMFGLGGIFVEILKDVSFRVAPITKEDALEMIREIKAYPILAGARGEKPVNIEALADIIVKVGELALELPEIKEIDINPIFAYEDSAIAVDARMIL | 6.2.1.13 | null | null | cytoplasm [GO:0005737] | acetate-CoA ligase (ADP-forming) activity [GO:0043758]; ATP binding [GO:0005524]; metal ion binding [GO:0046872] | PF13549; | 3.30.1490.20;3.30.470.20; | Acetate CoA ligase beta subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119024}. | CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate; Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=6.2.1.13; Evidence={ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:911... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for ADP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=60 uM for ADP (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=132 uM for GDP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=396 uM for phosphate (at 80 degrees Celsius) {ECO:... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024). {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is above 90 degrees Celsius. {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}; | FUNCTION: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetat... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FHU4 | HYD1D_PYRFU | MGKVRIGFYALTSCYGCQLQLAMMDELLQLIPNAEIVCWFMIDRDSIEDEKVDIAFIEGSVSTEEEVELVKKIRENAKIVVAVGACAVQGGVQSWSEKPLEELWKKVYGDAKVKFQPKKAEPVSKYIKVDYNIYGCPPEKKDFLYALGTFLIGSWPEDIDYPVCLECRLNGHPCILLEKGEPCLGPVTRAGCNARCPGFGVACIGCRGAIGYDVAWFDSLAKVFKEKGMTKEEIIERMKMFNGHDERVEKMVEKIFSGGEQ | 1.12.1.3 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7615063}; Note=Binds 1 nickel ion per tetramer. {ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7615063}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49... | null | cytoplasm [GO:0005737] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; hydrogen dehydrogenase (NADP+) activity [GO:0050583]; metal ion binding [GO:0046872] | PF01058; | 3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7704275, ECO:0000269|Ref.4}. | CATALYTIC ACTIVITY: Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.12.1.3; Evidence={ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:11265463, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 mM for methyl viologen {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=79 uM for ferredoxin {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=0.08 mM for methylene blue {ECO:0000269|PubMed:11054105... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for hydrogenase activity at >95 degrees Celsius. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is greater than 95 degrees Celsius for hydrogenase activity. Stable up to 100 degrees Celsius. Loses 50% of activity at 80 degrees Celsius after 21 hour incubation. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | FUNCTION: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits form the hydrogenase component that catalyzes th... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FHX4 | HJC_PYRFU | MYRKGAQAERELIKLLEKHGFAVVRSAGSKKVDLVAGNGKKYLCIEVKVTKKDHLYVGKRDMGRLIEFSRRFGGIPVLAVKFLNVGWRFIEVSPKIEKFVFTPSSGVSLEVLLGIQKTLEGKS | 3.1.21.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11071944}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11071944}; Note=Divalent cations, Mg(2+) has higher activity than Mn(2+). {ECO:0000269|PubMed:11071944}; | DNA recombination [GO:0006310]; DNA repair [GO:0006281] | Holliday junction resolvase complex [GO:0048476] | crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; magnesium ion binding [GO:0000287] | PF01870; | 3.40.1350.10; | Holliday junction resolvase Hjc family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).; EC=3.1.21.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01490, ECO:0000269|PubMed:11071944}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-10. {ECO:0000269|PubMed:11071944}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70-75 degrees Celsius, enzyme is fully active after 16 hours at 90 degrees Celsius. {ECO:0000269|PubMed:11071944}; | FUNCTION: A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are subsequently ligated to produce recombinant pro... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FI44 | HYD1A_PYRFU | MKNLYLPITIDHIARVEGKGGVEIIIGDDGVKEVKLNIIEGPRFFEAITIGKKLEEALAIYPRICSFCSAAHKLTALEAAEKAVGFVPREEIQALREVLYIGDMIESHALHLYLLVLPDYRGYSSPLKMVNEYKREIEIALKLKNLGTWMMDILGSRAIHQENAVLGGFGKLPEKSVLEKMKAELREALPLAEYTFELFAKLEQYSEVEGPITHLAVKPRGDAYGIYGDYIKASDGEEFPSEKYRDYIKEFVVEHSFAKHSHYKGRPFMVGAISRVINNADLLYGKAKELYEANKDLLKGTNPFANNLAQALEIVYFIER... | 1.12.1.3 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7615063}; Note=Binds 1 nickel ion per heterotetramer. {ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7615063}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:248... | null | [Ni-Fe] hydrogenase complex [GO:0044569]; cytoplasm [GO:0005737] | ferredoxin hydrogenase activity [GO:0008901]; hydrogen dehydrogenase (NADP+) activity [GO:0050583]; nickel cation binding [GO:0016151] | PF00374; | 1.10.645.10; | [NiFe]/[NiFeSe] hydrogenase large subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7704275}. | CATALYTIC ACTIVITY: Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.12.1.3; Evidence={ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:11265463, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 mM for methyl viologen {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=79 uM for ferredoxin {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=0.08 mM for methylene blue {ECO:0000269|PubMed:11054105... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for hydrogenase activity at >95 degrees Celsius. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is greater than 95 degrees Celsius for hydrogenase activity. Stable up to 100 degrees Celsius. Loses 50% of activity at 80 degrees Celsius after 21 hour incubation. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | FUNCTION: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits form the hydrogenase component that catalyzes th... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FI45 | ACDA1_PYRFU | MSLEALFNPKSVAVIGASAKPGKIGYAIMKNLIEYGYEGKIYPVNIKGGEIEINGRKFKVYKSVLEIPDEVDMAVIVVPAKFVPQVLEECGQKGVKVVPIISSGFGELGEEGKKVEQQLVETARKYGMRILGPNIFGVVYTPAKLNATFGPTDVLPGPLALISQSGALGIALMGWTILEKIGLSAVVSVGNKADIDDADLLEFFKDDENTRAILIYMEGVKDGRRFMEVAKEVSKKKPIIVIKAGRSERGAKAAASHTGSLAGSDKVYSAAFKQSGVLRAYTIGEAFDWARALSNLPEPQGDNVVIITNGGGIGVMATDA... | 6.2.1.13 | null | null | cytoplasm [GO:0005737] | acetate-CoA ligase (ADP-forming) activity [GO:0043758]; ATP binding [GO:0005524] | PF13380;PF19045;PF13607; | 3.40.50.720;3.40.50.261; | Acetate CoA ligase alpha subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119024}. | CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate; Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=6.2.1.13; Evidence={ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:911... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for ADP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=60 uM for ADP (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=132 uM for GDP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=396 uM for phosphate (at 80 degrees Celsius) {ECO:... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024). {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is above 90 degrees Celsius. {ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}; | FUNCTION: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetat... | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FKV8 | PK1L1_ORYLA | MFCLWIFSLAFLHLHLCSVSSSSLEGSGFFVGWINASSLQLFASIGGCDLSPCMDEGQEGMEALYRSEEPFQCSIRASASPGRRQAGRTCVRKVPGNLAVHCHLLSENEGLEEEDLLRITVMTPRGQSSLQVNVSHGGLLTACSDWIWNTSEKHKNNVPASGLHLGISLEVPCCTSCTRFGSDSELVEEQCSALHVSVSDVLVKDYICCLTPRDKDKTLNRTETPCLYSSNSLKDSLVRGRVYQMSFEECFRWHLLVVLLMLEAQYNHSQEVHEDPSSTVKLCDYAVRIHAEKQAYSTNTDIPLLAVVDILDPVEFLWDF... | null | null | detection of mechanical stimulus [GO:0050982]; detection of nodal flow [GO:0003127]; left/right axis specification [GO:0070986] | calcium channel complex [GO:0034704]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; membrane [GO:0016020]; non-motile cilium [GO:0097730] | calcium channel activity [GO:0005262] | PF01825;PF00801;PF08016;PF01477;PF20519; | 2.60.40.10;2.60.60.20; | Polycystin family | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:21307098}; Multi-pass membrane protein {ECO:0000269|PubMed:21307098}. | null | null | null | null | null | FUNCTION: Component of a ciliary calcium channel that controls calcium concentration within cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with pkd2l1 in cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and gli2 transcription. Does not consti... | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
