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
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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 levels of copper. Cu-mb contributes to the switchover from soluble methane monooxygenase (sMMO) to the membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO subunit A. It also stimulates the enzymatic activity of pMMO. In the absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+), Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active process, which may involve TonB-dependent transporters, and as such does not involve porins. Cu-Mb can be taken up by other methanotrophic bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like activity. Shows reductant-dependent oxidase and hydrogen peroxide reductase activities. Reduces copper-levels in liver in a rat model of Wilson disease. {ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16207923, ECO:0000269|PubMed:16332035, ECO:0000269|PubMed:16445286, ECO:0000269|PubMed:17070918, ECO:0000269|PubMed:17615240, ECO:0000269|PubMed:18372044, ECO:0000269|PubMed:20817303, ECO:0000269|PubMed:20961038, ECO:0000269|PubMed:21242075, ECO:0000269|PubMed:21254756, ECO:0000269|PubMed:21900235}. | Methylosinus trichosporium |
E4MYY0 | HCS_KITSK | MAEFEIPDFYVPFPLECNPHLEEASRAMWEWIDANGLAPTERARDRMRRTGADLSGAYVWPRADLDTLTIGLKWIALTFRIDDQIDEDDTAERLPARMTAIDELRGTLHGLPVSGRSPTARALGALWQETALGRPATWCDAFIGHFEAFLQTYTTEAGLNAHGAGLRLDDYLDRRMYSVGMPWLWDLDELRLPIFLPGSVRTCGPMNKLRRAGALHIALVNDVFSVERETLVGYQHNAVTIIREAQGCSLQEAVDQVAVLVEAQLHTVLQARQELLEELDRQALPSRAREAAVDYAANVAANLSGQLVWHSSVERYAVDDLQSAADPRATPTTSSLGI | 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 | MNDPRSKMMISPGLLPTESLLDSLILISNEVSSMQKFPLVQIKNVSSMIRRIKLLSSLFEEIQESDSPLPPSSILCFIEIFSVITRVKVLIQECTDGSSLWSLIQLDFISNQFFVLVKEMGRALDILPLNLLNVAQDIKEQVDLLHKQSKRVELELFIDPREVQRRENLFEVMSKNCLQNKKTNNNKGFIDFVKVEEIMCSIGLRTLSDYVEEISKLEVEAQNQAGTGGLIVVSNINNLMSLVSYTKSMVFRNDGESEECKPISMFLYNKSKIHDNDSSSSSSFSQSMMTVNIPDEFRCPISLDLMRDPVIVSSGHTYDRISIAEWINSGHHTCPKSGQRLIHTALIPNYALKSLVHQWCYENNVKMNEAITKNNNSSSKRHKNENAIDHISENKASKDAVKMTAEFLVGKLATGSTDIQRQSAYEIRLLAKTGMDNRRIIAEVGAIPFLVTLLVSKDSRIQEHVVTALFNLSIYDNNKILIMAAGAIDNIVEVLEFGKTMEARENAAAAIYSLSMIDDCKVQIGASSRAIPALVGLLKEGTIIGKRDAATALFNLAVYNPNKLSIVKSGAVTLLVELLMDDKAGITDDSLAVLAVLLGCSEGLEEIKNSKSLVPLLIDLLRFGSVKGKENSITLLLGLCKEEGELVAMRLLANPRSIPSLQSLAADGSLRARRKADALLRLLNRCCSQPHHSL | 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 ligase activity-dependent manner (PubMed:26839127). Negative regulator of the LYK3 signaling pathway leading to nitrogen-fixing symbiosis (eg. infection and nodulation) by rhizobia. May be involved in the discrimination of rhizobium strains producing variant Nod factors (PubMed:20971894). {ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:26839127}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
E4Q361 | GH1A_CALOW | MSFPKGFLWGAATASYQIEGAWNEDGKGESIWDRFTHQKGNILYGHNGDVACDHYHRHEEDVSLMKELGIKAYRFSTAWARIFPDGFGNINQKGLEFYDKLINELVENGIEPVVTLYHWDLPQKLQDIGGWANPEIVNYYFEYAMLIINRYKDKVKKWITFNEPYCIAFLGHWHGIHAPGIKNFKVAMDVVHNIMLSHFKVVKAVKENNIDVEIGITLNLTPVYLQTERLGYKVSEIEREMVNLSSQLDNELFLDPVLKGSYPQKLLDYLVQKDLLDSQKVNNMQQEVKENFIFPDFLGINYYTRSVRLYDENSGWIFPIRWEHPAGEYTEMGWEVFPQGLFDLLIWIKESYPQIPIYITENGAAYNDKVEDGRVHDQKRVEYLKQHFEAARKAIKNGVDLRGYFVWSLIDNFEWAMGYTKRFGIIYVDYETQKRIKKDSFYFYQQYIKENS | 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:0000269|PubMed:27141233}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:27141233}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.; EC=3.2.1.74; Evidence={ECO:0000269|PubMed:27141233}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:27141233}; | 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 for p-nitrophenyl beta-D-cellobioside (pNPC) (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; KM=7.18 mM for p-nitrophenyl beta-D-xylopyranoside (pNPX) (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; KM=15.65 mM for cellobiose (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Vmax=5100 umol/min/mg enzyme with pNPGal as substrate (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Vmax=4027 umol/min/mg enzyme with pNPGlu as substrate (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Vmax=1065 umol/min/mg enzyme with pNPC as substrate (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Vmax=736 umol/min/mg enzyme with pNPX as substrate (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Vmax=2424 umol/min/mg enzyme with cellobiose as substrate (at pH 5.5 and 75 degrees Celsius) {ECO:0000269|PubMed:27141233}; Note=kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate. {ECO:0000269|PubMed:27141233}; | 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 at 70 and 90 degrees Celsius and less than 50% below 60 degrees Celsius. Half-life is about 11 hours at 80 degrees Celsius and about 1.5 hours at 85 degrees Celsius. {ECO:0000269|PubMed:27141233}; | 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), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them. {ECO:0000269|PubMed:27141233}. | Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL) |
E4QP00 | HMFO_METS6 | MTDTIFDYVIVGGGTAGSVLANRLSARPENRVLLIEAGIDTPENNIPPEIHDGLRPWLPRLSGDKFFWPNLTIHRAAEHPGITREPQFYEQGRLLGGGSSVNMVVSNRGLPRDYDEWQALGADGWDWQGVLPYFIKTERDADYGDDPLHGNAGPIPIGRVDSRHWSDFTVAATQALEAAGLPNIHDQNARFDDGYFPPAFTLKGEERFSAARGYLDASVRVRPNLSLWTESRVLKLLTTGNAITGVSVLRGRETLQVQAREVILTAGALQSPAILLRTGIGPAADLHALGIPVLADRPGVGRNLWEHSSIGVVAPLTEQARADASTGKAGSRHQLGIRASSGVDPATPSDLFLHIGADPVSGLASAVFWVNKPSSTGWLKLKDADPFSYPDVDFNLLSDPRDLGRLKAGLRLITHYFAAPSLAKYGLALALSRFAAPQPGGPLLNDLLQDEAALERYLRTNVGGVWHASGTARIGRADDSQAVVDKAGRVYGVTGLRVADASIMPTVPTANTNLPTLMLAEKIADAILTQA | 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:24802551}; CATALYTIC ACTIVITY: Reaction=benzylthiol + O2 = benzothialdehyde + H2O2; Xref=Rhea:RHEA:53792, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:137674, ChEBI:CHEBI:137675; Evidence={ECO:0000269|PubMed:25284255}; | 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=0.3 mM for 4-hydroxybenzyl alcohol {ECO:0000269|PubMed:24271187}; KM=1.44 mM for 4-aminobenzyl alcohol {ECO:0000269|PubMed:24271187}; KM=0.08 mM for 4-chlorobenzyl alcohol {ECO:0000269|PubMed:24271187}; KM=0.07 mM for cinnamyl alcohol {ECO:0000269|PubMed:24271187}; KM=0.59 mM for 2,4-hexadien-1-ol {ECO:0000269|PubMed:24271187}; KM=0.73 mM for vanillyl alcohol {ECO:0000269|PubMed:24271187}; KM=3.5 mM for phenylmethanethiol {ECO:0000269|PubMed:25284255}; KM=15 mM for (4-nitrophenyl)methanethiol {ECO:0000269|PubMed:25284255}; KM=0.078 mM for (4-nitrophenyl)methanol {ECO:0000269|PubMed:25284255}; Note=kcat is 9.9 sec(-1) with 5-(hydroxymethyl)furfural as substrate. kcat is 21.1 sec(-1) with 1,4-benzenedimethanol as substrate. kcat is 14.0 sec(-1) with 1,3-benzenedimethanol as substrate. kcat is 13.5 sec(-1) with benzyl alcohol as substrate. kcat is 7.2 sec(-1) with 4-hydroxybenzyl alcohol as substrate. kcat is 17.1 sec(-1) with 4-aminobenzyl alcohol as substrate. kcat is 9.5 sec(-1) with 4-chlorobenzyl alcohol as substrate. kcat is 17.0 sec(-1) with cinnamyl alcohol as substrate. kcat is 13.3 sec(-1) with 2,4-hexadien-1-ol as substrate. kcat is 21.0 sec(-1) with vanillyl alcohol as substrate (PubMed:24271187). kcat is 2.1 sec(-1) with phenylmethanethiol as substrate. kcat is 3.0 sec(-1) with (4-nitrophenyl)phenylmethanethiol as substrate. kcat is 4.5 sec(-1) with (4-nitrophenyl)methanol as substrate (PubMed:25284255). {ECO:0000269|PubMed:24271187, ECO:0000269|PubMed:25284255}; | 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 and requires the spontaneous hydration of aldehyde groups for their oxidation (PubMed:24271187, PubMed:24802551). To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls (PubMed:25284255). {ECO:0000269|PubMed:24271187, ECO:0000269|PubMed:24802551, ECO:0000269|PubMed:25284255}. | 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-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648, ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700, ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704, ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; | 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 ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Shows complement-dependent hemolysis (PubMed:21692149). Also induces dermonecrosis, vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000250|UniProtKB:P0CE80, ECO:0000269|PubMed:21692149}. | Loxosceles laeta (South American recluse spider) (Scytodes laeta) |
E5D8F2 | POLG_HRV15 | MGAQVSRQNNGTHENGVTASNGSVIKYFNINYYKDSASSGLSRQDFSQDPSKFTQPLVDTLTNPALMSPSVEACGYSDRLKQITIGNSTITTQDSLHTVLAYGEWPTYLSDIDATSVDKPTHPETSADRFYTLDSVEWQVGSHGWWWKLPDALKDMGVFGQNMYYHSMGRSGFIIHTQCNATKFHSGALIVAVIPEHQLAYVGGVKVNVGYDHTHPGQSGHQIRGPSQSNDRSGGKPDEDPLFNCNGTLLGNITIFPHQIINLRTNNSSTIVVPYINCVPMDNMLKHNNLSLVIIPLVPLRPGSSGINSVPITVTIAPYKSEFSGAMEAQRQGLPTRLPSGSQQFMTTEDEQSPNILPGFHPSKKIHIPGMITNVMHMARVDSFIPINNIQGEVGKVSMYYITVTKKTVTERILVLPLEMSNTLFATTLLGEVLNYYANWSGSITITFMCVCDAFSTGKFLVAYTPPGGKLPEDRKQAMLGVHIIWDLGLQSSCTIVVPWISSGFYRRTKADSFTHGGYVSLWYQTAFVPPVSGGTGSILATCSACPDMSVRMLRDSPMMEQKNELQNNDDPVENFVESTLKEVLVVPDTKPSGPQHTTKPSILGAMEIGASSNATPESTIETRYVYNTNTNAEADVEMFLGRSALWGKVTLTRQYAKWEINFQEQAHIRKKFEFFTYLRFDMEVTIVTNNTGLMQIMFVPPGIDHPETHDDRKWDSASNPSVFFQPKSGFPRFTIPFTGLASAYYMFYDGYDKPKGSDNNEYGIAPTNDMGLLCFRTLDNSGGNDVKIYVKPKHITAWVPRPPRATQYTHKYSTNYHYKPNSSGPDEHVLKDRHFIKTRPLISSAGPSDMFVHTRDAIYKCAHLTNPTDETILLALTADLQVDSTNVPGPDVIPCCDCTAGCYYSRSKDRYFPVECVSHDWYEIQESGYYPKHIQYNLLIGEGHCEPGDCGGKLLCKHGVIGMITAGGDNHVAFTDLRPYSSLSEHQGVISDYFTQLGNAFGEGFTTNIQDHFSQITKSISDKFTSKAIKWLVRIISALTIMIRNNSDLPTILATLSLLGCSSSPWSFLKDKICSWLQIQRPASKQSDSWLRKFTECCNAAKGLEWISIKIGKFIDWLKGKLVPAVQRKRDTLDRCKKISLLEEQVNGFSSASSEAQQQLIVEVDTLKKGLDELAPLYASENKRVTKIQKDLKQLSAYLKNHRHEPVCLLLHGNPGCGKSLVTTIIARGLTQEAQVYSLPPDPKYFDGYDQQQVVILDDLGQNPDGKDLSTFCQMVSTTDFIVPMASLEDKGKSFTSQYVLASTNLDTLSPPTVTIPEAIKRRFFLDADLITTSKFRNTTGLLDVAKALQPCTGCPKPAHYKTCCPLLCGKAVVVQDRKTKANFSVNTIVEQLRHENATRKKVKHNLDAIFQGLGDSETPGFIVDLLSSSKDPKVIEYCAEQGWIGKANSTIERDFNYVHYMLNCLGSLIIILGTVYALYKLMCMTQGPYTGLPNPQTKRPELRKATLQGPEHEFVRALIKRNCHVITTSKGEFNMLGIHDNCAVVPTHAECGDSVTIDGREVRVLKQCILTDTNDTDTEITLLWLDQNEKFRDIRRFIPEHQREWSNMHLATNVTKFPMLDVEVGTVIPYGEVNLSGNPTCRLLKYNYPTKPGQCGGVIANTGNIVAIHVGGNGRVGYGAALLRKYFAQSQGEITAKHDVREKGLPQINTPNKTKLQPSVFYDVFPGVKEPAALSNGDPRLEVDLSTSVLSKYKGNTQVEWNDNIQIAVDHYSAQLYMLDINPQPLTMEQAVYGIEHLEPLDLTTSAGFPYVTMGIKKKDIVNKVTKDVTKLQEMIDKYGIDLPYVTYLKDELRAPEKIKKGKTRAIEAASINDTTHFRMVFGNLFSVFHANPGVLTGSAVGCNPDVFWSQMYACMDGELLAFDYTNYDGSLHPIWFKALGKVLDNLGFPGHLVNRLCNTTHIFKNLIYTVEGGMPSGICGTSIFNTMINNIIIRVLVLETYKNIDLDKLKIIAYGDDVVVSYPFELDPMEIANKAVRYGLTITPPDKGSTFHKIDWTNVTFLKRHFKPDTKYKFLIHPVYKMEDIYESIRWTKDPKNTQDHVHSLCLLAWHNGEEVYEKFREKIRSTSVGKVLYTPPYSLLYRQWIDQFI | 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 of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313}; | 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:0039522]; symbiont genome entry into host cell via pore formation in plasma membrane [GO:0044694]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell 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 [GO:0003968]; structural molecule activity [GO:0005198] | 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 a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}. | 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}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:27511920}. Host cytoplasm {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:27511920}. Host cytoplasm {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000269|PubMed:27511920}. Host cytoplasm {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23008}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23008}; Cytoplasmic side {ECO:0000250|UniProtKB:P23008}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P23008}. | 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 ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; CATALYTIC ACTIVITY: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; | 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:32152109). Capsid protein VP1 mainly forms the vertices of the capsid (PubMed:27511920, PubMed:32152109). The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion (PubMed:27511920). Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells (PubMed:32152109). This attachment induces virion internalization (PubMed:32152109). Tyrosine kinases are probably involved in the entry process (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:27511920, ECO:0000269|PubMed:32152109}.; FUNCTION: [Capsid protein VP2]: 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:32152109). {ECO:0000269|PubMed:27511920, ECO:0000269|PubMed:32152109}.; FUNCTION: [Capsid protein VP3]: 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:32152109). {ECO:0000269|PubMed:27511920, ECO:0000269|PubMed:32152109}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (PubMed:32152109). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:32152109}.; FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301, ECO:0000250|UniProtKB:P04936}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P04936}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}. | Human rhinovirus C (strain C15) (HRV-C15) |
E5KGE0 | BRIZ1_ARATH | MFILRVHSVDSERPISVEEEESGFTYASKRAQPPLKLIQPSLKLTDRKGLIHLYRKSSHSSLPNPSSRSTTLFIVAVPNYLSSLDFIRFCDSRISQVSDILFIRNDGMEDRYSVLITFSDQSEADGFYNNLNGKKFAPSEAEVCHILYVMSVEHTEFDEVAAEAPTGFTELPTCPICLERLDPDTSGIVSTLCDHSFQCSCTSKWTYLSCQVCRLCQQQDEILNCSICGKTENVWACLVCGFVGCGRYKEGHSIRHWKETHHCYSLDLRTQQIWDYVGDSYVHRLNHSKIDGKSVEMSTSCLSHQGDCGLCECSEDTGISGAIFNSKVDSIVIEYNDLLASQLKGQRQYYESLIVEARSKQESSIAEAVEQIVVNTMQELQNKIEKCEEEKSGITEVNTKLIKEQDTWRKKAKEIEEREAALLGSKDEMITDLQEQIRDITVFIEAKKTLKKMSSDTDGIREGTVLPVPISPEPVSSVRRQKKSNRRK | 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:0000269|PubMed:20805503, ECO:0000269|Ref.3}.; PTM: The configuration of reformed Cys-61 as the D form was attributed by similarity to related structures. {ECO:0000269|PubMed:20805503}. | 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 | MTESQSYETRQARPAGQSLAERVARLVAIDPQAAAAVPDKAVAERATQQGLRLAQRIEAFLSGYGDRPALAQRAFEITKDPITGRAVATLLPKFETVSYRELLERSHAIASELANHAEAPVKAGEFIATIGFTSTDYTSLDIAGVLLGLTSVPLQTGATTDTLKAIAEETAPAVFGASVEHLDNAVTTALATPSVRRLLVFDYRQGVDEDREAVEAARSRLAEAGSAVLVDTLDEVIARGRALPRVALPPATDAGDDSLSLLIYTSGSTGTPKGAMYPERNVAQFWGGIWHNAFDDGDSAPDVPDIMVNFMPLSHVAGRIGLMGTLSSGGTTYFIAKSDLSTFFEDYSLARPTKLFFVPRICEMIYQHYQSELDRIGAADGSPQAEAIKTELREKLLGGRVLTAGSGSAPMSPELTAFIESVLQVHLVDGYGSTEAGPVWRDRKLVKPPVTEHKLIDVPELGYFSTDSPYPRGELAIKTQTILPGYYKRPETTAEVFDEDGFYLTGDVVAEVAPEEFVYVDRRKNVLKLSQGEFVALSKLEAAYGTSPLVRQISVYGSSQRSYLLAVVVPTPEALAKYGDGEAVKSALGDSLQKIAREEGLQSYEVPRDFIIETDPFTIENGILSDAGKTLRPKVKARYGERLEALYAQLAETQAGELRSIRVGAGERPVIETVQRAAAALLGASAAEVDPEAHFSDLGGDSLSALTYSNFLHEIFQVEVPVSVIVSAANNLRSVAAHIEKERSSGSDRPTFASVHGAGATTIRASDLKLEKFLDAQTLAAAPSLPRPASEVRTVLLTGSNGWLGRFLALAWLERLVPQGGKVVVIVRGKDDKAAKARLDSVFESGDPALLAHYEDLADKGLEVLAGDFSDADLGLRKADWDRLADEVDLIVHSGALVNHVLPYSQLFGPNVVGTAEVAKLALTKRLKPVTYLSTVAVAVGVEPSAFEEDGDIRDVSAVRSIDEGYANGYGNSKWAGEVLLREAYEHAGLPVRVFRSDMILAHRKYTGQLNVPDQFTRLILSLLATGIAPKSFYQLDATGGRQRAHYDGIPVDFTAEAITTLGLAGSDGYHSFDVFNPHHDGVGLDEFVDWLVEAGHPISRVDDYAEWLSRFETSLRGLPEAQRQHSVLPLLHAFAQPAPAIDGSPFQTKNFQSSVQEAKVGAEHDIPHLDKALIVKYAEDIKQLGLL | 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_02247, ECO:0000269|PubMed:28719588}; | 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:0000269|PubMed:28719588}. | Segniliparus rugosus (strain ATCC BAA-974 / DSM 45345 / CCUG 50838 / CIP 108380 / JCM 13579 / CDC 945) |
E6LHV7 | CAS10_ENTI1 | MNKKLELMYGSLLHDIGKIVYRSNSVDFAKGTHSKIGSQFLNKFKPFQLSGIVDSVSYHHYKELASSSLLDDSVAYITYIADNIASGTDRRASEGDYEGEGNRQRFDKRAPLASIFNVVNSETKGLANYTYSFEKEQVYRYPTDAKKEYTSSQYAALVNKMTDDLSNKLKVGPDSFSSLLQWTESLWSYIPSSTDTNQVMDVSLYDHSKITCAIASCIYDYLTEMNCVNYRKELFSPYEKTKQFYQEDVFLLVSLDMSGIQDFIYNISGSKALKSLRSRSFYLETMLESLVDDLLSDLELSRANLLYTGGGHAYLLLPNTERARDVLASFEGEMKEWFIKIFKTDLSVAIAYKACTGEDLMNSNGTYSDLWQTVSRKLSDKKAHKYSLNEIKLFNSTIHAGTQECKECLRSDIDISEDSLCKICEGIIAISNDLRDYSFFVVSPEGKVPLPRNRYLSVENQDGAERKIKMNKETRIYSKNQPFVGKQLVTNLWMCDYDFSTLNPETKKQGIASYVNREVGIPRLGVLRADIDNLGTTFIKGIPEQYRSISRTATLSRQLSMFFKFELSNILKGARISVIYSGGDDLFLIGAWDDVISKALVLRKAFTRFSAGKLTFSAGIGMYPVKYPISKMASETGVLEDLAKRGEKNQVALWNDSKVFGWSQLEEQILKEKMIPLQEALTNSQEHGKSFLYKMLELLRNEDQINIARLAYLLARSSLSEELTQSIFAWSQNKQQKVELITAIEYLVYQIREAD | 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 invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host the appropriately targeted Csm effector complex prevents growth of dsDNA phage phiNM1-gamma6. {ECO:0000269|PubMed:28722012}.; FUNCTION: ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases. {ECO:0000250|UniProtKB:A0A0A7HFE1}.; FUNCTION: This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity. {ECO:0000250|UniProtKB:B6YWB8}.; FUNCTION: When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing (mostly) cyclic hexaadenylate (cA6). cA6 synthesis occurs in the Csm effector complex and requires cognate target RNA and ATP; other NTPs are not incorporated. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids. {ECO:0000269|PubMed:28722012}. | Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5) |
E6MVD9 | NALP_NEIMH | MRTTPTFPTKTFKPTAMALAVATTLSACLGGGGGGTSAPDFNAGGTGIGSNSRATTAKSAAVSYAGIKNEMCKDRSMLCAGRDDVAVTDRDAKINRPPPPNLHTGDFPNPNDAYKNLINLKPAIEAGYTGRGVEVGIVDTGESVGSISFPELYGRKEHGYNENYKNYTAYMRKEAPEDGGGKDIEASFDDEAVIETEAKPTDIRHVKEIGHIDLVSHIIGGRSVDGRPAGGIAPDATLHIMNTNDGTKNEMMVAAIRNAWVKLGERGVRIVNNSFGTTSRAGTADLFQIANSEEQYRQALLDYSGGDKTDEGIRLMQQSDYGNLSYHIRNKNMLFIFSTGNDAQAQPNTYALLPFYEKDAQKGIITVAGVDRSGEKFKREMYGEPGTEPLEYGSNHCGITAMWCLSAPYEASVRFTRTNPIQIAGTSFSAPIVTGTAALLLQKYPWMSNDNLRTTLLTTAQDIGAVGVDSKFGWGLLDAGKAMNGPASFPFGDFTADTKGTSDIAYSFRNDISGTGGLIKKGGSQLQLHGNNTYTGKTIIEGGSLVLYGNNKSDMRVETKGALIYNGAASGGSLNSDGIVYLADTDQSGANETVHIKGSLQLDGKGTLYTRLGKLLKVDGTAIIGGKLYMSARGKGAGYLNSTGRRVPFLSAAKIGQDYSFFTNIETDGGLLASLDSVEKTAGSEGDTLSYYVRRGNAARTASAAAHSAPAGLKHAVEQGGSNLENLMVELDASESSATPETVETAAADRTDMPGIRPYGATFRAAAAVQHANAADGVRIFNSLAATVYADSTAAHADMQGRRLKAVSDGLDHNGTGLRVIAQTQQDGGTWEQGGVEGKMRGSTQTVGIAAKTGENTTAAATLGMGRSTWSENSANAKTDSISLFAGIRHDAGDIGYLKGLFSYGRYKNSISRSTGADEHAEGSVNGTLMQLGALGGVNVPFAATGDLTVEGGLRYDLLKQDAFAEKGSALGWSGNSLTEGTLVGLAGLKLSQPLSDKAVLFATAGVERDLNGRDYTVTGGFTGATAATGKTGARNMPHTRLVAGLGADVEFGNGWNGLARYSYAGSKQYGNHSGRVGVGYRF | 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 is released into the medium (PubMed:23258267). {ECO:0000269|PubMed:14617158, ECO:0000269|PubMed:23258267}. | 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:0000269|PubMed:16788193}. Note=Newly synthesized protein appears in distinct foci on the cell surface; there are 1 or more foci scattered across the cell surface. {ECO:0000269|PubMed:16788193}.; SUBCELLULAR LOCATION: [NalP passenger domain]: Secreted {ECO:0000269|PubMed:14617158, ECO:0000269|PubMed:23258267}. Note=An approximately 70 kDa, unlipidated form is secreted. Upon expression of the protein in E.coli this form starts on Gly-65. {ECO:0000269|PubMed:14617158}.; SUBCELLULAR LOCATION: [NalP translocator]: Cell outer membrane {ECO:0000305}. Note=An approximately 30 kDa form is detected in membranes; this is probably the beta-barrel translocation domain. {ECO:0000269|PubMed:15014442}. | 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) extracellularly, releasing it from the cell surface. LbpB release protects bacteria against complement-mediated killing by anti-LbpB antibodies (PubMed:20421383). Processes NHBA (PubMed:23258267). Lipidation slows its auto-processing, probably allowing it to act on endogenous substrates on the cell surface before the passenger domain is released into the medium (PubMed:23258267). The C-terminal beta-barrel domain inserts into the outer membrane where it probably exports the N-terminal passenger domain (PubMed:15014442). Both the cell surface protein (Neisserial autotransporter lipoprotein NalP) and the passenger domain cleave human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal (By similarity). {ECO:0000250|UniProtKB:Q9JXM7, ECO:0000269|PubMed:14617158, ECO:0000269|PubMed:15014442, ECO:0000269|PubMed:20421383, ECO:0000269|PubMed:23258267}.; FUNCTION: Plays a role in extracellular-DNA (eDNA) mediated biofilm formation. In some strains (including cc32 strain H44/76 but not cc11 strain B16B6) eDNA stimulates biofilm formation. When NalP is not expressed (and no longer processes NHBA or IgA) biofilm formation increases (PubMed:23163582). This is probably because the number of positively charged, DNA-binding peptides on the cell surface rises, resulting in increased biofilm formation (Probable). {ECO:0000269|PubMed:23163582, ECO:0000305|PubMed:23163582}.; FUNCTION: [NalP passenger domain]: Cleaves human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal. Does not act on mouse or rabbit C3. Cleavage causes C3b degradation by human CFI and CFH, decreases deposition of C3b on the bacteria surface and probably facilitates complement escape. {ECO:0000250|UniProtKB:Q9JXM7}. | Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) |
E6Y2X0 | PILR2_LINUS | MAAGFLFHMGSLPAIATVGHKSKVLVIGGTGYLGKRLVTASLAAGHETYVLQRPEIGVDIEKIQLLLSFKKAGASLVSGSFNDYRSLVDAVKLVDVVICAVSGVHIRSHQILLQLKLVDAIKEAGNVKRFLPSEFGTDPATMENAMEPGRVTFDDKMVVRKAIEEAGIPFTYISANCFAGYFLGGLCQPGFILPSREQVTLLGDGNQKAVYVDEDDIARYTIKMIDDPRTLNKTVYIKPPKNVLSQREVVGIWEKYIGKELKKTTLSVEEFLAMMKEQDYAEQVGLTHYYHVCYEGCLTNFEIGDEAGEATKLYPEVGYTTVVEYMKRYV | 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(+) = (+)-lariciresinol + H(+) + NADPH; Xref=Rhea:RHEA:34423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65004, ChEBI:CHEBI:67246; EC=1.23.1.2; Evidence={ECO:0000269|PubMed:20514607}; | 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 | MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVIRDGMGQSSGHPPAMSLDTVITSAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFPNMIIGVNTEVICGEGLIVTAGGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF | 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|PubMed:21893219}; | 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:21893219). {ECO:0000250|UniProtKB:P07374, ECO:0000269|PubMed:21893219}. | Canavalia ensiformis (Jack bean) (Dolichos ensiformis) |
E6Z0R3 | VBHT_BARSR | MRKYEGSNDPYTDPETGVMYNLLGIKDQARLERVESAFAYIRSFELGRTSISGKFDLDHMKKIHKKLFGDVYEWAGKTRLVDIVKDNSKFAHYTQIESYAPQITQQLAREQHLRGLDANEFSQRAGYYMGELNALHPFREGNGRTLREFIWQLAREAGYHIDWDRVERQEMTRASIESYYGNSDLMSALIRRNLTEFTVNRRVDVSQGINERVLSHIDIDKEWPQKGFNIAIQTTQQAPYLSSYTDTSNLEEKAQNALRNEQSYVDTFKELNDHLKTIYKDPQAAALKIEQTILAGKGDKLPDILAKAPNKVGELRGSDRLIDKLKSAGKERKAALYNVPLAISTIRRLQSFYKNSYEKHMDKLTREREQLKVEVPSLSQEAVAYMKNVEVGRNNYSKIPENINKEFVQLESALNRRFGKDVIYKRNFNLSKEIASKQTYDKKLVNELQTAIKFLQQRHIQKQNNLAITRTPSKGITR | 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|PubMed:23738009}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:23738009}; | 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 does not affect mammal F11 sodium channels. {ECO:0000269|PubMed:21605585}. | Rhopalurus junceus (Caribbean blue scorpion) |
