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UR2R_MOUSE
ID   UR2R_MOUSE              Reviewed;         385 AA.
AC   Q8VIH9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Urotensin-2 receptor;
DE            Short=UR-2-R;
DE   AltName: Full=G-protein coupled receptor 14;
DE   AltName: Full=Urotensin II receptor;
DE            Short=UR-II-R;
GN   Name=Uts2r; Synonyms=Gpr14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Qi J.-S., Santulli R., de Garavilla L., D'Andrea M., Smith C.,
RA   Andrade-Gordon P.;
RT   "Mouse urotensin II receptor GPR14.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11976263; DOI=10.1038/sj.bjp.0704671;
RA   Elshourbagy N.A., Douglas S.A., Shabon U., Harrison S., Duddy G.,
RA   Sechler J.L., Ao Z., Maleeff B.E., Naselsky D., Disa J., Aiyar N.V.;
RT   "Molecular and pharmacological characterization of genes encoding
RT   urotensin-II peptides and their cognate G-protein-coupled receptors from
RT   the mouse and monkey.";
RL   Br. J. Pharmacol. 136:9-22(2002).
CC   -!- FUNCTION: High affinity receptor for urotensin-2 and urotensin-2B. The
CC       activity of this receptor is mediated by a G-protein that activate a
CC       phosphatidylinositol-calcium second messenger system (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF441863; AAL34551.1; -; mRNA.
DR   EMBL; AY065981; AAL55427.1; -; mRNA.
DR   CCDS; CCDS25769.1; -.
DR   RefSeq; NP_663415.1; NM_145440.1.
DR   AlphaFoldDB; Q8VIH9; -.
DR   SMR; Q8VIH9; -.
DR   STRING; 10090.ENSMUSP00000046920; -.
DR   BindingDB; Q8VIH9; -.
DR   ChEMBL; CHEMBL2346494; -.
DR   GuidetoPHARMACOLOGY; 365; -.
DR   GlyGen; Q8VIH9; 2 sites.
DR   iPTMnet; Q8VIH9; -.
DR   PhosphoSitePlus; Q8VIH9; -.
DR   PaxDb; Q8VIH9; -.
DR   PRIDE; Q8VIH9; -.
DR   DNASU; 217369; -.
DR   Ensembl; ENSMUST00000039044; ENSMUSP00000046920; ENSMUSG00000039321.
DR   GeneID; 217369; -.
DR   KEGG; mmu:217369; -.
DR   UCSC; uc007mvj.1; mouse.
DR   CTD; 2837; -.
DR   MGI; MGI:2183450; Uts2r.
DR   VEuPathDB; HostDB:ENSMUSG00000039321; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000156819; -.
DR   HOGENOM; CLU_009579_1_0_1; -.
DR   InParanoid; Q8VIH9; -.
DR   OMA; WGPRAHR; -.
DR   OrthoDB; 1076228at2759; -.
DR   PhylomeDB; Q8VIH9; -.
DR   TreeFam; TF334200; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 217369; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q8VIH9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8VIH9; protein.
DR   Bgee; ENSMUSG00000039321; Expressed in tarsal region and 22 other tissues.
DR   ExpressionAtlas; Q8VIH9; baseline and differential.
DR   Genevisible; Q8VIH9; MM.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0001604; F:urotensin II receptor activity; ISO:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR   GO; GO:0003105; P:negative regulation of glomerular filtration; ISO:MGI.
DR   GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR   GO; GO:0035811; P:negative regulation of urine volume; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0046005; P:positive regulation of circadian sleep/wake cycle, REM sleep; ISO:MGI.
DR   GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; ISO:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000670; Urot_II_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00647; UROTENSIN2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..385
FT                   /note="Urotensin-2 receptor"
FT                   /id="PRO_0000070195"
FT   TOPO_DOM        1..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..76
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..145
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..185
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..283
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        122..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   385 AA;  42523 MW;  64F853C07014B5F7 CRC64;
     MALSLESTSF PMLAVSRSTA SELPGGFNVS HNSSWTGPTD PSSLQDLVAT GVIGAVLSTM
     GVVGVVGNVY TLVVMCRFLR ASASMYVYVV NLALADLLYL LSIPFIVATY VTKDWHFGDV
     GCRVLFSLDF LTMHASIFTL TIMSSERYAA VLRPLDTVQR SKGYRKLLAL GTWLLALLLT
     LPMMLAIRLV RRGSKSLCLP AWGPRAHRTY LTLLFGTSIV GPGLVIGLLY IRLARAYWLS
     QQASFKQTRR LPNPRVLYLI LGIVLLFWAC FLPFWLWQLL AQYHQAMPLT PETARIINYL
     TACLTYGNSC INPFLYTLLT KNYREYLRGR QRSLGSSCRG PGSAGSFLSS RVHLQQDSGR
     SLSSNSQQAT ETLVLSPVPP NGAFV
 
 
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