E8MGH8 | HYBA1_BIFL2 | MNVTITSPFWKRRRDQIVESVIPYQWGVMNDEIDTTVPDDPAGNQLADSKSHAVANLKVAAGELDDEFHGMVFQDSDVYKWLEEAAYALAYHPDPELKALCDRTVDLIARAQQSDGYLDTPYQIKSGVWADRPRFSLIQQSHEMYVMGHYIEAAVAYHQVTGNEQALEVAKKMADCLDANFGPEEGKIHGADGHPEIELALAKLYEETGEKRYLTLSQYLIDVRGQDPQFYAKQLKAMNGDNIFHDLGFYKPTYFQAAEPVRDQQTADGHAVRVGYLCTGVAHVGRLLGDQGLIDTAKRFWKNIVTRRMYVTGAIGSTHV... | 3.2.1.185 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24680821, ECO:0000269|Ref.7}; Note=Zn(2+) ion is involved in the catalytic reaction through maintaining the proper configuration of active site. {ECO:0000269|Ref.7}; | polysaccharide catabolic process [GO:0000272] | null | beta-L-arabinofuranosidase activity [GO:0102478]; metal ion binding [GO:0046872] | PF20737;PF20736;PF07944; | 1.50.10.10; | Glycosyl hydrolase 127 family | null | null | CATALYTIC ACTIVITY: Reaction=beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose; Xref=Rhea:RHEA:36051, ChEBI:CHEBI:15377, ChEBI:CHEBI:28272, ChEBI:CHEBI:73180; EC=3.2.1.185; Evidence={ECO:0000269|PubMed:24385433}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.85 mM for L-arabinofuranose-beta-1,2-L-arabinofuranose disaccharide (beta-Ara2) {ECO:0000269|PubMed:24385433}; KM=0.43 mM for Ara-Hyp {ECO:0000269|PubMed:24385433}; KM=0.31 mM for Ara(2)-Hyp {ECO:0000269|PubMed:24385433}; Note=kcat is 2.0 sec(-1) with beta-Ara2. ... | null | null | null | FUNCTION: Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2... | Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) |
E8PLM2 | OLD_THESS | MLKRLQVKNFRCLEDIDLPLGPLTAIVGPNGAGKTTILRAIDLVLGDVWPSLRSFRIPQDFINFDTTRAIEITVHFDPPYTQGSFNITAFRLTCKGEDADFHVDLEPLDEGGNVPRYPSGNPLRVGTDMRNHARVLFLDHRRNLAQHLPSIRGSILGRLLQPVRREFKLQDNFKQVYEQAMDLLRTEQVKQIEKTIAETAKQMLGFLGKDAMKSMEIGFGFADPANPFNSLRLQYRESDLTLPGDELGLGIQSAIVVGIFEAFRQLGEKIGTVIIEEPEMYLHPQAQRYFYRLLCEMADKDQCQIIYSTHSPIFADVNRF... | 3.1.11.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32009148}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:32009148}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:32009148}; Note=Probably binds 2 metal cations. In vitro during a short incubation, Mn(2+)... | null | null | ATP binding [GO:0005524]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF13175;PF20469; | 3.40.50.300; | Class 1 OLD nuclease family | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000269|PubMed:32009148}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=180 uM for ATP {ECO:0000269|PubMed:32009148}; Note=kcat is 0.44 min(-1) for ATPase at 65 degrees Celsius. {ECO:0000269|PubMed:32009148}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius for the ATPase activity. {ECO:0000269|PubMed:32009148}; | FUNCTION: An exodeoxyribonuclease that degrades linear or supercoiled dsDNA from 5'-3'. Nicks and linearizes circular DNA. Activity is not stimulated by ATP or AMP-PNP, although it has DNA-stimulated ATPase activity. {ECO:0000269|PubMed:32009148}. | Thermus scotoductus (strain ATCC 700910 / SA-01) |
E8WYN5 | MDL_GRATM | MEIKRVGSQASGKGPADWFTGTVRIDPLFQAPDPALVAGASVTFEPGARTAWHTHPLGQTLIVTAGCGWAQREGGAVEEIHPGDVVWFSPGEKHWHGAAPTTAMTHLAIQERLDGKAVDWMEHVTDEQYRR | 4.1.2.10 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23981508, ECO:0000269|Ref.3}; | null | null | lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF07883; | 2.60.120.10; | Cupin domain-containing hydroxynitrile lyase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-mandelonitrile = benzaldehyde + hydrogen cyanide; Xref=Rhea:RHEA:18313, ChEBI:CHEBI:17169, ChEBI:CHEBI:18407, ChEBI:CHEBI:18450; EC=4.1.2.10; Evidence={ECO:0000269|PubMed:23981508, ECO:0000269|Ref.3}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.3 mM for (R)-mandelonitrile (at pH 4.5 and at 25 degrees Celsius) {ECO:0000269|PubMed:23981508}; KM=6.1 mM for (R)-mandelonitrile (at pH 5.5 and at 5 degrees Celsius) {ECO:0000269|Ref.3}; Vmax=0.12 umol/min/mg enzyme (at pH 4.5 and at 25 degrees Celsius) {ECO:00... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:23981508}; | null | FUNCTION: Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese. {ECO:0000269|PubMed:23981508, ECO:0000269|Ref.3}. | Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9) |
E9AE57 | FUM2_LEIMA | MSLCDQCEIGCRRVGIKDIEDASAVNADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGK... | 4.2.1.2 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:27528683}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:27528683}; | fumarate metabolic process [GO:0006106]; generation of precursor metabolites and energy [GO:0006091]; malate metabolic process [GO:0006108] | ciliary plasm [GO:0097014]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glycosome [GO:0020015] | 4 iron, 4 sulfur cluster binding [GO:0051539]; fumarate hydratase activity [GO:0004333]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF05681;PF05683; | 3.20.130.10; | Class-I fumarase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22569531}. | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:22569531, ECO:0000269|PubMed:27528683, ECO:0000269|PubMed:30645090}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.7 mM for fumarate (in anaerobic conditions) {ECO:0000269|PubMed:22569531}; KM=1.9 mM for fumarate (in aerobic conditions) {ECO:0000269|PubMed:22569531}; KM=12.6 mM for (S)-malate (in anaerobic conditions) {ECO:0000269|PubMed:22569531}; KM=5.7 mM for (S)-malate (i... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:22569531}; | null | FUNCTION: Cytosolic fumarate hydratase that catalyzes the reversible hydration of fumarate to (S)-malate. {ECO:0000269|PubMed:22569531, ECO:0000269|PubMed:27528683, ECO:0000269|PubMed:30645090}. | Leishmania major |
E9F5E9 | SUBD_METRA | MSPSAPNTNELNSPVLETQPLAGDAALLHSSIAAGYEEIIRAPFDYLLNLPGKDVRSKMISAFNEWLCIPADKLEVIKRIVMLLHNASLLIDDIQDSSKLRRGLPVSHHIFGVPQTINAANYAYFLAQQELPKLGDPKAFEIYTEELLSLHRGQGMDIYWREASKCPTEEEYFSMVSHKTGGLFRLAIRLMQLASDKNWFVFHTRDFVPLVNVLGVIFQIRDDYLNLQSHAYTVNKGFGEDLTEGKYSFPIIHSIRSDPTNIQLSSILKQRTTDVDVKLFAVECIKATGSFEHCKEKIAELVAEARQLIKEMGNSVPGSA... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27189118}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside ch... | Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium anisopliae (strain ARSEF 23)) |
E9L7A5 | PAT_PETHY | MAATTTTSSSSRIAYSRHNIPGLHSDSLNPKSISFSSNLHTFSLKSSGSRRQLYSRRTGAVVIMQSMDKVEVDISLSPRVNSVKPSKTVAITDQATALVQAGVPVIRLAAGEPDFDTPAPIVEAGINAIREGHTRYTPNAGTMELRSAISHKLKEENGLSYTPDQILVSNGAKQSIIQAVLAVCSPGDEVLIPAPYWVSYPEMARLADATPVILPTSISEDFLLDPKLLESKLTEKSRLLILCSPSNPTGSVYPRKLLEQIAEIVARHPRLLVISDEIYEHIIYAPATHTSFASLPGMWDRTLTVNGFSKAFAMTGWRLG... | 2.6.1.1; 2.6.1.78; 2.6.1.79 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:21102469}; | aromatic amino acid family biosynthetic process, prephenate pathway [GO:0009095]; L-phenylalanine biosynthetic process [GO:0009094] | chloroplast [GO:0009507] | aspartate-prephenate aminotransferase activity [GO:0033853]; glutamate-prephenate aminotransferase activity [GO:0033854]; identical protein binding [GO:0042802]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:21102469}; CATALYTIC ACTIVITY: Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=317 uM for prephenate (with 20 mM aspartate as cosubstrate) {ECO:0000269|PubMed:21102469}; KM=478 uM for prephenate (with 20 mM glutamate as cosubstrate) {ECO:0000269|PubMed:21102469}; KM=1045 uM for 2-oxoglutarate (with 20 mM aspartate as cosubstrate) {ECO:0000269... | PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-arogenate from prephenate (L-Asp route): step 1/1. {ECO:0000269|PubMed:21102469}.; PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-arogenate from prephenate (L-Glu route): step 1/1. {ECO:0000269|PubMed:21102469}. | null | null | FUNCTION: Prokaryotic-type aspartate aminotransferase. Has also a prenate transaminase activity (PubMed:21102469). Involved in the aromatic amino acids biosynthesis pathway via the arogenate route (PubMed:21102469). Required for the transamination of prephenate into arogenate (PubMed:21102469). Can use 2-oxoglutarate, ... | Petunia hybrida (Petunia) |
E9LVH9 | PETH2_THECS | MANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF | 3.1.1.101; 3.1.1.74 | null | null | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | cutinase activity [GO:0050525] | PF12146; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. | CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for pNP-acetate (at 25 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; KM=1.9 mM for pNP-acetate (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:23592055}; KM=2133 uM for pNP-butanoate (at 25 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; KM=3.4 mM for p... | null | null | null | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:23592055, Ref.1). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyes... | Thermobifida cellulosilytica |