E7EAU8 | GCY9_CAEEL | MRLYLFFISSLLLAESRRSISKISHDEINQHVKTTLSSEGIVRIGHLHPTNPIIAHEPDVLKMCADDLKMRNILPQNYTLTVFTMESCNKYSGVEHAAFLHYLKNASVYFGPGCNNEMLVIGRLAPRWNVPIIAHMSGDDALSDRVQFPTLGSVALTSASEMAKATVTYLNLNNWDQIGIVRPSVGYERLSVYSLQHQIKKRDINLNVILDIEPFSSPEEIISTGKLTTLKSMARIIVVELGMDIHSVTNFMLAIHRSEIKNEEFVFVIPWLAHQNDHYPWEAANVDKQEVKLAFENTIIITAHGYDKKFFDDFQMKFSAVTGVLANHYATLSYMSLYDALFLYGLALRDAFEDGGGYNVHMNGSLIWSRMTNRQFIGMTGQVLMNNKAIRVPSYATYHAINGTLKIVVELEAKNNDRGQCEKNEEMCSEHVAHETIQYYWPSDSGKLPPAVPKCGFTGAECDYRPYFIGASLLAFILTVGPLSYFIYLKQKERLLYDMTWRIPRESIKMLEGKSKSEHSLASKSQSSGSFSGSMNSKQNGLIAAKQAVSNGVKLAIKRYQQVRNITFPKSELRLLKELKICENDNLNKFYGISFNQQNEFIVMWVLCSRGSLEDILFNDELKLGRNFQVSFAKDVVKGLNFLHTSPLLHHGMLCLQNCLVDSNWTVKLTNFATEAVIFEKLDHNELRPFINTDSESADDVSDPTKDFARKKYLQQAPEIIREIVTTKTIPEGSQSADIYALGMVLYQILFRVEPFHERNKSINKLMETLAMANDDDQLIRPTFPSSNTGEGYNLQLLSCIEACWLEIPEMRPPIKKVRTMVNANLKSTGKGSLVDQMMKMMEEYTANLENMVRDRTALLEEAQKQADRLLNSMLPKSIAEDLKIGKPVLPQLYSCATVLFSDIRGFTRISSTSTPLQVVTFLNDMFSGFDAIIAKHDAYKVETIGDAYMIVSGVPTENGNSHAQNIADVALKMRAFICNFKLAHRPEELMMVRIGFHSGPVAAGVVGLAAPRYCLFGDTVNTASRMESTGVANKIQISEGAYNLLHCFFPQFQMVERGKIEVKGKGECLTYYLEGRTGKQ | 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 neuronal action potential [GO:1904457]; receptor guanylyl cyclase signaling pathway [GO:0007168] | 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:0000269|PubMed:24240097}. | Caenorhabditis elegans |
E7EM37 | DOPR2_CAEEL | MEAGETWNVSLEWPPPSLDLSTITQTPSTIVGSGIPLNYAGLSLIVIPLITLLGNLLVIISVLRYRALQSAINFLILGLAVADLLVAIIVMPYAVYVYVTNGDWYLGNLMCDIYMASDVCCSTASILLLAVISFDRYRAVSLPIQYSRQSQNVKRVWTLIAVIWLVSLTLASPMVFGVNVRPPDANPYECRFYNAEFSILSSMISFVIPCFLVLFVYIRIIIALKKREKAAKMRREKNTIAHGLTMRPDTGEEQVDEEAAGRIVAGPVVNVMMAALPSMTRRMRQFERHRRAIELAGDEEWEEDELDVMDECCGGDDAGDDDDDYHADNGQGVVEASAPRTTSMLRRIINAASVGTANSTAQSVASASGMPAFFAQNISTTSPSSSSCARTTTTTSAIPKASGDLPLPMLLNEREFGNSSTPRSSLESLSENVNVITNDFVSENCTTFSRRSSYADDSQPTSSQTSSGDGRSYSIKGQKRFRNLSRNYSTKHHRKVVKVNRGNSRNNSRTASITNQSDDALIPAIIRTISRKSPRLFRRDKTDIKKHSMILANPITEPPKEYRRVSMPIHPTNSQTETETISASRDIENLPTTTISRSTTANSAELLGSPDDFEKFPALITETVLEDVLAETREGCFMQPTVSFALTVREMEGNALNNLKGCSVESSRRVSQVDPPLAIQILTRPSLPHLDLQRMDSIGTTCSSKTRADSLRSVDSKGSKKSNRNGIAVKLVKRAIKHEHSLKRKVSKAQRKEKRATKTLGVVVGVFLVCWVPFFVINILNAVCILLNKDSCQVGYDLFFYCTWIGYMNSFMNPIIYTIFNTEFRRAFKSIIFGRNSTRHHFSNKQAHV | 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 signaling pathway [GO:0007212]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; negative regulation of dopamine secretion [GO:0033602]; negative regulation of locomotion involved in locomotory behavior [GO:0090327]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of male mating behavior [GO:1902437]; regulation of male mating behavior [GO:1902435]; regulation of neuronal signal transduction [GO:1902847]; regulation of potassium ion transport [GO:0043266]; response to food [GO:0032094]; spicule insertion [GO:0034609]; vulval location [GO:0034608] | 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 synaptic vesicle fusion to negatively regulate the release of dopamine at dopaminergic neuron synapses (PubMed:31494966). Antagonizes octopamine signaling in response to food by promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons (PubMed:19609300). This is most likely in association with the G(o)-alpha G-protein subunit goa-1 (PubMed:19609300). In association with the G-alpha protein gpa-14, modulates two types of learning behavior: touch habituation and chemosensory associative conditioning (PubMed:23607404). May act partly via tsp-17 to negatively regulate dopamine reuptake transporter dat-1 activity (PubMed:25474638). Plays a role in behavioral plasticity and regulates the decision-making process when conflicting alternatives are present (PubMed:25536037). Promotes male mating behavior by antagonizing acetylcholine signaling to control the protrusions of copulatory spicules from the tail of males during hermaphrodite vulval location (PubMed:23166505, PubMed:26156999). Modulates unc-7 activity at gap junctions to promote inhibitory neuronal signaling transduction between chemosensory and mechanosensory neurons, and thus ensures spicule insertion attempts are confined to the hermaphrodite vulva during copulation (PubMed:26156999). {ECO:0000269|PubMed:12887685, ECO:0000269|PubMed:19609300, ECO:0000269|PubMed:23166505, ECO:0000269|PubMed:23607404, ECO:0000269|PubMed:25474638, ECO:0000269|PubMed:25536037, ECO:0000269|PubMed:26156999, ECO:0000269|PubMed:31494966}.; FUNCTION: [Isoform a]: 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). {ECO:0000269|PubMed:12887685}. | Caenorhabditis elegans |
E7EZF3 | UHRF1_DANRE | MWIQVRTMDGKETHRVDSLSKLTKVDELRVKIAELFNVEPERQRLFYRGKQMEDGHTIFDYNVGLNDIVQLLVRQAVAATVLPKDKEAELSDSDSGCGSAQSESDKGSTHGESDVQSAGASGQTDTADLIDPGFGFYKINEFVDARDLNMGAWFEAQIVKVTKTPAEDGGAEDIVYHVKYEDYPENGVVQLRGKDVRPRARTVYQWHQLEPGMIVMVNYNPDDPKERGYWYDAEIQRKRETRTQREVFGKILLGDAGDSLNDCRIMFVTEIYKIEEPGSAEGPGASSDSPLKKGSNGPECKVCKDDPKKNCRVCNCHVCGIKQDPDKQLLCDECDMAFHTYCLNPPLTTIPDDEDWYCPDCRNDASEVVLAGEKLKESKKKAKMASASSSSQRDWGKGMACVGRTKQCTIVPSNHYGPVPGVPVGTLWKFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDDGNEFTYTGSGGRDLSGNKRTAEQSCDQKLTNMNRALALNCNAAVNDKEGAEAKDWKAGKPVRVVRSSKGRKHSKYSPEDGNRYDGIYKVVKYWPEKGKSGFLVWRYLLKRNDEESAPWTRDGKERIKKLGLTMQYPEGYLEAVAAKEKEKENKNEDDIEETPTKGKRKRKSQSMEEKSSPTKGTPKKMKVEAYKLSKEQKALIKDDELNKKLWDEAMESLSLGPRFVNKVEEVFLCICCQEVVYQPITTECQHNVCRECLQRSFKAKVYTCPACRHDLGKNYQMAVNKPLQAILTQLFPGYSSGRC | 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 via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | 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 through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins. However, it is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo (By similarity). Required for pregastrula and lens development. {ECO:0000250, ECO:0000269|PubMed:21126517}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7EZG2 | MY9AA_DANRE | MSVHDVGGRRRFEDSELTLRIYPGIIAEGTIYCPVAARKITSAAEVIEQVIDRLQLDRTKCYVLAEVKEFGGEEWILNPTDYPVQRMMLWPRMALENRFSSEDYRFLLREKNLDGSIHYGNLQMWLQVTEERRRMVERGFLPQPLPKDFDDLCNLPDLNEKTLLDNLRSRFKQEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQSRQNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGTSEEERTAFHLKKPEEYHYLNQMTKKPHRPHWGNYYENEPDCFTVEGEDLKHDFERLQLAMEMVGFLPTTRKQIFSLLSAILHLGNIRYKKKIYRDDSIDICNPEVLPVVSELLEVKEEMLFEALTTRKTVTVGEKLIVPYKLAEAGTVRDSMAKSLYSALFDWIVFRINHALLNQRDLEESAKILSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRAEGITWHNIDYIDNTSCITLISKKPTALLHLLDEECNFPQATNQTLLDKFKRQHEGNSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLKSSKNAFICGLIGIDPVATFRWAVLRAYFRAMVAFRDAGKRHVEKRSGHDAAAPAVKSVDSFSFLHHPVHQRSLEILQRCKEEKYSVNRRNPRTPLSDLQGSNAINQREGWNGRPGRQNRLSSFGSFSEEEGIFINSTSSKLLERAHGILMRNKNYKMKPSLPKHLLDVKSLKYLSNLTLQDRITKSLLHLHKKKKPPSISAQFQASLNKLMETLGQSQPYFVKCIRSNSEKLPLRFNDSLVLRQLRYTGMLETVRIRQSGYSIKYTFQDFARHFHVLLPEGSNQASQEAIRQYLQQVDLTPEGFQVGRTMVFLREIERQRLQDLLHKEVLSRIVYLQRRFRALLERKNFLRVRQAACQIQNWWRSCQSLQRDSQLEYDMRVQEGAVVCIQSAWRGFRERRRLLLWREASVLIQRTWRLYRQRRAALQIQTAWRRHRARELFLRQRDATIRLQAVGRGYLARQRFRELQKQRLKITHLPNGKASLLTEEDKLEDMGLDASMLEDSFEEQDRSKQALSSAVEASGAGVLEEMEVEMMEGMAPAQPSPEVTIRERPRTLEDPNQRTRAKRESRRMRELEQAKFSLELLKVRSTGGTSPSDERRWSMELVSEIAHTPQGTPDSQSSKGSFELLNIDDYFKDKAPCAEPEDLGSPSSVPDQHNVLPSDTSTPDILSKPDDQSKPPRMQYSLPTFYTPPSESSSLVIKSTTNSVTPCPDGLSKPSKDKKESTRRPMVVVISMQKETLLNEADVKPLEVKDSAAQTSEPPSPAQPSTDSSYVLEKLEKLNEEKEERQKHQRQQNEKEMMEQIRQQTHILEEQRRNLVQNEREKLEKQRAETLRRIEQSRQESSGGRTDRPAPIAQPEPDLTSQRPAREKDGAPLILRDRPKDAQNLAEGWAPKLTLESRGDEARSRINKKPSNQNVNISMSERPGNIFFSPKTKIAYSKLNKDLANQEKTPGAQNEVSLLGYKSTKTEVGRPGHKKARMARTRSDFLTRSSSTQGEGESEEEEYDETPLYAGTPLPKQDSEESAVEACHSDSEMLTTAAEEQKNRCKTLPSGELGKHDTRKNSHGDGRVRGKMRFWGKAKNAEKKSSRERLLCGSDTLEGDYTEATLLMEEGVERLSPPHSPDLTLQREFKENKEPSPKVKRRRSVKISSVALEPVQWQNDALQILTCTSDYKSMNDFLMKKITDLDTEDGKKDTMVDVVFKKALKEFRVNIFNSYSTALAMDDGKSIRYKDLYALFEQILEKNMRQEQRDWSESPVKVWVNTFKVFLDEFMTEHKPLDSSLGKAPKPDRKKRRKKDTDVVEEHNGHIFKSTQYSIPTYCEYCSSLIWMMDKACVCKLCRYACHRKCCQKMTTKCSKKYDPELSSRQFGVELSRLTNDERTVPLVVEKLVNYIEMHGLYTEGIYRKSGSTNKIKELKQGLDTDVNGVNLDDYNINVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQDKKEVIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRCPDTIDPLRSVQDIGKTTACVELIICEQMNKYRARLKDINTLEFAENKAKSRLTFIRRSMGKGPVHRLRYRTPSPPTSPRSPTAPEVMQDSGEEEPGRDPEVSEQQQVAMQQEEKVLTEQIESLQKEKEELTFEMLALEPRASDDETLESEASIGTADSSENLNVDSEGATSDYSERGPALAATRPKKSEGKSRRVLRKQPESLDSIDSCSTVSSVSSSYMQPTSRTHKLSLRSKSPSKRLYLSSPSESLDQPEQDGEERPQFTSRGTFNPEKGKQRLQGAKSSPQRHREQKKDPELSPQQVVVYGSNEFMV | 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 hints of an enrichment near the plasma membrane. Localized at the neuromuscular junction. {ECO:0000250|UniProtKB:Q8C170, ECO:0000250|UniProtKB:Q9Z1N3}. | 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|UniProtKB:Q9Z1N3, ECO:0000269|PubMed:27259756}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F1H9 | YTHD2_DANRE | MSASSLLEQRPKGQANKVQNGAVTQKDTLNDDEFEPYLNAQPRQSNAYTAMSDSYMPSYYSPSIGFTYSLNEAAWSTGGDPPMPYLASYGQLSNGEHHFLPDAMFGQSGALGNNPFLGQHGFNFFPSGIDFPAWGNSSSQGQSTQSSGYSSSYAYAPSTLGGAMIDGQSPFAANEPLNKAVGMNSLDQGMAGLKIGAGDMAPKVVGSGLPGGPLSQVSTAPTMPPASMAPAKTASWADIASKPAKPQPKLKTKGGLGGTNLPPPPIKHNMDIGTWDNKGNMPKPAAPQQTSLPTNGQPPNQSSPQPGATAGGVPQLPLSNGQLVPPTGQLVQHPLPPGGQPGAVPPQLSQGPPASQPSQPTRWVPPRNRANGFGDAAGGPGQSPPNSGMGGITVPAEPHPVLEKLRMVNNYNPKDFDWNPKHGRVFIIKSYSEDDIHRSIKYNIWCSTEHGNKRLDAAYRSLANKGPLYLLFSVNGSGHFCGVAEMRSPVDYNTCAGVWSQDKWKGRFDVRWIFVKDVPNSQLRHIRLENNENKPVTNSRDTQEVPLDKARQVLKIIASYKHTTSIFDDFSHYEKRQEEEESVKKVEVQGSDPYSNNSSRSHYRMQDRQGRVK | 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 regulation of stem cell differentiation [GO:2000737]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; oocyte maturation [GO:0001556]; organelle assembly [GO:0070925]; regulation of cell adhesion [GO:0030155]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of meiotic cell cycle process involved in oocyte maturation [GO:1903538]; regulation of neurogenesis [GO:0050767]; regulation of rRNA processing [GO:2000232]; RNA catabolic process [GO:0006401]; spermatogonial cell division [GO:0007284]; stress granule assembly [GO:0034063] | 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 partition into different structures: into P-bodies in unstressed cells, and into stress granules during stress. {ECO:0000250|UniProtKB:Q9Y5A9}. | 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 stability by promoting degradation of m6A-containing mRNAs (By similarity). The YTHDF paralogs (ythdf1, ythdf2 and ythdf3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (By similarity). Plays a key role in maternal-to-zygotic transition during early embryonic development, the process during which maternally inherited mRNAs are degraded: acts by binding m6A-containing maternal mRNAs and promoting their degradation (PubMed:28192787). More than one-third of maternal mRNAs can be modified by m6A (PubMed:28192787). Binding to m6A-containing mRNAs results in mRNA degradation (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A-containing mRNAs, such as notch1a, and promote their degradation (PubMed:28869969). The decreased Notch signaling following notch1a degradation promotes endothelial to hematopoietic transition (PubMed:28869969). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (By similarity). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (By similarity). {ECO:0000250|UniProtKB:Q9Y5A9, ECO:0000269|PubMed:28192787, ECO:0000269|PubMed:28869969}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F3F0 | MY9AB_DANRE | IMSCHDVGGRRRFEDSEFTLRVYPGSLSESTIYCPVSARKVTTAAEVIERVIERLQLDRTRLYVLAEVKEFGGEEWILNPSDCPAQRMMLWPRMALENRLLGEDYRFLLREKNLDGSIHYGSLQMWLRVTEERRRMVERGLLPQPPAAQFVADLCSLPDLNEHTMLENLRGRFRQENIYTYVGSILIAVNPFKFLPIYNPKYVKMYDKHRLGQLEPHIFAVADAAYHAMLQRHRNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEKYLLEKSRLVYQEHNERCSCVNIFSKLVCHELKVCVCMCVQDCFSVEAEDLKHDFERLQLAMEMVGFLPTTRKQIFSLLSAILHLGNIRYKKKTFRDDSIDICNPEVLPIVSELLEVKEEMLFEALTTRKTVTVGERLIVPYKLAEVRKGTSHQLIQTFRTSHSLLHQRYFHIHTSPTRILSIGVLDIFGFEDYENNSFEQFCINFANETLQHYFNQHVFKLEQEEYRSEGINWHMIDYIDNTACINLISKKPTALLHLLDEECNFPQASNQTLLDKFKRQHEGNAYMEFPAVMEPAFIIRHYAGKVKYSVKDFREKNTDHLRPDIVSLLKSSRKAFICGLMGLDPVASFRWAVIRAFFRALVAFRHAGLQHRDNRSSSDVHLQPQKSVDSFSFLHHPVHQRSLEILQRCKDDRYNSCVSRRSPRTPLSDLQGANTFSSNGRGWRSERVSSFAHEDEGIFVNSVNNRLLERAQGILMRNKNYKPKPSLPKHLLDVKSLKYLSSLTLHDRITKSLLHLHKKKKPPSISAQFNVSLNKLMETLGQSEPYFVKCIRSNAEKLPLRFNDALVLRQLRYTGMLETVRIRQSGYSVKYSFKDFAHHFHVLLPAGFSASQMGIREFLRSADLEPSGYQVGRSMVFLHERLRQRLQDELHQEVLRRIVCLQRSFRTQRDRKHFCRQRRAARLIQRWWRSCISQADGSVCALELQQGAALRLQAVWRGFRARRLYLQQRRAVLIIQRCWRRVLNTRNTAATLIQAVWRTRTHRRSFLQQRRAAVTLQAACRGQQSRQRCRILREQQCREQSKHPSTVTKSLHQNTEEAEKLEEVWEKQTTDPPPKAVDDSTLKSRNKRESRRQRELEQATFSLELLKVRSGSNTEDAQIPPSKHHPPHQASTDSQESFELLENEDSASAKLELSKSEPMEVNQTSPAASFKPHFYIPDEDGSPINSAPQTPNRAKQIREKKESVVVIISMQKENPVDRSSLQTLEAQDVPLSNGESASDCSIIPEPRTNHELDTGSSFSVSSKPLQLDLRSAASNEEPSEPKADVQKKFVSQSISISMKETAANVAFPPKRSRLTFSKSDKDLVNQERSLAIQREAGFRSLKNRDVTRAGCKKKARMARTRSDFLSRACSTEADCEEDEDDEYEDTPVLSCTRPPHSPSSPDIDCVFHSDSEMSSQKEQKRIQKTMSSGDLGKMDSLRKSMSQTDSRVRGKMRFWSKSKHGDKKISSRGRSADSELTDRRNDSPPGSPEHAGVSERRRDSKENREPMLGMMSMKRRRSLKISSVSLESTAWQNDALHILTSTADYRSMNDFLMKKISDLDAEDGQKDTAVDVVFKKALKEFRLNIFNSYSTALAMDDGRSIRYKDLYALFEHILEKSMRLEQRDWSESPVKVWVNTFKVFLDEFMTEYKPMDGTISKAPKPERKKRRKKESDTVEEHMGHIFKSTQYSIPTYCEFCSSLIWMMDKACVCKLCRYACHKKCCLRMTTKCSKKFDPELSSRQFGVELSRLTSDERSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELKQGLDTDANSVNLDDYNIHVIASVLKQWLRDLPNPLMTFELYEEFLRAMGLQDKREVVQGVYSIIDQLSRTHLNTLERLIFHLVRISFQEETNRMSANALAIVFAPCILRCPDTTDPLQSVRDISKTTACVELIICEQMRKYKARLKDINTLEFAENKAKSRLTHIRRSMGKSRARKSGHHTPSPPLSPRASEREEPVDEGAEPVLSEQQQAAMQQEEKVLTQQIENLQKEKEELTYEMLALEPRASDDEMLESEASIGTADSSENLMESEGAASDPWEKSPGAVSASRWRKSESKSRRCLRRQPESLDSVDSAVASLSSVSSTPHYRFRSSSSGPLFSSSSPTGDLHILPDPESCEQASLSARCASSSEKTRPRPRANRSCPPKPREPGDTGGRRREHEFGSSQPLVLYGSNEFMV | 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 hints of an enrichment near the plasma membrane. Localized at the neuromuscular junction. {ECO:0000250|UniProtKB:Q8C170, ECO:0000250|UniProtKB:Q9Z1N3}. | 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|UniProtKB:Q9Z1N3, ECO:0000269|PubMed:27259756}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F3I6 | CLP1_DANRE | MTAEAAEKSVEEGLSSSGSAGSSGTRFDLDKETELRFEVEAGERVQLELLSGLAEIFGSELNRNKKYTFGPGSKIAVFTWQGCGVALSGKTEVAYVSKDTPMLLYLNTHAALEQMRRQAEKDNERGPRVMVVGPTDVGKSTVCRMLLNYAVRLGRRPTLVELDVGQSSVSVPGTMSALCIERPADVEEGFSVQAPLVFHFGSTTPGTNIKLYNKLTSSLADAFSQRCEVNRRASVGGCIINTCGWVKGSGYQALVHCASAFQVDVVLVLDQERLYNELKRDLPHFVRVVLLPKSGGVVERSKDCRRETRDEKIREYFYGFRGTSFYPHAFDVRFSDVRIYKIGAPSIPDSCLPLGMSQDDTQLKLVPVSPGRDLTHHVLSVSSVDDEAEVGQSRGILESPACGFIVVTAVDTQAQVMTVLSPAPRPLPRHTLLIMDIRFIDLK | 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; CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'-phospho-ribonucleoside-RNA + ADP + H(+); Xref=Rhea:RHEA:54580, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:15179, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:138282, ChEBI:CHEBI:138284, 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 more efficiently than the DNA component. Plays a role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Its role in tRNA splicing and maturation is required for cerebellar development. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by dicer1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing. {ECO:0000269|PubMed:24766810}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F4N7 | STING_DANRE | MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRMSEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSFYIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKITHNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSRELFQNLKQQDGEIFMDPTNEVHPVPEEGPVGNCNGALQATFHEEPMSDEPTLMFSRPQSLRSEPVETTDYFNPSSAMKQN | 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 to virus by host [GO:0002230]; positive regulation of macroautophagy [GO:0016239]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of type I interferon production [GO:0032481]; regulation of autophagy [GO:0010506]; regulation of type I interferon production [GO:0032479]; response to virus [GO:0009615]; reticulophagy [GO:0061709] | 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:0048471] | 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 other cytokines. {ECO:0000250|UniProtKB:E1C7U0}. | 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:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}. | 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 delivered to the cytoplasm (PubMed:23091644). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and irf3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842662). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30842662). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate LC3 lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:23091644, ECO:0000269|PubMed:30842662}. | 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 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P28328}; | 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 subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity). {ECO:0000250|UniProtKB:P28328, ECO:0000250|UniProtKB:P32800}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F568 | COBL_DANRE | MNLGDATTRPPVGRRMKAQAPPPPRPPQPAPRRIFRNAVPDGGGSSGGDCKENMLRSYVDLHISLPTGYQTTINVDGRKALMDLLVDLCSQYHLNPAYHTLELLSPDAQPVSFKPNALLGALDVSCALIKERVLEDRVIRKPPPKVPEKTVRLVVNYHRSQKAVVRVNPLAPLQTLVPVICQKCEFDPAHVLLFKDNINHQQLDLDKSLSDLGIRELYVLDQTLVLQPKMASTPALNYSAESLRSNSLSGSEKKGLLGFLKFNRRKSKGMSVVASGPCVEARPSTLGQSQSVMNISKMSPKVELKKRRAPAPPPAPTQTLPPTSQISLGSPSSHNLLKKRKAPAPPPTPPPSTPEPDISTYVPTATVQEHYIPASVERTPRASTPADDSDLSHSIEDSEPARSICSSSSGDDAAAVGSSSSSLAEEPVTHRADVIAPFTTSTPEPEPKPEYEPELKKEASPRSTPELEPGPRPEVPAAEDLEVEMELKMEETENNRHSGIAWLHSAHESVLERRVQQEVETVSVASSESFADHGYAASEDMAEESGPVSPSERMQSVSPMDIMSLNSDSTLPVKQSKESSSDSDEGCATWGSRQSSGHIQDGQKSIKRQNGYEEDPEITAQIHLTLADLDANLADLNHSDGASVFVDDEIPVSIVDMDIPVTAIDEVLDDDQCSASECESVLLRSTQSISSKPCTPCGVIQNKNNNACLTEEKHRSPFPDIEKQLQTATLTVIDKPTIQSPTSKKPSQDAKITDNMEQKTTFNSEAKSKSETVELTSQKDTVLQKSQSFVRPDVQSVQKERTSSTRVLPTQGKITLSSFSRFGMKTFTVIPPKPAVSQTKPAGSLVTGAIKIDEQGNMVTQRQISSGPEKNNTPSVDTTRADKTPLVKAKAFWSTTEKQEKLTTAKTEPIVNNGDTDVFKASAVTGSFKLSPPEETHKEVIIVERKPISGVASKPSFSENHAEKRDLSFLIPSRRTSSQYVASVIAKNNKNSSIPKTKIDTTPAPLSISGVQNPVNQLLNNEVKPTSIHKPAVTVKPTENPVPSFRPKCLQSYVAEKPTSSERISTLHGGDKTKSLDSQPLSIKIQPFPHVSAHIKSFSEEATSINNFPDTSSARQTPTDTTHPPLAKKPELHKSEIPSEPNQGNVFGPVKKFKPVIFKPVQQETSIHSSLMEAIQSGEGIERLRKVSDLPTSCTVKKPSYNDPENERSALLSAIRASSTSAKLKKTKSVASKELEQLRKVEEDRNVHTEVISPRPTSPDFVPPLPPSFSPPPPPPPPLAPAKPPVVLPPGGNPEAAREALLEAIRSGSGAQQLRKVPVTQTRRQVNGRLGTIQATSPLSYGH | 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. Recruited to the cell membrane via interaction with pacsin1. Detected at the apical surface of cells at the basis of forming cilia, but not in the cilia themselves. {ECO:0000250}. | 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 depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain, heart and kidney development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior. {ECO:0000250, ECO:0000269|PubMed:21129373, ECO:0000269|PubMed:23203810}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F590 | VPS41_DANRE | MAEVEEQGRKLSEESTDESEEEDTEEEPKLKYERLTNGVTEILQKDAASCMTVHDKFLALGTHFGKVFLLDIQGNVTQKFEISSVKINQISLDESGDHVGICSEDGKVQVFGLYTREGFHENFDCPIKVVALHPQFSKSNNKQFVTGGNKLLLYERNWLNRWKTSVLHEGEGNITSVKWRGNLIAWANNVGVKIYDIGSKQRITNVLRDNTSLRPDMYPCSLCWKDNTTLIIGWGCSVKICAVKERDPTEMRDLPSRYVEIVSAFETEFFISGLAPLADQLVTLYYVKENSDHMEEEFRTRPRLDIIQPLPEGCEEISSDALTVRNFQENQCRDYRLEHSEGESLFYIISPKDIVVAKERDQDDHIDWLLEKKKYEEALMAAEISFKNIKRHDVQKIGMAYINHLVEKGDYDTAARKCQKVLGKNMDLWENEVYRFKTIGQLKAISQYLPRGDLRLRPAIYEMILHDFLKTDYEGFATLIREWPGELYNNMAIVQAVNEHLKKDPTNSILLTTLAELYTYDQRYDRALEIYLRLRHKDVYQLIHKHNLFSSIKDKIVLLMDFDKEKAVDMLLDNEDKISMDKVVEELKDRPELLHVYLHKLFKRDHHKGQKYHERQISLYAEFDRPNLLPFLRESMHCPLEKALEICQQRHFVEETVFLLSRMGNCRRALQMIMEELANVDKAIEFAKEQDDRELWEDLISYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILHDYNLQILLREGCKKILVADSLSLLQRMHRTQKKGVRVDEENICESCHTPILPSDTAQAFGVVVFHCRHMFHKECLPSPGSIPGIQYCNICSAKRRGPGSGILEMKK | 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 membrane protein {ECO:0000250|UniProtKB:P49754}. Lysosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P49754}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P49754}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49754}. | 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 | MQKDSLPTLSPAVPPYVMLGLTVAYTIFYCLLFVFVYVQLWLVLRYRHKRFSYQTVFLFLCLLWAALRALLFSFYFKNCVTANTLGPFCFWLLYCFPVCLQFFTLSLMNLYFAQVIFKAKSKYSPELQKYRLPLYLLFLSISLLFLLVNLTCALLVKINRANTETVVLVRVTVNDSLFVLCAVSLSLCLYRIAKMSLANIYLEAKGTSVCQVTLIGVTVVLLYSSRACYNLVVLALTKIKSINSFDYDWYNVSDQADLKSTLGDAGYVVFGVILFVWELLPTSLVVYFFRVRKPTLDRSASVIPGHMFSSRAYFFDNPRRYDSDDDLAWSIIPQNIQASFTSDSYDWSCRNNSFTAYTEAEESHLAPEELNPY | 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 [GO:0010506]; regulation of GTPase activity [GO:0043087] | 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 and thereby regulates mTORC1 translocation and activity in lysosome (PubMed:31036939). Acts also as a negative regulator of osteoclast activity (PubMed:31173907). May be involved in interleukin-4-induced M2 macrophage polarization (By similarity). {ECO:0000250|UniProtKB:O60478, ECO:0000250|UniProtKB:Q8BNQ3, ECO:0000269|PubMed:31036939, ECO:0000269|PubMed:31173907}.; FUNCTION: Acts also as a negative regulator of osteoclast activity (PubMed:31173907). May be involved in interleukin-4-induced M2 macrophage polarization (By similarity). {ECO:0000250|UniProtKB:Q8BNQ3, ECO:0000269|PubMed:31173907}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F654 | NOL9_DANRE | MTMKVHKVHSRSQQRQRNASKQHGKNKWNKKVRSLDSTLLNTSSGTAKLEQEIAKKEKPAIKRLKKLYAKPVTLLSDNNCADEDKVKPTSVTFAHVHTNGGTELDDSSRSVDSQEWSEYANSVLQNGMETSTLPDSDQAEDGLQFHAHLDHTKNRAVLVMKQSQVLCFRGKCLLTCLYGHVEVLGFTIEEGQQPYPVFSPPTHCPLTITALGNNQSSSKNKKEGQLEAKAIVRKYFTTEPSKKLMNEVDSDSCVVLLESLDTPLTRFLSSFSELTELFGLNSKELKSQAAIYSPVLSAVGVTALRGPCAQGLVMSRSYKETISSLLSAWAGEFDRCPIILVCGGKSSGKSTFNRHLINSLLNHTASVEYLECDLGQTEFTPPGCLSLCTVTEPLLGPPFTHLRDPEHMVYYGQADCQSDIDRYLESLKSLWRNVSGESPVIINTMGWIRGHGFQILVDLVRLFSVTHVVQLSYGTAPQCQLLTSEFIRSAHGWQTHPPTTPALTEDSHSPSRSHVFLSVQSEFEGAGVSGEMRFQRSNELRDLALLSYISKLQSSDPGPIRPLHCFIPYQVPHSSVAIGVTHCEVAPNNILYAANASVVGLCCLSEKVVGRGGPVILSQTPICQCVGLGVLRGVDMGRGLYFLVTPVSPSVLKHVNCLLLGEISLPKILLTQQHGVEGDLPYITTDYSFEVQGAGKLHIFKGLTRPGFIKSDN | 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]; phosphorylation [GO:0016310]; rRNA processing [GO:0006364] | 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; Evidence={ECO:0000250|UniProtKB:Q5SY16}; CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'-phospho-ribonucleoside-RNA + ADP + H(+); Xref=Rhea:RHEA:54580, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:15179, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:138282, ChEBI:CHEBI:138284, ChEBI:CHEBI:456216; EC=2.7.1.78; Evidence={ECO:0000250|UniProtKB:Q5SY16}; | 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 morphogenesis (PubMed:26624285). {ECO:0000250|UniProtKB:Q5SY16, ECO:0000269|PubMed:26624285}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F6F7 | ABCB7_DANRE | MAPLLVPLKCGFHMQRRKLSLLLQRSSAVQAWTFHDHRAANKRKERNTYLLSDPSRESSTWANNRGQNSQQILEAVKHLHLQERQCWHGNAGGGLSADPKNVLKEVNSSKILGAMFTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMLNLSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANLWNTQNSRILSNGSKPEPVPERVSQKEEERKKLQEEIMNSVKGCGNCSC | 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]; positive regulation of heme biosynthetic process [GO:0070455]; transmembrane transport [GO:0055085] | 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:O75027}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029; Evidence={ECO:0000250|UniProtKB:O75027}; | 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 cadmium, zinc and mercury detoxification (PubMed:27734548). {ECO:0000250|UniProtKB:O75027, ECO:0000269|PubMed:27734548}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7F7X0 | LMOD3_DANRE | MSERTEQESYTDKIDEDEILAGLSAEELKQLQSEMDDIAPDERVPVGLRQKDASHEMTVRDCTEPESEEEIDEDEILAGLSAEELKQLQSEMEEIAPDERVPVGMRQRDQTDKPPTGSFDHRSLVEYLYWEKESKRMLEEERVPTTLLPSQKTNEEHEAKNEDKVEELELVYEEIVEEVEGGQGDAVVDEVIEEVIMEVEEEDKVCDKPVKTDLDATDPTVTSEDGLQRPSESADANVEAKTDQSGLDTETKVNEEKKEDSTEPAPSSYENWVPEKEERVISKLKIPKLALGGNTFVKKTARPSGNETNLESTLDKIRNNNPSVTDVNLNNIENIPKEMLLDYVNSLKKNRHVKTFSIANTGADENVAFTLANMLKENRSITTLNIESNFITGKGIVAIIRCLQFNETLTELRFHNQRHMLGHHAEMEVSRLLKANNTLLKMGYHFELPGPRMVVTNLLTRNLDRQRQQRMEEQKLQQMKEQRKVMEMYEDSLNLPPGMLEMLGGYIPLSLLQNCQNGAEDIPEDSPEPSPQPSPPHQLCKTQHLAPQQHPPNLSTGNLFEEVQLKKTPKRRDPLLEWNQCDERKDGRPNVHLRSVPKKRSIAREGPVDERANLKDMIKTLKPVPRRREPPKVDLTPRDHLLSEIRQSNVAYLKAVPLPKILESQETSLF | 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 | MAEHESLEFGKADFVLLDNVSLEEFMANLKLRFEKGRIYSYIGEVVVSVNPYRAMNIYGRDVIEQYKGRELYERPPHLFAIADAAYKAMKRRNKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIFQQEGERSFHSFYQLVKGAPDAQLRSLHIQRDPTAYNYIKVGGQLKSSINDSAEFKAVADAMKVIGFTTEEIQTVYKILATILHLGNLKFGTDGDVTLIENSKLVSVLGDLLSTKEENVEKAMLYRTVATGRDVIDKQHTHQEASYGRDALAKAIYERLFCWIVGRINDIIEVKNYDARVHGKNTVIGVLDIYGFEIFQNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIFAVLDEACMNVGKVTDEMFLQALNGKLAKHAHYTSRKLSPTDKNLEFERDFRIRHYAGDVTYSVVGFIDKNKDTLFQDFKRLLYNSSNPVLKAMWPEGKLSITEVTKRPLTAATLFKNSMISLVEKLASKEPYYVRCIKPNDVKSPLLFEHERCKHQVEYLGLLENVRVRRAGFANRQTYPRFLQRYKMISEFTWPNHDLSSDKEAVKRLLQGCGFEHDVAYGKTKVFIRTPRTIFSLEEQRAEMVKRIVLFLQKVWRGTLARMRYRRMRAALIIIRAYRRYKVKSYIREVIRRFKNVRDMKDHGKHVKWPTPPKVLRKFEEALRSIYNRWWAWTLIKPLSPEKTVQIRAKVATLECLKGQRADLGLQRAWEGNYLKKDSPGTASSFTLVSSDLQRKDKFMRVLFSSNVRKINRFNKAEDRALLITDRHLYKMDPLKQYKPMKSIPLYNVTGVSISPGKDQLVVFHTKDNRDLIVCLQGMVPAGDSRIGELVGTLLSHFKSEKRKLQVNTVSPIHCSMNGRKCTVVVETKISQSQPDFTKSRSGYILSVPGN | 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:0060287]; establishment of left/right asymmetry [GO:0061966]; heart jogging [GO:0003146]; Kupffer's vesicle development [GO:0070121]; protein transport [GO:0015031]; vesicle transport along actin filament [GO:0030050] | 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 cell cortex close to the apical cell membrane. Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles. {ECO:0000250|UniProtKB:Q63357}. | 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 that are required for normal lumen expansion of Kupffer's vesicle (PubMed:30139971). Required for normal orientation of cilia in Kupffer's vesicle, and thus for normal, unidirectional circular flow and normal angular flow velocity, which then mediates asymmetric gene expression and left-right asymmetric development (PubMed:29769531). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement (By similarity). {ECO:0000250|UniProtKB:F1PRN2, ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:29769531, ECO:0000269|PubMed:30139971}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FAG6 | AMR1A_DANRE | MKLGQRNSVCILSSRERGAPGLASYRVLQQLVEEKTQRMKWQSQKVELPDSPRSTFLLAFSPDRSLMASTHVNHNIYITEVKSGKCVHSLVGHRRTPWCLTFHPIIPGLIASGCLDGEVRIWDLHGGSESWLTESNSAIASLAFHPTAQLLLIATNNEVHLWDWSRKEPFTVVKTASETERVRLVRFDPLGHYLLTAIVNPSNQPNDDDPEIPMDSVEMPHLRQRSFLQSQPARRTPILHNFLHILTSRNSVPQAGGAHSASTDGSSDSSGPYTLMCVQPLGMVCFCSRCSAARVPSPPDEDPSDSASLEAQAHTFSSARTEPLQMSRFSVESRAANRSSAFSSVYGGGSNMRNHSSSSGRRGVTGMAPVPHFRQHPPGREGGGRHPGADWTVSGLNGQSSSMTPQRTGASSVSLLSVLRQQETSFQSPVYTSASDRWGSTPGTSSSRHRPPEEEGQSSSSSIHSVLRCNLYRYFMDYEGTQDTVQPLDGSRQDQQTQEMLNNNMDPEQPGPSHYQSPYSGENPPHSHMNRCRVCHNLFTYNQGSRRWDRTGQPSSTERNTPWQPSSSAFHSVAPVSQSNEHLLEHRPIESTPNTPEPHVPFSQRTDTGQHEEQAVGLVFNQETGQLERVYRQSASSRSANISQGALNQEMPEDTPDNDYLRRLSPAAYYAQRMIQYLSRRDSVRQHSHRPPSRPRPLSSNPSSLSPSPVPNAESSEVDFEEFEENGSRYRTPRNARMSAPSLGRFVGTRRFLLPEFLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVPNCKIYNDASCDISADGQLLAVFIPSSQRGFPDEGILAVYSLAPHNLGEMLYSKRFGPNAISVSLSPMGRYVMVGLASRRILLHQISDHMVAQVFRLQQPHAGETSMRRVFDVVYPMAPDQRRHVSINSARWLPDPGLGLAYGTNKGDLVICRPVDVHSDGSSTSEHSERMFTINNGGGVGPSSSRSGDRAGSSRTDRRSRRDIGLMNGVGLQPQPPAASVTSQGTQTQNQRLQHAETQTDRDLPDDPQQPSTSQGSQVTDATESLDFETLPEDSGSEVVPETPPHSRPQEDEGSDPSEPSTDSTGQAEYVSRIRRLMAEGGMTAVVQREQSTTMASMGSFGNNIIVSHRIHRGSQTGADAQNRTRLSPIPGPSSGAPESLAAASYSRVLTNTLGFRGDTAQGIDLTEQERLHTSFFTPEFSPLFSSAVDATGPSSSIGADSVLEGEDFHDFASLPPSLLSSSPSLSPVNNSNYSNSDSSYLGDEYGR | 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 regulation of protein dephosphorylation [GO:0035307]; positive regulation of regulatory T cell differentiation [GO:0045591]; protein polyubiquitination [GO:0000209]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; skeletal muscle fiber development [GO:0048741] | 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 [GO:0005634] | 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|UniProtKB:Q9C0C7}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:A2AH22}. Note=Localizes to the cytoskeleton in absence of autophagy induction. Upon autophagy induction, ambra1a relocalizes to the endoplasmic reticulum to enable autophagosome nucleation. Partially localizes at mitochondria in normal conditions. {ECO:0000250|UniProtKB:Q9C0C7}. | 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 transition from G1 to S cell phase: ambra1a specifically recognizes and binds phosphorylated cyclin-D (ccnd1, ccnd2 and ccnd3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation (By similarity). Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (eloc) component of CRL5 complexes (By similarity). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation (By similarity). In normal conditions, ambra1a is tethered to the cytoskeleton via interaction with dyneins light chains (By similarity). Upon autophagy induction, ambra1a is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (By similarity). Also acts as an activator of mitophagy (By similarity). Required for skeletal muscle development (PubMed:24922546). {ECO:0000250|UniProtKB:A2AH22, ECO:0000250|UniProtKB:Q9C0C7, ECO:0000269|PubMed:23348054, ECO:0000269|PubMed:24922546}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FAM5 | LIN41_DANRE | MCEVILWSSAQMASFPDSDLQTCPLCKELCGCSAPISSNSSTSSSSSQTSNSSSTSSTRRLHVLPCLHAFCRQCLEGQRSPGDPLKLRCPTCDQKVSLSESGVDALPSSNFLFSNLLDVVVSAEEQGKNGRSSAVVHHGGLLRPQHLSDPQCSSCDEGNPATSHCLDCQEYLCDNCVRAHQRVRLTKDHFIEGLLESLHLANRTNNSNTPVSISQSFHNSFSMLNVFQERMDFCQHHDDAVLRFFCDSCTVPICRECSLGRHAGHSFTYLQDALQDSRALTIQLLADAQQGRQAIQLSIEKAQAIAEQVELKAKVVQSEVKTITLRHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLHQNLTKLDSTIATVTQVLEEGRSIDVLLAREHMLNQLQELKSLRCILQPQEDDRIMFTPPDQALLIAIKSLGLISSGAFATASKAHGEGIKRALQGKPASFTVVGYDHDGEPRLSGGDSVSVVLMSPDGNLSSAEVSDHQDGTYTVSYLPKGEGEHLLSVLICNQHIEGSPFKVMVKSGRSYGGVGLPMASFGGEGDGDGQLCRPWGICVDKEGYVVVADRSNNRVQIFKPCGTFHHKFGTLGSRPGQFDRPAGVACDSQRRIIVADKDNHRIQIFTFDGQFLLKFGEKGTKNGQFNYPWDVAVNFEGKILVSDTRNHRVQLFGPDGTFLNKYGFEGALWKHFDSPRGVAFNQEGHLVVTDFNNHRLLVIRPDCQSARFLGSEGTGNGQFLRPQGVAVDQEDRIIVADSRNHRIQVFEPNGNFLCKFGTHGNGFGQMDRPSGIAVTPDGVIVAVDFGNNRILMF | 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 autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; regulation of neural precursor cell proliferation [GO:2000177]; stem cell proliferation [GO:0072089] | 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 neural progenitor cells during early neural development. {ECO:0000250|UniProtKB:Q1PSW8}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FB98 | UBIA1_DANRE | MQEMKPAALSGSNGLNGASGSSVRVPCSRLSRAGRMALDLQSKCAAYVLALRPWSFSASLTPVALGSALAYKLEGSVDLLLLLVCAVAVLLVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILKPQDVVMFGAVLYSAGCLCATLLYFLSSLKLEHLALIYFGGLSSSFLYTGGIGLKYVALGDVVILITFGPLAVMFAHAVQVGYLSVLPLVYAVPLALNTEAILHSNNTRDMDSDKQAGIVTLAILLGPTLSYVIYNLLLFVPYLLFCILATRYTISMALPLLTLPMAFPLERQFRCRCYAKIPQKTAKLNLLMGLFYVFGIILAPQGSLPLL | 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 3,4-dihydroxy-5-polyprenylbenzoate [GO:0032194]; vitamin K biosynthetic process [GO:0042371] | 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:0000255}. | 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={ECO:0000250|UniProtKB:Q9Y5Z9}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-hydroxy-3-all-trans-decaprenylbenzoate + diphosphate; Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39; Evidence={ECO:0000269|PubMed:23374346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565; Evidence={ECO:0000269|PubMed:23374346}; | 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) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4 (By similarity). Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system (PubMed:23374346). Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from nos3/eNOS-dependent oxidative stress (PubMed:23533172). {ECO:0000250|UniProtKB:Q9Y5Z9, ECO:0000269|PubMed:23374346, ECO:0000269|PubMed:23533172}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FBF7 | FCHO1_DANRE | MIHFFHTLQGEKNAGFDVLYHNMKHGQIATKELAEFVRERAAIEETYSKSMSKLAKMASNGSPLGTFAPMWDVFRVSSDKLALCHLELMRKMNDLIRDINKYSDEQVKIHRKTKEEAIGTLESVQSLQVQNGHLQKTREGYHSKCVELERLRKEGVPQKELEKAELKCKKAAESFAGSIEKFNRAGGDFEQKMSESAQKFQDIEEAHLRQMKLLIKGYSHSIEDTHVQVGQVHEEFKQNVENIGIENLIQKFTEQKGTGKERPEGPVGFEEYLSSLASENSKKSRAKAFRIPGLGKRDKEPDSTVHVYFLQNNSPLEVDDEGFVIRADVKQNDIEKEGNFYSSDSDFDDEEPKKFHIQIRPVASSNRSNSAANEQELKATVGALTLPPNRVVSVKKQLSRRSEGEGESVPQRVIAKVEVCACRLSSTASGSDALFGPPLESAFKSHSFSGREQLQNAFAASEFFSKFYSSSLENVEDSGLDSPSHQPLGVSPDPTGWAAWPSSQSQSKDSINAASQSRGGSNRPTPSPNPAPSSQSNTEWMNDIIREGPYSQIMQDSSERLALAPPRSVRSKRSSVAITRKNSDFSRSLCSSPLPDPNASTCVLYSKMLNCAPAGLSRGPSPISLSAQESWPVAAAITEYINAYFRGGEHNRCLVKITGDLTMSFPAGITRIFTANPNAPVLSFRLVNISRVDHFLPNQKLLYSDPSQSDPDTKDFWFNMQALTLHLQREAELNPQASYYNVALLKYQASSQDPSRAPLLLSAECQRSGTVTRVSLDYHCCPATAPATQLTSVQVLLPLDHSATDLQCQPPAAWNAEERRLLWKLDDLSSVSGSGTLCASWQCLEVPRGPAPSLAVQFVGSGASLSGLDVELVGSRYRMSLVKKRFATGKYMAGCSL | 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 | MSGPCVRIPFWVRVFLLLLLYRIAAGCPELFSSGCSCTEDRSKAHPTPGTRRKVSCGGKELTETPEVSLLPNRTVSLNLSNNRIRMLKNGSFAGLSSLEKLDLRNNLISTIMPGAFLGLTALRKLDLSSNRIGCLTPEMFQGLTNLTKLNISGNIFSSLDPNVFMELHSLKLVNFHSEFLSCDCGLRWVPSFFRSGSARLGDETLCAYPRRLQNKPLRLLRESDLSCEGPLELHTLSLLPSQRQVVFKGDRLPFHCTASLVDKITALHWRQNGQPVTSDPTKGIHLEESVQHDCTFITSELILSNVHVEASGEWECVVSTGRGNTSCSVEIVVLENSASFCPEQKVNNNRGEFRWPRTLAGITSYQHCLQLRYPSLTLGGGVEQKKASRNCDRSGRWEEADYSQCLYTNDITRILHTFILMPVNASNAVTLAHQVRSYTLEAAGFTDTVDVLYVAQMMHKFMDYVTELRELSEVLVEMGSNLMQVDDQILARAQREERACSSIVYTLETLAWPQLHSHAQDLSRYSRNIVMEAHLIRPAHFTGISCTVYQRREGAAGSQVHDGADLSLEQQLRFRCTTGTHNTSLNAFHLKNAVALATVSLPATLFPPNAPPDCKLQFVAFRNGRFFPFTSNFTGHSDLARRRGISTPVIYAGLDGCSMWNQSDPIIVSLRHTSPGHDPVAAHWNSQALGHHGSWSLDGCQLIHSDVSISTLRCSVLSNYAVLQEIPDFPGSPSIPVEVLHPVIYTCTAVLLLCLFTIIITYILHHSSIRITRKSWHTLLNTSFHVAMTSAVFAGGITLTGYPIVCQAVGIVLHYSSLSTLLWIGVSARVIYKEALLRTPQQLEGESAVQPTQRPMLRFYLIAGGVPLIICGITAAVNINNYGDNIPYCWLVWQPSFGAFYIPAGLIILVTWIYFLCTVFCLRQRNFQESKDLQCSASDPSNLPESQPALSGSTSLLSTDSGVSPVHAGTTVEDQYSLKVQCLALMATQFVFVGLWCCGAMAVWHVDRERKLFSCLYGGTATGLGIFLVLHHCFKRLDVQAAWLGCCPGYHRSQPMPAYSHPCTVTVGVQSASERGSQLFVACHPPTDPNHYSSSARSSSTQSGTASITVVPSKLTNLLQVSQDNANNASRAPAGTNTNTSTSTENNKPTNNLLPSLLPVQQPQRRKACSRTKGGNTQYHHRGDARSHYRLKALRAGGGGSMGALGPSGTEHSNIYHVHKHASSENGSLRNSHSEGQNGLLTNGRHRGEGLATSPSEGSDGGSSGSRKPFPLLPSVARRAAMQQNAQCRSASKDNLKLAAAAERESKRSSFPLNMSSNVTATASLSTVSAPNGTLKGSVVELDTSGTDQSQGSVGMKSRVWKSETTV | 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 cell-autonomously in the tip cells of sprouting vessels (PubMed:26051822). Has a role in development of dorsal root ganglia (PubMed:26051822). Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (PubMed:30026314). Adgra2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly (PubMed:30026314). {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:30026314}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FCP8 | NAGS_DANRE | MAKVNSGSSGCRAMVMAGQFWTKPFALSSQRSGPHRRSAAEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTLIYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGSIAELLNLLPVESSAVLTSANTLLTELFSHKGSGTLFKNGDPIRRYSSLEDIDVDRLLALINKSFEKNLREDYIASLEGRLHSVYLSEGYSAAAIITTEPVNSGTPYLDKFVVSSSKQGQGTGQILWECIRQDFSKLFWRSRTTNRINPWYFKHCDGSFVNGHWIVFWLGLSDIRESYELVEFAKSHPDSFCSLSTTETKPLQQHHGS | 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=right-to-left; Xref=Rhea:RHEA:32481; Evidence={ECO:0000269|PubMed:24153409}; CATALYTIC ACTIVITY: Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH; Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; CATALYTIC ACTIVITY: Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:24153409}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459; Evidence={ECO:0000269|PubMed:24153409}; CATALYTIC ACTIVITY: Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH; Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; CATALYTIC ACTIVITY: Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH; Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349; Evidence={ECO:0000250|UniProtKB:Q6PHW0}; | 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 | MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTGTINLESLTLTGTKIRSIPADLCEDLTVLRTVDLSYNDIEDLPSFQGCVRLQDINLQHNQIKQIDRGTFQGMTSLRVLDLSRNQIKFIHRDAFLSLSALTNLDLSLNSLASVPTAGLSALNQLKLTGNMELRNGLMSKTLPKLRSITVPYAYQCCAFVAYDSAVNPAEDDERRNAFGGEEDMERIPMVMHCSPLPGAFKPCEHLLGSWMIRLTVWFICLVALLFNCLVLAATFSPRTSSLSPSRFLVALLASANLLTGVYVAALTLLDTVTWGSFAEYGVWWETGAGCQVVGFLAVFSSEWAVLLLALAAVERCLAVRALMGKAGALRSRGERRERRRRFAIAALLLGLVSVAAACLSLYHGSAMGSPLCLPFSEGSSPGLGFTVALVLMNTLAYLLSAVVYTRLYCRLGRAQLADPEQAGSVRHIAWLIFTNCIFFCPVAAFSFAPLLAGTSNAVGGPEMAKSVTLIFFPLSACLNPVLYVCFSPSFRYDWLHLRGRGRTGGCGRLVAKTVTKGTVAGGSPVSDDGEGLSSDCGMYTKLHGDSRGMCEHCDAALHIRTSSSSGSSSSSACRHLVKSHSCPALMGNVPQCLSSEGYWPDTGTLSAQSEYGDEGDSFVSDSSEQVQACGRACFCQSRGLPLVHYSYNIPRMTD | 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 production [GO:0001818]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; osteoblast differentiation [GO:0001649]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; rhythmic process [GO:0048511]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055] | 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 the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids. Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (PubMed:32493844). {ECO:0000250|UniProtKB:A2ARI4, ECO:0000250|UniProtKB:B0BLW3, ECO:0000269|PubMed:32493844}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E7FHC4 | HYD2A_PYRFU | MIIELDEFTRVEGNGKAEIVIENGEVKDARVKIVEGPRFFEILTLGRDYWDVPDLEARICAICYIAHSVASVRAIEKALGIDVPESVEKLRELALWGEIIESHALHLYLLALPDVFGYPDAISMIPRHGELVKEGLTIKAFGNAIRELIGGREIHGINIKPGGFGRYPSEEELEKIAEHSKSLIKFARRIVGIFASQEAGGAVGEVLMATSDYLWGDELIINGERVQYYEVDEVPVGYSFAKHSYYKGNPVFVGALPRLLLKGESIEGEAARMLEEYRDKLESKYVIYNNLAQAIELLYALERVPQLVEEILSEGIERGNGEISQESGEGVGYVEAPRGVLVHHYRIENGKVVWSNTITPTAFNQRLMELSLLEEAKRLYGSESEENMKKRLEVIVRAFDPCISCSVHFVKL | 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, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.12.1.5; Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463}; | 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:10714990}; KM=63 uM for NADPH (H(+) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=71 uM for NADH (H(+) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=17 uM for NADP (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=125 uM for NAD (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.2 mM for sulfur (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.67 mM for polysulfide (NADPH as cosubstrate) {ECO:0000269|PubMed:10714990}; Note=Measured for the whole complex. {ECO:0000269|PubMed:10714990}; | 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 the reduction of protons to evolve hydrogen. {ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11133967, ECO:0000269|PubMed:11265463}. | 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}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:10714990}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10714990}; | 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, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.12.1.5; Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463}; | 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:10714990}; KM=63 uM for NADPH (H(+) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=71 uM for NADH (H(+) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=17 uM for NADP (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=125 uM for NAD (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.2 mM for sulfur (H(2) as cosubstrate) {ECO:0000269|PubMed:10714990}; KM=0.67 mM for polysulfide (NADPH as cosubstrate) {ECO:0000269|PubMed:10714990}; Note=Measured for the whole complex. {ECO:0000269|PubMed:10714990}; | 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 the reduction of protons to evolve hydrogen. {ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11133967, ECO:0000269|PubMed:11265463}. | 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:9119024}; | 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:0000269|PubMed:8830684}; KM=200 uM for phosphate (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=25 uM for acetyl-CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=17 uM for acetyl-CoA (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=29 uM for isobutyryl-CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=477 uM for ATP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=80 uM for ATP (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=430 uM for GTP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=18 uM for CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=30 uM for CoA (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=1100 uM for acetate (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=660 uM for acetate (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=457 uM for isobutyrate (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; Note=kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate. {ECO:0000269|PubMed:8830684}; | 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 acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. {ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}. | 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:49883; Evidence={ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:7615063}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:7615063}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:10439073}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10439073}; | 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, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=70 uM for ferredoxin (sodium dithionate as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=1 uM for ferredoxin (pyruvate and NADP as cosubstrates) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=40 uM for NADP (pure H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=0.2 mM for NADPH (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=3 mM for NADH (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=5 mM for methyl viologen (H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7615063, ECO:0000269|Ref.4}; Vmax=2900 umol/min/mg enzyme with methyl viologen as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=18 umol/min/mg enzyme with ferredoxin as substrate (pyruvate and NADP as cosubstrates) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=250 umol/min/mg enzyme with ferredoxin as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=261 umol/min/mg enzyme with methylene blue as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=67 umol/min/mg enzyme with ferredoxin as substrate (sodium dithionate as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=75 umol/min/mg enzyme with NADP as substrate (pure H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=10 umol/min/mg enzyme with NADPH as substrate (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=6 umol/min/mg enzyme with NADPH as substrate (H(+) as electron acceptor) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=1.6 umol/min/mg enzyme with NADH as substrate (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=250 umol/min/mg enzyme with methyl viologen as substrate (H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Note=Measured for the whole complex. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | 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 the reduction of protons to evolve hydrogen. {ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:11265463, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7704275, ECO:0000269|Ref.4}. | 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 products. Cleaves both mobile and immobile junctions. Binds 4-way junction DNA, a synthetic Hj, binding is not competed by dsDNA. {ECO:0000255|HAMAP-Rule:MF_01490, ECO:0000269|PubMed:10430863, ECO:0000269|PubMed:11005813, ECO:0000269|PubMed:11071944}. | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FI44 | HYD1A_PYRFU | MKNLYLPITIDHIARVEGKGGVEIIIGDDGVKEVKLNIIEGPRFFEAITIGKKLEEALAIYPRICSFCSAAHKLTALEAAEKAVGFVPREEIQALREVLYIGDMIESHALHLYLLVLPDYRGYSSPLKMVNEYKREIEIALKLKNLGTWMMDILGSRAIHQENAVLGGFGKLPEKSVLEKMKAELREALPLAEYTFELFAKLEQYSEVEGPITHLAVKPRGDAYGIYGDYIKASDGEEFPSEKYRDYIKEFVVEHSFAKHSHYKGRPFMVGAISRVINNADLLYGKAKELYEANKDLLKGTNPFANNLAQALEIVYFIERAIDLLDEALAKWPIKPRDEVEIKDGFGVSTTEAPRGILVYALKVENGRVSYADIITPTAFNLAMMEEHVRMMAEKHYNDDPERLKILAEMVVRAYDPCISCSVHVVRL | 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:24875; Evidence={ECO:0000250}; | 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, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=70 uM for ferredoxin (sodium dithionate as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=1 uM for ferredoxin (pyruvate and NADP as cosubstrates) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=40 uM for NADP (pure H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=0.2 mM for NADPH (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=3 mM for NADH (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; KM=5 mM for methyl viologen (H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=2900 umol/min/mg enzyme with methyl viologen as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=18 umol/min/mg enzyme with ferredoxin as substrate (pyruvate and NADP as cosubstrates) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=250 umol/min/mg enzyme with ferredoxin as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=261 umol/min/mg enzyme with methylene blue as substrate {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=67 umol/min/mg enzyme with ferredoxin as substrate (sodium dithionate as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=75 umol/min/mg enzyme with NADP as substrate (pure H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=10 umol/min/mg enzyme with NADPH as substrate (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=6 umol/min/mg enzyme with NADPH as substrate (H(+) as electron acceptor) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=1.6 umol/min/mg enzyme with NADH as substrate (H(+) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Vmax=250 umol/min/mg enzyme with methyl viologen as substrate (H(2) as cosubstrate) {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; Note=Measured for the whole complex. {ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:2538471, ECO:0000269|Ref.4}; | 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 the reduction of protons to evolve hydrogen. {ECO:0000269|PubMed:10439073, ECO:0000269|PubMed:11054105, ECO:0000269|PubMed:11265463, ECO:0000269|PubMed:2538471, ECO:0000269|PubMed:7704275, ECO:0000269|Ref.4}. | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FI45 | ACDA1_PYRFU | MSLEALFNPKSVAVIGASAKPGKIGYAIMKNLIEYGYEGKIYPVNIKGGEIEINGRKFKVYKSVLEIPDEVDMAVIVVPAKFVPQVLEECGQKGVKVVPIISSGFGELGEEGKKVEQQLVETARKYGMRILGPNIFGVVYTPAKLNATFGPTDVLPGPLALISQSGALGIALMGWTILEKIGLSAVVSVGNKADIDDADLLEFFKDDENTRAILIYMEGVKDGRRFMEVAKEVSKKKPIIVIKAGRSERGAKAAASHTGSLAGSDKVYSAAFKQSGVLRAYTIGEAFDWARALSNLPEPQGDNVVIITNGGGIGVMATDAAEEEGLHLYDNLEELKIFANHMPPFGSYKNPVDLTGMADGKSYEGAIRDALAHPEMHSIAVLYCQTAVLDPRELAEIVIREYNESGRKKPLVVAIVGGIEAKEAIDMLNENGIPAYPEPERAIKALSALYKWSKWKAKHKEK | 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:9119024}; | 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:0000269|PubMed:8830684}; KM=200 uM for phosphate (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=25 uM for acetyl-CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=17 uM for acetyl-CoA (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=29 uM for isobutyryl-CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=477 uM for ATP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=80 uM for ATP (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=430 uM for GTP (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=18 uM for CoA (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=30 uM for CoA (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=1100 uM for acetate (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; KM=660 uM for acetate (at 55 degrees Celsius) {ECO:0000269|PubMed:9119024}; KM=457 uM for isobutyrate (at 80 degrees Celsius) {ECO:0000269|PubMed:8830684}; Note=kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate. {ECO:0000269|PubMed:8830684}; | 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 acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. {ECO:0000269|PubMed:10482538, ECO:0000269|PubMed:8830684, ECO:0000269|PubMed:9119024}. | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