E9NA96 | IR25A_DROME | MILMNPKTSKILWLLGFLSLLSSFSLEIAAQTTQNINVLFINEVDNEPAAKAVEVVLTYLKKNIRYGLSVQLDSIEANKSDAKVLLEAICNKYATSIEKKQTPHLILDTTKSGIASETVKSFTQALGLPTISASYGQQGDLRQWRDLDEAKQKYLLQVMPPADIIPEAIRSIVIHMNITNAAILYDDSFVMDHKYKSLLQNIQTRHVITAIAKDGKREREEQIEKLRNLDINNFFILGTLQSIRMVLESVKPAYFERNFAWHAITQNEGEISSQRDNATIMFMKPMAYTQYRDRLGLLRTTYNLNEEPQLSSAFYFDLAL... | null | null | behavior [GO:0007610]; detection of chemical stimulus involved in sensory perception [GO:0050907]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; entrainment of circadian clock [GO:0009649]; modulation of chemical synaptic transmission [GO:0050804]; rhythmic process [GO:0048511]; s... | axon [GO:0030424]; cilium [GO:0005929]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; sensory dendrite [GO:0071683] | coreceptor activity [GO:0015026]; glutamate receptor activity [GO:0008066]; ligand-gated monoatomic ion channel activity [GO:0015276]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF07885;PF00060;PF10613;PF00497; | 1.10.287.70;3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:19135896}. Cell projection, dendrite {ECO:0000269|PubMed:19135896, ECO:0000269|PubMed:26580016, ECO:0000269|PubMed:27126188}. Perikaryon {ECO:0000269|PubMed:19135896, ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Integral part of various neural sensory systems in the antenna that provide the neural basis for the response to environmental changes in temperature (thermosensation), humidity (hygrosensation) and odor detection (PubMed:21220098, PubMed:27161501, PubMed:27656904). Required for odor-evoked electrophysiologic... | Drosophila melanogaster (Fruit fly) |
E9P162 | TRP6H_STRT5 | MNTRNPDKVVIVGGGTAGWMTASYLKKAFGERVSVTLVESGTIGTVGVGEATFSDIRHFFEFLDLREEEWMPACNATYKLAVRFQDWQRPGHHFYHPFEQMRSVDGFPLTDWWLQNGPTDRFDRDCFVMASLCDAGRSPRYLNGSLLQQEFDERAEEPAGLTMSEHQGKTQFPYAYHFEAALLAEFLSGYSKDRGVKHVVDEVLEVKLDDRGWISHVVTKEHGDIGGDLFVDCTGFRGVLLNQALGVPFVSYQDTLPNDSAVALQVPLDMEARGIPPYTRATAKEAGWIWTIPLIGRIGTGYVYAKDYCSPEEAERTLRE... | 1.14.19.59 | null | null | null | monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166] | PF04820; | 3.50.50.60; | Flavin-dependent halogenase family, Bacterial tryptophan halogenase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=chloride + FADH2 + L-tryptophan + O2 = 6-chloro-L-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:55900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57912, ChEBI:CHEBI:58307, ChEBI:CHEBI:139335; EC=1.14.19.59; Evidence={ECO:0000269|PubMed:21424165, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for L-tryptophan {ECO:0000269|PubMed:21424165}; KM=0.8 uM for tryptophan {ECO:0000269|PubMed:26840773}; KM=241 uM for kynurenine {ECO:0000269|PubMed:26840773}; KM=1075 uM for anthranilamide {ECO:0000269|PubMed:26840773}; Note=kcat is 1.53 min(-1) with L-trypt... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:21424165}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:21424165}; | FUNCTION: Catalyzes the chlorination of tryptophan (Trp) at C6 position to yield 6-chloro-tryptophan (PubMed:21424165, PubMed:26840773). Accepts both L and D-Trp as the substrates (PubMed:21424165). The enzyme also uses bromide to yield 6-bromo-Trp (PubMed:21424165). In vitro, can also catalyze the halogenation of 3-in... | Streptomyces toxytricini (Actinomyces toxytricini) |
E9P860 | ZNFX1_CAEEL | MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFLQYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYEELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPGLPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENS... | 3.6.4.13 | null | regulatory ncRNA-mediated heterochromatin formation [GO:0031048] | nuclear RNA-directed RNA polymerase complex [GO:0031380]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270] | PF13086;PF13087; | 3.40.50.300; | ZNFX1 family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}. Cytoplasm {ECO:0000269|PubMed:29775580}. Cytoplasmic granule {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580, ECO:0000269|PubMed:32843637}. Note=Co-localizes with wago-4 in P-granules in germline bl... | 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:0000305|PubMed:29775580}; | null | null | null | null | FUNCTION: Epigenetic inheritance factor which, in association with the Argonaute protein wago-4, mediates small RNA-directed transgenerational epigenetic inheritance and thus balances the transgenerational inheritance of epigenetic information (PubMed:29769721, PubMed:29775580). Specifically, maintains a balanced produ... | Caenorhabditis elegans |
E9P8D2 | MPR1_YEASX | MDAESIEWKLTANLRNGPTFFQPLADSIEPLQFKLIGSDTVATAFPVFDTKYIPDSLINYLFKLFNLEIESGKTYPQLHSLTKQGFLNYWFHSFAVVVLQTDEKFIQDNQDWNSVLLGTFYIKPNYAPRCSHNCNAGFLVNGAHRGQKVGYRLAQVYLNWAPLLGYKYSIFNLVFVTNQASWKIWDKLNFQRIGLVPHAGILNGFSEPVDAIIYGKDLTKIEPEFLSME | 2.3.1.271 | null | null | mitochondrion [GO:0005739]; nucleus [GO:0005634] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747] | PF00583; | 3.40.630.30; | Acetyltransferase family | PTM: Not glycosylated. {ECO:0000269|PubMed:11555637}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11555637, ECO:0000269|PubMed:20550582}. Mitochondrion {ECO:0000269|PubMed:20550582}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate 5-semialdehyde = CoA + H(+) + N-acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:48232, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58066; EC=2.3.1.271; Evidence={ECO:0000269|PubMed:15308773}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.9 mM for azetidine-2-carboxylate {ECO:0000269|PubMed:23818613}; KM=0.9 mM for azetidine-2-carboxylate {ECO:0000269|PubMed:15308773}; KM=7.019 mM for (S)-1-pyrroline-5-carboxylate {ECO:0000269|PubMed:15308773}; KM=4.3 mM for acetyl-CoA {ECO:0000269|PubMed:2381861... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9 for azetidine-2-carboxylate and 6.5-7 for (S)-1-pyrroline-5-carboxylate. {ECO:0000269|PubMed:12761200, ECO:0000269|PubMed:15308773}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:12761200}; | FUNCTION: N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been sho... | Saccharomyces cerevisiae (Baker's yeast) |
E9PSK7 | JIP3_RAT | MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGGGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVTKNNKRAREKRNSRNMEV... | null | null | anterograde axonal protein transport [GO:0099641]; axon development [GO:0061564]; axon guidance [GO:0007411]; axon regeneration [GO:0031103]; forebrain development [GO:0030900]; in utero embryonic development [GO:0001701]; JNK cascade [GO:0007254]; lung alveolus development [GO:0048286]; lung morphogenesis [GO:0060425]... | axolemma [GO:0030673]; axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; smooth endopl... | JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; MAP-kinase scaffold activity [GO:0005078]; mitogen-activated protein kinase kinase binding [GO:0031434]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; signaling receptor complex adaptor activity [GO:0030159] | PF16471;PF09744;PF19056; | 1.20.58.1770;1.20.5.1000;2.130.10.10; | JIP scaffold family | PTM: Phosphorylation by ROCK1 is crucial for the recruitment of JNK. {ECO:0000250|UniProtKB:Q9UPT6}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9ESN9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, axon {ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431}. Cell projecti... | null | null | null | null | null | FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor p... | Rattus norvegicus (Rat) |
E9PSL7 | CTRO_RAT | MLKFKYGVRNPSEASAPEPIASRASRLNLFFQGKPPLMTQQQMSALSREGVLDALFVLLEECSQPALMKIKHVSSFVRKYSDTIAELRELQPSVRDFEVRSLVGCGHFAEVQVVREKATGDVYAMKIMKKAALRAQEQVSFFEEERNILSQSTSPWIPQLQYAFQDKNNLYLVMEYQPGGDLLSLLNRYEDQLDENMIQFYLAELILAVHSVHQMGYVHRDIKPENILIDRTGHIKLVDFGSAAKMNSNKVDAKLPIGTPDYMAPEVLTVMNEDRRGTYGLDCDWWSVGVVAYEMLYGKTPFTEGTSARTFNNIMNFQRF... | 2.7.11.1 | null | actomyosin structure organization [GO:0031032]; dendrite development [GO:0016358]; G2/M transition of mitotic cell cycle [GO:0000086]; generation of neurons [GO:0048699]; Golgi organization [GO:0007030]; liver development [GO:0001889]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic cell cycle... | actin cytoskeleton [GO:0015629]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi cisterna [GO:0031985]; midbody [GO:0030496]; neuronal cell body [GO:0043025]; ruffle [GO:0001726]; vacuole [GO:0005773] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine kinase inhibitor activity [GO:0030291]; scaffold protein binding [G... | PF00780;PF00169;PF00069;PF00433; | 1.20.5.170;1.20.5.340;3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49025}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P49025}; CATALYTI... | null | null | null | null | FUNCTION: Plays a role in cytokinesis (By similarity). Required for KIF14 localization to the central spindle and midbody (By similarity). Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1 (By similarity). It probably binds p21 with a tighter specificity in vivo (By similarity). Displays serin... | Rattus norvegicus (Rat) |