E7FKV8 | PK1L1_ORYLA | MFCLWIFSLAFLHLHLCSVSSSSLEGSGFFVGWINASSLQLFASIGGCDLSPCMDEGQEGMEALYRSEEPFQCSIRASASPGRRQAGRTCVRKVPGNLAVHCHLLSENEGLEEEDLLRITVMTPRGQSSLQVNVSHGGLLTACSDWIWNTSEKHKNNVPASGLHLGISLEVPCCTSCTRFGSDSELVEEQCSALHVSVSDVLVKDYICCLTPRDKDKTLNRTETPCLYSSNSLKDSLVRGRVYQMSFEECFRWHLLVVLLMLEAQYNHSQEVHEDPSSTVKLCDYAVRIHAEKQAYSTNTDIPLLAVVDILDPVEFLWDFGDFTSARANSRTITKRYTNPGIYKLVVVASWGQMSVRSHVLSLVVQRAVKLNRLVHEPSVLQNHTVTVSCRVNVGTNLTFLWNFGDGTVRTGLSTEQHVFTRTGEFRVMVIASNLVSSASLSSYLFVVDRPCQPPPVKNLGPPNIQVRRNEVVFLGVTFESELNCNVSRELHYSWTVYDSAGLTFPLPLTNTHRQSLVLQSYTLPYGIYKAIARVQIVGSVVYSNYSVRLQVVPNSVVVVIQGGTNIYVNTKSSNEVTLDGQASYDPDFPLNPLRYSWTCQPVSTISSSCFSQSIPTSYPVLKFPTSLLKSNFDQFKFTLTVHSGERSASSEIFLTLTSHLAGKLFVHCPECQGDQVSWDQSFSVRAECEDCNVSAEFIQYSWSLFRVNASSKPVAEIPFCYTVDLNAPSAVLENASTPTPAPEMSPSHHFNADWTRFTEDSLASSSPSRIYKSKNRNSELTDSPVSSVTVGFSGSESFNGPPGVDRGSSQFSNFPGQRDMFSEFQSDPESSAEWEFTFPYLESEDLRGQRGDSRVPFPRPEEGDPGISAGRPKETDMESFPSDSDSFSHSSSNKGEGSNLVDPRPSVRLQKPGLLDLHRDSVDKSLFESYTYTGISSCFLSFRSFSLKPSSTYMLELTAKSQRRFYGQTQLFLKVKPVPKGVACQVQPVRGIELYTHFSIFCTSGREDLIYTYSFSVGGRMPRILYQGRDFLYYFSLPSGDPTDDYKVIIYTEIRSSMYGSAKKLCPVTVRVEPSFVRNASSSYSHHEPDLMISDSGLRNVSVLVQLGNIAEIYNYISLLSTILNRLSLDSQANTHALKHLRNVLICIVCKLEYSAQASPADGIFILNELLRVTSQVTVQSARWVTAHVGALSVQFSESNRSILSALVSLLSSSLQVVTSSPETSDSADSPQPLESHLVTGKSRNAFVDDADHCITDLSETTYNKQSEPVPKRLMMRLVNDLLQTTSDLMLRNFDLQKTKELQVQSDLITLCAGFLNKTSTAINCGLITFFLPASLIKMLLLHDGISAKRGFSQREQPSCVQRIGMELLHNPYEWGRYPIQLKGPVADLSLYSCKTRRKIPVHSFLQPITVELRHPQKTSSMSEYTLLRSQINYHNFSITQEHLQQAVQVTVVFTAPPHMAFPVKILFRMFERPTPSMHHLHRLLNWRNNTILLTLPPSYLSAAGVGHLALLDANFGKTPTRRHLAEQISYSLTVESSLCLSWEDQQGSWTQNGCRAQTNDKTSAVNCSCHHLKPLKVLQQQIQSSHFRADLDQFLSVSRDLTVVFVLLLCVSLNIPVLVWCKKTDATSEENNRAHFLPDNSATDQHFYAVTVHTGLCSAARMSARVYVVLHGEDGCSQTKELHVPGCTLFRRNSQNTFILSVADSLGSVQGVHIWHNNSGPSPEWYLKQVQVSELMPGHMEGRSWQFISQCWLAVNKGDGQVERMLRVSTHGLTFSKMLFLKLFEYMPDYHIWMSVYTCPSPHLFTRAQRLCVCLLLFLGYACVNIIITHQRDDQLPFDLGVIDVTSVSIATGLVSVVAVLPVAMVISFLFRVKSGRMTLENYDNVFSKRPSGKTKYQDTDFLSVSTTNLENKDADDKEAVTPQRNKRRKDSVSFESIHELLFQEVLQVSRRRSLFLKKSKGNDSELSPQSSEFCGALKATKNEAQSVRVKRRYRLASLLYHCVAWTLCLLFCLSCLILSAVLGTRLNSGKILHWIHSLFVSLTFCFFVIHPATILVLAAVVSWRFKRSQDFHCFFNKMNSHLEDLKHQDPDQLRPSAFTRTRAPNAEKILEARQRARYLRRVHPPTRAELRKTRTKRKKQAVIHKMLRDLCLCGSMFFLMVCITYGSPVDEHYPLNAAFRRHFIRAHGDDFMSIKKYEDWWKWAQTSLLSSLYYNESENPQMSFISIGAPLVQKTEVCGTFHSQVSMVTPPRPRYHTGSSSKQEVTVGLGYTRSEGASKLRLLHLSGWLSEQTVALKVQFSLYSPAPNLFSSVTLLSEQSSTGLLQSSATVQSVRLYHSPSMLDYTVMVWQLLFLLLSLVNLYHQTSTAAQHGLMGYWKTTSISVEVSLVIVSLVYYVHYVYHPTMVMEVAEQLRRNHREHVDVSTLANSEQFSRTLRGIILFLLAVKCVTVVRLNRILAPSMPLLSLSSLLWPAISGLLLLSIFSCMGRLLYIERTFHSIQTVLWHFWSLRKSRDLISLWRDFYYFGLLYASSAMLTTMVFAVMIRKAKRSPSTKNDPTIREVLGCISQKFTGMKTQIPDCHTQKTYFLEECESLVDELLFKLNALSNSLHHTLPPKLHTYTDKDSPDASSTTELCKERLQDLVRSLSVGQGEAALTFPHDRSLLELQEEEEVKHQEGRCSVGCKESRLPETLWTADYRESMDEHWTEKKSSNGLGGATYSHVVVVEALVHHEQGTKN | 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 constitute the pore-forming subunit (By similarity). Also involved in left/right axis specification downstream of nodal flow: forms a complex with pkd2 in cilia to facilitate flow detection in left/right patterning. {ECO:0000250, ECO:0000269|PubMed:21307098}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
E8MGH8 | HYBA1_BIFL2 | MNVTITSPFWKRRRDQIVESVIPYQWGVMNDEIDTTVPDDPAGNQLADSKSHAVANLKVAAGELDDEFHGMVFQDSDVYKWLEEAAYALAYHPDPELKALCDRTVDLIARAQQSDGYLDTPYQIKSGVWADRPRFSLIQQSHEMYVMGHYIEAAVAYHQVTGNEQALEVAKKMADCLDANFGPEEGKIHGADGHPEIELALAKLYEETGEKRYLTLSQYLIDVRGQDPQFYAKQLKAMNGDNIFHDLGFYKPTYFQAAEPVRDQQTADGHAVRVGYLCTGVAHVGRLLGDQGLIDTAKRFWKNIVTRRMYVTGAIGSTHVGESFTYDYDLPNDTMYGETCASVAMSMFAQQMLDLEPKGEYADVLEKELFNGSIAGISLDGKQYYYVNALETTPDGLDNPDRHHVLSHRVDWFGCACCPANIARLIASVDRYIYTERDGGKTVLSHQFIANTAEFASGLTVEQRSNFPWDGHVEYTVSLPASATDSSVRFGLRIPGWSRGSYTLTVNGKPAVGSLEDGFVYLVVNAGDTLEIALELDMSVKFVRANSRVRSDAGQVAVMRGPLVYCAEQVDNPGDLWNYRLADGVTGADAAVAFQADLLGGVDTVDLPAVREHADEDDAPLYVDADEPRAGEPATLRLVPYYSWANREIGEMRVFQRR | 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. kcat is 0.013 sec(-1) with Ara-Hyp. kcat is 6.3 sec(-1) with Ara(2)-Hyp. {ECO:0000269|PubMed:24385433}; | 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)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. {ECO:0000269|PubMed:24385433}. | Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) |
E8PLM2 | OLD_THESS | MLKRLQVKNFRCLEDIDLPLGPLTAIVGPNGAGKTTILRAIDLVLGDVWPSLRSFRIPQDFINFDTTRAIEITVHFDPPYTQGSFNITAFRLTCKGEDADFHVDLEPLDEGGNVPRYPSGNPLRVGTDMRNHARVLFLDHRRNLAQHLPSIRGSILGRLLQPVRREFKLQDNFKQVYEQAMDLLRTEQVKQIEKTIAETAKQMLGFLGKDAMKSMEIGFGFADPANPFNSLRLQYRESDLTLPGDELGLGIQSAIVVGIFEAFRQLGEKIGTVIIEEPEMYLHPQAQRYFYRLLCEMADKDQCQIIYSTHSPIFADVNRFEALRLVRKDRDDRVVVSYVREEDKSALDNVRNRFKLGGRFDTARNEVLFAKRALLVEGYGDRVAALQLFNQLEVDPDAECIAVVDCGGKAGIELIVGVCKALDIPFVVVHDEDVWPIDERADEETRRKQEQENKAEQEKNQRIQACAGAERVFVVQPSLEAALGIGRNASDKPYRIAEILKTVDVGQPPDALRPFVEAIRQVTRPMEE | 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+) is most efficient on linear or supercoiled dsDNA, nicks but only poorly digests dsDNA with Co(2+), Ni(2+) or Zn(2+). When purified from E.coli Ca(2+) and Mg(2+) are the most abundant metals. {ECO:0000269|PubMed:32009148}; | 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:0000269|PubMed:23981508}; Vmax=1.74 umol/min/mg enzyme (at pH 6 and at 25 degrees Celsius) {ECO:0000269|PubMed:23981508}; Note=kcat is 0.03 sec(-1) with (R)-mandelonitrile as substrate (at pH 4.5 and at 25 degrees Celsius). kcat is 0.0075 sec(-1) with (R)-mandelonitrile as substrate (at pH 5.5 and at 5 degrees Celsius). {ECO:0000269|PubMed:23981508, ECO:0000269|Ref.3}; | 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 | MSLCDQCEIGCRRVGIKDIEDASAVNADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVSCSADRQILAHINKSGIYIEQLEQNPAQYLPDIPEVHLSTTSVKVDLKRPIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGEPLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMDSYVDLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSIGGPAAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFIVVDDKGNDMYSKTLA | 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:0000269|PubMed:22569531}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462; Evidence={ECO:0000269|PubMed:22569531}; | 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 (in aerobic conditions) {ECO:0000269|PubMed:22569531}; Vmax=186.2 umol/min/mg enzyme with fumarate as substrate (in anaerobic conditions); Vmax=44.3 umol/min/mg enzyme with fumarate as substrate (in aerobic conditions); Vmax=138.1 umol/min/mg enzyme with (S)-malate as substrate (in anaerobic conditions); Vmax=22.7 umol/min/mg enzyme with (S)-malate as substrate (in aerobic conditions); Note=kcat is 204.2 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). kcat is 48.6 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). kcat is 151.4 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). kcat is 24.9 sec(-1) for (S)-malate (in aerobic conditions) (PubMed:22569531). {ECO:0000269|PubMed:22569531}; | 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 | MSPSAPNTNELNSPVLETQPLAGDAALLHSSIAAGYEEIIRAPFDYLLNLPGKDVRSKMISAFNEWLCIPADKLEVIKRIVMLLHNASLLIDDIQDSSKLRRGLPVSHHIFGVPQTINAANYAYFLAQQELPKLGDPKAFEIYTEELLSLHRGQGMDIYWREASKCPTEEEYFSMVSHKTGGLFRLAIRLMQLASDKNWFVFHTRDFVPLVNVLGVIFQIRDDYLNLQSHAYTVNKGFGEDLTEGKYSFPIIHSIRSDPTNIQLSSILKQRTTDVDVKLFAVECIKATGSFEHCKEKIAELVAEARQLIKEMGNSVPGSAEAVDRVLDLIGLEPESS | 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 diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | 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 chain (PubMed:27189118). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase subA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (PubMed:27189118). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase subD through the action of the prenyltransferase subC to yield a linear alpha-pyrone diterpenoid (PubMed:27189118). Subsequent steps in the subglutinol biosynthetic pathway involve the decalin core formation, which is thought to be initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase subE (Probable). The following cyclization cascade would be catalyzed by the terpene cyclase subB (Probable). Lastly, the FAD-dependent dehydrogenase subF probably catalyzes the five-membered cyclic ether formation to complete the formation of subglutinol A (Probable). Subsequent redox reactions appear to give rise to subglutinol C and D, however, it remains unclear which enzymes are responsible for these transformations (Probable). SubD may have secondary function in the conversion of the identified subglutinols to subglutinol analog 45, which seems to be the major product of the cluster (PubMed:34863012). {ECO:0000269|PubMed:27189118, ECO:0000305|PubMed:27189118, ECO:0000305|PubMed:34863012}. | Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium anisopliae (strain ARSEF 23)) |
E9L7A5 | PAT_PETHY | MAATTTTSSSSRIAYSRHNIPGLHSDSLNPKSISFSSNLHTFSLKSSGSRRQLYSRRTGAVVIMQSMDKVEVDISLSPRVNSVKPSKTVAITDQATALVQAGVPVIRLAAGEPDFDTPAPIVEAGINAIREGHTRYTPNAGTMELRSAISHKLKEENGLSYTPDQILVSNGAKQSIIQAVLAVCSPGDEVLIPAPYWVSYPEMARLADATPVILPTSISEDFLLDPKLLESKLTEKSRLLILCSPSNPTGSVYPRKLLEQIAEIVARHPRLLVISDEIYEHIIYAPATHTSFASLPGMWDRTLTVNGFSKAFAMTGWRLGYIAGPKHFIAACNKIQSQFTSGASSISQKAAVAALGLGYAGGELVATMVKSFRERRDYLVKSFGEIEGVKISEPRGAFYLFIDLSSYYGVEVDGFGSINNSESLCRYLLDKAQVALVPGDAFGDDTCIRISYAASLSTLQAAVERIKKALVTIKPPVPV | 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; Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934, ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78; Evidence={ECO:0000269|PubMed:21102469}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20447; Evidence={ECO:0000269|PubMed:21102469}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate; Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934, ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79; Evidence={ECO:0000269|PubMed:21102469}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22882; Evidence={ECO:0000269|PubMed:21102469}; | 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|PubMed:21102469}; KM=3328 uM for glutamate (with 3 mM prephenate as cosubstrate) {ECO:0000269|PubMed:21102469}; KM=3238 uM for aspartate (with 3 mM prephenate as cosubstrate) {ECO:0000269|PubMed:21102469}; KM=2060 uM for arogenate (with 20 mM 2-oxoglutarate as cosubstrate) {ECO:0000269|PubMed:21102469}; KM=11629 uM for oxaloacetate (with 20 mM glutamate as cosubstrate) {ECO:0000269|PubMed:21102469}; Vmax=115 nmol/sec/mg enzyme toward prephenate with 20 mM aspartate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=253 nmol/sec/mg enzyme toward prephenate with 20 mM glutamate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=654 nmol/sec/mg enzyme toward 2-oxoglutarate with 20 mM aspartate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=85 nmol/sec/mg enzyme toward glutamate with 3 mM prephenate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=81 nmol/sec/mg enzyme toward aspartate with 3 mM prephenate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=120 nmol/sec/mg enzyme toward arogenate with 20 mM 2-oxoglutarate as cosubstrate {ECO:0000269|PubMed:21102469}; Vmax=1057 nmol/sec/mg enzyme toward oxaloacetate with 20 mM glutamate as cosubstrate {ECO:0000269|PubMed:21102469}; | 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, oxaloacetate and prephenate as substrates, but not phenylpyruvate or 4-hydroxyphenylpyruvate (PubMed:21102469). {ECO:0000269|PubMed:21102469}. | 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:RHEA:47349; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1, ECO:0000305|PubMed:28671263}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:28671263}; | 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 pNP-butanoate (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:23592055}; Note=kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 16 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). {ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; | 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 polyester plastic in the world (PubMed:23592055, Ref.1). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263). {ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:28671263, ECO:0000269|Ref.1}. | Thermobifida cellulosilytica |
E9NA96 | IR25A_DROME | MILMNPKTSKILWLLGFLSLLSSFSLEIAAQTTQNINVLFINEVDNEPAAKAVEVVLTYLKKNIRYGLSVQLDSIEANKSDAKVLLEAICNKYATSIEKKQTPHLILDTTKSGIASETVKSFTQALGLPTISASYGQQGDLRQWRDLDEAKQKYLLQVMPPADIIPEAIRSIVIHMNITNAAILYDDSFVMDHKYKSLLQNIQTRHVITAIAKDGKREREEQIEKLRNLDINNFFILGTLQSIRMVLESVKPAYFERNFAWHAITQNEGEISSQRDNATIMFMKPMAYTQYRDRLGLLRTTYNLNEEPQLSSAFYFDLALRSFLTIKEMLQSGAWPKDMEYLNCDDFQGGNTPQRNLDLRDYFTKITEPTSYGTFDLVTQSTQPFNGHSFMKFEMDINVLQIRGGSSVNSKSIGKWISGLNSELIVKDEEQMKNLTADTVYRIFTVVQAPFIMRDETAPKGYKGYCIDLINEIAAIVHFDYTIQEVEDGKFGNMDENGQWNGIVKKLMDKQADIGLGSMSVMAEREIVIDFTVPYYDLVGITIMMQRPSSPSSLFKFLTVLETNVWLCILAAYFFTSFLMWIFDRWSPYSYQNNREKYKDDEEKREFNLKECLWFCMTSLTPQGGGEAPKNLSGRLVAATWWLFGFIIIASYTANLAAFLTVSRLDTPVESLDDLAKQYKILYAPLNGSSAMTYFERMSNIEQMFYEIWKDLSLNDSLTAVERSKLAVWDYPVSDKYTKMWQAMQEAKLPATLDEAVARVRNSTAATGFAFLGDATDIRYLQLTNCDLQVVGEEFSRKPYAIAVQQGSHLKDQFNNAILTLLNKRQLEKLKEKWWKNDEALAKCDKPEDQSDGISIQNIGGVFIVIFVGIGMACITLVFEYWWYRYRKNPRIIDVAEANAERSNAADHPGKLVDGVILGHSGEKFEKSKAALRPRFNQYPATFKPRF | 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]; synaptic transmission, glutamatergic [GO:0035249]; temperature compensation of the circadian clock [GO:0010378]; transmission of nerve impulse [GO:0019226] | 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|PubMed:26580016}. Cell projection, cilium {ECO:0000269|PubMed:19135896}. Note=Low levels detected in the axon segment adjacent to the perikaryon in some sensory neurons of the antenna but not detected along axons as they enter the brain or at synapses within antennal lobe glomeruli. In coeloconic neurons, prominently expressed both in the perikaryon and in the distal tip of the dendrite which corresponds to the ciliated outer dendritic segment innervating the sensory hair. Relatively low levels detected in inner dendrites (PubMed:19135896). Detected in dendritic bulbs of the dorsal organ cool cells (PubMed:27126188). {ECO:0000269|PubMed:19135896, ECO:0000269|PubMed:27126188}. | 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 electrophysiological responses in multiple neuron classes in the antenna and is likely to function as part of an olfactory receptor complex with Ir76a and Ir76b (PubMed:21220098). Together with Ir21a and Ir93a, mediates the response of the larval dorsal organ cool cells, a trio of cool-responsive neurons, to cooling and is required for cool avoidance behavior (PubMed:27126188, PubMed:27161501, PubMed:27656904). Required in chordonotal organ neurons for behavioral synchronization to low-amplitude temperature cycles and mediates circadian clock resetting by temperature (PubMed:26580016). Together with Ir40a and Ir93a, mediates the response of the hydrosensory sacculus neurons to changes in relative humidity, and is required for dry detection and humidiy preference behavior (PubMed:27161501, PubMed:27656904). {ECO:0000269|PubMed:21220098, ECO:0000269|PubMed:26580016, ECO:0000269|PubMed:27126188, ECO:0000269|PubMed:27161501, ECO:0000269|PubMed:27656904}. | Drosophila melanogaster (Fruit fly) |
E9P162 | TRP6H_STRT5 | MNTRNPDKVVIVGGGTAGWMTASYLKKAFGERVSVTLVESGTIGTVGVGEATFSDIRHFFEFLDLREEEWMPACNATYKLAVRFQDWQRPGHHFYHPFEQMRSVDGFPLTDWWLQNGPTDRFDRDCFVMASLCDAGRSPRYLNGSLLQQEFDERAEEPAGLTMSEHQGKTQFPYAYHFEAALLAEFLSGYSKDRGVKHVVDEVLEVKLDDRGWISHVVTKEHGDIGGDLFVDCTGFRGVLLNQALGVPFVSYQDTLPNDSAVALQVPLDMEARGIPPYTRATAKEAGWIWTIPLIGRIGTGYVYAKDYCSPEEAERTLREFVGPEAADVEANHIRMRIGRSEQSWKNNCVAIGLSSGFVEPLESTGIFFIHHAIEQLVKHFPAGDWHPQLRAGYNSAVANVMDGVREFLVLHYLGAARNDTRYWKDTKTRAVPDALAERIERWKVQLPDSENVFPYYHGLPPYSYMAILLGTGAIGLRPSPALALADPAAAEKEFTAIRDRARFLVDTLPSQYEYFAAMGQRV | 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:0000269|PubMed:26840773}; CATALYTIC ACTIVITY: Reaction=chloride + D-tryptophan + FADH2 + O2 = 6-chloro-D-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:56528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57719, ChEBI:CHEBI:58307, ChEBI:CHEBI:140509; EC=1.14.19.59; Evidence={ECO:0000269|PubMed:21424165}; | 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-tryptophan as substrate (PubMed:21424165). kcat is 0.65 min(-1) with tryptophan as substrate (PubMed:26840773). kcat is 0.51 min(-1) with kynurenine as substrate (PubMed:26840773). kcat is 1.21 min(-1) with anthranilamide as substrate (PubMed:26840773). {ECO:0000269|PubMed:21424165, ECO:0000269|PubMed:26840773}; | 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-indolepropionic acid, N-methyltryptophan and non-indolic aromatic substrates such as kynurenine, anthranilamide and N-phenylanthranilic acid (PubMed:26840773). {ECO:0000269|PubMed:21424165, ECO:0000269|PubMed:26840773}. | Streptomyces toxytricini (Actinomyces toxytricini) |
E9P860 | ZNFX1_CAEEL | MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFLQYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYEELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPGLPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENSSSSRRRFRDEEVQEEEGDHILSSEDVHAARNVCETKILVRGVPQKNDSELSKLINGSKLYVRFERPFVKLAHNLELLYVVNYAISSRKSIVRDHSKAIIRGLFEKDFLLKLKSKFLESSFDNDTWTPEGTELLFEIFHLFFTTARYKGGFMLTLPRFAPSWHDFSMAFDIADMDGLEEAGVGDDELRNLRRLIGYIETWIKRAERERNPSPLALRSYSVYEKAGSSDSGRQVLSESRGAGSSNVYGHDEVDFVDHRRRDEFGHRDNYRTENRRHKSPDNFGEVHRRLDEQQQQRHEDESSRYRDDSRQSRRADDRRDQYQYNESTSMENHLGFHNGGGTVSEHSRDDKFVSPQNCEEKRKYCEEDTDAKPQQPYRFEEIKFEPIWVKCEKSEPPEDFKTLPSVPVLSEYVNPVEPYLRRIQDDGKYKSVHHYLDVQFRLLKEDLVSPLRDGIDLYKKNGTCKGRRIEGAPCSDISIFNVEKVDGKQVTERDGYEMRIIWPAQYDILKLLDNDREMKELGLVMLSCDRFKEDFHLGHIQSSYLMRNGSLHFAVHEETSPFKPNTTYQMAQGTSYLPCYKHVLENLKRISSFKPLPFERYLVHGSKIIFRPNFQQAEKSEYQISEEKKLMKTYNELRSLAACARYTKGKPIPRGVDDDDEDYEFSKSRELSKEDIDLEYRQLQEPIFRPLVGVDIKDSNLIQINKKWYNVSRLLDEFHPDYMDESQRLAFCNTFKYELSLIQGPPGTGKTHIGVQIVKTILQNRSYWKITEPILVVCFTNSGLDNLLERIYQMIENDEELSKDNGRPKIIRFGSKCDSNYLKRQNVMRQDVYEQYKSKVSDGAQKKMSKAGAARRHKADNLAISSYTLFCSRNKLLSYEMLSRVMDPNHQMEIQQFTYDHVDTKGIPLSPDEAIGCWLLERDFGKATKSQTKKAKKPKFQGAQLDSEDENKDYFTVEDSDDEEDELDDEKLLDKLFEKMNLECSGADILSAVHASHADEYYTKGPWEIVQDKRPSVVVLMEKKTKPCNAKFTVDEQINNLVSEIKDMILSSQPVPKKDLNDIKYIFSLARLKRWSLYITWCDALRSIVTENLPRQIREYREACENFKNAQNRVDAEIMRMTMIIGATTTGCSRLRPTLEKVGPRILIVEEAAEVLEAHIISAMISTVEHVVMIGDHKQLRPNPAVHELGVAYGLRISMFERLVERGLPFSQLRQQHRMNLTISDKIVKLSFYDNVTDAENVGLYPDVQGMATNLFFWSHTSMEESPDEVSWLNKHEISMTVALVKHLLKQNYTTNDIVVLATYSAQKNLMYREYANVFGSTPDSNVIPVETVDSFQGKERKIVIVSLVRSHRGGRENTGIGFLAVANRICVALTRAQHGMYIIGNGAYIMNNSELWNKIVNNLRRSNLIEYNLPLKCVAHGNIVTVKDPQDFATKSPEGGCMQKCDTKKFCGHVCERLCHPNMEEEHLQRCLYNCDKKCSNPQFQHRCKKACYEECGSCLYLVEVTLDCGHRITTPCSRINSSKCDQSCTKKLLCGHACAAKCGEECTLVSECSQLVGMPLSCGHIKQLTCSKISANEIDLTCDQRCEKTMLACPHKCAEICGQPCTVECMEVVNVTLGCSHSQDVVCSSFMPGMTDHIECLTKVPKTLSPCKHTELVLCKQAPSTKLCTRRCTSYLEKCGHTCENDCGICFTTKTHICQNMCQKVLNCGHTCSAKCGESCPPCKAFCTNKCEHQSCGAGERGFGRDCSKLCALCVNNCSNKCAHRSCTLKCFEECNVKPCTEPCTDKLKCGHACLGICGEQCPKICGTCERNKYIECVSGTSSTSRVHRLIMIPKCYHVFPVEVLDDHVKKQKEANEKLKCPKCSAFIVGVLRYARYTKKYYLNENMRKLESNIRNIHQSTLEGRVFQAVQDSIGEIRNVTTNLTNASEDILRNFHQKILDIRTSAETFKGKPEHKFKFASLLQVANCCLAITRLLSVSSKFRVSRRKDIPPTFDLMSVRVLGDMPFPKLIDELNRVNIHLSNTYETFMPGAIIPKLKWLISRMTVLQQLTSMCHQLVLEKKDIADSDAHAINDACLNMFRYNEQHNYALNIENFEAIVVKVAPKLLEPTPKFWSWRRLQVPEL | 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 blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with wago-4 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to perinuclear and cytoplasmic P-granules in germline blastomeres and germ cells (PubMed:29769721, PubMed:29775580). In the adult germline, co-localizes with deps-1 in P-granules (PubMed:32843637). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580, ECO:0000269|PubMed:32843637}. | 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 production of small RNAs by preventing the spread of epigenetic signals towards the 5'-end of target mRNAs (PubMed:29775580). Plays a role in small RNA-induced gene silencing in the germline (PubMed:29775580). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}. | 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:23818613}; Note=kcat is 17.9 sec(-1) with azetidine-2-carboxylate as substrate and 121 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate. {ECO:0000269|PubMed:15308773}; | 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 shown to increase the levels of reactive oxygen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress (PubMed:15308773, PubMed:20550582, PubMed:22698729). Also acetylates and thereby detoxifies the proline analog azetidine-2-carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family (PubMed:11555637). Does not acetylate proline (PubMed:11555637, PubMed:12761200). {ECO:0000269|PubMed:11555637, ECO:0000269|PubMed:12761200, ECO:0000269|PubMed:15308773, ECO:0000269|PubMed:20550582, ECO:0000269|PubMed:22698729}. | Saccharomyces cerevisiae (Baker's yeast) |