E9PT37 | RBM20_RAT | MVLAAAMSQDADPSGPEQPDRDACIVPGVQGPPAPQGQQGMQPLPPPLPPPPQPQSSLPQIIQNAAKLLDKNPFSVSSQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTTHGPTGVSQHAATVPSAHFPSTAIAFSPPSQAGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSIGKAGPTPATTGFYDYGKANPGQAYGSETEGQPGFLPASASAAASGGVTYEGHYSHTGQDGQATFSKDFYGPSAQGSHAAGGFPADQAGSMKGDVGGLLQGTNSQ... | null | null | heart formation [GO:0060914]; mRNA processing [GO:0006397]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of RNA splicing [GO:0033120]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of mRNA splicing, via spliceosome [GO:0048024]; regulation o... | cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634] | mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157]; RNA binding [GO:0003723]; splicing factor binding [GO:1990935]; zinc ion binding [GO:0008270] | null | 3.30.70.330; | null | PTM: Phosphorylation regulates the subcellular localization. Phosphorylation of Ser-638 and Ser-640 in the RS (arginine/serine-rich) region promotes nuclear localization of the protein (PubMed:35394688). In contrast, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprot... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:23307558, ECO:0000269|PubMed:35394688}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:35394688}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:35394688). Also locali... | null | null | null | null | null | FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH (PubMed:22466703, PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899, PubMed:27289039, PubMed:... | Rattus norvegicus (Rat) |
E9PT87 | MYLK3_RAT | MSGVSEEDPEGLGPQGLPALGGACLVTVDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQGLHRLEASQELGLAGPGSTSPAAAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTIQNSKVDDFILQGTVPWRKGSLADGPEENKEQAEVAGVKPKHVLNTGSVQAATSRALWEESQKQDTPVGTVEGLPLIIDTSLKGADLTQAGASLRQGVEALDPGQEPPPTEAESRLPALASEDTGTTLELSVAIDRISEVLTSLRMSQSAGEGTSSSKPDCSEPGPQPLGPLTTDSDIHSDEGLPR... | 2.7.11.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cardiac myofibril assembly [GO:0055003]; cellular response to interleukin-1 [GO:0071347]; intracellular signal transduction [GO:0035556]; positive regulation of apoptotic process [GO:0043065]; positive regulation of sarcomere organization [GO:0060298]; protein phosphorylation [GO:0006468]; regulation of vascular permea... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain kinase activity [GO:0004687] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17885681}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Calmodulin-dependent kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes. Increases cardiomyocyte contractility. {ECO:0000269|PubMed:17885681, ECO:0000269|PubMed:20615916}. | Rattus norvegicus (Rat) |
E9PTA2 | TRPM2_RAT | MEPLDQRRTDSDQEEGFGVQSRRATDLGMVPNLRRSNSSLCKSRRLLCSFSSEKQENLSSWIPENIKKKECVYFVESSKLSDAGKVVCECGYTHEQHIEVAIKPHTFQGKEWDPKKHVHEMPTDAFGDIVFTGLSQKVGKYVRLSQDTSSIVIYQLMTQHWGLDVPSLLISVTGGAKNFNMKLRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSCKEGDVITIGIATWGTIHNREALIHPMGGFPAEYMLDEEGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTKLEKFISEQTKERGGVAI... | null | null | calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to calcium ion [GO:0071277]; cellular response to hydrogen p... | cell projection [GO:0042995]; cytoplasmic vesicle membrane [GO:0030659]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; intracellularly gated calcium channel activity [GO:0015278]; ligand-gated calcium channel activity [GO:0099604]; manganese ion transmembrane transporter activity [GO:0005384]; mono-ADP-D-ribose binding [GO:0072571]; monoatomic cation channel activity [GO:0005261]; sodium channel activi... | PF00520;PF18139; | 3.40.50.450;3.90.79.10; | Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:16260005, ECO:0000269|PubMed:16601673, ECO:0000269|PubMed:16651700, ECO:0000269|PubMed:19454650}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O94759}. Perikaryon {ECO:0000269|PubMed:16651700}. Cell projection {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:11804595, PubMed:16260005, PubMed:16601673, PubMed:16651700, PubMed:19454650). Functions as a ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic Nudix ... | Rattus norvegicus (Rat) |
E9PTT0 | ZDH17_RAT | MADGPDEYDTETGCVPLLHPEEIKPQSHYNHGYGEPLGRKTHVDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGGNVDAQNVKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLRKLKADKEFRQKVMLGTPFLVIWLVGFIADLNIDSWLI... | 2.3.1.-; 2.3.1.225 | null | axonogenesis [GO:0007409]; lipoprotein transport [GO:0042953]; protein palmitoylation [GO:0018345]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386]; regulation of programmed cell death [GO:0043067] | cell projection [GO:0042995]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; presynaptic membrane [GO:0042734] | identical protein binding [GO:0042802]; 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]; signaling receptor binding [GO:0005102] | PF12796;PF01529; | 1.25.40.20; | DHHC palmitoyltransferase family, AKR/ZDHHC17 subfamily | PTM: Autopalmitoylated. Autopalmitoylation has a regulatory role in ZDHHC17-mediated Mg(2+) transport. {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:000... | 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}; CATALYT... | 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 octad... | Rattus norvegicus (Rat) |
E9PU28 | IMDH2_RAT | MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNESDELVAIIARTDLKKNRDYPLASKDTKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNLQVIGGNVVTAAQAKNLIDAGVDA... | 1.1.1.205 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03156}; | 'de novo' XMP biosynthetic process [GO:0097294]; cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; GMP biosynthetic process [GO:0006177]; GTP biosynthetic process [GO:0006183]; lymphocyte proliferation [GO:0046651]; purine nucleotide biosynthetic process [GO:0006164]; retina development in... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family | PTM: Acetylated by CLOCK in a circadian manner. {ECO:0000250|UniProtKB:P12268}.; PTM: Ubiquitinated leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P12268}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12268}. Nucleus {ECO:0000250|UniProtKB:P12268}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P12268}. Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine-nucleotide depletion. {ECO:0000250|UniProtKB:P12268}. | CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000250|UniProtKB:P12268}; | null | PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000250|UniProtKB:P12268}. | null | null | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding ac... | Rattus norvegicus (Rat) |
E9PUL5 | PRRT2_MOUSE | MAASSSQVSEMKGVEDSSKTQTEGPRHSEEGLGPVQVVAEIPDQPEALQPGPGITAAPVDSGPKAELAPETTETPVETPETVQATDLSLNPEEGSKASPSPSPSEARQEPASKPDVNRETAAEEGSEPQSTAPPEPTSEPAFQINTQSDPQPTSQPPPKPPLQAEPPTQEDPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAK... | null | null | negative regulation of short-term synaptic potentiation [GO:1905513]; negative regulation of SNARE complex assembly [GO:0035544]; neuromuscular process controlling posture [GO:0050884]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; synaptic vesicle fusion to presynaptic active zone... | axon terminus [GO:0043679]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]; synaptic vesicle [GO:0008021]; synapt... | SH3 domain binding [GO:0017124]; syntaxin-1 binding [GO:0017075] | PF04505; | null | CD225/Dispanin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000305|PubMed:26797119}. Presynaptic cell membrane {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}; Single-pass membrane protein {ECO:0000305|PubMed:26797119}. Synapse {ECO:00002... | null | null | null | null | null | FUNCTION: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing (PubMed:27052163). In the c... | Mus musculus (Mouse) |
E9PUN2 | NRX2B_MOUSE | MPPGGSGQGGCPRRPPALAGPLPPPPPPPPLPLLLGLLLLLGAAEGARVSSSLSTTHHVHHFHSKHGTVPIAINRMPFLTRSGHAGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTT... | null | null | cell adhesion [GO:0007155]; chemical synaptic transmission [GO:0007268]; neurotransmitter secretion [GO:0007269]; synapse assembly [GO:0007416] | cell projection [GO:0042995]; glutamatergic synapse [GO:0098978]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991] | calcium channel regulator activity [GO:0005246]; metal ion binding [GO:0046872] | PF02210; | 2.60.120.200; | Neurexin family | PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins. {ECO:0000269|PubMed:30100184}. | SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. {ECO:0000305}. | Mus musculus (Mouse) |
E9PUQ8 | DGKD_MOUSE | MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTILKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQNKEHFEPTQYSMDHFSGMHNWYACSHARPTYCNVCREVLSGVTSHGLSCEVCKFKAHKRCAVRATSNCKWTTLASIGKDIIEDEDGIAMPHQWLEGNLPVSAKCIVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLVMKCPLGLCKVSVIPPTALNSIDSDGFWKATCPPSCTS... | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; endocytosis [GO:0006897]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; negative regulation of protein kinase C signaling [GO:0090038]; phosphatidic acid biosynthetic process [GO:0006654]; positive regulation of clathrin-dependent endo... | clathrin-coated pit [GO:0005905]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00130;PF00609;PF00781;PF00169;PF07647; | 2.60.200.40;3.30.60.20;2.30.29.30;1.10.150.50; | Eukaryotic diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16760}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16760}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q16760}. Cytoplasm {ECO:0000250|UniProtKB:Q16760}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:17021016}; PhysiologicalDirection=left-to-right... | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:17021016}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:17021016). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targ... | Mus musculus (Mouse) |