E9PSK7 | JIP3_RAT | MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGGGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVTKNNKRAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTTAGFSQRRNHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPNEEDSSNGPKPAPGRDPLTCDREGEGEPKSTHPSPEKKKAKEVPEADATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGDMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVAATANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTQSSSTQPASENGSESDGSIVQPQVEPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLMDLGHPHHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTRPGGIIHVYGDDSSDKTASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKLKNALVLSGGEGYIDFRIGDGEDDETEEGTGDVNQTKPSLSKAERSHIIVWQVSYTPE | 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]; negative regulation of apoptotic process [GO:0043066]; neuron projection development [GO:0031175]; positive regulation of JNK cascade [GO:0046330]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron migration [GO:2001224]; post-embryonic development [GO:0009791]; protein localization [GO:0008104]; protein stabilization [GO:0050821]; regulation of gene expression [GO:0010468]; regulation of JNK cascade [GO:0046328]; respiratory gaseous exchange by respiratory system [GO:0007585]; vesicle-mediated transport [GO:0016192] | 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 endoplasmic reticulum [GO:0005790] | 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 projection, dendrite {ECO:0000269|PubMed:21775604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21775604}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells. KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation. {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:23576431}. | 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 proteins (By similarity). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation. {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:21076496, ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905}. | Rattus norvegicus (Rat) |
E9PSL7 | CTRO_RAT | MLKFKYGVRNPSEASAPEPIASRASRLNLFFQGKPPLMTQQQMSALSREGVLDALFVLLEECSQPALMKIKHVSSFVRKYSDTIAELRELQPSVRDFEVRSLVGCGHFAEVQVVREKATGDVYAMKIMKKAALRAQEQVSFFEEERNILSQSTSPWIPQLQYAFQDKNNLYLVMEYQPGGDLLSLLNRYEDQLDENMIQFYLAELILAVHSVHQMGYVHRDIKPENILIDRTGHIKLVDFGSAAKMNSNKVDAKLPIGTPDYMAPEVLTVMNEDRRGTYGLDCDWWSVGVVAYEMLYGKTPFTEGTSARTFNNIMNFQRFLKFPDDPKVSSELLDLIQSLLCVQKERLKFEGLCCHPFFARTDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGYLGRSESVVSGLDSPAKISSMEKKLLIKSKELQDSQDKCHKMEQEMARLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKAKDLGKPEVGECSRLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLETMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKEASTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKVSSPGLQSKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDVSPNIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLSKFCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFASSTNSFPVSIVQANSTGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGTPARAYLEIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEQHRVPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYRDREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV | 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 [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of hippo signaling [GO:0035331]; neuron apoptotic process [GO:0051402]; phosphorylation [GO:0016310]; positive regulation of cytokinesis [GO:0032467]; regulation of actin polymerization or depolymerization [GO:0008064]; spermatogenesis [GO:0007283] | 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 [GO:0097110]; transcription coactivator binding [GO:0001223] | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P49025}; | 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 serine/threonine protein kinase activity (By similarity). Plays an important role in the regulation of cytokinesis and the development of the central nervous system (PubMed:24695496). Phosphorylates MYL9/MLC2 (By similarity). {ECO:0000250|UniProtKB:O14578, ECO:0000269|PubMed:24695496}. | Rattus norvegicus (Rat) |
E9PT37 | RBM20_RAT | MVLAAAMSQDADPSGPEQPDRDACIVPGVQGPPAPQGQQGMQPLPPPLPPPPQPQSSLPQIIQNAAKLLDKNPFSVSSQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTTHGPTGVSQHAATVPSAHFPSTAIAFSPPSQAGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSIGKAGPTPATTGFYDYGKANPGQAYGSETEGQPGFLPASASAAASGGVTYEGHYSHTGQDGQATFSKDFYGPSAQGSHAAGGFPADQAGSMKGDVGGLLQGTNSQWERPSGFSGQNKADITAGPGLWAPPASQPYELYDPEEPTSDRAPPAFGSRLNNSKQGFNCSCRRTKEGQAMLSVRPLQGHQLNDFRGLAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSESAGLRSICATGEGTLSASANSTAVYNPTGNEDYTSTLGTSYAAIPTRAFAQSNPMFPSASSGTNFAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKPALINGEKLLIRMSTRYKELQLKKPGKNVAAIIQDIHSQRERCMLREADRYGPERPRSRSPMSRSLSPRSHSPPGPSRADWGNGRDSYAWRDEDRETVPRRENGEDKRDRLDVWAHDRKHYPRQLDKAELDERLEGGRGYREKYLKSGSPGPLHSASGYKGREDGYHRKETKAKLDKHPKQQQQDVPGRSRRKEEARLREPRHPHPEDSGKEEDLEPKVTRAPEGTKSKQSEKSKTKRADRDQEGADDKKEGRGAENEAGTEEQEGMEESPASVGTQQEGTESSDPENTRTKKGQDCDSGSEPEGDNWYPTNMEELVTVDEVGEEDFIMEPDIPELEEIVPIDQKDKILPEICPCVTATLGLDLAKDFTKQGETLGNGDAELSPKLPGQVPSTSTSCPNDTDMEMAGLNLDAERKPAESETGLSPEVSNCYEKEARGAEGSDVRLAPAAQRMSSPQPADERAQQSSPFLDDCKARGSPEDGPHEVSPLEEKASPTTESDLQSQACQENSRYTETRSLNSRSPEFTEAELKEPLSLPSWEPEVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEAAKVSHCRSTVHYRNLQKYLSQLAEEGLKETEGVDSPSPERSGIGPHLERKKL | 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 of RNA splicing [GO:0043484]; RNA splicing [GO:0008380] | 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 ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:35394688}. | 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 localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role (By similarity). Subcellular localization is regulated by phosphorylation of different parts of the protein: while phosphorylation of the RS (arginine/serine-rich) region promotes nuclear localization, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (PubMed:35394688). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:35394688}. | 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:33805770, PubMed:35394688). Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts (PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899, PubMed:33805770, PubMed:35394688). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (PubMed:27289039). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23307558, ECO:0000269|PubMed:24367651, ECO:0000269|PubMed:24960161, ECO:0000269|PubMed:25573899, ECO:0000269|PubMed:27289039, ECO:0000269|PubMed:33805770, ECO:0000269|PubMed:35394688}. | Rattus norvegicus (Rat) |
E9PT87 | MYLK3_RAT | MSGVSEEDPEGLGPQGLPALGGACLVTVDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQGLHRLEASQELGLAGPGSTSPAAAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTIQNSKVDDFILQGTVPWRKGSLADGPEENKEQAEVAGVKPKHVLNTGSVQAATSRALWEESQKQDTPVGTVEGLPLIIDTSLKGADLTQAGASLRQGVEALDPGQEPPPTEAESRLPALASEDTGTTLELSVAIDRISEVLTSLRMSQSAGEGTSSSKPDCSEPGPQPLGPLTTDSDIHSDEGLPRISVRMREMTTPEELFETQGGSPIGSAEAPGPGTVLEDQIPKGARPFPPLPKRSCNNGGASAEEATGPGAEPIRGPSLVTRDWRDEPVGTTDLQQGRDPGAVSPEPGKDHAAQGPGRTEAGRRVSSAAEAAIVVLDDSAAPPAPFEHRVVSIKDTLISTSYTVSQHEVLGGGRFGQVHRCTERSTGLALAAKIIKVKNIKDREDVKNEINIMNQLSHVNLIQLYDAFESKNSFTLIMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVSQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFKGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLNHLIAKASGSNVRLRSQLLLQKYMAQRKWKKHFHVVTAVNRLRKFPTCP | 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 permeability involved in acute inflammatory response [GO:0002528]; sarcomere organization [GO:0045214]; sarcomerogenesis [GO:0048769] | 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: Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900, Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.18; | 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 | MEPLDQRRTDSDQEEGFGVQSRRATDLGMVPNLRRSNSSLCKSRRLLCSFSSEKQENLSSWIPENIKKKECVYFVESSKLSDAGKVVCECGYTHEQHIEVAIKPHTFQGKEWDPKKHVHEMPTDAFGDIVFTGLSQKVGKYVRLSQDTSSIVIYQLMTQHWGLDVPSLLISVTGGAKNFNMKLRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSCKEGDVITIGIATWGTIHNREALIHPMGGFPAEYMLDEEGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTKLEKFISEQTKERGGVAIKIPIVCVVLEGGPGTLHTIYNAITNGTPCVIVEGSGRVADVIAQVAALPVSEITISLIQQKLSVFFQEMFETFTENQIVEWTKKIQDIVRRRQLLTVFREGKDGQQDVDVAILQALLKASRSQDHFGHENWDHQLKLAVAWNRVDIARSEIFTDEWQWKPSDLHPMMTAALISNKPEFVRLFLENGVRLKEFVTWDTLLCLYENLEPSCLFHSKLQKVLAEEHERLAYASETPRLQMHHVAQVLRELLGDSTQLLYPRPRYTDRPRLSLPMPHIKLNVQGVSLRSLYKRSTGHVTFTIDPVRDLLIWAIIQNHRELAGIIWAQSQDCTAAALACSKILKELSKEEEDTDSSEEMLALADEFEHRAIGVFTECYRKDEERAQKLLVRVSEAWGKTTCLQLALEAKDMKFVSHGGIQAFLTKVWWGQLCVDNGLWRIILCMLAFPLLFTGFISFREKRLQALCRLARVRAFFNAPVVIFYLNILSYFAFLCLFAYVLMVDFQPSPSWCEYLIYLWLFSLVCEETRQLFYDPDGCGLMKMASLYFSDFWNKLDVGAILLFIAGLTCRLIPATLYPGRIILSLDFIMFCLRLMHIFTISKTLGPKIIIVKRMMKDVFFFLFLLAVWVVSFGVAKQAILIHNESRVDWIFRGVIYHSYLTIFGQIPTYIDGVNFSMDQCSPNGTDPYKPKCPESDWTGQAPAFPEWLTVTLLCLYLLFANILLLNLLIAMFNYTFQEVQEHTDQIWKFQRHDLIEEYHGRPPAPPPLILLSHLQLLIKRIVLKIPAKRHKQLKNKLEKNEEAALLSWELYLKENYLQNQQYQHKQRPEQKIQDISEKVDTMVDLLDMDRVKRSGSTEQRLASLEEQVTQMGRSLHWIVTTLKDSGFGSGAGALTLAQRAFDEPDAELSIRKKGEEGGDGYHVSARHLLYPDARIMRFPVPNEKVPWEAEFLIYDPPFYTAEKKDATLTDPVGDTAEPLSKINYNVVDGLMDRCSFHGTYVVQYGFPLNPMGRTGLRGRGSLSWFGPNHTLQPVVTRWKRNQGGGICRKSVRKMLEVLVVKLPQSEHWALPGGSREPGKMLPRKLKQVLQQEYWVTFETLLRQGTEVYKGYVDDPRNTDNAWIETVAVSIHFQDQNDVELKRLEENLQTHDPKESARGLEMSTEWQVVDRRIPLYVNHKKILQKVASLFGAHF | 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 peroxide [GO:0070301]; cellular response to purine-containing compound [GO:0071415]; cellular response to temperature stimulus [GO:0071502]; dendritic cell chemotaxis [GO:0002407]; dendritic cell differentiation [GO:0097028]; estrous cycle [GO:0044849]; manganese ion transport [GO:0006828]; positive regulation of cellular response to oxidative stress [GO:1900409]; positive regulation of insulin secretion [GO:0032024]; protein homotetramerization [GO:0051289]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of filopodium assembly [GO:0051489]; release of sequestered calcium ion into cytosol [GO:0051209]; response to heat [GO:0009408]; response to hydroperoxide [GO:0033194]; response to purine-containing compound [GO:0014074]; temperature homeostasis [GO:0001659]; zinc ion transmembrane transport [GO:0071577] | 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 activity [GO:0005272] | 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:16651700}. Cytoplasmic vesicle {ECO:0000269|PubMed:16651700}. Lysosome {ECO:0000269|PubMed:19454650}. Note=Detected at the cell membrane and in intracellular vesicles in cortical neurons. Detected on neuronal cell bodies and neurites (PubMed:16651700). Detected on the cell membrane in polymorphonuclear neutrophils. Detected on cytoplasmic vesicles and lysosomes in immature bone marrow dendritic cells (By similarity). {ECO:0000250|UniProtKB:Q91YD4, ECO:0000269|PubMed:16651700}. | 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 domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening. Extracellular calcium passes through the channel and increases channel activity (By similarity). Also contributes to Ca(2+) release from intracellular stores in response to ADP-ribose (PubMed:19454650). Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels (PubMed:25562606). Activated by moderate heat (35 to 40 degrees Celsius) (PubMed:16601673). Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species (PubMed:16260005, PubMed:16601673, PubMed:25562606). The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate. Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius) (By similarity). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (PubMed:16601673). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its function in increasing cytoplasmic Ca(2+) and Zn(2+) levels (By similarity). Confers susceptibility to cell death following oxidative stress (PubMed:11804595, PubMed:16651700, PubMed:19454650, PubMed:25562606). {ECO:0000250|UniProtKB:O94759, ECO:0000250|UniProtKB:Q91YD4, ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:16260005, ECO:0000269|PubMed:16601673, ECO:0000269|PubMed:16651700, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:25562606, ECO:0000305}. | Rattus norvegicus (Rat) |
E9PTT0 | ZDH17_RAT | MADGPDEYDTETGCVPLLHPEEIKPQSHYNHGYGEPLGRKTHVDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGGNVDAQNVKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLRKLKADKEFRQKVMLGTPFLVIWLVGFIADLNIDSWLIKGLMYGGVWATVQFLSKSFFDHSMHSALPLGIYLATKFWMYVTWFFWFWNDLSFLSIHLPFLANSVALFYNFGKSWKSDPGIIKATEEQKKKTIVELAETGSLDLSIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCVSYWGLHCETTYTKDGFWTYITQIATCSPWMFWMFLNSVFHFMWVAVLLMCQMYQITCLGITTNERMNARRYKHFKVTTTSIESPFNHGCVRNIIDFFEFRCCGLFRPVIVDWTRQYTIEYDQISGSGYQLV | 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:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi membrane vesicles. {ECO:0000250|UniProtKB:Q8IUH5}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q8IUH5}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; Evidence={ECO:0000250|UniProtKB:Q80TN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; Evidence={ECO:0000250|UniProtKB:Q80TN5}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; Evidence={ECO:0000250|UniProtKB:Q80TN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; Evidence={ECO:0000250|UniProtKB:Q80TN5}; | null | null | null | null | FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (By similarity). Also palmitoylates neuronal protein GPM6A as well as SPRED1 and SPRED3 (By similarity). Could also play a role in axonogenesis through the regulation of NTRK1 and the downstream ERK1/ERK2 signaling cascade (By similarity). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (By similarity). May play a role in Mg(2+) transport (By similarity). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Palmitoylates CASP6, thereby preventing its dimerization and subsequent activation (By similarity). {ECO:0000250|UniProtKB:Q80TN5, ECO:0000250|UniProtKB:Q8IUH5}. | Rattus norvegicus (Rat) |
E9PU28 | IMDH2_RAT | MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNESDELVAIIARTDLKKNRDYPLASKDTKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHGLHSYEKRLF | 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 camera-type eye [GO:0060041] | 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 activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. {ECO:0000250|UniProtKB:P12268}. | Rattus norvegicus (Rat) |
E9PUL5 | PRRT2_MOUSE | MAASSSQVSEMKGVEDSSKTQTEGPRHSEEGLGPVQVVAEIPDQPEALQPGPGITAAPVDSGPKAELAPETTETPVETPETVQATDLSLNPEEGSKASPSPSPSEARQEPASKPDVNRETAAEEGSEPQSTAPPEPTSEPAFQINTQSDPQPTSQPPPKPPLQAEPPTQEDPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK | 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 membrane [GO:0031629] | 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]; synaptic vesicle membrane [GO:0030672]; vesicle [GO:0031982] | 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:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747, ECO:0000305|PubMed:22632720}. Cell projection, axon {ECO:0000269|PubMed:29056747}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic density membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}. | 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 cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation (PubMed:29056747). {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}. | Mus musculus (Mouse) |
E9PUN2 | NRX2B_MOUSE | MPPGGSGQGGCPRRPPALAGPLPPPPPPPPLPLLLGLLLLLGAAEGARVSSSLSTTHHVHHFHSKHGTVPIAINRMPFLTRSGHAGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTMRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPSSGGPCQAERDDSDCEEPVEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPRPNLRTDGATGAPGVLFAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGVPTAFEPRRPPPLRPGVTSAPGFPRLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV | 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 | MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTILKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQNKEHFEPTQYSMDHFSGMHNWYACSHARPTYCNVCREVLSGVTSHGLSCEVCKFKAHKRCAVRATSNCKWTTLASIGKDIIEDEDGIAMPHQWLEGNLPVSAKCIVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLVMKCPLGLCKVSVIPPTALNSIDSDGFWKATCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGSACDDDTQLPQILAKLERASTKMLDRWSVMAYETKLPRQASSSTVTEDFSEDSEVQQILFYEDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSQESEVMAKKCSVLKEKLDSLLKTLDDESQASSSLSNPPPTIAEEAEDGDGSGNICSSTGDHLVGSACPSRPQIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQQGFVLGLSESEKKDLKTDNRVCTSSVHSESCVIAKGRSQRKASRAPCEKLVSKGLSLGSSASLPPGTGSRDSLPALNTKILYPSVRAGMSGSLPGGSVISRLLINADPFNAEPENLEYYTEKCVMNNYFGIGLDAKISLDFNNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYRNLEQKVLLECDGRPIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIKLQHHRIAQCRTVKISILGDEGVPVQVDGEAWIQPPGYIRIVHKNRAQTLTRDRAFENTLKSWEDKQKCELSRPPSFSLHPEILSEEEATQMDQFGQAAGGLIHSIREIAQSHRAMEQELAHAVNASSKAMERVYGKPRTAEGLNCSFVLEMVNNIRALRSETELLLAGKMALQLDPPQKERLGAALIEMDQQLRKLTDTPWLCQPLEPGEEESLQQNVMLDLTKRSRSGKFRLVTKFKKEKNNKNKEVHSNLGGPVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILCGIKELSRSSPAAEA | 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 endocytosis [GO:2000370]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; protein transport [GO:0015031] | 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; Xref=Rhea:RHEA:10273; Evidence={ECO:0000269|PubMed:17021016}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q16760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000250|UniProtKB:Q16760}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q16760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000250|UniProtKB:Q16760}; | 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 targets and opposite effects in numerous biological processes (PubMed:17021016). By controlling the levels of diacylglycerol, regulates for instance the PKC and EGF receptor signaling pathways and plays a crucial role during development (PubMed:17021016). May also regulate clathrin-dependent endocytosis (By similarity). {ECO:0000250|UniProtKB:Q16760, ECO:0000269|PubMed:17021016}. | Mus musculus (Mouse) |
E9PV24 | FIBA_MOUSE | MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSDGNRNPGTTGSDGTGDWGTGSPRPGSDSGNFRPANPNWGVFSEFGDSSSPATRKEYHTGKAVTSKGDKELLIGKEKVTSSGTSTTHRSCSKTITKTVTGPDGRREVVKEVITSDDGSDCGDATELDISHSFSGSLDELSERHPDLSGFFDNHFGLISPNFKEFGSKTHSDSDILTNIEDPSSHVPEFSSSSKTSTVKKQVTKTYKMADEAGSEAHREGETRNTKRGRARARPTRDCDDVLQTQTSGAQNGIFSIKPPGSSKVFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYRGTAGDALVQGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVVWVPFRGADYSLRAVRMKIRPLVGQ | 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 death domain receptors [GO:1902042]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of smooth muscle cell migration [GO:0014911]; protein polymerization [GO:0051258] | 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 epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. {ECO:0000250|UniProtKB:P02671}.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. {ECO:0000250|UniProtKB:P02671}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02671}. | 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 early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (PubMed:11389004). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood (PubMed:7649481). However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (PubMed:10930441). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (PubMed:7649481). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (PubMed:12629066). May also facilitate the immune response via both innate and T-cell mediated pathways (PubMed:23487423). {ECO:0000250|UniProtKB:P02671, ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:11389004, ECO:0000269|PubMed:12629066, ECO:0000269|PubMed:15972474, ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:23487423, ECO:0000269|PubMed:7649481}. | Mus musculus (Mouse) |
E9PV87 | TALD3_MOUSE | MKNVEFSLERGQRLKMPARKLREIVSPNQGNKLAVVEDELPRVPPALAANKRLAVETRTSSNGTLCGSLDLTSARLYHQPLLESPPASKKSDFSKDAVVRQLPLNKTEENNAPKANDIFISQYTMGQKDALRTVLKQKAQSMPVFKAVKVHLFEDTSTEKNTVAQETETPPNRIDSATTVAAATAAAIATAAPLIKVQSDLEAKVNCVGELLTKLQETDKQLQRVTEHQASVQSKQEKVHCHDHDKQMNAFMEQHIRHLEKLQQQQIDIQTHFIDAALKASSLQLGMSTSRAVGKYSGKLGSPSVGSSVFSHNTFVSKRVPLSEDTDFDGQKSPLETPAPRRFAPVPVSRDGKITKRESPTEEKENMEMNSPKGNVRLLEQVLNSNECLTRKTESSDITSLTQPKMGWNLEKRDSTETLHSQIFPSSEERGTAQVPVPKYNDVVHDLGQKKQASDMLQIKQSPVTLRLSDHPHNPALLQTTNTRSVLKDAAKILRGVQNNKKVLEENLEAIVRAKDGAAMYSFINALATNREMSEKIRIRKQVDEWIKIISAEIQDELMRKDYEQKRFDPKNQRNKKALTMSRDIKANNQEKTVNRSVIPRSHYQKQTQEQFTSPPVRNLPASGPQKERSGLLKSATTLQDEDYMLQIYGKPVYQGHRSTLKKGPYLRFSSPSPKAKPQRPRVIELVKGTKVKSAKTQTDFHAASRMKMDSKIQHPITALPHADQQYMVSPSREMPTVSGTLEGHLIPMAILLGQTQSNSDSMPPAGVTVNKPRPVTVTTSIPPASRKGNAGVKKPNVAIVEMKSEKKDPPQLSVQILPSVDIDSVSYSSTDGASSPPSPKEASLPPLHTWIQTPDFMKVDEEEVPLPGTNFDEVIDVIQEEEKRDEIPECSAPMLEFNRSVKVVPTKYNGPSFPPVVSAYHPTTDILDKVIERKETLENSLIQWVEQEIMSRIISGLFPLQQQARLDASVSVSEASEPSASDIVAGTSSGALQRMVDARVPVNSDMVSHFVNEALTETIAVMLADREAERQRAAATSVPGDLSGTETNLLARVCAPVATPQPTPPCSPSPVREHVRVKTPDSSPCESDPDAASSIKEIRVEKGSDMPAVMLVSTPTRTPVATPPPAAALTPTLSETSIDKLKLSSPELPKPWDSGDLPLDEENPNSLQELPHPRAVVMSVANEEPESVDFSAQPAPPEPAPSAPLPEGTKAPSLQRVPSSGSSTLENTLSTVTETETLDRHISEGEILFSCGQNLATKRPGDLFLMNINDSLSSTLQDALEMEDDPPSEGQVIRRPHKKRHEDAIVALLTKQQRELLVSQQEEDLDNSVGELSEGQRLVLKAAEDISAGPSGQMLPPTSPAEPSYQHADPRLVLQQSDMASGNICEDLCASHGPMSLRELELQPDSNLILPITHTTTAVSDGNLPEAAEDFSQYQQKQDSDIKQVEHKPIQRHLTSVRNKPDSTLSQHQGGPADLLLIAHVSPARMSVTLPSANLEDCSQSLSTSSMHGGTESSGTDTF | 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 basal body {ECO:0000269|PubMed:26386247}. Note=In photoreceptor cells localized to the joint between the inner and outer segments, specifically localized at the mother centriole (basal body) and the adjacent centriole as well as between the two centrioles but not in the connecting cilium (PubMed:26386247). {ECO:0000269|PubMed:26386247}. | 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 preceeds ciliary vesicle formation (By similarity). Involved in regulation of cell intracellular organization (PubMed:26386247). Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles (PubMed:25251415). {ECO:0000250|UniProtKB:Q1G7G9, ECO:0000269|PubMed:21750036, ECO:0000269|PubMed:25251415, ECO:0000269|PubMed:26386247}. | Mus musculus (Mouse) |