E9PV24 | FIBA_MOUSE | MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSD... | null | null | adaptive immune response [GO:0002250]; blood coagulation [GO:0007596]; blood coagulation, common pathway [GO:0072377]; fibrinolysis [GO:0042730]; innate immune response [GO:0045087]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via ... | blood microparticle [GO:0072562]; cell cortex [GO:0005938]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; synapse [GO:0045202] | extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102] | PF08702;PF12160;PF00147; | 1.20.5.50;3.90.215.10;4.10.530.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsil... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7649481}. | null | null | null | null | null | FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots (PubMed:7649481). In addition, functions during the... | Mus musculus (Mouse) |
E9PV87 | TALD3_MOUSE | MKNVEFSLERGQRLKMPARKLREIVSPNQGNKLAVVEDELPRVPPALAANKRLAVETRTSSNGTLCGSLDLTSARLYHQPLLESPPASKKSDFSKDAVVRQLPLNKTEENNAPKANDIFISQYTMGQKDALRTVLKQKAQSMPVFKAVKVHLFEDTSTEKNTVAQETETPPNRIDSATTVAAATAAAIATAAPLIKVQSDLEAKVNCVGELLTKLQETDKQLQRVTEHQASVQSKQEKVHCHDHDKQMNAFMEQHIRHLEKLQQQQIDIQTHFIDAALKASSLQLGMSTSRAVGKYSGKLGSPSVGSSVFSHNTFVSKRV... | null | null | cilium assembly [GO:0060271]; regulation of establishment of protein localization [GO:0070201]; smoothened signaling pathway [GO:0007224] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; photoreceptor inner segment [GO:0001917] | null | PF15324; | null | TALPID3 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BVV6}. Photoreceptor inner segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, cilium... | null | null | null | null | null | FUNCTION: Required for ciliogenesis and sonic hedgehog/SHH signaling (PubMed:21750036). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceed... | Mus musculus (Mouse) |
E9PVA8 | GCN1_MOUSE | MAADTQVSETLKRFAVKVTTASVKERREILSELGRCIAGKDLPEGAVKGLCKLFCLTLHRYRDAASRRALQAAIQQLAEAQPEATAKNLLHSLQSSGVGSKACVPSKSSGSAALLALTWTCLLVRIVFPLKAKRQGDIWNKLVEVQCLLLLEVLGGSHKHAVDGAVKKLTKLWKENPGLVEQYFSAILSLEPSQNYAAMLGLLVQFCTNHKEMDAVSQHKSTLLEFYVKNILMSKAKPPKYLLDNCAPLLRFMSHSEFKDLILPTIQKSLLRSPENVIETISSLLASVTLDLSQYALDIVKGLANQLKSNSPRLMDEAVL... | null | null | cellular response to amino acid starvation [GO:0034198]; GCN2-mediated signaling [GO:0140469]; regulation of translation [GO:0006417]; rescue of stalled ribosome [GO:0072344] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626] | molecular adaptor activity [GO:0060090]; protein kinase regulator activity [GO:0019887]; protein serine/threonine kinase activator activity [GO:0043539]; stalled ribosome sensor activity [GO:0170011] | null | 1.25.10.10; | GCN1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32324833, ECO:0000305|PubMed:23447528}. Note=Associates with ribosomes in undifferentiated neuroblastoma cells and increases after neuronal differentiation (PubMed:23447528). {ECO:0000269|PubMed:23447528}. | null | null | null | null | null | FUNCTION: Ribosome collision sensor that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Directly binds to th... | Mus musculus (Mouse) |
E9PVD3 | PCD16_MOUSE | MQKELSVALSCPGMKSLRTLLPLLVLLGATVPGSWGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPARDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLRLERPLDFEQRR... | null | null | anatomical structure morphogenesis [GO:0009653]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration [GO:0016477]; cell migration involved in endocardial cushion formation [GO:0003273]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; coc... | apical part of cell [GO:0045177]; catenin complex [GO:0016342] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF00028; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and DCHS1 accumulated at the cell-cell boundaries located apical to the adherens junction. {ECO:0000269|PubMed:19506035}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation (PubMed:26258302). {ECO:0000269|PubMed:2... | Mus musculus (Mouse) |
E9PVX6 | KI67_MOUSE | MASSAHLVTIKRSGDDGAHFPLSLSSCLFGRSIECDIRIQLPVVSKRHCKIEVKEQEAILYNFSSTNPTQVNGVTIDEPVRLRHGDIITIIDRSFRYEDGNHEDGSKPTEFPGKSLGKEPSRRASRDSFCADPDGEGQDTKASKMTASRRSFVYAKGLSADSPASDGSKNSVSQDSSGHVEQHTGRNIVEPTSGDLFKKSRSTGSSYREPKSSPTQSLSNSNEKESPFEKLYQSMKEELDVKSQKSCRKSEPQPDRAAEESRETQLLVSGRARAKSSGSTPVTAASSPKVGKIWTERWRGGMVPVQTSTETAKMKTPVRH... | null | null | cell population proliferation [GO:0008283]; cholangiocyte proliferation [GO:1990705]; epithelial cell proliferation [GO:0050673]; hepatocyte proliferation [GO:0072574]; meiotic cell cycle [GO:0051321]; regulation of chromatin organization [GO:1902275]; regulation of chromosome segregation [GO:0051983]; regulation of mi... | chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA binding [GO:0003677] | PF00498;PF08065;PF15276; | 2.60.200.20; | null | PTM: Phosphorylated. Hyperphosphorylated in mitosis. Hyperphosphorylated form does not bind DNA. {ECO:0000250|UniProtKB:P46013}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Nucleus {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Nucleus, nucleolus {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Note=Associates with the surface of the mitotic chromosome, the perichromosomal lay... | null | null | null | null | null | FUNCTION: Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface (PubMed:27362226). Prevents chr... | Mus musculus (Mouse) |
E9PX95 | ABCAH_MOUSE | MEVLKKLKLLLWKNFILKRRKTLITLLEMLMPLLFCAIVLYLRLNSMPRKKSSTNYPAVDVSLLPVYFYNYPLKSKFQLAYIPSKSETLKAVTEVVEQTFAVDFEVLGFPSVPLFEDYIIKDPKSFYILVGIIFHHDFNSSNEPLPLVVKYDLRFSYVQRNFVSPPRHLFFQEEIEGWCTAFLYPPNLSQAPREFSYADGGNPGYNKEGFLAIQHAVDKAIMRHHAPKAALNMFKDLHVLVQRFPFGPHIQDPFLVILQNEFPLLLMLSFICVELIITNSVLSEKERKQKEYMSMMGVESWLHWVAWFITFFISVSITVS... | null | null | lipid transport [GO:0006869]; neutral lipid metabolic process [GO:0006638] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319] | PF12698;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCA family | PTM: N-glycosylated. {ECO:0000269|PubMed:15810880}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15810880}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:22237709}. | CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:22237709}; PhysiologicalDirection=left-to-right; Xre... | null | null | null | null | FUNCTION: Promotes cholesterol efflux from sperm which renders sperm capable of fertilization (PubMed:22237709). Has also been shown to decrease levels of intracellular esterified neutral lipids including cholesteryl esters, fatty acid esters and triacylglycerols (PubMed:15810880). {ECO:0000269|PubMed:15810880, ECO:000... | Mus musculus (Mouse) |
E9PXF8 | MTMRD_MOUSE | MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHYCSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQ... | null | null | autophagy [GO:0006914] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; vacuolar membrane [GO:0005774] | guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; phosphatase binding [GO:0019902]; phosphatase regulator activity [GO:0019208]; phosphatidylinositol binding [GO:0035091] | PF02141;PF02893;PF06602;PF00169;PF12335;PF03456; | 3.30.450.200;3.40.50.11500;2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:16750429, ECO:0000269|PubMed:23297362}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16750429}. Membrane {ECO:0000250|UniProtKB:Q86WG5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q86WG5}. Endosome membrane {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) which activates RAB21 and possibly RAB28 (By similarity). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). In response to starvation-induced autophagy, activates RAB21 which in turn binds ... | Mus musculus (Mouse) |
E9PXX9 | S28A1_MOUSE | MADDTPRQRESISLTPVAHGLENMGAEFLEIMEEGQLPHRHSSLPEGGGSRSKAVWKPFSRWRSLQPTVQARSLCREHWQLFEWISKGLLSTAYIGFLIVACLLDFPRALALFVITCVVLVFLAYNLLKRLLGSKLKKCVKFQGHSCLSLWLKRGLALAAGLGVILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFVAFQWLGDQIRVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQT... | null | null | cytidine transport [GO:0015861]; nucleoside import across plasma membrane [GO:0180015]; nucleoside transmembrane transport [GO:1901642]; pyrimidine nucleobase transport [GO:0015855]; uridine transport [GO:0015862] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | azole transmembrane transporter activity [GO:1901474]; pyrimidine nucleobase transmembrane transporter activity [GO:0005350]; pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]; uridine transmembrane transporter activity [GO:0015213] | PF07670;PF07662;PF01773; | null | Concentrative nucleoside transporter (CNT) (TC 2.A.41) family | PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity. {ECO:0000250|UniProtKB:O00337}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. | CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + thymidine(out) = Na(+)(in) + thymidine(in); Xref=Rhea:RHEA:69891, ChEBI:CHEBI:17748, ChEBI:CHEB... | null | null | null | null | FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum ... | Mus musculus (Mouse) |
E9PY46 | IF140_MOUSE | MALYFDHRIKAPDTPSSPSHITWHPTHPFLAVASISPSSGGNVDIYLEQGEPVPDTHIERSFQATSLCWHPTRLILAIGWETGEVIMFNKQDKEQHTVPLPHTTDIAILSWSTSGSCLVSGDKLGVLLLWRLDQRGRVQGTPLLKHEYGKALTHCIFRLPPPGEDLVQLAKAAVSGDEKALDMFNWRKSSFGSFLKTGSQEGLSFFVSLMDGTVHYVDEKGKTAQVASTDSSIQTLFYIERREALVVVTENLLLSLYVVTPEGEAEEVMKVKLSGKTGCRADITLIEGSLLVTAIGEPVLRFWDLERGENYILSLQEKFG... | null | null | cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; embryonic brain development [GO:1990403]; embryonic camera-type eye development [GO:0031076]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic digit morphogenesis [GO:0042733]; heart development [GO:0007507]; intraciliary r... | axoneme [GO:0005930]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cone photoreceptor outer segment [GO:0120199]; intraciliary transport particle A [GO:0030991]; non-motile cilium [GO:0097730]; photoreceptor connecting cilium [GO:0032391] | null | null | 1.25.40.470;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22282595, ECO:0000269|PubMed:24009529, ECO:0000269|PubMed:24619649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96RY7}. Cell projection, cilium {ECO:0000269|PubMed:22282595, ECO:0000269|P... | null | null | null | null | null | FUNCTION: 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) (By similarity). Plays a pivotal role in proper development and function of ciliated cells through its role in ciliogenesis and/or cilium maintenance (PubMed:... | Mus musculus (Mouse) |
E9PY61 | GP179_MOUSE | MGARAVVISSLAWGLLSCCFLCSGALGSQRPLRSLPPLPSQAKPRSEPMWMPPKGAEAALAFLYSGDVQRLSGANCSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLECHEGQLRPGWLVTVSATFYGLKPDLTPEVRGQVQMDIDLQSVDINQCASGPGWYSNTHLCDLNSTQCVPLESQGFVLGRYLCRCR... | null | null | protein localization to plasma membrane [GO:0072659]; response to light stimulus [GO:0009416]; visual perception [GO:0007601] | dendrite terminus [GO:0044292]; postsynaptic membrane [GO:0045211] | G protein-coupled receptor activity [GO:0004930] | PF00003; | null | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22689652}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:24114537}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:22325362, ECO:0000269|PubMed:24114537, ECO:0000269|PubMed:24790... | null | null | null | null | null | FUNCTION: Orphan receptor involved in vision (PubMed:22325362, PubMed:24114537, PubMed:24790204, PubMed:30282023). Required for signal transduction through retinal depolarizing bipolar cells (PubMed:22325362, PubMed:24114537, PubMed:24790204, PubMed:33922602). Acts as an atypical G-protein coupled receptor that recruit... | Mus musculus (Mouse) |
E9PYH6 | SET1A_MOUSE | MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVSDSKYTPVEDLQDPRCHVRSKARDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAAAETTEARRRSSSDTAAYPAGTTVGGTPGNGTPCSQDTNFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDSFSRRHFSTSSAP... | 2.1.1.364 | null | brain development [GO:0007420]; DNA damage response [GO:0006974]; methylation [GO:0032259]; positive regulation of gene expression [GO:0010628]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of stem cell proliferation [GO:2000648]; regulation of chromatin organization [GO:... | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; histone methyltransferase complex [GO:0035097]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]; histone H3K4 trimethyltransferase activity [GO:0140999]; RNA binding [GO:0003723] | PF11764;PF00076;PF00856; | 3.30.70.330;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550110}. Nucleus speckle {ECO:0000250|UniProtKB:O15047}. Chromosome {ECO:0000250|UniProtKB:O15047}. Cytoplasm {ECO:0000250|UniProtKB:O15047}. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B... | CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1... | null | null | null | null | FUNCTION: Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where tr... | Mus musculus (Mouse) |
E9PYI1 | ZN568_MOUSE | MERLSQMAGRRAWCAEDSVPRQEEEDRTRPSKTVTFKDVAVDLTQEEWQQMKPAQRALYRDVMLETYSNLVTVGCQVTKPDVIFKLEQAEEPWVLEEEMFWRRSPEAARGRMKSFAFKDMAKDLRFEDVVIYFSLEEWECLRHSHRNLYRAVMLDNYSNLLSLSLADTKPRVVSLLEQGKEPWMVMRNETKIWHPDWVSRTEAKDSSKIKTLQEKMAKKHTCPTLEDSKTRGDREVTRELEGQQVHQEGHLRQAAVTSVERPDSVQCTAHREAHPGGKPCSSEKSQKTSLCQPPPIEREQLHSKAKASEHAQHGKVFNSC... | null | null | convergent extension involved in axis elongation [GO:0060028]; convergent extension involved in neural plate elongation [GO:0022007]; embryonic placenta morphogenesis [GO:0060669]; in utero embryonic development [GO:0001701]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transc... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor binding [GO:0001222] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:23071813}. | null | null | null | null | null | FUNCTION: Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction (PubMed:22110054, PubMed:27658112). Essential during embryonic development, where it acts as direct repressor of IGF2-P0, placental-specific t... | Mus musculus (Mouse) |
E9PYK3 | PARP4_MOUSE | MTLGIFANCIFCLKVKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQRRLLDVRNYDPLSPAPAAPPAERSRSEVQSEYLPSDNTPEKENTEVTEVSAENVEIPPFLQDFEVVKYNILEKVGGPETVVVELQSSQDPESCPFVITAHFLLADQKTRRESTGKQTSEGAIEYYESYVEDLKRQGFLLQEHFTAEATQLASEKLQALLLEEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDSPGQLQKTMAEFYRL... | 2.4.2.- | null | inflammatory response [GO:0006954]; protein modification process [GO:0036211] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spindle [GO:0005819]; spindle microtubule [GO:0005876] | enzyme binding [GO:0019899]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; nucleotidyltransferase activity [GO:0016779] | PF00533;PF06346;PF00644;PF08487;PF13768; | 3.90.228.10;3.40.50.10190;3.40.50.410; | ARTD/PARP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}. | CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:Q9UKK3}; CATALYTIC ACTIVITY:... | null | null | null | null | FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000250|UniProtKB:Q9UKK3}. | Mus musculus (Mouse) |
E9PYY5 | DNAI4_MOUSE | MHSSPTSTRKQASFAASASAQPRKSISFINPSKSSAGKGYAASNPNKLAVSRTMGFLTDMKPAEKLNVPSAKTVQVLDSKGVDVTPRPLYHPDPHAASAKPNKLLTSQEGSLGSDYISSYSLYQNTLNPSMLGQYTRSVLGSSSVSKSSISTTESMSEDLEDSSYKRDRLASFTDVRVLRSTAEAAISKEELEKTIEIILTETETLRFFDLPTVMFSTESEEAEKIIEKNKKYETLCRNRLGNDLYVERMMQTFNGAPKNKEVQCEKIILEEKGVVATTWDLYDSYNIPETLLAAKRSGYSSKGSLPAKDRDPKIQDSES... | null | null | axonemal dynein complex assembly [GO:0070286]; cilium movement [GO:0003341]; hematopoietic progenitor cell differentiation [GO:0002244] | axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; dynein axonemal particle [GO:0120293]; motile cilium [GO:0031514] | dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503] | PF00400; | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30060180}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30060180}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6GPB9}. | null | null | null | null | null | FUNCTION: Plays a critical role in the assembly of axonemal dynein complex, thereby playing a role in ciliary motility. {ECO:0000269|PubMed:30060180}. | Mus musculus (Mouse) |
E9PZ19 | TUTLB_MOUSE | MIWYVATLIASVISTRGLVAQGAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLGASAKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLT... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; nervous system development [GO:0007399]; positive regulation of inhibitory postsynaptic potential [GO:0097151]; synaptic membrane adhesion [GO:0099560] | dendrite [GO:0030425]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; postsynaptic specialization of symmetric synapse [GO:0099629] | kinase binding [GO:0019900] | PF13895;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, Turtle family | PTM: N-glycosylated and sialylated. Not significantly O-glycosylated. {ECO:0000250|UniProtKB:D3ZB51}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23751499}; Single-pass type I membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:D3ZB51}; Single-pass type I membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:D3ZB51}. | null | null | null | null | null | FUNCTION: Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development (By similarity). May mediate homophilic cell adhesion (PubMed:23751499). {ECO:0000250|UniProtKB:D3ZB51, ECO:0000269|PubMed:23751499}. | Mus musculus (Mouse) |