E9PVA8 | GCN1_MOUSE | MAADTQVSETLKRFAVKVTTASVKERREILSELGRCIAGKDLPEGAVKGLCKLFCLTLHRYRDAASRRALQAAIQQLAEAQPEATAKNLLHSLQSSGVGSKACVPSKSSGSAALLALTWTCLLVRIVFPLKAKRQGDIWNKLVEVQCLLLLEVLGGSHKHAVDGAVKKLTKLWKENPGLVEQYFSAILSLEPSQNYAAMLGLLVQFCTNHKEMDAVSQHKSTLLEFYVKNILMSKAKPPKYLLDNCAPLLRFMSHSEFKDLILPTIQKSLLRSPENVIETISSLLASVTLDLSQYALDIVKGLANQLKSNSPRLMDEAVLALRNLARQCSDSSATEALTKHLFAILGGSEGKLTIIAQKMSVLSGIGSLSHHVVSGPSGQVLNGCVAELFIPFLQQEVHEGTLVHAVSILALWCNRFTTEVPKKLTDWFKKVFSLKTSTSAVRHAYLQCMLASFRGDTLLQALDFLPLLMQTVEKAASQGTQVPTVTEGVAAALLLSKLSVADAQAEAKLSGFWQLVVDEKRQTFTSEKFLLLASEDALCTVLRLTERLFLDHPHRLTNSKVQQYYRVLVAVLLSRTWHVRRQAQQTVRKLLSSLGGVKLANGLLDELKTVLNSHKVLPLEALVTDAGEVTEMGKTYVPPRVLQEALCVISGVPGLKGDIPSTEQLAQEMLIISHHPSLVAVQSGLWPALLTRMKIDPDAFITRHLDQIIPRITTQSPLNQSSMNAMGSLSVLSPDRVLPQLISTITASVQNPALCLVTREEFSIMQTPAGELFDKSIIQSAQQDSIKKANMKRENKAYSFKEQIIEMELKEEIKKKKGIKEEVQLTSKQKEMLQAQMDKEAQIRRRLQELDGELEAALGLLDAIMARNPCGLIQYIPVLVDAFLPLLKSPLAAPRVKGPFLSLAACVMPPRLKTLGTLVSHVTLRLLKPECALDKSWCQEELPVAVRRAVSLLHTHTIPSRVGKGEPDAAPLSAPAFSLVFPMLKMVLTEMPYHSEEEEEQMAQILQILTVHAQLRASPDTPPERVDENGPELLPRVAMLRLLTWVIGTGSPRLQVLASDTLTALCASSSGEDGCAFAEQEEVDVLLAALQSPCASVRETALRGLMELRLVLPSPDTDEKSGLSLLRRLWVIKFDKEDEIRKLAERLWSTMGLDLQSDLCSLLIDDVIYHEAAVRQAGAEALSQAVARYQRQAAEVMGRLMEIYQEKLYRPPPVLDALGRVISESPPDQWEARCGLALALNKLSQYLDSSQVKPLFQFFVPDALNDRNPDVRKCMLDAALATLNAHGKENVNSLLPVFEEFLKDAPNDASYDAVRQSVVVLMGSLAKHLDKSDPKVKPIVAKLIAALSTPSQQVQESVASCLPPLVPAVKEDAGGMIQRLMQQLLESDKYAERKGAAYGLAGLVKGLGILSLKQQEMMAALTDAIQDKKNFRRREGALFAFEMLCTMLGKLFEPYVVHVLPHLLLCFGDGNQYVREAADDCAKAVMSNLSAHGVKLVLPSLLAALEEESWRTKAGSVELLGAMAYCAPKQLSSCLPNIVPKLTEVLTDSHVKVQKAGQQALRQIGSVIRNPEILAIAPVLLDALTDPSRKTQKCLQTLLDTKFVHFIDAPSLALIMPIVQRAFQDRSTDTRKMAAQIIGNMYSLTDQKDLAPYLPSVTPGLKASLLDPVPEVRTVSAKALGAMVKGMGESCFEDLLPWLMETLTYEQSSVDRSGAAQGLAEVMAGLGVEKLEKLMPEIVATASKVDIAPHVRDGYIMMFNYLPITFGDKFTPYVGPIIPCILKALADENEFVRDTALRAGQRVISMYAETAIALLLPQLEQGLFDDLWRIRFSSVQLLGDLLFHISGVTGKMTTETASEDDNFGTAQSNKAIITALGVDRRNRVLAGLYMGRSDTQLVVRQASLHVWKIVVSNTPRTLREILPTLFGLLLGFLASTCADKRTIAARTLGDLVRKLGEKILPEIIPILEEGLRSQKSDERQGVCIGLSEIMKSTSRDAVLFFSESLVPTARKALCDPLEEVREAAAKTFEQLHSTIGHQALEDILPFLLKQLDDEEVSEFALDGLKQVMAVKSRVVLPYLVPKLTTPPVNTRVLAFLSSVAGDALTRHLGVILPAVMLALKEKLGTPDEQLEMANCQAVILSVEDDTGHRIIIEDLLEATRSPEVGMRQAAAIILNMYCSRSKADYSSHLRSLVSGLIRLFNDSSPVVLEESWDALNAITKKLDAGNQLALIEELHKEIRFIGNECKGEHVPGFCLPKRGVTSILPVLREGVLTGSPEQKEEAAKGLGLVIRLTSADALRPSVVSITGPLIRILGDRFNWTVKAALLETLSLLLGKVGIALKPFLPQLQTTFTKALQDSNRGVRLKAADALGKLISIHVKVDPLFTELLNGIRAVEDPGIRDTMLQALRFVIQGAGSKVDAAIRKNLVSLLLSMLGHDEDNTRISTAGCLGELCAFLTDEELNTVLQQCLLADVSGIDWMVRHGRSLALSVAVNVAPSRLCAGRYSNEVQDMILSNAVADRIPIAMSGIRGMGFLMKYHIETGSGQLPPRLSSLLIKCLQNPCSDIRLVAEKMIWWANKEPRPPLEPQTIKPILKALLDNTKDKNTVVRAYSDQAIVNLLKMRRGEELLQSLSKILDVASLEALNECSRRSLRKLACQADSVEQVDDTILT | 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 the ribosome and acts as a sentinel for colliding ribosomes: activated following ribosome stalling and promotes recruitment of RNF14, which directly ubiquitinates EEF1A1/eEF1A, leading to its degradation (By similarity). In addition to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal protein (By similarity). GCN1 also acts as a positive activator of the integrated stress response (ISR) by mediating activation of EIF2AK4/GCN2 in response to amino acid starvation (PubMed:15937339, PubMed:24333428, PubMed:32324833). Interaction with EIF2AK4/GCN2 on translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading to phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) (PubMed:24333428, PubMed:32324833). EIF2S1/eIF-2-alpha phosphorylation converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:24333428, PubMed:32324833). {ECO:0000250|UniProtKB:Q92616, ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:24333428, ECO:0000269|PubMed:32324833}. | Mus musculus (Mouse) |
E9PVD3 | PCD16_MOUSE | MQKELSVALSCPGMKSLRTLLPLLVLLGATVPGSWGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPARDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLRLERPLDFEQRRVHELVVQARDGGAHPELGSAFVTVHVRDANDNQPSMTVIFLSADGSPRVSEAAPPGQLVARISVSDPDDGDFAHVNVSLEGGEGHFALSTQDSVIYLVCVARRLDREERDVYNLRVTATDSGSPPLRAEAAFVLHVTDVNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQITYSLAPGTHTHWFSIDPTSGIITTAATLDYELEPQPQLIVVATDGGLPPLVSSATVSVALQDVNDNEPQFQRTFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGASGSPPFRIDAHSGDVCTTRTLDRDQGPSSFDFTVTAIDGGGLKSMVYVKVFVADENDNPPQFYPREYAASLSAQSTPGTAVLRVHAHDPDQGPHGRLSYHILAGNSPPLFALDAHSGLLTVAWPLGRRANSVVQLEIGAQDGGGLQAEPIARVNISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGIIQAHNPPGRLGPVTLTLSGGDPRGLFSLDSPSGLLKTLRPLDRELLGPVLELEVRAGSGTPPVFAVARIRVLLDDVNDNSPAFPAPEDTVLLPQNTAPGTPIYTLRALDPDSGANSRITFNLLAGGDGLFTVDPTTGHVRLMGPLGPPGGPAHELEVEARDGGSPPRTSHFRLRVVIQDLGIHGLAPRFDSPTYRVDLPSGTTTGTQILQVQAQAPDGSPVTYHLAADGASSPFGLESQSGWLWVRTALDRESQELYTLKVMAVSGSKAELGQQTGTATVRVIILNQNDHSPRLSEEPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQTGEVTTLQTLDREQQSSFQLLVQVQDGGSPPRSATGTVHVAVLDLNDNSPTFLQASGAAGGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHTGELHTAASLVRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSTRVVESPDLIEADSAATVPVVLTVTAAEGLRPGSLLGSVAPQEPASVGVLTYTLVGGADPEGTFALDSASGRLYLARPLDFEAGPAWRALTVRAEGPGGAGARLLRVQVRVQDENEHAPTFARDPLALALPENPDPGATLYTFRASDADGPGPNSEVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPALLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALHVVARDPDLGEAARVSYRLAAGGDGHFRLHATTGALSVVRPLDREQRAEHVLTVVALDHGSPPRSSTQLLTVSVVDVNDEAPAFPQQEYNVILRENSPPGTSLLTLKATDPDLGANGQVTYGGVSGESFSLDPNTGVLTTLRALDREEQEEIYLTVYARDRGLPPLLTHITVRVTVEDENDHTPTFGNTHLSLEVPEGQDPQTLTTLRASDPDGGLNGQLQYRILDGDSSGAFALDLTSGEFGTMRPLDREVEPAFQLQIEARDGGQPALSATLLVTVTVLDANDHAPVFPVPSYSVEVPEDAPVGTLLLQLQAHDPDDGDNGRVMYYLGAGTAGAFLLEPTSGELSTATALDREHCASYAFSVTAVDGAAAGPLSTTVPITITVRDVNDHAPAFPTSPLRLRLPRPGPSLNKPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALGPQDRVLFIVATDLGRPARSATGVVVVGIQGEPERGPRFPRTSSEAVLRENAPPGTPVISPKAVHSGGSNGPITYSILSGNERGIFSIQPSTGAITVRSAEGLDFETSPRLRLVLQAESGGAFAFSVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEADDLDQGSGGQISYSLAASQPARGLFHVDPATGTITTTAILDREIWAETRLVLMATDRGSPALVGSATLTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQDPFSIGRYGGRVSLTGPLDFEQCDHYHLQLLAHDGPHEGHANLTVLVEDVNDNVPTFSQSLYQVMMLEHTPPGSAILSVSATDRDSGANGHISYHLASPAEGFRVDPNNGTLFTTVGAMALGHEGPGVVDVVLEARDHGAPGRTAQATVHVQLKDQNDHAPSFTLPHYRVAVSEDLPPGSTLLTLEATDADGSRTHATVDYSIISGNRGRVFQLEPRLAEVGDGVGPGPQALGCLVLLEPLDFESLTQYNLTVAAADRGQPPRSSAVPVTVTVLDVNDNPPVFTRASYRVTVPEDMPVGAELLHVEASDADPGPHGLVHFTLSSGDPLGLFELDENSGALRLSRPLDCETQAQHQLVVQAADPAGTHFSLVPVTVEVQDVNDHGPAFPLSLLSTSLAENQPPGTLVTTLHAIDGDAGTFGRLRYSLLEAVPGPEGREAFSLNSSTGELRARVPFDYEHTGSFRLLVGAADAGNLSASVTVSVLITGEDEYDPVFLAPSFHFQVPEGAQRGHSLGHVQATDEDGGADGLVLYSLATSSPYFGINQTTGALYLRVDSRAPGSGTTTSGGGGRTRREAPRELRLEVVARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVLGLVRARSRKAEAAPGPMSQTAPIASSSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAGGPYPRGGSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDADGLSDTSCEPPAPDTWYKGRKAGLLLPGAGATLYREEGPPATATAFLGGCGLSPAPAGDYGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAHPGAKSVPPKPASTAVARAIFPPASHRSPISHEGSLSSAAMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSTESGLEPPDDTELRI | 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]; cochlea development [GO:0090102]; condensed mesenchymal cell proliferation [GO:0072137]; digestive tract development [GO:0048565]; establishment of planar polarity [GO:0001736]; heart morphogenesis [GO:0003007]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; hippo signaling [GO:0035329]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; kidney development [GO:0001822]; mitral valve formation [GO:0003192]; mitral valve morphogenesis [GO:0003183]; nephron development [GO:0072006]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; ossification involved in bone maturation [GO:0043931]; pattern specification process [GO:0007389]; post-anal tail morphogenesis [GO:0036342]; protein localization to plasma membrane [GO:0072659] | 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:24056717, ECO:0000269|PubMed:26258302}. | Mus musculus (Mouse) |
E9PVX6 | KI67_MOUSE | MASSAHLVTIKRSGDDGAHFPLSLSSCLFGRSIECDIRIQLPVVSKRHCKIEVKEQEAILYNFSSTNPTQVNGVTIDEPVRLRHGDIITIIDRSFRYEDGNHEDGSKPTEFPGKSLGKEPSRRASRDSFCADPDGEGQDTKASKMTASRRSFVYAKGLSADSPASDGSKNSVSQDSSGHVEQHTGRNIVEPTSGDLFKKSRSTGSSYREPKSSPTQSLSNSNEKESPFEKLYQSMKEELDVKSQKSCRKSEPQPDRAAEESRETQLLVSGRARAKSSGSTPVTAASSPKVGKIWTERWRGGMVPVQTSTETAKMKTPVRHSQQLKDEDSRVTGRRHSVNLDEGESAQAVHKTVTPGKLATRNQAAVEAGDVASPADTPEHSSSKKRSIPAKVEAPSAETQKRLSLTQRLVPGEKKTPKGSFSKPEKLATAAEQTCSGLPGLSSVDISNFGDSINKSEGMPMKRRRVSFGGHLRPELFDENLPPNTPLKRGETPTKRKSLGTHSPAVLKTIIKERPQSPGKQESPGITPPRTNDQRRRSGRTSSGSKFLCETDIPKKAGRKSGNLPAKRASISRSQHGILQMICSKRRSGASEANLIVAKSWADVVKLGVKQTQTKVAKHVPQKQTSKRQRRPSTPKKPTSNLHNQFTTGHANSPCTIVVGRAQIEKVSVPARPYKMLNNLMLNRKVDFSEDLSGLTEMFKTPVKEKQQQMSDTGSVLSNSANLSERQLQVTNSGDIPEPITTEILGEKVLSSTRNAAKQQSDRYSASPTLRRRSIKHENTVQTPKNVHNITDLEKKTPVSETEPLKTASSVSKLRRSRELRHTLVETMNEKTEAVLAENTTARHLRGTFREQKVDQQVQDNENAPQRCKESGELSEGSEKTSARRSSARKQKPTKDLLGSQMVTQTADYAEELLSQGQGTIQNLEESMHMQNTSISEDQGITEKKVNIIVYATKEKHSPKTPGKKAQPLEGPAGLKEHFETPNPKDKPITEDRTRVLCKSPQVTTENITTNTKPQTSTSGKKVDMKEESSALTKRIHMPGESRHNPKILKLECEDIKALKQSENEMLTSTVNGSKRTLEKSKKKAQPLEDLTCFQELFISPVPTNIIKKIPSKSPHTQPVRTPASTKRLSKTGLSKVDVRQEPSTLGKRTKSPGRAPGTPAPVQEENDSTAFMETPKQKLDFAGNSSGSKRRSRTSKNRSQPLEDLDGFQELFQTPAGASDSVTVEESAKISLESSQAEPVKTPASTKRRSKMSLMKVDMKELSILEKQTQSRGRDAGTPAPMQEGNGTTAIMETPKQKLDFTGNSTGHKRRPRTPKIRAQPLEDLDGFQELFQTPAGANDSVTVEESAKMSLESSQAEPVKTPASTKRLSKTDLSKVDVREDPSILGKKTKSPGRAPGTPAPVQEENDCTAYMETPKQKLESIENLTGLRKQSRTPKDITGFQDSFQIPDHANGPLVVVKTKKMFFNSPQPESAITRKSRERQSRASISKIDVKEELLESEEHLQLGEGVDTFQVSTNKVIRSSRKPAKRKLDSTAGMPNSKRMRCSSKDNTPCLEDLNGFQELFQMPGYANDSLTTGISTMLARSPQLGPVRTQINKKSLPKIILRKMDVTEEISGLWKQSLGRVHTTQEQEDNAIKAIMEIPKETLQTAADGTRLTRQPQTPKEKVQPLEDHSVFQELFQTSRYCSDPLIGNKQTRMSLRSPQPGFVRTPRTSKRLAKTSVGNIAVREKISPVSLPQCATGEVVHIPIGPEDDTENKGVKESTPQTLDSSASRTVSKRQQGAHEERPQFSGDLFHPQELFQTPASGKDPVTVDETTKIALQSPQPGHIINPASMKRQSNMSLRKDMREFSILEKQTQSRGRDAGTPAPMQEENGTTAIMETPKQKLDFIGNSTGHKRRPRTPKNRAQPLEDLDGFQELFQTPAGASDPVSVEESAKISLASSQAEPVRTPASTKRRSKTGLSKVDVRQEPSTLGKRMKSLGRAPGTPAPVQEENDSTAFMETPKQKLDFTGNSSGHKRRPQTPKIRAQPLEDLDGFQELFQTPAGANDSVTVEESVKMSLESSQAEPVKTPASTKRLSKTGLSKVDVREDPSILEKKTKSPGTPAPVQEENDCTAFMETPKQKLDFTGNSSGHKRRPRTPKIRAQPLEDLDGFQELFQTPAGASDSVTVEESAKMSLESSQAKPVKTPASTKRLSKTGLSKVDVREDPSTLGKKTKSPGRAPGTPAPVQEENDSTAFMETPKQKLDFAENSSGSKRRSRTSKNRSQPLEDLDGFQELFQTPAGASNPVSVEESAKISLESSQAEPVRTRASTKRLSKTGLNKMDVREGHSPLSKSSCASQKVMQTLTLGEDHGRETKDGKVLLAQKLEPAIYVTRGKRQQRSCKKRSQSPEDLSGVQEVFQTSGHNKDSVTVDNLAKLPSSSPPLEPTDTSVTSRRQARTGLRKVHVKNELSGGIMHPQISGEIVDLPREPEGEGKVIKTRKQSVKRKLDTEVNVPRSKRQRITRAEKTLEDLPGFQELCQAPSLVMDSVIVEKTPKMPDKSPEPVDTTSETQARRRLRRLVVTEEPIPQRKTTRVVRQTRNTQKEPISDNQGMEEFKESSVQKQDPSVSLTGRRNQPRTVKEKTQPLEELTSFQEETAKRISSKSPQPEEKETLAGLKRQLRIQLINDGVKEEPTAQRKQPSRETRNTLKEPVGDSINVEEVKKSTKQKIDPVASVPVSKRPRRVPKEKAQALELAGLKGPIQTLGHTDESASDKGPTQMPCNSLQPEQVDSFQSSPRRPRTRRGKVEADEEPSAVRKTVSTSRQTMRSRKVPEIGNNGTQVSKASIKQTLDTVAKVTGSRRQLRTHKDGVQPLEVLGDSKEITQISDHSEKLAHDTSILKSTQQQKPDSVKPLRTCRRVLRASKEDPKEVLVDTRDHATLQSKSNPLLSPKRKSARDGSIVRTRALRSLAPKQEATDEKPVPEKKRAASSKRHVSPEPVKMKHLKIVSNKLESVEEQVSTVMKTEEMEAKRENPVTPDQNSRYRKKTNVKQPRPKFDASAENVGIKKNEKTMKTASQETELQNPDDGAKKSTSRGQVSGKRTCLRSRGTTEMPQPCEAEEKTSKPAAEILIKPQEEKGVSGESDVRCLRSRKTRVALDSEPKPRVTRGTKKDAKTLKEDEDIVCTKKLRTRS | 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 mitotic nuclear division [GO:0007088]; stem cell proliferation [GO:0072089] | 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 layer, and covers a substantial fraction of the mitotic chromosome surface (PubMed:12355204, PubMed:8834799). Associates with satellite DNA in G1 phase (By similarity). Binds tightly to chromatin in interphase, chromatin-binding decreases in mitosis when it associates with the surface of the condensed chromosomes (By similarity). Predominantly localized in the G1 phase in the perinucleolar region, in the later phases it is also detected throughout the nuclear interior, being predominantly localized in the nuclear matrix (By similarity). {ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. | 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 chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (By similarity). Does not contribute to the internal structure of mitotic chromosomes (PubMed:26949251). May play a role in chromatin organization (PubMed:26949251). It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed. {ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:26949251, ECO:0000269|PubMed:27362226, ECO:0000305}. | Mus musculus (Mouse) |
E9PX95 | ABCAH_MOUSE | MEVLKKLKLLLWKNFILKRRKTLITLLEMLMPLLFCAIVLYLRLNSMPRKKSSTNYPAVDVSLLPVYFYNYPLKSKFQLAYIPSKSETLKAVTEVVEQTFAVDFEVLGFPSVPLFEDYIIKDPKSFYILVGIIFHHDFNSSNEPLPLVVKYDLRFSYVQRNFVSPPRHLFFQEEIEGWCTAFLYPPNLSQAPREFSYADGGNPGYNKEGFLAIQHAVDKAIMRHHAPKAALNMFKDLHVLVQRFPFGPHIQDPFLVILQNEFPLLLMLSFICVELIITNSVLSEKERKQKEYMSMMGVESWLHWVAWFITFFISVSITVSVMTVLFCTKINRVAVFRNSNPTLIFIFLMCFAIATIFFAFMMSTFFQRAHVGTVIGGTVFFFTYLPYMYITFSYHQRTYTQKILSCLFSNVAMATGVRFISLFEAEGTGIQWRNIGSVWGDFSFAQVLGMLLLDSFLYCLIAFLVESLFPRKFGIPKSWYIFAKKPVPEIPPLLNIGDPEKPSKGNFMQDEPTNQMNTIEIQHLYKVFYSGRSKRTAIRDLSMNLYKGQVTVLLGHNGAGKTTVCSVLTGLITPSKGHAYIHGCEISKDMVQIRKSLGWCPQHDILFDNFTVTDHLYFYGQLKGLSPQDCHEQTQEMLHLLGLKDKWNSRSKFLSGGMKRKLSIGIALIAGSKVLILDEPTSGLDSPSRRAIWDLLQQQKGDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSPSFLKQKYGAGYYMTIIKTPLCDTSKLSEVIYHHIPNAVLESNIGEEMIVTLPKKTIHRFEALFNDLELRQTELGISTFATSVTTMEEVFIRVCKLADPSTNVLTEKRHSLHPLPRHHRVPVDRIKCLHSGTFPVSTEQPMRLNTGFCLLCQQFYAMLLKKITYSRRNWMLVLSVQVLLPLAIIMLSLTFFNFKLRKLDNVPLELTLQTYGQTIVPFFIAENSHLDPQLSDDFVKMLVAAGQVPLRIQGSVEDFLLKKAKEAPEGFDKLYVVAASFEDVNNHTTVKALFNNQAYHSPSLALTLVDNLLFKLLSGANASITTTNYPQPQTAIEVSESILYQGPKGHYLVVNFLFGIAFLSSSFSILTVGEKSVKSKSLQFVSGVSTAVFWLSALLWDLISFLVPTLLLVLVFLWYKEEAFAHHESIPAVVLIMMLYGWAVIPLVYTVSFSFNTPGSACVKLVVMLTFLSISPVVLVTVTSEKDLGYTELSDSLDHIFLILPGHCLGMALSNLYYNFELKKFCSAKNLSDIDCNDVLEGYVVQENIYAWESLGIGKYLTALAVLGPVYITMLFLTEANAFYVLKSRLSGFFPSFWKEKSGMIFDVAEPEDEDVLEEAETIKRYLETLVKKNPLVVKEVSKVYKDKVPLLAVNKVSFVVKEEECFGLLGLNGAGKTSIFNMLTSEQPITSGDAFVKGFNIKSDIAKVRQWIGYCPEFDALLNFMTGREMLVMYARIRGIPECHIKACVDLILENLLMCVCADKLVKTYSGGNKRMLSTGIALVGEPAVILLDEPSTGMDPVARRLLWDTVERVRESGKTIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGISYSLQAKVRRKWQQQMLEEFKAFVDLTFPGSNLEDEHQNMLQYYLPGPNLSWAKVFSIMEQAKKDYMLEDYSISQLSLEDIFLNFTRPESSTKEQIQQEQAVLASPSPPSNSRPISSPPSRLSSPTPKPLPSPPPSEPILL | 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; Xref=Rhea:RHEA:39052; Evidence={ECO:0000305|PubMed:22237709}; | 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:0000269|PubMed:22237709}. | Mus musculus (Mouse) |
E9PXF8 | MTMRD_MOUSE | MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHYCSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQSALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLNGMAFAGFVSERGPPYRACDLFDELVAFEVERIKVEEKNPLKMIKHIRELAEQLFKNENPNPHMAFQKVPRPTEGSHLRVHILPFPKINEARVQELIQENLAKNQNAPPATRIEKKCVVPAGPPVVSIMEKVITVFNSAQRLEVVRNCISFIFENKTLETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKDDNHIPHLKQKLPDGQHQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRASAPGDWESGSNSIVTNSIAGSVAESYDTESGFEDSENSDVANSVVRFIARFIDKVCTESGVTQDHIRSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLPGEEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQLQQSVQEGLQITSASFQLIKVAFDEEVSPEVVDIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFSKTIVKGAKKAGKMTIGRQYLLKKRTGTIVEERVNRPGWNEEDDISVSDDSELPTSTTLKASEKSTMEQLVEKACFRDYQRLGLGTISGNSSRSKPEYFRVTASNRLYSLCRSYPGLLVIPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGFHGKGVVGLFKSQNSPQAVSTSSLESSSSIEQEKYLQALLTAVIVHQKLRGSSTLTVRPALALSPVHGYRDKSFTQSNPKSSAKEPVHNQGVWASLRSSTRLISSPTSFIDVGARLAGKDHSASFSNSTYLQNQLLKRQAALYIFGEKSQLRSSKVEFAFNCEFVPVEFHEIRQVKASFKKLMRACIPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVWVCLEEGWDITTQVTSLAQLLSDPFYRTIAGFRTLVEKEWLSFGHKFSQRSSLALNSQGGGFAPIFLQFLDCVHQVHNQYPTEFEFNLYYLKFLAFHYVSNRFKTFLLDSDYERLEHGTLFDDKGDKHAKKGVCIWECIDKMHTRSPIFFNYLYSPVEVEALKPNVNVSSLKKWDYYTEETLSAGPSYDWMMLTPKHFPYEESDVAGGAGPQSQRKTVWPCYDDVTCSQPDALTRLFSEIEKLEHKLNQTPERWHQLWEKVTTDLKEEPRTAHSLRHSAGSPGIASTNVPSYQKRPALHPLHRGLGEDQSTTTAPSNGVEHRAATLYSQYTSKNDENRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKYTSDKAFFDLKTSKRVYNFCAQDGQSAQQWMDRIQSCISDA | 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:23297362}; Peripheral membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23297362}. Note=Associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (PubMed:16399794). Membrane localization is likely to be mediated via its interaction with MTMR2 (PubMed:23297362). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}. | 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 to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Acts as an adapter for the phosphatase MTMR2 (PubMed:16399794). Increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate (PubMed:16399794). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794}. | Mus musculus (Mouse) |
E9PXX9 | S28A1_MOUSE | MADDTPRQRESISLTPVAHGLENMGAEFLEIMEEGQLPHRHSSLPEGGGSRSKAVWKPFSRWRSLQPTVQARSLCREHWQLFEWISKGLLSTAYIGFLIVACLLDFPRALALFVITCVVLVFLAYNLLKRLLGSKLKKCVKFQGHSCLSLWLKRGLALAAGLGVILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFVAFQWLGDQIRVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDASSLIAASVMAAPCALALSKLVYPEVEESKFRSEEGVKLTYGDAQNLVEAASAGAAISVKVVANIAANLIAFLAVLAFINAALSWLGDMVDIQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQELSQYKQRRLAGAEEWLGDKKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRRSDFSQIVLRALITGAFVSLVNACVAGILYVPRGVEVDCMSLLNQTVSSSSFEVYLCCRQVFQNTSLEFGQEALHNCCRFYNHTVCT | 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:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337}; CATALYTIC ACTIVITY: Reaction=cytidine(out) + Na(+)(out) = cytidine(in) + Na(+)(in); Xref=Rhea:RHEA:69895, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337}; CATALYTIC ACTIVITY: Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337}; | 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 velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit). Involved in renal nucleoside (re)absorption. {ECO:0000250|UniProtKB:O00337}. | Mus musculus (Mouse) |
E9PY46 | IF140_MOUSE | MALYFDHRIKAPDTPSSPSHITWHPTHPFLAVASISPSSGGNVDIYLEQGEPVPDTHIERSFQATSLCWHPTRLILAIGWETGEVIMFNKQDKEQHTVPLPHTTDIAILSWSTSGSCLVSGDKLGVLLLWRLDQRGRVQGTPLLKHEYGKALTHCIFRLPPPGEDLVQLAKAAVSGDEKALDMFNWRKSSFGSFLKTGSQEGLSFFVSLMDGTVHYVDEKGKTAQVASTDSSIQTLFYIERREALVVVTENLLLSLYVVTPEGEAEEVMKVKLSGKTGCRADITLIEGSLLVTAIGEPVLRFWDLERGENYILSLQEKFGFEKGESINCVCFCKAKGLLAAGTNKGRVAMWKKVPSFPNGRGAEGKDMWALQTPTELEGNITQIKWGSRKNLLAVSSTESVSILSEQAMSSHFHQQVAAVQISPSLVNVSFLSTGGTHSLHTDMHISGVFATKDAVAVWNGKQVAIFEPSGSTLRNAGTFLCETSVLAMHEESIYTVEPNRLQVRTWQGTVKQLLLFSETEGSPCFLDVCGTFLVAGTDLAHFKSFDLSRREAKVHCSCKNLAQLVPDVGSITSLRCNANGNKISILLSKVNNSPDSKIYIYDVEMDTVNVFNFTTGQIGQIQTLPFNEPPTNETRSFMDKSLAGYTPVNHFWDQSEPRLFVCEALQEAPGAQPQAVDKQPRVEEGTCHKEEVLILSFFASEEHGFLLHDSFPRPSTYQSLLGMEVPHYYFTKKPGEADKEDRVDSGYYHIPQMVAKRPLRDFVGLEDCDKSTRDAMLNFSFFVTIGDMDEAFKSIKLIKSEAVWENMARMCVKTQRLDVAKVCLGNMGHARGARALREAEQEPELEARVAMLAIQLGMLEEAEQLYKKCKRYDLLNKFYQASDQWQKAVEVAELHDRVHLRTTYYNYAKHLEASADCGQALSYYEKSDTHRFEVPRMLSEDLQSLELYINRMKDKTLWRWWAQYLESQAEMDTALRYYELAQDYFSLVRIHCFQGNIQKAAEIANETGDWAASYHLARQYESQDEVKQAVHFYTRAQAFNNAIRLCKENGLDDQLMNLALLSSPEDMIEAARYYEEKGEQMDRAVMLYHKAGHFSKALELAFTTQQFAALQLIAEDLDEKSDPALLARCSDFCIEHRQFEKAVELLLAAKKYHEALQLCLEQNMTITEDMAEKMTVSKDSKDMSEESRRELLEQIANCCMRQGNYHLATKKYTQAGNKLKAMRALLKSGDTEKIVFFAGVSRQKEIYIMAANYLQSLDWRKEPEIMKSIISFYTKGRALDLLAGFYDACAQVEIDEYQNYDKAHGALTEAYKCLSKAKTKNPLDQETKLAQLQSKMTLVKRFIQARRTYTEDPKESLRQCELLLEEPDLDSTIRVGDVYGFLVEHHVQMEEYQMAYKYLEEMRKRLPSANMSYYVDQRTVDTVHQGLGLLPPSRIMPERVRHNSMEDHKEVYEEVIEEVDNDP | 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 retrograde transport [GO:0035721]; intraciliary transport [GO:0042073]; limb morphogenesis [GO:0035108]; neural tube patterning [GO:0021532]; non-motile cilium assembly [GO:1905515]; photoreceptor cell outer segment organization [GO:0035845]; protein localization to cilium [GO:0061512]; regulation of cilium assembly [GO:1902017]; regulation of smoothened signaling pathway [GO:0008589] | 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|PubMed:24009529, ECO:0000269|PubMed:24619649}. | 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:22282595). Required for the development and maintenance of the outer segments of rod and cone photoreceptor cells. Plays a role in maintenance and the delivery of opsin to the outer segment of photoreceptor cells (PubMed:24619649). {ECO:0000250|UniProtKB:Q96RY7, ECO:0000269|PubMed:22282595, ECO:0000269|PubMed:24619649}. | Mus musculus (Mouse) |
E9PY61 | GP179_MOUSE | MGARAVVISSLAWGLLSCCFLCSGALGSQRPLRSLPPLPSQAKPRSEPMWMPPKGAEAALAFLYSGDVQRLSGANCSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLECHEGQLRPGWLVTVSATFYGLKPDLTPEVRGQVQMDIDLQSVDINQCASGPGWYSNTHLCDLNSTQCVPLESQGFVLGRYLCRCRPGFYGASGSGGLEESATQAAGQFGSPQDSLGKLLRCQPCPEGCTSCLDATPCLVEEALALRTAVLACQACCMLAVFLSMLVAYRCRGSKRIRASGIVLLETILFGSLLLYFPVFILYFKPSVFRCVALRWVRLLGFAVVYGTIILKLYRVLQLFLSRTAQRVPHPSSGQLLRRLGQLLLLVLGFLVVWTAGALEPGTQHTALVTRGHTPTGRHFYLCHHDHWDYIMVVAEMLLLCWGSFLCYATRAVPSAFHEPRYMSIALHNELLLSTAFHTARFVLVPSLHPDWTLLLFFLHTHSTVTATLALIFIPKFWKPGAPPREEILDEVYEDELDLQRSGSYLNSSIASAWSERSLEPGDIRDELKKLYAQLEIRKTKEMAANNPHLPKKRGSSHQGLGRSFMRYLAEFPEALARQHSRDSGSLGLGSLPGSSRRRLLSSSLQETEKPPALRKTRSTYDHHREHNTLPFDSTLRRTLSKKASPTDGRESLADGPPALGFRSASAHNLTVGERLPRARPISLQKSLSVAAGSREKALLVASQAYLEETYRQAKEREERKKAEAAMVSPVRRPSTRRLEWPLRAPLSAPPSPGKSSSMDSSQTTARPHEEAGRRLPHPPIRHQVSTPVLALSGICLGEPRMLSPTPASTLAPILLPAPAPAPAPVLAPVSKPPQSPTLLTFICPWENAELPGKKENVVQEDPAGPERSGHSPASARTKIWRALSVAVEKRGTGESEALTEGGHVQGEADDTDEEKPKVFSKSHSLKTPLQQGSVRSLGLAIKALTRSRSTYKEKDGGEGTPETEKGKPTEVSTGAPLRSPRLGRPKAVSKQVALAPCEDEESLQNQQNAHTSRMLHVCQKEGSREQEDRNKRVAPGPGERKVERTGKITMTTLRQVFGEKNAEQAKESPAGYQEVPNPALQSLGSADHRVAEVCPWEVTEPESGMDPPESVNKAKVYSWERTEGGSLEKKPSRQVLSRSWEEREKVLAESETEGVGAIPRKKPERLVRSQEAVCPWESPDSGGLSPQLVHQESDRTGGRFVVVSKGDAHPEALPSHAAKAELCLWEMSDVGEGTSTQRVQELPEERQKSPKKATFWGERNLGGDLVSLCPWESTDFRGPSAVSLQAPGSSGSLGSGIAEVCPWEAENIANDKKAEVCPWELGEELAGSDGLNPGADGKSLPGKETPSRKGCLAESGEQTVRAKPTVPQGQESVCPWEDEAPERSSPQPDKASSKAGEKLLSHGGSQVLQVCPWEAVKPEEKQATLSTAEICPWEVDGQPETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQKQEAICPWESMAPGSTPQRDTEKAQASLQRQGSVAGRAAEICPWEVGTEVGEERTIGAEASEARPNDAGHASTDSGSRQVAASAPKKSERLGSEKEVVCPWDSLSPGDSSQQPDTPNTEKLKDELQEHGSSRPIEVCPWEAEEVPTGEKAKICPWELNEGTVGKGLEREPGCEPERQRRQNLEEAGLPFQEEGTSKGDTKLCREQEGEAICPWKPPAQVPKVSDLPLSTVGQGVEGQSLEASDRASEKGELRQDLKMGSLPEYITQVVPVDGGGASSELQPISLQEGMVLAGSSSHPHIQCPDQPRVSSQPLVSTGDGTAEVCPWDAPDSDSDTKVEPCAQKVTGRVTETEMSRQDEKEKSQEEKERAPETRDHEGVAVQKMPQTSNFGKQEAVCPRESQDFGVQAATDASDGSKGGSEKVCPWEVEEVPSIKEAEICPWEASPGAVGEGALDLGQDGESQGEGRAERHLLKAAETVCPLEGTMSSGLFTQEDVVDTDLPKVGLHGASSPGKGLAELCVWEVTDPEGNKIKGTMADICPWEETRAQSDESGPLALPVTQAGVPAAPEKSVCLSVHGPLESFLPESKSVRPDISKPPGSSRPEGVREQEPLELETGAKSVPKPSPTETEAPESFTLTDDQGLMASEGEAGELSPPPDYPWDCE | 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:24790204}. Note=Specifically localizes to the tips of retinal ON-bipolar dendrites. {ECO:0000269|PubMed:22325362, ECO:0000269|PubMed:24790204}. | 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 recruits and regulates the R7 group RGS-GNB5 complexes instead of activating G proteins: promotes the GTPase activator activity of R7 RGS proteins, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:22689652, PubMed:24790204). Associates with components of metabotropic signaling cascade in retina ON-bipolar neurons, such as TRPM1 and GRM6: may control the ability of the GRM6 cascade to gate TRPM1 (PubMed:24114537, PubMed:24790204). {ECO:0000269|PubMed:22325362, ECO:0000269|PubMed:22689652, ECO:0000269|PubMed:24114537, ECO:0000269|PubMed:24790204, ECO:0000269|PubMed:30282023, ECO:0000269|PubMed:33922602}. | Mus musculus (Mouse) |
E9PYH6 | SET1A_MOUSE | MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVSDSKYTPVEDLQDPRCHVRSKARDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAAAETTEARRRSSSDTAAYPAGTTVGGTPGNGTPCSQDTNFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDSFSRRHFSTSSAPATTATATSATAAATAASSSSSSSSSSSSSSSSSSSASQFRGSDSSYPAYYESWNRYQRHTSYPPRRATREDPSGASFAENTAERFPPSYTSYLAPEPNRSTDQDYRPPASEAPPPEPPEPGGGGGGSGGGGGGGGGGGGGAPSPEREEARTPPRPASPARSGSPAPETTNESVPFAQHSSLDSRIEMLLKEQRSKFSFLASDTEEEEENSSAGPGARDAGAEVPSGAGHGPCTPPPAPANFEDVAPTGSGEPGAARESPKANGQNQASPCSSGEDMEISDDDRGGSPPPAPTPPQQPPPPPPPPPPPPPPYLASLPLGYPPHQPAYLLPPRPDGPPPPEYPPPPPPPPPHIYDFVNSLELMDRLGAQWGGMPMSFQMQTQMLTRLHQLRQGKGLTAASAGPPGGAFGEAFLPFPPPQEAAYGLPYALYTQGQEGRGSYSREAYHLPLPMAAEPLPSSSVSGEEARLPHREEAEIAESKVLPSAGTVGRVLATLVQEMKSIMQRDLNRKMVENVAFGAFDQWWESKEEKAKPFQNAAKQQAKEEDKEKMKLKEPGMLSLVDWAKSGGITGIEAFAFGSGLRGALRLPSFKVKRKEPSEISEASEEKRPRPSTPAEEDEDDPEREKEAGEPGRPGTKPPKRDEERGKTQGKHRKSFTLDSEGEEASQESSSEKDEDDDDEDEEDEEQEEAVDATKKEAEASDGEDEDSDSSSQCSLYADSDGENGSTSDSESGSSSSSSSSSSSSSSSSSSESSSEEEEQSAVIPSASPPREVPEPLPAPDEKPETDGLVDSPVMPLSEKETLPTQPAGPAEEPPPSVPQPPAEPPAGPPDAAPRLDERPSSPIPLLPPPKKRRKTVSFSAAEEAPVPEPSTAAPLQAKSSGPVSRKVPRVVERTIRNLPLDHASLVKSWPEEVARGGRNRAGGRVRSTEEEEATESGTEVDLAVLADLALTPARRGLATLPTGDDSEATETSDEAERPSPLLSHILLEHNYALAIKPPPTTPAPRPLEPAPALAALFSSPADEVLEAPEVVVAEAEEPKQQLQQQHPEQEGEEEEEDEEEESESSESSSSSSSDEEGAIRRRSLRSHTRRRRPPLPPPPPPPPSFEPRSEFEQMTILYDIWNSGLDLEDMSYLRLTYERLLQQTSGADWLNDTHWVQHTITNLSTPKRKRRPQDGPREHQTGSARSEGYYPISKKEKDKYLDVCPVSARQLEGGDTQGTNRVLSERRSEQRRLLSAIGTSAIMDSDLLKLNQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQMVADMREKRYVQEGIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVDEEITYDYKFPLEDNKIPCLCGTESCRGSLN | 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:1902275]; regulation of erythrocyte differentiation [GO:0045646]; stem cell population maintenance [GO:0019827]; stem cell proliferation [GO:0072089]; transcription initiation-coupled chromatin remodeling [GO:0045815] | 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 each bind to a unique set of target genes (By similarity). Predominantly nuclear (By similarity). {ECO:0000250|UniProtKB:O15047}. | 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=2.1.1.364; Evidence={ECO:0000305|PubMed:24550110}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265; Evidence={ECO:0000305|PubMed:24550110}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000305|PubMed:24550110}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269; Evidence={ECO:0000305|PubMed:24550110}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000305|PubMed:24550110}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60273; Evidence={ECO:0000305|PubMed:24550110}; | 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 transcription and DNA repair take place (By similarity). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis (PubMed:24550110, PubMed:29490266, PubMed:31197650). Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent nucleosome remodeling and RAD51 nucleofilaments stabilization at reversed forks, protecting them from nucleolytic degradation. Does not methylate 'Lys-4' of histone H3 if the neighboring 'Lys-9' residue is already methylated (By similarity). Has RNA binding activity towards transcripts involved in RNA processing and the DNA damage response (By similarity). {ECO:0000250|UniProtKB:O15047, ECO:0000269|PubMed:24550110, ECO:0000269|PubMed:29490266, ECO:0000269|PubMed:31197650}. | Mus musculus (Mouse) |
E9PYI1 | ZN568_MOUSE | MERLSQMAGRRAWCAEDSVPRQEEEDRTRPSKTVTFKDVAVDLTQEEWQQMKPAQRALYRDVMLETYSNLVTVGCQVTKPDVIFKLEQAEEPWVLEEEMFWRRSPEAARGRMKSFAFKDMAKDLRFEDVVIYFSLEEWECLRHSHRNLYRAVMLDNYSNLLSLSLADTKPRVVSLLEQGKEPWMVMRNETKIWHPDWVSRTEAKDSSKIKTLQEKMAKKHTCPTLEDSKTRGDREVTRELEGQQVHQEGHLRQAAVTSVERPDSVQCTAHREAHPGGKPCSSEKSQKTSLCQPPPIEREQLHSKAKASEHAQHGKVFNSCTSDTAVHPRPQESRKDSERKKSALAGGPDTSKPQSAQGSERPHKCKECGKAFHTPSQLSHHQKLHVGEKPYKCQECGKAFPSNAQLSLHHRVHTDEKCFECKECGKAFMRPSHLLRHQRIHTGEKPHKCKECGKAFRYDTQLSLHLLTHAGARRFECKDCDKVYSCASQLALHQMSHTGEKPHKCKECGKGFISDSHLLRHQSVHTGETPYKCKECGKGFRRGSELARHQRAHSGDKPYKCKECGKSFTCTTELFRHQKVHTGDRPHKCKECGKAFIRRSELTHHERSHSGEKPYECKECGKTFGRGSELSRHQKIHTGEKPYKCQQCGKAFIRGSHLTQHQRIHTGRRSE | 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 transcription by RNA polymerase II [GO:0000122]; regulation of cell communication [GO:0010646]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; 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 transcript of IGF2, in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers (PubMed:18701545, PubMed:22110054, PubMed:28522536). Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta (PubMed:18701545, PubMed:21094155). May enhance proliferation or maintenance of neural stem cells (PubMed:23071813). {ECO:0000269|PubMed:18701545, ECO:0000269|PubMed:21094155, ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:23071813, ECO:0000269|PubMed:27658112}. | Mus musculus (Mouse) |
E9PYK3 | PARP4_MOUSE | MTLGIFANCIFCLKVKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQRRLLDVRNYDPLSPAPAAPPAERSRSEVQSEYLPSDNTPEKENTEVTEVSAENVEIPPFLQDFEVVKYNILEKVGGPETVVVELQSSQDPESCPFVITAHFLLADQKTRRESTGKQTSEGAIEYYESYVEDLKRQGFLLQEHFTAEATQLASEKLQALLLEEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDSPGQLQKTMAEFYRLLPHRHPASEEVNLRLLAQKEDLCQLVRDMVNVCETNLSKPNPPSLAKYRALRCKIEHVDQNTEEFSRVRKEVLQNNRSEQPVDILQIFRVGRVNEATEFLSKLGNVRLLFHGSPVRNILGILSRGLLLPKVAEDRGVQRTDVGNLGSGIYFSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQDDEFVVYKTNQVKMKYIVKFCTPGDQIKEFHPHENTEVEEQRAEPSSVPEAGDFQLPDIKPFTNIKAGLQDASANPVPLDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEARQEYREAVSQGHGAYLMDQDTPDVFTVSVGNLPPRAKVLIKITYITELSIQSPVAIFFIPGTVAPWQQDKALNENLQDTVETIRIKEIGAEQSFSLAMSIEMPYMIEFISSDTHELRQKSTDCKAVVSTVEGSSLDSGGFSLHIGLRDAYLPRMWVEKHPEKESEACMLVFQPELADVLPDLRGKNEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDFWKVLRYLSLLYPSEGFRNILLISDGHLQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFEYFNSKSKHSWKKQIEAQMTRIRSPSCHSVSVKWQQLSRDAPEPLQAPAWVPSLFHNDRLLVYGFIPHCTQATLQAFIQEKEFCTMVSTTELQKTTGTMIHKLAARALIRDYEDGILHDDETNHEMKKNIMKSLIIELSKENSLITQFTSFVAVEKRDVNEIPFANVPNISELVAKEDVDFLPYVSWQEKQPEASISQTEIDSSRLKHNKLSDGHGVLQPVSVSSEVNEKPSLLLAAKKRKIKTIKKCSLDISEDFEDRTAVAQSPATAQSLNFHLPLSVRPQLKAVEQQLHGNRLEPKQRGGFRKLLMAKKCRNVPDSLVSSAPAVTAEFSYLSACSSSSAFLSPLCDIPSSLPPHPLGGTHPPPPLPLPDGTHLPSPLFGSTHPPPPLFGGTLIPPPSSLFGGTHLPPPPPLPGGTHIPPPPPIPGGTLIPPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPLPGGTHIPPPPPIPGGTLIPSPSSLFGGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPAGTQFSLSPIGFIPPKLGPPKLSHSHKLVGDTNIHDSEPPLLGFKDLCSRDMGFSCGTAFSGSFASSKDFDPGKFSQGPNNISFSPKAPEMGVLHQSPFCSPPKPPSAPPLVTNVLCSEAPQSYFLNLQSAAVHQSPNNRVSEIIMESVESSLPSDYSSRDASSYLALEGAEDSLLGGSSFETDTDEAAAFIANDLLTSIETSSDEECAFCDEDQESPVPWASLFALQTENGFWKLTPELGLILNLNVNALLTSLEEKGIRSLGTKGRERLLDLIATLLVLQFLYTKLEQEGMVAKSLIKMDDAFISRNIPWAFENIKKAREWARKTEGQYPSICQRLELGKDWESATKQLLGIQPQANTSLHRILYYSQG | 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: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:Q9UKK3}; | 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 | MHSSPTSTRKQASFAASASAQPRKSISFINPSKSSAGKGYAASNPNKLAVSRTMGFLTDMKPAEKLNVPSAKTVQVLDSKGVDVTPRPLYHPDPHAASAKPNKLLTSQEGSLGSDYISSYSLYQNTLNPSMLGQYTRSVLGSSSVSKSSISTTESMSEDLEDSSYKRDRLASFTDVRVLRSTAEAAISKEELEKTIEIILTETETLRFFDLPTVMFSTESEEAEKIIEKNKKYETLCRNRLGNDLYVERMMQTFNGAPKNKEVQCEKIILEEKGVVATTWDLYDSYNIPETLLAAKRSGYSSKGSLPAKDRDPKIQDSESSSLMDIENVILAKVQEDEEDNSEAILKSDKLHQDLFYMERVLMENVFQPKLAAYRQLPVYKEHEPEEPEETLQVENLKVAEDEPKKEDEEEVEMELELEIATEQSTIPANLERLWSFSCDLTKGLNVSSLSWNKANPDLLAVGYGNFGFREQKKGMACCWSIKNPMWPERIYQSSYGVTSVDFSNSSPNLLAVGYHNGTVAIYNVQSSHNIPVLDSSESPQKHLGPVWQVQWIEQDRGTTGDDKREILVSISADGRISKWIIRKGLDCHDLMRLKRTTATGGKKGGEKEKKGEALISRQAPGMCFAFHPKDTNIYLAGTEEGLIHKCSCSYNEQYLETYRGHKGPVYKVTWNPFCPDVFLSCSADWGVMIWHQDTVKPFLSFYPTTYVVYDVSWSPKSAYIFAAANENRVEIWDLQISTLDPLIVNVANPGIKFTTVLFAKETDCLLVGDSDGQVAVYELRNMPTASDTSRGDVINILLGPKTNHTG | 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 | MIWYVATLIASVISTRGLVAQGAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLGASAKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLTVQYPARVLNMPPVIYVPVGIHGYIRCPVDAEPPATVVKWNKDGRPLQVEKNLGWTLMEDGSIRIEEATEEALGTYTCVPYNTLGTMGQSAPARLVLKDPPYFTVLPGWEYRQEAGRELLIPCAAAGDPFPVITWRKVGKPSRSKHNALPSGSLQFRALSKEDHGEWECVATNVVTSITASTHLTVIGTSPHAPGSVRVHVSMTTANVSWEPGYDGGYEQTFSVWMKRAQFGPHDWLSLSVPPGPSWLLVDSLEPETAYQFSVLAQNRLGTSAFSEVVTVNTLAFPVTTPEPLVLVTPPRCLTANRTQQGVLLSWLPPANHSFPIDRYIMEFRVGERWEMLDDAIPGTDGDFFAKDLSQDTWYEFRVLAVMQDLISEPSNIAGVSSTDIFPQPDLTDDGLARPVLAGIVATICFLAAAILFSTLAACFVNKQRKRKLKRKKDPPLSITHCRKSLESPLSSGKVSPESIRTLRAPSESSDDQGQPAAKRMLSPTREKELSLYKKTKRAISSRKYSVAKAEAEAEATTPIELISRGPDGRFVMGPSEMEPSVKGRRIEGFPFAEETDMYPEFRQSDEENEDPLVPTSVAALKPQLTPMSSSQDSYLPPPAYSPRFQPRGLEGPSGLGGRLQATGQARPPAPRPFQHGQYYGYLSSSSPGEVEPPPFYMPEVGSPLSSVMSSPPLHTEGPFGHPTIPEENGENASNSTLPLTQTPTGGRSPEPWGRPEFPFGGLETPAMMFPHQLHPCDVAESLQPKACLPRGLPPAPLQVPAAYPGMLSLEAPKGWVGKSPGRGPIPAPPATKWQERPMQPLVSQGQLRHTSQGMGIPVLPYPEPAEPGGHGGPSTFGLDTRWYEPQPRPRPSPRQARRAEPSLHQVVLQPSRLSPLTQSPLSSRTGSPELAARARPRPGLLQQAEMSEITLQPPAAVSFSRKSTPSSTGSPSQSSRSGSPSYRPTMGFTTLATGYPSPPPGPAPPAPGDTLDVFGQTPSPRRMGEEPLRPEPPTTLPTSG | 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 | MMLAWLVSLLSMEVLLLAKPYSSFQFEPAEGSLAGGTWITVVFDGLDRSILYPNNGSQLQIDLVSVAIPTLRIPCDVSPAFVDLPVVTCQTRSLPSEADAGPYSLEMRSGEQVLGTPCPGSLDSCTFKFSKDQTPVLYQVYPASGVPGEVVSVYGRVITTWLETFDPDVDYIESPLILEAREDKWLTPCSLINRQTGSCFPIQEEHGLGNVQCRVEGDYIGSQNVSFSVFNKGRSMVHKEAWLISAKQELFLYQTYPEILSVFPKVGSLGGRTDIIITGDFFDPSARVTIAGIPCDIRYVSPRKIECTTRAPGNEARLTAPQAGNRGLRFEVGDATKDVELTEATPGYRWQIVPNASSPSGFWSKEGRPFRARLSGFFVAPQTNNYTFWIQADSQASLCFSSSEEPRTKVEVASVGVGTADWFDSWEQIGNEGSWHQKTTKLELQGGAKYYLEAEQHGIAPSRGMRIGVQIHNTWLNPDVVNTYLLEKHQIRARAQRLPEIQVLHVSGKGNFFLTWGNVSSQPVPANATAQQIQTTIEELLVVKCNLAPFSAHVLLRLGFEQGLEGSRSDGVRTSSTEPFCGRFSLGQLGHLILIPEAADKGYQLDRYPYLCLAYRGHMNKTLDMTVSFLFGFQTIMKNITCDWSLTDPHPESWQFTCINLWDTCLCHSEDIQSSLANTPLLAHRIDIRPVVPEAGLLYVDEIILADTNVTVSQADSGRACPGGNVVESVSVVGVPPVYSISSWLAGCGSELPLITACSVSTEGTGDGSELIEVTAQRLQRTSPPLGGHFFLYLSDTVIPDVPVRMSARQLHKLLQDSADESTSGYLNAGDFTVTEDLNSCYEHVWTLSWTTQTGDLPNFIRVSDQNLTGVNPTVTARVVYDGGVFLGPIFGDMLATANQQTQVAVQVNDIPAYCSGSCSFQYQQESTPSVDHVWYSLGSDVNLLVHFTGTGFPRDTQFLQVTVNKTSCEVLFSNETNVACELALLPVGVHQIFMLVIPSGLAVHASGEDLLLHVEPRLDAVEPSTAAEIGGRWVTLRGSSLEGVSLVLFGTQSCVIDAIRSNSQQIQCKVPPRGKDGYTVNVTVISGDHSTVLARAFTYVSSLNPVIVSLSRNRSSIAGGEILFLGMSLLVNYTDLDVQIHVQDTSAQVLSQTAWGLEVVLPPLVPGIHVISAFINGVSIRSQGVDLYIQYLTEVFSVEPCSGSLLGGTLLSLLGTGLGRDPALIRVLVDNHPCDIVNLTEVNIWCETPPAVLPPRADVLTVLASVEIWAGNTSFFHGPSLVGKGFTFTYEAAATPVVTAMWGEFRNNSVRFYVEGSNISDSVILLGSLKCELEVQFFGDSMNLSGCFFPLHSLEAGVYTLQVRHKRMGFANMSVVPQKFELSPQIIAIFPTHGSKCGGTVLTVKGMAFSSRKRSVHVDISGPFACMILSLEDHTVLCQTRFVGDQFSEASLALNITVLVNGLTSKCKGNCTLFIEEAATPIVDALTISISGSLTMVLMRGRRLATTADEPIAFVDDQLPCHTTFFNTSHVACQIRDLAPGFHYLSAVHTSAGYACLNSVSRNFFIVPQVLDYFPKDFSIHGGSLLTIKGTALRGWKATVVYVGRQACLTVNFSSDFIQCIVPAGNGSAALEIDVNGVLYHIGLVDYSSIFTPELLSVSRSQDILTFTVARISGAANVDIFIGTSPCLGVAGNRTVLQCMVPLLPAGEYLVTGYDHSRGWASSTLILVLRATVTSVTKNYGCLGGRLLHVLGAGFSPGNISAAVCGAPCQVLANATVSAFSCLVLPLHVSLAFLCDLRHAEDSCKVRSSTYLRCDLTVSMGTERLPGSWPYVYLCEESSLCLFEPDHWTESVFPSFSGLFLSPKVERDEVLIYNSSCNITMETEAEMECEMPNQPITAKITEIQKSWGQNTQGNFSFQFCRRWSRPHSWFPQRVPHDGDSVTVETGHLLLLDANTSFLNSLHIKGGKLIFMDPGPIELRAHSILITDGGELHIGSEEKPFQGKARIKIYGSVHSTPFFPYGVKFLAVRNGTLSLHGSVPEVTVTYLQAAAHAGDKVLTLGEAVDWKPGDEAVITSGMTVAGAEATEVVVVETVHNADLHLRNPLRYSYDFRENWVAGENPILKPTVALLSRNIIIQGNFTLERVKLLNSCQEANTAKGNLKHCLYSKSEKMLGARDLGARVIIQSFPEEPSFVKLKGVQFRDLGQAFHKHLSSLALVGAMRGSYIQSCSVWNSFSRGLSMHRTWGLKVDSNVFYKIVGHALLLGSYLDGRFSTSETVTGRKNGWWEQGSTIRNNVIISVSAAEGLSGSEMLAPAGIYTFSPTNVMEGNRVCAAGYGYVFHLVTSQTLQAPLLSFNWNTAHSCTRYGLLVYPKFQPPWNNDTGFTLFQNFMVWGSAGGAQIFRSNNLHLKNFQVYACRDFGIDILESDANTLITDSFLLGHFTHKGSLCMSAGIKTPQRWELTISNTTFVNFDGNCVAIRTCSGCFQGQGGYTVKTRQLKFVNSSNLVAFPFPHAAVLEDLDGSLSGKNGSHVLASMETLSDTCLTNASFSQIVPGSVCGEAVLFHRMSIALANSLDVPKNLTITDISNKTITVNYVEDTLSNYYGWMALLLDQETYSLQFESPWMNRSLQYSATFDSFAPGNYLLIMHRDLPPYPDILLRCGSQVGHSLPFHPLPSQDRACDWFFNRQLRQLTYLVSGEGQVKVFLQLKPGVPPSVSASTSVPESASRWSLPETWQDVEKGWGGYNHTIPGPGDDVLILPNKTVLVDTDLPVLRCLYVMGTLEFPVDRSNVLSVACLLIAGGELKVGTLENPLEKDQRLLIFLRASEEVVCDYFEGIHVDPGTIGVYGKLRLHSAYPKKSWVHLGADIAPGNERIIVHNAVDWQPHDTIVLSSSSYEAHEAEVLTVKEVKGHHIRIYERLKHRHIGSTHTMEDGQQVHLAAEVGLLTRNIRIQPDSSCRGRLLVGSFRKSSGEDFSGVLQLLNVEIQNMGLPLYSSIEFTGVSAGSWVISSTVHQSCSVGIHASSSHGVILTDNVVFGTNGHGIDVEGQNYSLTNNLVILTMQSANSSPWVAGIKVNYAEDIILHGNVVAGSERLGFHVGGHGCSSEVLWSDNVVHSSLHGLHLYKKHESNNCTGVSGFMAFKNFDYGAMVQTENSVDIQNITLVDNTVGLLAITYVSSALLSSVSTVQITLRNSVIVATSSSFDCIHDRKAPQSANWTSTDRAPSNPRGGRIGILWPVSASEPNAWPQEPWHKVRSRHSVPGIMKLQDVTFSSFVKSCYSNDLDVCILPNEYSTGVMYPITAERTRMLGIKDKNKFYFPVLQSSKDLVGTICPTLVCEYPRKYLFTDLDGRTLGLPPPVSVFPRTEEEWTGSFLNTGIFREEQKCTFRAMNQGFFCKQTEHAVLILDNVDATWTIPKSHPLVSVTNGFVDTFSIVKDSDLCPPTSSLSTFYSILPTRQMTKVCFPEQTPPFLRFLLLGNQRASKLILAVFYNEIQSPHVFLDKSFIPPTPLESAFSLLAEPSGANYFDIMNNLLYVVLQGEEPVEIHSSVSIHLALTVTFSVLEKGWERAMLESLSDFFQIDPNQIRLTLEMPGNKETLEAIANSERKRKRNCPSVTCGGPSIRYGQRRPLMAEMTSLKITPATTLETFSKVIVIEVGDLPNIRNSEPIQSLPSNRLQRLVNQVITAQQTGALENVLGMTVGALLVTQSKGVTGYRNASSLITGNLIYTRPSELSILVQPSDGEVGIELPVQPRLVFLDEKNERVESLGLPSEPWIISVSLEGASESVLKGCTLAETRDGYVTFSRLAVLISGSNWHLFFTVISPPGTNFTARSRTFVVLPVASKERSTIILALSLCSVASWVALSCLVCCWFKKSKTRKIKPEDISESQAKEQKKNTHNSSKPRGLQAKTAKENTLMGEDMRMKVMQGMQSQFPQHSMDGVSKRKVSRLAVTEERTTTPAPKIPRITCVPGSLAQQLTLQEPGNWQEAQQQLLRYQLAGRNQLLLLRPDLRQERKQGQEPSQLDKGSDCTGLSQEKATCIPTETFSLHTAPPETIQ | 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 homeostasis [GO:0006874]; kidney development [GO:0001822]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; positive regulation of epithelial cell proliferation [GO:0050679]; regulation of cell adhesion [GO:0030155]; regulation of cell-cell adhesion [GO:0022407]; regulation of cell-matrix adhesion [GO:0001952]; regulation of centrosome duplication [GO:0010824]; regulation of cholangiocyte proliferation [GO:1904054]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of establishment of planar polarity [GO:0090175]; regulation of TOR signaling [GO:0032006] | 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:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | 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 domain, whereas at least one cleavage occurs within the cytoplasmic domain (PubMed:16956880). Cleaved by a probable proprotein convertase which produces an extracellular domain (polyductin extracellular domain, (PECD)) and a C-terminal fragment (polyductin transmembrane fragment (PTM)) which are tethered together by disulfide bonds (PubMed:17470460, PubMed:28729032). This extracellular domain (PECD) is then shed from the primary cilium by activation of a member of the ADAM metalloproteinase disintegrins family, resulting in concomitant release of an intra-cellular C-terminal fragment (ICD) via a gamma-secretase-dependent process (PubMed:17470460, PubMed:28729032). The proteolytic cleavage of the C-terminal intracellular fragment (ICD) is controlled by cytosolic calcium concentration and activation of PKC (PubMed:16956880). {ECO:0000269|PubMed:16956880, ECO:0000269|PubMed:17470460, ECO:0000269|PubMed:28729032}. | 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|PubMed:17470460, ECO:0000269|PubMed:18202188, ECO:0000269|PubMed:20048263, ECO:0000269|PubMed:22021705, ECO:0000269|PubMed:28154160}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P08F94}. Chromosome, centromere {ECO:0000250|UniProtKB:P08F94}. Nucleus {ECO:0000269|PubMed:16956880}. Secreted, extracellular exosome {ECO:0000269|PubMed:22021705, ECO:0000269|PubMed:28729032}. Secreted {ECO:0000269|PubMed:22021705, ECO:0000269|PubMed:28729032}. Endoplasmic reticulum {ECO:0000269|PubMed:28729032}. Golgi apparatus {ECO:0000269|PubMed:28729032}. Note=The intra-cellular C-terminal fragment (ICD) translocates to the nucleus and is not detected in primary cilia (PubMed:16956880, PubMed:28729032). The extracellular domain (PECD) traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (PubMed:22021705, PubMed:28729032). In the urine, the extracellular domain (PECD) exists as an highly abundant secreted form and a less abundant PECD form that is either tethered to or shed with the C-terminal fragment (PTM) in ELVs (PubMed:28729032). The majority of full length PKHD1 protein resides at the endoplasmic reticulum and cannot pass beyond the mid-Golgi apparatus and is not detected in primary cilia (PubMed:28729032). {ECO:0000269|PubMed:16956880, ECO:0000269|PubMed:22021705, ECO:0000269|PubMed:28729032}. | 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 regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (PubMed:19959710). During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (By similarity). Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (PubMed:20875407). May act in collecting-duct and biliary differentiation (By similarity). May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity). {ECO:0000250|UniProtKB:E2RK30, ECO:0000250|UniProtKB:P08F94, ECO:0000269|PubMed:18235088, ECO:0000269|PubMed:19959710, ECO:0000269|PubMed:20875407}. | Mus musculus (Mouse) |
E9PZJ8 | ASCC3_MOUSE | MALPRLTGALRSFSNVTKQDNYNEEVADLKLKRSKLHEQVLDFGLTWKKIVKFLNEKLEKNKMQNINEDLKDILQAAKQIVGTDNGREAIESGAAFLFMTFHMTDSVGYMETKAIRQTFGPFPSSSATSACNATNRIISHFSQDDLTAFVQMAENPCNDRVVFGKNLAFSFDMYDLDHFDELPINGESQKTISLDYKKFLNEQFQEPYTPELKPVEKTNGSLLWCEVEKYLNATLKEMTEAARVEDLCCTLYDMLASAKSGDELQDELFELLGPEGLDLIEKLLQNRITIVDRFLNSSSDHKFQVLQDSCKKILGENSKPNYGCQVTIQSEQEKQLMKQYRREEKRIARREKKAGEDGEVSGEGVLPFDPKELRIQREHALLNARNAPILGRQRDVEFEKIRYPHVYDSQAQARETSAFIAGAKMILPEGIQRENTKLYEEVRIPYGEPMPVGFEEKPVYIKDLDEVGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFDGRFRPVPLGQTFLGIKSTNKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSGQISCFLPTEGPEYGHALKQVQKSRNKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDKLSHYLSLLTQQNPIESQFLESLADNLNAEIALGTVTNVEEAVRWMSYTYLYVRMRANPLAYGISHKAYQIDPTLRKHREQLLIEVGQKLDKAKMIRFEERTGYFSSTDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSYGKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHILTRLEEKNLTVDKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVINKEAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINFQHLILPERHPPHTELLDLQPLPITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEQEMDNIIGTVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRYVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIKKDFYKKFLYEPFPVESSLLGVLSDHLNAEIAGGTITSKQDAMDYITWTYFFRRLIMNPSYYSLGDVSQDSINKFLSHLIGQSLVELELSHCIEVGEDNRTIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPHTKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIEQHHLHLFRKWKPPVKSSHAKCRTSIECLPELIHACEGKDHVFSSMVEKELQPAKTKQAWNFLSRLPVINVGISVKGSWDDLVEGHNELSISTLTADKRDENKWIKLHADQEYVLQVSLQRVHFGLPKGKHENHAVTPRFPKLKDEGWFLILGEVDKRELMAVKRVGFVRTHHDASISFFTPETPGRYIFTLYLMSDCYLGLDQQYDIYLNVIKANISTKDSDVFTDLSV | 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 in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation. Drives the splitting of stalled ribosomes that are ubiquitinated in a ZNF598-dependent manner, as part of the ribosome quality control trigger (RQT) complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. {ECO:0000250|UniProtKB:Q8N3C0}. | Mus musculus (Mouse) |
E9PZM4 | CHD2_MOUSE | MMRNKDKSQEEDSSLHSNASSRSASEEVSGSDSGSQSESEQGSEPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNVKEEASSGSESGSPKRRGQRQLKKQEKWKQDPSEDEQEQGTSAESEAEQKKGKARRPVPRRTVPKPQVKKQPKIQRGKRKKQESSDDDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSDDLIEMTGEGGDEQQDNSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSDDFDTEREEGEVQYLIKWKGWSYIHSTWESEDSLQQQKVKGLKKLENFKKKEDEVKQWLGKVSPEDVEYFSCQQELASELNKQYQIVERVIAVKTSKSTLGQTDFPAHSRKPAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSRNNSKTIPTRECKALKQRPRFVALKKQPAYLGGESLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGTRGSTSGFLNIVMELKKCCNHCYLIKAPEDSERESGQEVLQSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRMDTTGRTVLENNSGRSNSNPFNKEELTAILKFGAEDLFKEIEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQFKVANFATMEDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYMLPRIRSSTKKAQTNDSDSDTESKRQAQRSSASESETDDSDDDKKPKRRGRPRSVRKDLVEGFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCVSAMQEYEEQLKESTSEGKGPGKRRGPTIKISGVQVNVKSIIQHEEEFEMLHKSIPVDPEEKKKYCLTCRVKAAHFDVEWGVEDDSRLLLGIYEHGYGNWELIKTDPELKLTDKILPVETDKKPQGKQLQTRVDYLLKLLRKGLEKKGTVASGEEAKLKKRKPRVKKENKAPRLKDEHGLEPASPRHSDNPSEEGEVKDDGLEKSPTKKKQKKKENKENKEKPVSSRKDREGDKERKKSKDKKEKVKGGDGKSSSKSKRSQGPVHITAGSEPVPIGEDEDDDLDQETFSICKERMRPVKKALKQLDKPDKGLSVQEQLEHTRNCLLKIGDRIAECLKAYSDQEHIKLWRRNLWIFVSKFTEFDARKLHKLYKMAHKKRSQEEEEQKKKDDSLGGKKPFRPEASGSSRDSLISQSHTSHNLHPQKPHLPASHGPQMHGHPRDNYSHPNKRHFSNADRGDWQRERKFNYGGGNSAPWGGDRHHQYEQHWYKDHHYGDRRHMDAHRSGSYRPNNMSRKRPYEQYNSDRDHRGHRDYYDRHHHDSKRRRSDDFRPQNYHQQDFRRMSDHRPTMGYHGQGPSDHYRSFHTDKLGEYKQPMPSLHTALSDPRSPPSQKSPHDSKSPLDHRSPLERSLEQKNNPDYNWNVRKT | 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:0000978] | 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 the onset of myogenic gene expression, promoting their expression. {ECO:0000269|PubMed:22569126}. | Mus musculus (Mouse) |
E9PZQ0 | RYR1_MOUSE | MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSGCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLGLTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIYSTAGLYNQFIKGLDSFSGKPRGSGPPAGSALPIEGVILSLQDLIGYFEPPSEELQHEEKQTKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFLTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLQPIKEYRREGPRGPHLVGPSRCLSHLDFVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVDSQSRGDRARIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFRDIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPLEHPHYEVARMDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLASPGLQPPAEDEARAAEPDTDYENLRRSAGGWGEAEGGKDGTAKEGTPGGTAQAGVEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPSTPALPRLPRDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVDTRRAGERLGWAVQCQEPLMMMALHIPEENRCMDILELSERLDLQRFHSHTLSLYRSVCALGNNRVAHALCSHVDQAQLLHALEDARLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRSAEDGPRRHGLPGVGVTTSLRPPHHFSPPCFVVALPAAGATEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGVFSDEDVKQILKMIEPEVFREEEEVEEEGEEEEEDEEEKEEDEEEEAHEKEDEEKEEAEDAAEEEKEELEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAECYVDKMQGNQRGRYGLLMKAFTMSAAETARRTREFRSPPQEQINMLLHFKNGADEEECPLPEEIRQELVNFHQDLLAHCGIQLEGEEEEPEEESTLGSRLMSLLEKVKLVKKTEEKPEEEPAPEEHKPQSLQELVSHTVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISVSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPETHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRIAMPCLCAIAGALPPDYVDASYSSKTEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTVEKAREGEEEKTEKKKTRKISQTAQTYDPREGYNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGSHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTRNPYVEKLRPALGECLARLAAAMPVAFLEPELNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMAEIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLRSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNPNAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADNKSKMAKAGDVQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIVLAKARYALKDTDEEVREFLQNNLNLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYHLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKASWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEEGGEEEEVEVSFEEKEMEKQRLLYQQSRLHNRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGESEKMEMFVSFCEDTIFEMQIAAQISEPEGEPEEDEDEGAEEAEEGAAGSDGSGSAAAAGVWVWLAATAGRTLRGLSYRSLRRRVRRLRRLTAREAATAVAALLWALVTRAGGAGAGAAAGALRLLWGSLFGGGLVDSAKKVTVTELLAGMPDPTGDEVHGQQPSGAGSDAEGEGEGEGEGDAADGAGDEEAAADQAGTGGADGAVAVADGSPFRPEGAGGLGDMGDTTPVEPPTPEGSPILKRKLGVDGEEEEPPPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKTPPPPPPKKEEAGGAGLEEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMSGAGSGDGSGWGSRAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWIMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS | 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 bone maturation [GO:0043931]; outflow tract morphogenesis [GO:0003151]; protein homotetramerization [GO:0051289]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of muscle contraction [GO:0006937]; regulation of response to osmotic stress [GO:0047484]; release of sequestered calcium ion into cytosol [GO:0051209]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to caffeine [GO:0031000]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; skeletal muscle fiber development [GO:0048741]; skin development [GO:0043588]; striated muscle contraction [GO:0006941] | 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:0048471]; protein-containing complex [GO:0032991]; ryanodine receptor complex [GO:1990425]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; vesicle [GO:0031982]; Z disc [GO:0030018] | 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 very high-level exercise increases S-nitrosylation. {ECO:0000250, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:22036948}. | 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 high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (PubMed:18268335). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain (PubMed:22036948). Required for normal embryonic development of muscle fibers and skeletal muscle (PubMed:7515481). Required for normal heart morphogenesis, skin development and ossification during embryogenesis (PubMed:18003898, PubMed:7515481). {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7515481, ECO:0000269|PubMed:7621815}. | Mus musculus (Mouse) |