E9PZ36 | PKHD1_MOUSE | MMLAWLVSLLSMEVLLLAKPYSSFQFEPAEGSLAGGTWITVVFDGLDRSILYPNNGSQLQIDLVSVAIPTLRIPCDVSPAFVDLPVVTCQTRSLPSEADAGPYSLEMRSGEQVLGTPCPGSLDSCTFKFSKDQTPVLYQVYPASGVPGEVVSVYGRVITTWLETFDPDVDYIESPLILEAREDKWLTPCSLINRQTGSCFPIQEEHGLGNVQCRVEGDYIGSQNVSFSVFNKGRSMVHKEAWLISAKQELFLYQTYPEILSVFPKVGSLGGRTDIIITGDFFDPSARVTIAGIPCDIRYVSPRKIECTTRAPGNEARLTA... | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell-cell junction organization [GO:0045216]; cilium assembly [GO:0060271]; epithelial cell morphogenesis [GO:0003382]; establishment of centrosome localization [GO:0051660]; establishment of mitotic spindle orientation [GO:0000132]; intracellular calcium ion ... | 9+0 non-motile cilium [GO:0097731]; apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitotic spindle [GO:0... | null | PF13229;PF10162;PF01833; | 2.60.40.10;2.160.20.10; | null | PTM: Palmitoylated (PubMed:20048263). Palmitoylation facilitates the trafficking to the cilia and membrane targeting (PubMed:20048263). {ECO:0000269|PubMed:20048263}.; PTM: N-glycosylated. {ECO:0000269|PubMed:22021705, ECO:0000269|PubMed:28729032}.; PTM: Several proteolytic cleavages occur within the extracellular doma... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08F94}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P08F94}. Apical cell membrane {ECO:0000269|PubMed:18202188}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P08F94}. Cell projection, cilium {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/or ensures the maintenance of the architecture of the lumen of the kidney (PubMed:18235088, PubMed:20875407). Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulat... | Mus musculus (Mouse) |
E9PZJ8 | ASCC3_MOUSE | MALPRLTGALRSFSNVTKQDNYNEEVADLKLKRSKLHEQVLDFGLTWKKIVKFLNEKLEKNKMQNINEDLKDILQAAKQIVGTDNGREAIESGAAFLFMTFHMTDSVGYMETKAIRQTFGPFPSSSATSACNATNRIISHFSQDDLTAFVQMAENPCNDRVVFGKNLAFSFDMYDLDHFDELPINGESQKTISLDYKKFLNEQFQEPYTPELKPVEKTNGSLLWCEVEKYLNATLKEMTEAARVEDLCCTLYDMLASAKSGDELQDELFELLGPEGLDLIEKLLQNRITIVDRFLNSSSDHKFQVLQDSCKKILGENSKP... | 3.6.4.12 | null | cell population proliferation [GO:0008283]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA duplex unwinding [GO:0032508]; rescue of stalled ribosome [GO:0072344]; ribosome disassembly [GO:0032790]; ribosome-associated ubiquitin-dependent protein catabolic process [GO:1990116] | activating signal cointegrator 1 complex [GO:0099053]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; DNA repair complex [GO:1990391]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; nucleic acid binding [GO:0003676] | PF00270;PF00271;PF02889; | 1.10.150.20;2.60.40.150;3.40.50.300;1.10.3380.10;1.10.10.10; | Helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}. Nucleus speckle {ECO:0000250|UniProtKB:Q8N3C0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N3C0}. Note=Colocalizes with ALKBH3 and ASCC2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. {ECO:0000250|UniProtKB:Q8N3C0}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q8N3C0}; | null | null | null | null | FUNCTION: ATPase involved both in DNA repair and rescue of stalled ribosomes. 3'-5' DNA helicase involved in repair of alkylated DNA: promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3, enabling ALKBH3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions. Also involved... | Mus musculus (Mouse) |
E9PZM4 | CHD2_MOUSE | MMRNKDKSQEEDSSLHSNASSRSASEEVSGSDSGSQSESEQGSEPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNVKEEASSGSESGSPKRRGQRQLKKQEKWKQDPSEDEQEQGTSAESEAEQKKGKARRPVPRRTVPKPQVKKQPKIQRGKRKKQESSDDDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSDDLIEMTGEGGDEQQDNSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSDDFDTEREEGEVQYLIKWKGWSYIHST... | 3.6.4.12 | null | DNA damage response [GO:0006974]; gene expression [GO:0010467]; hematopoietic stem cell differentiation [GO:0060218]; muscle organ development [GO:0007517]; nucleosome organization [GO:0034728]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:00009... | PF18375;PF13907;PF00385;PF00271;PF00176; | 2.40.50.40;6.10.140.1440;1.10.10.60;3.40.50.300;3.40.50.10810; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22569126}. Note=Binds to myogenic gene promoters. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to th... | Mus musculus (Mouse) |
E9PZQ0 | RYR1_MOUSE | MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSGCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLGLTEDQGLVVVDASKAHTKATSFCFRIS... | null | null | calcium ion transport [GO:0006816]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; muscle contraction [GO:0006936]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; ossification involved in ... | calcium channel complex [GO:0034704]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; junctional membrane complex [GO:0030314]; membrane [GO:0016020]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0... | ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; protease binding [GO:0002020]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; voltage-gated calcium channel activity [GO:0005245] | PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR1 subfamily | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844. {ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754}.; PTM: Activated by reversible S-nitrosylation (PubMed:22036948). Repeated... | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:7621815}; Multi-pass membrane protein {ECO:0000255}. Note=The number of predicted transmembrane domains varies between orthologs. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:7621815}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:18003898, PubMed:21156754, PubMed:7515481, PubMed:7621815). Repeated very... | Mus musculus (Mouse) |
E9PZZ1 | PRD13_MOUSE | MPAHVTPRTEDARRGAGPSSACGCSWFCHLRPVEDPASPSVCLAAVATMHGTSRTSATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVLSGGGGRAFLPQEHAARPGASPVAEGLGLPPKPTVPDLTAPVQAIALRPQAPAAQLAQACGARESIKREASLAPLATSPPPGKWGTPKKGKEQPDRAHSQFLGIVGGSSGG... | 2.1.1.- | null | GABAergic neuron differentiation [GO:0097154]; hypothalamus cell differentiation [GO:0021979]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neurogenesis [GO:0022008]; regulation of gene expression [GO:0010468] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone methyltransferase activity [GO:0042054]; metal ion binding [GO:0046872]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. Is required for the differentiation of Kiss1-expressing neurons in the arcuate (Arc) nucleus of the hypothalamus. Is a critical regulator of GABAergic cell fate in the cerebellum, required for normal postnatal cerebellar development (PubMed:34730112). {ECO:000025... | Mus musculus (Mouse) |
E9Q0N2 | PTPRH_MOUSE | MARAGGNCGVWRSLVLLGLYGCSVVRAAGTSVTVDRHAPASSYEFSMWVEKDGVSSSPQIPVTTAAPNPVRNLRVEGQNNISISLSWEPPDQSSLQGLTYWTQCSRHGGQTETRNTTDTSVTVDGLDPGSSYECSVWVEKDGLYSKNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTTDTSITVDGLDPGSSYECSVWVEKDG... | 3.1.3.48 | null | peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [GO:1990264] | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; receptor complex [GO:0043235] | protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF00102; | 1.20.5.100;2.60.40.10;3.90.190.10; | null | null | SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD43}. Apical cell membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membran... | 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:0000269|PubMed:26195794}; | null | null | null | null | FUNCTION: Protein phosphatase that may contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibitio... | Mus musculus (Mouse) |
E9Q0S6 | TENS1_MOUSE | MGCTVSLVCCEALEPLPSCGPQPPGTPPGPARPERCEPGGAAPDPRRRLLLQPEDLEAPKTHHFKVKAFKKVKPCGICRQAITREGCVCKVCSFSCHRKCQAKVAAPCVPPSSHELVPITTETVPKNVVDVGEGDCRVGSSPKNLEEGGSMRVSPSIQPQPQSQPTSLSRNTSVSRAMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRF... | 3.1.3.- | null | cell-substrate junction assembly [GO:0007044]; fibroblast migration [GO:0010761] | cell surface [GO:0009986]; cell-substrate junction [GO:0030055]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925] | actin binding [GO:0003779]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721] | PF08416;PF10409;PF00017; | 2.60.40.1110;3.30.60.20;2.30.29.30;3.90.190.10;3.30.505.10; | PTEN phosphatase protein family | PTM: Extensively phosphorylated on serine and threonine residues in a p38 MAPK-dependent manner which reduces interaction with DLC1 and increases interaction with tyrosine-phosphorylated proteins including BCAR1/p130cas and PTK2/FAK. The majority of the phosphorylated Ser/Thr residues are immediately adjacent to a prol... | SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:Q9HBL0}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9HBL0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9HBL0}. Note=Localizes to both focal adhesions and fibrillar adhesions. Localized at the cell periphery preferentially to fibrillar adhesions r... | null | null | null | null | null | FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase (By similarity). Involved in fibrillar adhesion formation (By similarity). Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMe... | Mus musculus (Mouse) |
E9Q236 | MRP4_MOUSE | MLPVHTEVKPNPLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKKDSRKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMN... | 7.6.2.-; 7.6.2.2; 7.6.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O15439}; | bile acid and bile salt transport [GO:0015721]; cAMP transport [GO:0070730]; cilium assembly [GO:0060271]; export across plasma membrane [GO:0140115]; fatty acid derivative transport [GO:1901571]; leukotriene transport [GO:0071716]; organic hydroxy compound transport [GO:0015850]; positive regulation of smooth muscle c... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; external side of apical plasma membrane [GO:0098591]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088] | ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; alcohol transmembrane transporter activity [GO:0015665]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transme... | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | null | PTM: N-glycosylated; leading to substrate-selective effects on its transport activity. {ECO:0000250|UniProtKB:O15439}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12883481, ECO:0000269|PubMed:15314169}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:15314169}; Multi-pass membrane protein {ECO:0000255}. Note=Its localization to the basolateral or apical membranes is tissue-dep... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000305|PubMed:15314169, ECO:0000305|PubMed:17210706}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=R... | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cycl... | Mus musculus (Mouse) |
E9Q2M9 | WDFY4_MOUSE | MEAEDLSKTEDRPEDPGFQNEGQSPAVKPSFSLEGQSPGPSVLWDMLEQKFLDYQQLMPRNPEERRKNLLSLLPLFLKAWEHSVGIICFRSLQRLAEDVSDQLAQEIQQALAGKPAEQARAAAGQLLQWKSDADQDGNLLLKSVYVLTGTDSETLGRVVDSGLPALLLQCLYLFFAFPVEKDDLLESDVQGQRMFVQMLLNICSESQGLEGLLSGSELQSLLIATTCLREHSCLFWKQPTFCVLRAISKAQSPSVIQYLRTADCVRLSVQNLSKLADTLPAPEVSEAVSLILNFVRDSYPISSALLLEFENGEGYPLLLK... | null | null | antigen processing and presentation [GO:0019882]; autophagy [GO:0006914]; CD8-positive, alpha-beta T cell activation [GO:0036037]; cellular response to virus [GO:0098586] | early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783] | null | PF02138;PF14844;PF00400; | 1.10.1540.10;2.30.29.30;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:30409884}. Endoplasmic reticulum {ECO:0000269|PubMed:30409884}. | null | null | null | null | null | FUNCTION: Plays a critical role in the regulation of cDC1-mediated cross-presentation of viral and tumor antigens in dendritic cells (PubMed:30409884). Mechanistically, acts near the plasma membrane and interacts with endosomal membranes to promote endosomal-to-cytosol antigen trafficking (PubMed:30409884). Also plays ... | Mus musculus (Mouse) |
E9Q2Z1 | CECR2_MOUSE | MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRWELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQLYKLLSEDFLPEICNMIAQKGKRPQRTKPELQHRFMSDHLSIKSIKLEET... | null | null | chromatin remodeling [GO:0006338]; cochlea development [GO:0090102]; execution phase of apoptosis [GO:0097194]; inner ear receptor cell stereocilium organization [GO:0060122]; neural fold formation [GO:0001842]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; single fertilization [GO:0007338] | CERF complex [GO:0090537]; euchromatin [GO:0000791]; ISWI-type complex [GO:0031010] | ATP-dependent chromatin remodeler activity [GO:0140658] | PF00439; | 1.20.920.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BXF3}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the ATP-dependent CERF-1 and CERF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity). The complexes do not have the ability... | Mus musculus (Mouse) |
E9Q394 | AKP13_MOUSE | MKLSPQQAPLYGDCVVTVLLAEEDKVEDDAIFYLIFSGSTLYHCTSTRKVSSDTLETIAPGHDCCETVKVLLCASREGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLDRSGPPSRDVNSLDEKVALAFRHLKLPAEWNVLGTDHTLHDGGPRETLMHFAVRLGLLRLTWFLLQKPGGRGALSIHNKEGATPVSLALERGYHELHQLLTEENAGEPDSWSSLSYEIPYGDCSVRHHRELDIYTLTSESESHREPHGDSCTGHISKLMNIQQQLMKTNLKQMDNLMPLMVTAQDSSCVPSVPETDGLFLP... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process [GO:0086023]; adrenergic receptor signaling pathway [GO:0071875]; bone development [GO:0060348]; cardiac muscle cell differentiation [GO:0055007]; cell growth involved in cardiac muscle cell development [GO:0061049]; G protein-... | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | guanyl-nucleotide exchange factor activity [GO:0005085]; MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090] | PF17838;PF00621; | 3.30.60.20;1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12802}. Cytoplasm {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20139090}. Nucleus {ECO:0000250|UniProtKB:Q12802}. Membrane {ECO:0000250|UniProtKB:Q12802}; Peripheral mem... | null | null | null | null | null | FUNCTION: Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. May also activate other Rho family mem... | Mus musculus (Mouse) |
E9Q3E1 | AL3B2_MOUSE | MSAAETGSEPSQGAGPSEATLHSLREAFNAGRTRPTEFRTAQLRSLGRFLQENKELLQDALAKDVGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSSAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETRQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQERLVPALQNSITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGG... | 1.2.1.3 | null | cellular aldehyde metabolic process [GO:0006081]; ethanol catabolic process [GO:0006068]; lipid metabolic process [GO:0006629] | cytoplasm [GO:0005737]; lipid droplet [GO:0005811] | 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878] | PF00171; | null | Aldehyde dehydrogenase family | PTM: Geranylgeranylation is important for localization to lipid droplets and enzyme activity. {ECO:0000269|PubMed:25286108}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25286108}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:25286108}; CATALYTIC ACTIVITY: Reaction=2 H(+) + hexad... | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. {ECO:0000250|UniProtKB:P48448}. | null | null | FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty acids. {ECO:0000269|PubMed:25286108}. | Mus musculus (Mouse) |
E9Q3L2 | PI4KA_MOUSE | MAAAGARGGGGGGGGGGGGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEAILQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVSPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGIPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSISPLFNGI... | 2.7.1.67 | null | modulation by host of viral process [GO:0044788]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; reorganization of cellular membranes to establish viral sites of replication [GO:0140754] | cytoplasm [GO:0005737]; Golgi-associated vesicle membrane [GO:0030660]; plasma membrane [GO:0005886] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF00454;PF00613;PF19274; | 1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42356}. Cell membrane {ECO:0000250|UniProtKB:P42356}. Note=Localization to the plasma membrane is mediated by the PI4K complex and association with EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Localization to the plasma membrane is regul... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|... | null | null | null | null | FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000250|UniProtKB:P42356}. | Mus musculus (Mouse) |
E9Q3M5 | S4A5_MOUSE | MKVDEEKAGVKKLDPTSYKRRQPEQDFPSIHIGFPVPSYSQRKSDSKGHLSGLQKVQWSLKPGKPQQELAGPGIRASSQGGAVDFTKRTRSPAAEQLQDILGEEDEAPNPTLFTEMDTLQHDGDQMEWKESARWIKFEEKVEEGGERWSKPHVSTLSLHSLFELRTCLQTGTVLLDLDSCSLPQIIDDVIEKQIEDGLLRPELRERVSYVLLRKHRHQTKKPIHRSLADIGKSVSTTNRSSARSSSAGPTLHRSTEDLRIRQSTSYGHLCHAQSRSMNDISHTPNTDQRKNKFMKKIPKDSEASNVLVGEVDFLDQPFIA... | null | null | bicarbonate transport [GO:0015701]; cerebrospinal fluid secretion [GO:0033326]; epithelial cell development [GO:0002064]; mitochondrion distribution [GO:0048311]; monoatomic ion transport [GO:0006811]; regulation of gene expression [GO:0010468]; regulation of intracellular pH [GO:0051453]; regulation of systemic arteri... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | monoatomic anion transmembrane transporter activity [GO:0008509]; sodium:bicarbonate symporter activity [GO:0008510]; solute:inorganic anion antiporter activity [GO:0005452] | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9BY07}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6RI88}; Multi-pass membrane protein {ECO:0000255}. Note=Localized predominantly to the basolateral sinusoidal membrane in hepatocytes. {ECO:0000250|UniP... | CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9BY07}; CATALYTIC ACTIVITY: Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3 hydrogencarbonate(in) + Na(+)(in); Xref=Rh... | null | null | null | null | FUNCTION: Mediates sodium- and bicarbonate-dependent electrogenic sodium bicarbonate cotransport, with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. {ECO:0000269|PubMed:18588858}. | Mus musculus (Mouse) |
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