E9PZZ1 | PRD13_MOUSE | MPAHVTPRTEDARRGAGPSSACGCSWFCHLRPVEDPASPSVCLAAVATMHGTSRTSATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVLSGGGGRAFLPQEHAARPGASPVAEGLGLPPKPTVPDLTAPVQAIALRPQAPAAQLAQACGARESIKREASLAPLATSPPPGKWGTPKKGKEQPDRAHSQFLGIVGGSSGGGGGLPFYPGVRSAFKPAGLARAAAQSDPYREEGGGKGPGLALGRLLGGGRAGGRPGSGESPAGHHHHHHHAHHHHHHHPKCLLAGEPPPAGLPCPGALRAFPLLAGHPEEASAFKHVERAPPAAATTSLPSARYAALPAPGLPVERCALQPLDGGSLKAYPGGGGGGECSPLPAVMPAFTVYSGDLLYGPPAAYYPLKLHLGGLLKYPESISYLSGPAAAAAAAAAAAAAAAAIGPAELGSLASIDREIAMHTQQLSEMAAGKSRARLDSGTLPPAVVAATGPGGGGGGGSAAGKPKTGHLCLYCGKLYSRKYGLKIHMRTHTGYKPLKCKVCLRPFGDPSNLNKHIRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLMAKAGDGPGPEPSYALEPGDPKSEDSDVDVCFTDDQSDPEAGGRGEHDS | 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:0000250, ECO:0000269|PubMed:34730112}. | Mus musculus (Mouse) |
E9Q0N2 | PTPRH_MOUSE | MARAGGNCGVWRSLVLLGLYGCSVVRAAGTSVTVDRHAPASSYEFSMWVEKDGVSSSPQIPVTTAAPNPVRNLRVEGQNNISISLSWEPPDQSSLQGLTYWTQCSRHGGQTETRNTTDTSVTVDGLDPGSSYECSVWVEKDGLYSKNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTTDTSITVDGLDPGSSYECSVWVEKDGVYSTNETLSNTTAPNPVRNLRVKSQNNFSISLSWEPPDQPSLQGLIYWAQCSRHGGQTETRNTTDTSVTVDGLDPGFLYKCSVWVEKDGVYSTNETLNTSTVPISASNPVRNLRVEGQNNFSISLSWEPPDQSSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTVPAAVNITSCISTSGGYGVLLTWSCPSGGYESFEVKVGRKWRSENGSLCGKGVTVSDLEPAQSYTATVTTVFKDLKAQSLSTTCHTESAAIIAGAIVGILLLFILVGLLIVFLKRRRKKRQPKEVPKDLVCSCPGDILAKDFADHVRENEKDSNCGFAEEYQQLALEGQGQSQITASALENRSKNRYRNVLPYDWSRVPLQPLQEEPGSDYINASFMPGLWSPKEFIATQGPLPNTVGDFWRMVWEQQSHTLVMLTNCMESGRVKCEHYWPLDAQPCIHGQLQVMLISEEASENWTVRHLQLFHMKEQQTLSLRQFHYLAWPDHGVPYSPDPLLAFRKMLRQWMDQTTDGGPPIVHCSAGVGRTGTLIALDVLLRQLECEGLVGPFSFVKKMRESRPLMVQTEAQYVFLHQCILKSLQKPAPALVPEEAMYENVASLVYENASAIMAHESEFSASGC | 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 membrane protein {ECO:0000305}. Note=Colocalizes with CEACAM20 at the apical brush border of intestinal cells. {ECO:0000269|PubMed:26195794}. | 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: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces migratory activity of Jurkat cells (By similarity). Reduces tyrosine phosphorylation of CEACAM20 and thereby contributes to suppress the intestinal immune response (PubMed:26195794). {ECO:0000250|UniProtKB:Q9HD43, ECO:0000269|PubMed:26195794}. | Mus musculus (Mouse) |
E9Q0S6 | TENS1_MOUSE | MGCTVSLVCCEALEPLPSCGPQPPGTPPGPARPERCEPGGAAPDPRRRLLLQPEDLEAPKTHHFKVKAFKKVKPCGICRQAITREGCVCKVCSFSCHRKCQAKVAAPCVPPSSHELVPITTETVPKNVVDVGEGDCRVGSSPKNLEEGGSMRVSPSIQPQPQSQPTSLSRNTSVSRAMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQASICITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKDDRFPDYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHREDGMEEVVGHTQGPLDGSLYAKVKKKDSLNGSSGPVTTARPALSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVSGATTAPAALSPQEKKELDRLLSGFGVDREKQGAMYRAQQLRSHPGGGPTVPSPGRHIVPAQVHVNGGALASERETDILDDELPIQDGQSGGSMGTLSSLDGVTNTSESGYPETLSPLTNGLDKPYSTEPVLNGGGYPYEAANRVIPVHSSHSAPIRPSYSAQEGLAGYQREGPHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSSREAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLGSSRQSHPLTQSRSGYIPSGHSLGTPELVSSGRPYSPYDYQLHPAGSNQSFHPKSPASSTFLPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPLNLEGLVAHRVAGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSALGLKPHNPADILLHPTGVARRLIQPEEDEGEEVTKPPEEPRSYVESVARTAVAGPRAQDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPILSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSGSLGQPSPAALSYQSSSPVPVGGSSYNSPDYSLQPFSSSPESQGQPQYSAASVHMVPGSPQARHRTVGTNTPPSPGFGRRAVNPTMAAPGSPSLSHRQVMGPSGPGFHGNVVSGHPASAATTPGSPSLGRHPVGSHQVPGLHSSVVTTPGSPSLGRHPGAHQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDRHAAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSSPVANGMASGSSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRDPTDESKDSSGPANSTTDLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLSAGQKR | 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 proline residue. Also phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q9HBL0}.; PTM: Rapidly cleaved by calpain II. {ECO:0000250|UniProtKB:Q9HBL0}. | 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 rather than to focal adhesions. Translocates from the cell edge to the cell center in an ITGB1BP1-dependent manner. {ECO:0000250|UniProtKB:Q9HBL0}. | 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 (PubMed:26427649). Plays a role in cell polarization and migration (By similarity). May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity). {ECO:0000250|UniProtKB:Q9HBL0, ECO:0000269|PubMed:26427649}. | Mus musculus (Mouse) |
E9Q236 | MRP4_MOUSE | MLPVHTEVKPNPLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKKDSRKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRIKNFLLLDELPQRKAHVPSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSTAPGTPTLRKRTFSEASIWSQQSSRPSLKDGAPEGQDAENTQAVQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECKKRPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQQLGKGEAAALTETAKQVYFRRNYPDITFTSPAVMNTSNGQPSALTIFETAL | 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 cell proliferation [GO:0048661]; prostaglandin secretion [GO:0032310]; prostaglandin transport [GO:0015732]; transmembrane transport [GO:0055085]; urate transport [GO:0015747]; xenobiotic transmembrane transport [GO:0006855] | 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 transmembrane transporter activity [GO:0042626]; efflux transmembrane transporter activity [GO:0015562]; glutathione transmembrane transporter activity [GO:0034634]; guanine nucleotide transmembrane transporter activity [GO:0001409]; prostaglandin transmembrane transporter activity [GO:0015132]; urate transmembrane transporter activity [GO:0015143]; xenobiotic transmembrane transporter activity [GO:0042910] | 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-dependent. {ECO:0000269|PubMed:15314169}. | 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=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene B4(in) = ADP + H(+) + leukotriene B4(out) + phosphate; Xref=Rhea:RHEA:66424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57461, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out); Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57746, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58165, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + prostaglandin E2(in) = ADP + H(+) + phosphate + prostaglandin E2(out); Xref=Rhea:RHEA:66388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66389; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + prostaglandin E1(in) = ADP + H(+) + phosphate + prostaglandin E1(out); Xref=Rhea:RHEA:66392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57397, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66393; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycodeoxycholate(in) + H2O = ADP + glutathione(out) + glycodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:82982, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66381; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + glutathione(in) + H2O = ADP + cholate(out) + glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:66396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66397; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycocholate(in) + H2O = ADP + glutathione(out) + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66401; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + taurocholate(in) = ADP + glutathione(out) + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:66404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66405; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycochenodeoxycholate(in) + H2O = ADP + glutathione(out) + glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66409; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + taurochenodeoxycholate(in) = ADP + glutathione(out) + H(+) + phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:66412, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66413; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + glycoursodeoxycholate(in) + H2O = ADP + glutathione(out) + glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66417; Evidence={ECO:0000250|UniProtKB:O15439}; CATALYTIC ACTIVITY: Reaction=ATP + glutathione(in) + H2O + tauroursodeoxycholate(in) = ADP + glutathione(out) + H(+) + phosphate + tauroursodeoxycholate(out); Xref=Rhea:RHEA:66420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66421; Evidence={ECO:0000250|UniProtKB:O15439}; | 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 cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (Probable). Confers resistance to anticancer agents (Probable). {ECO:0000305|PubMed:15314169, ECO:0000305|PubMed:17210706}. | Mus musculus (Mouse) |
E9Q2M9 | WDFY4_MOUSE | MEAEDLSKTEDRPEDPGFQNEGQSPAVKPSFSLEGQSPGPSVLWDMLEQKFLDYQQLMPRNPEERRKNLLSLLPLFLKAWEHSVGIICFRSLQRLAEDVSDQLAQEIQQALAGKPAEQARAAAGQLLQWKSDADQDGNLLLKSVYVLTGTDSETLGRVVDSGLPALLLQCLYLFFAFPVEKDDLLESDVQGQRMFVQMLLNICSESQGLEGLLSGSELQSLLIATTCLREHSCLFWKQPTFCVLRAISKAQSPSVIQYLRTADCVRLSVQNLSKLADTLPAPEVSEAVSLILNFVRDSYPISSALLLEFENGEGYPLLLKVLLRYNGLTQGVVEPHLEELIELVMWLTTCGRSELKVFDSVTYPQLEGFKFHQEASGVTVKNLQAFQVLQNLFHRASDSVLCIQVLLAIKTMWAWNPRNFFLLEWTLQPISQFAEIIPLKPTPVQEHFFQLLETLVFKLLYVPHEVLAKVQRLIKESSELSCTLVALRSILRITASDRLFTDIFRDSGLLGLLLAQLRKQAKIMRKSGNKECSPDVQDPERELTYVMLSTVVTLLQGSVRNAVVLKDHGMVPFIKIFLDDECYRGPSLSILEQLSVINAEEYMSIIVGALCSSTQGELQLKLDLLKSLLRILETPKGHAAFRVSSGFNGLLSLLSDLEGSLQVPEVTTCGAVSPSQTLELVLHTLCVVSAALHLDPVNEHFFRSNGLFEKLAEDLCLLGCFGTPEEERTRWDSSSDMKARPFMDLLSCAFSSSCQFPPRLQSCLQILSFLESMASGTLHLRGDLMEPARAGQEPSVDAQKAEAGGRQGKFKQWPDMEDRMDEGDVMIMHPGIICIMVRLLPRLYLEDHPQLSEEIQCSVARHLLSLVKSEKNRQVMCEAGMLRTLMTFCPRTLSTGGSDLHSILIRIFEKLGSQAIEPDVLRQFLGLGIRPPRSAAVKSLHLPPGHEDNPGCSGSCAATAEKPTDSSPRPGGSQALRPSWASQYSATALQTTLSLISMTSPRNLQPQRAALTPSFVEFDMSSEGYGCLFTPTLSTVMGTSTEHSISGGTGSGAPRPFPPPGGLTFSCWFLISRQANVMEGHPLRFLTLVRHLARTEQPFVCFSISLCMDDLSLVVSTEEKEFQPLDAMEPEDEAEPSAGRQLQVRCSQLLTCGQWYHLAVVVSKEMKRNCSVTTYLDGQAIGSAKMLYIQALPGSFFSMDPSSFVDVYGYIGTPRVWKQKSSLTWRLGPAYLFEEDISADTLALIIKLGPRYCGNFQAVHLQGEDPDGEATPLIAEERVSFGLYVPSSSITSIMNIRNTYNEVDSRLIAKEMNISSRDNATPVFLLRNCAGHLSGPLRTLGAVAVGQLGVRVFHSSPAASSLDYIGGPAILLGLISLATDDHTMYAAMKVLHSVLTSNAMCDYLMQHICGYQILAFLLRKKTSFLNHRIFQLILSVAGTAELGFRPSAVTNMCIFQHVLCNFELWTNTADNLELTLFSHLLEILQSPREGPRNAEVAHQAQLLPKLLFLFNEPSLALSKVSTIIAILGCQLKGHFNIQDLLRVGLFVIYTLKPSSVNERQICLDGAQDPSRPAGSQTSGKAIWLRNQLLEMLFGVISSSQLHLTSELKEQVFLSLGPDWFLLLLQGHLHPSTTTLALKLLLYFLSSPPLRGRFRDGLSAGCWVENCMDGVDIVMDNLKSRPAVPDQSPCLLPGFRVLNDFLAYHVLIPEVYLIVSSFFLQTPLTELTNGPRENLDLMLQWLLQKHHQQEVLQAGLCIEGALLLLGMLKAIMNQPPAGSGDGAWEQTLPSSVLQFLRLVHRSYPQDSAWRTPDFLQTVAIITFPLETQKETTSESSRNTSSPGASAEASHAAEGFQASFQPHPALRQLREFMQVLLRELLLGGSNPKQWLPLEVILEASPDGATSQQKRDFQTEVLLSTMDIFQVPSGDGMPTLRGSKEPLPNAEAGAVPSLASVSYFTQKLVEKIYSGVFSADPRHILLFITEHIIAVIENPSSQKDTVMSALYSSLNKVILHCLSKPQQSLSECLGLLTILDFLQEHWDIIFATYNSNVSFLLCLMHCLLLLNARSYPEGFGLEPKPRITPYHQVFLSPNEEVKDKKEEGLPSLGDVQHSIQKSVRALWQQLVAQRRQTLEDAFKIDLSVKAGEIEVKIEEITPLWEETMLRAWQHYLASEKKSLASRSSVMHHSKVTSWSGSLSSAMRLMPGRQAKDPECRAEDFVSCIENYRRKGQELYASIYKDYVQRRKSGSIKAATAWARMREQLFGELGLWGQMTESTRCSRWELDGREGPARMRKRIRHLLAWEPLNLGYKESQEGKGDVSQTNTGNQVFMTADELTTEEAESRPDEVGVDCTQLTFFPALHESLHSEDFLELCRERQVILQELLDGEKVSQKVPMVIVQGHLVSEGILLFGQHHFYICENFTLSPTGDVYCTHHCLSNISDPFIFNMCSKDRSSDHYSCQRHAYSDLRELRQARFLLQDIALEIFFQNGYSKLLVFYNSDRSKALKSFSTFQPSLKGKGTTEDPFNLRKHPGFDRTMLQRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVEKIEGDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASKENMSDVRELTPEFFYLPEFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPYFYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSRNTTGKNPGPGKDASTPVGLPGHSQSFLHSLPALRPSQVTVKDMYLFSLGSESPKGAIGHIVPTEKSILAVEKNKLLMPPLWNRTFSWGFDDFSCCLGSYGSDKILMTFENLAAWGPCLCAVCPSPTMIVTSGASAVVCIWELSLVKGRPRGLKLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGAHLSLWNVNGQPLASITTAWGPEGTITCCCIVEGPAWDASHVIITGSKDGMVRIWKTEDVKMPVPRQAVMEEPSTEPLSPRGHKWAKNLALSRELDVSVALSGKPSKASPAVTALAITRNQSKLLVGDEKGRIFCWSADG | 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 a role in B-cell survival through regulation of autophagy (PubMed:30257884). {ECO:0000269|PubMed:30257884, ECO:0000269|PubMed:30409884}. | Mus musculus (Mouse) |
E9Q2Z1 | CECR2_MOUSE | MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRWELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQLYKLLSEDFLPEICNMIAQKGKRPQRTKPELQHRFMSDHLSIKSIKLEETPMLTKIEKQKRREEEEERQLLLAVQKKEQEQMLKEERKREMEEKVKAVEDRAKRRKLREERAWLLAQGKELPPELSHLDLNSPMREGKKTKDLFELDDDFTAMYKVLDVVKAHKDSWPFLEPVDESYAPNYYQIIKIPMDISSMEKKLNGGLYCNKEEFVNDMKTMFRNCRKYNGDSSEYTKMSDNLERCFHRAMTKHFPGEDGDTDEEFWIKEDEKREKRRSRSGRSSGSHVWTRSRDTEGSSRKQPPVENGGKSLPPARRAASSGDDQSRSSIQLPPEVGTSHGQGFSRPLHCGRVPSHAPPLNQMRPAAPGTFGSLQGSDPTNLHGSSRIPEAPPGEPLQHPPFAIQAPVGISNHRGSLLSAPDLSNMGSHVPSLQLGQMNCPSQDGNMYPPAPFQAGFIPSRHGGTPARPPDFPESSEIPPGHIYHSYKYLNRAHPAVWNGNHGTTNPGRLGPDEKPHLGPGPSHHPHTLGHMMDGRVMRQPIPPNQWTKQSSFLPHGVPSSGYMQPPCKSAGHRLQPPPTPAPSPRFRGPSQALRGAQGGESMMDSPEMIAMQQLSSRVCPPGVPYHPRQPTPPQLPGPFPQVAHSASVCVSAPKPALDNPGSTQEMTETHEPEEDPAEPLPGHEEKAASICSSEGVYLKQLPHPAPPLQASCTRQSSPQERETEDSQLKSDASDSADTYKTSKNKNTWPLDNSYSSPAVQGCLRDLSIVAETGNLPENGVVGEASPCRSEGKGLDGSGSEKPLCPRGKTLQEAVPCTGPNATTPPCTDPSLMAATVNQFSPLYMPGIEYSNSATQYPMSPSLQGLASMMGGKSSGSQPQSFPPRGFQANGPHPGLFPRYRPQQGMRYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSPSGPPGSHPPRSLFSEKNVLSSLQGCETLNTALTSPTQMDVVTAKVVPPDGHNSGPEEEKMDESVERPESPKEFLDLDNHNAATKRQNSLSTSDYLYGTPPPSLSSGMTFGSSAFPPHSVMLQTGSPYTPQRSASHFQPRAYPSPVPAHPPPHPVATQPNGLSPEDSLYCCQEEGLGHFQASMMEQTGTGSGLRGSFQEVHRPPGLQMHPVQSQSLFPKTPAPAASPEQLPPHKTPTLPLDQS | 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 to slide mononucleosomes to the center of a DNA template (By similarity). The CERF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the CERF-5 ISWI chromatin remodeling complex (By similarity). Plays a role in various processes during development: required during embryogenesis for neural tube closure and inner ear development (PubMed:15640247, PubMed:20589882, PubMed:21246654). In adults, required for spermatogenesis, via the formation of ISWI-type chromatin complexes (PubMed:22154806). In histone-modifying complexes, CECR2 recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (By similarity). May also be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9BXF3, ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:20589882, ECO:0000269|PubMed:21246654, ECO:0000269|PubMed:22154806}. | Mus musculus (Mouse) |
E9Q394 | AKP13_MOUSE | MKLSPQQAPLYGDCVVTVLLAEEDKVEDDAIFYLIFSGSTLYHCTSTRKVSSDTLETIAPGHDCCETVKVLLCASREGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLDRSGPPSRDVNSLDEKVALAFRHLKLPAEWNVLGTDHTLHDGGPRETLMHFAVRLGLLRLTWFLLQKPGGRGALSIHNKEGATPVSLALERGYHELHQLLTEENAGEPDSWSSLSYEIPYGDCSVRHHRELDIYTLTSESESHREPHGDSCTGHISKLMNIQQQLMKTNLKQMDNLMPLMVTAQDSSCVPSVPETDGLFLPCVPEPSDHQHPPFEETKSTLCCQRSPGRMAESSCDLSSMVEEENVICSHKKNKDVGRKGEEAEPASAMDSGSASHQDSCLQSVPDCGVKGREGLPSCGNRNEVTGTNYSGVATCQQPLSSRSSVLQDAMVTEPDACQHSSGRELPDSSSTDVGAPEKAGELEHSLLTPDATTQNNKPQVGEGTKERLENSDSSTTETTAVQVLSEPMEKADITNHVFATSAVGVNTPAEASPALSSEEIPTEKPGMETQERGCEGGTTSDQSSPVLPAAAIENKVLGGQEPDTSIAGFCKTASPLDLTMPGPSSDGMPEQNSESHARPAQSLSGQALLCSTAEAGTPSAEATHQPSTVTSSGRLEECGSGKASLPESTMVQPSTQELCTTLCPEDPQADTVTSDTVKNTQKSVGVCHLCVSDAKNQGNGLKQDTPLTNVLEDVPRLPSVVSQTEKELAPDQVSPPASSFSLASSPESESVTKDDALSLVPSQKEKGTATPQLHRTTACRDGPDGRDLSDTDKVGDGATDPPPSSAVELRTSMGNTSPVGIGGEQEGSSPTATLEVLSDSLLHNVDKAALVSDFTLPEEGVSVVVPESSTALGQDGKDRAMSCSSVKEDVHSSEMSREDQRTPPSGQEIPGLCEKPMSALCAEEKAQQHTPSACLKTETKDIKEVAPQVSLLTEGGAAKSLVPPRTSLSADSKQKASSTEQSGSSLLPSGLPGASEALHCNQPSALDVVVENTQFQGETNACEVSRSAMEDVTVADASPATAEPRKKDASHCIKDIPISELLNQEKQMTPSLPEAFLDKGVTDLQEVITPEIEPLDCKRETLEGTDLNCATSNSKETPIEKPMQPLARDLPTETGLSVINNNVPQADMKQVAQASIPAEESNATTVSTQAADVPTRADSIEETATRIVEAVIRQVRASNALMAKVETQNPSLSSPETKQLENAYTESACAFLPGETPQIEKTHEDTTGQCGAETEEPEKIILPESAPGKQGKMPDTRTGDEVDLLSRISAASEEEAVGNGAATPKMKQGPGTQAINRESWCAIEPCPEAASLLASKQSSECRSFIDVGLGTECASKEGMLQRVSGSESDLFHSPSDEMDSIIFPKPEEEQLLCDTTGSSSSTDDTASLDRHSSHGSDVSLPQTSKLNRSRNHQSANGFFSPGVEAPESRESESEPAGSGEMEEEEMDSITEVPANCSFLRSSMRSLSPFRRHSWGPGKNAASDAEMNQRSSMRALGHVVRRPPIHRRSFSLEGLTGGGVGNKPSSSLEMSSANSSELRNPFGGEEQRNSLMSLSEEHLEPDQRQHHRMFDQQTCYRSKQQGFNYCTSAISSPLTKSISLMTISHPGLDSSRPFHSTSANLTESITEENCNFLPPSPSKKNFEEKSGTKVSRTFSYIRNKMSSSKKSKEKEKEKDKIKEKEKDSKEKEKDKKTLNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMKQPKGSLQAHDTSSLPTVIMRNKSSQPKERPRSAVLLADEATAAPMFTNRRSQQSVSLSKSVSIQNITGVGNDENMSNTWKFLSHSTDSLNKICKVNESTESLTDEGVGTDMNEGQLMGDFESDSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVSQFSGESAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYEKKVRLGEIYTKTDSKSIMRMKSGQMFAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSLNRDEDEGIPSENEEEKKLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLPEDCSPTHSPRVLFRSNTEEALKGGPLMKSAINEVEILQSLVSGSLGGTLGQSISSPVEQEVMAAPISLPRRAETFGGFDCHQMNASKGGEKEEGDDGQDLRRTESDSGLKKGGNGNLVFMLKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQNLCQVSNKHGRLMRIPSFLPNSDEFSSPSAPSVTKSGSLDSELSVSPKRNSISRTQKDKGPFHILGSASQTKVPEGQSQAPSSTSTSTRLFGLSKPKEKKEKKKKSKGSRTQPGDGPASEVPAEGEEIFC | 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-coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; nuclear export [GO:0051168]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of glucocorticoid mediated signaling pathway [GO:1900169]; regulation of Rho protein signal transduction [GO:0035023]; regulation of sarcomere organization [GO:0060297] | 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 membrane protein {ECO:0000250|UniProtKB:Q12802}. Note=Colocalizes with actin and myosin filaments in developing cardiomyocytes (PubMed:20139090). Colocalizes with the actin cytoskeleton at the cell cortex (By similarity). {ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:20139090}. | 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 members (PubMed:23658642). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14. Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity. Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (By similarity). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2. Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (PubMed:24161911). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (By similarity). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (PubMed:20139090). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:23658642, PubMed:24161911). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:17537920, PubMed:24161911). Plays a role in osteogenesis (PubMed:25892096). {ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:23658642, ECO:0000269|PubMed:24161911, ECO:0000269|PubMed:25892096}. | Mus musculus (Mouse) |
E9Q3E1 | AL3B2_MOUSE | MSAAETGSEPSQGAGPSEATLHSLREAFNAGRTRPTEFRTAQLRSLGRFLQENKELLQDALAKDVGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSSAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETRQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQERLVPALQNSITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFINRREKPLALYAFSNNNQVVNQMLERTSSGGFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNDLRYPPYGPWNQQLISWAIGSRSCTLL | 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(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+); Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108}; | 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 | MAAAGARGGGGGGGGGGGGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEAILQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVSPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGIPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSISPLFNGITYKEFCIPLEMLRELLNLVKKIVEEPVLKSLDAIVAGVMEANPSADLYYTTFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNMSQGELQKILHDADRIHSEMSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGSDIKISVTNEHSESTLNVLPGKKNQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQEEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMAEKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLTERPACVKKDYSNFMASLNLRNRYAGEVHGMIRFSGATGQMSDLNKMMVQDLITALDHSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKNGVEVPFMREMAGAWHMTVEQKFGLFSVETKEADPLAASEASQPRPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGARGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLQCRSDAEDECFSQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQNCFLSNRSRTYDMIQYYQNDIPY | 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 regulated by TMEM150A. {ECO:0000250|UniProtKB:P42356}. | 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|UniProtKB:P42356}; | 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 | MKVDEEKAGVKKLDPTSYKRRQPEQDFPSIHIGFPVPSYSQRKSDSKGHLSGLQKVQWSLKPGKPQQELAGPGIRASSQGGAVDFTKRTRSPAAEQLQDILGEEDEAPNPTLFTEMDTLQHDGDQMEWKESARWIKFEEKVEEGGERWSKPHVSTLSLHSLFELRTCLQTGTVLLDLDSCSLPQIIDDVIEKQIEDGLLRPELRERVSYVLLRKHRHQTKKPIHRSLADIGKSVSTTNRSSARSSSAGPTLHRSTEDLRIRQSTSYGHLCHAQSRSMNDISHTPNTDQRKNKFMKKIPKDSEASNVLVGEVDFLDQPFIAFVRLVQSAMLGGVTEVPVPTRFLFILLGPSGRAKSYNEIGRAIATLMVDDLFSDVAYKARNREDLIAGIDEFLDEVIVLPPGEWDPNIRIEPPKKVPSADKRKSVFSLAEPGQMNGSVGGGGASAGGGGSGGGAGGSGAGGVGSGDEAEMPAMHEIGEELIWTGRFFGGLCLDVKRKLPWFPSDFYDGFHLQSISAVLFIYLGCITNAITFGGLLGDATDNYQGVMESFLGTAMAGSLFCLFSGQPLIILSSTGPILIFEKLLFDFSKANGLDYMEFRLWIGLHSAIQCLILVATDASFIIKYITRFTEEGFSTLISFIFIYDAIKKMIGAFKYYPINTDFKPDFITTYKCECVAPDTVNTTTVNASAPLAPNTNTSLYTPLNLTALDWSLLSKKECLSYGGRLLGSSCQFVPDLALMSFILFFGTYSMTLTLKKFKFSRYFPTKVRTLVADFSIVFSILLFCGIDACFGLQTPKLHVPSVIKPTRPDRGWFVAPFGKNPWWVYPASILPALLVTILIFMDQQITAVIVNRKENKLRKAAGYHLDLFWVGILMALCSFTGLPWYVAATVISIAHIDSLKMETETSAPGEQPQFLGVREQRVTGVMVFILTGISVFLAPILKYIPMPVLYGVFLYMGVASLNGIQFWERCKLFLMPAKHQPDHAFLRHVPLRRIHLFTLVQILCLALLWILKSTMAAIIFPVMILGLIIVRRLLDLIFSQHDLAWIDNILPEKDKKETDKKKKRRKEVHETAEKEVAMPQFLPPSVVKIPMEGIPSDPQNGIHCVARKRSSSWSYSL | 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 arterial blood pressure [GO:0003073]; renal system process [GO:0003014]; retina development in camera-type eye [GO:0060041]; transmembrane transport [GO:0055085] | 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|UniProtKB:Q6RI88}. | 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=Rhea:RHEA:72219, ChEBI:CHEBI:17544, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:18588858}; | 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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