UR2R_HUMAN
ID UR2R_HUMAN Reviewed; 389 AA.
AC Q9UKP6; B2RMV8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10499587; DOI=10.1038/45809;
RA Ames R.S., Sarau H.M., Chambers J.K., Willette R.N., Aiyar N.V.,
RA Romanic A.M., Louden C.S., Foley J.J., Sauermelch C.F., Coatney R.W.,
RA Ao Z., Disa J., Holmes S.D., Stadel J.M., Martin J.D., Liu W.-S.,
RA Glover G.I., Wilson S., McNulty D.E., Ellis C.E., Elshourbagy N.A.,
RA Shabon U., Trill J.J., Hay D.W.P., Ohlstein E.H., Bergsma D.J.,
RA Douglas S.A.;
RT "Human urotensin-II is a potent vasoconstrictor and agonist for the orphan
RT receptor GPR14.";
RL Nature 401:282-286(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION AS A UROTENSIN-2B RECEPTOR.
RX PubMed=14550283; DOI=10.1016/j.bbrc.2003.09.102;
RA Sugo T., Murakami Y., Shimomura Y., Harada M., Abe M., Ishibashi Y.,
RA Kitada C., Miyajima N., Suzuki N., Mori M., Fujino M.;
RT "Identification of urotensin II-related peptide as the urotensin II-
RT immunoreactive molecule in the rat brain.";
RL Biochem. Biophys. Res. Commun. 310:860-868(2003).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-146.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
CC {ECO:0000269|PubMed:14550283}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundant expression in the heart and pancreas.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF140631; AAD55578.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89768.1; -; Genomic_DNA.
DR EMBL; BC136490; AAI36491.1; -; mRNA.
DR CCDS; CCDS11810.1; -.
DR RefSeq; NP_061822.1; NM_018949.2.
DR PDB; 6HVK; NMR; -; A=153-166.
DR PDBsum; 6HVK; -.
DR AlphaFoldDB; Q9UKP6; -.
DR SMR; Q9UKP6; -.
DR BioGRID; 109097; 1.
DR STRING; 9606.ENSP00000323516; -.
DR BindingDB; Q9UKP6; -.
DR ChEMBL; CHEMBL3764; -.
DR GuidetoPHARMACOLOGY; 365; -.
DR GlyGen; Q9UKP6; 2 sites.
DR PhosphoSitePlus; Q9UKP6; -.
DR BioMuta; UTS2R; -.
DR DMDM; 8928474; -.
DR MassIVE; Q9UKP6; -.
DR PaxDb; Q9UKP6; -.
DR PeptideAtlas; Q9UKP6; -.
DR PRIDE; Q9UKP6; -.
DR Antibodypedia; 19903; 241 antibodies from 32 providers.
DR DNASU; 2837; -.
DR Ensembl; ENST00000313135.5; ENSP00000323516.2; ENSG00000181408.5.
DR GeneID; 2837; -.
DR KEGG; hsa:2837; -.
DR MANE-Select; ENST00000313135.5; ENSP00000323516.2; NM_018949.3; NP_061822.1.
DR UCSC; uc010wvl.3; human.
DR CTD; 2837; -.
DR DisGeNET; 2837; -.
DR GeneCards; UTS2R; -.
DR HGNC; HGNC:4468; UTS2R.
DR HPA; ENSG00000181408; Tissue enhanced (brain, testis, thyroid gland).
DR MIM; 600896; gene.
DR neXtProt; NX_Q9UKP6; -.
DR OpenTargets; ENSG00000181408; -.
DR PharmGKB; PA28857; -.
DR VEuPathDB; HostDB:ENSG00000181408; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157017; -.
DR HOGENOM; CLU_009579_1_0_1; -.
DR InParanoid; Q9UKP6; -.
DR OMA; WGPRAHR; -.
DR OrthoDB; 1076228at2759; -.
DR PhylomeDB; Q9UKP6; -.
DR TreeFam; TF334200; -.
DR PathwayCommons; Q9UKP6; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; Q9UKP6; -.
DR SIGNOR; Q9UKP6; -.
DR BioGRID-ORCS; 2837; 10 hits in 1065 CRISPR screens.
DR GeneWiki; Urotensin-II_receptor; -.
DR GenomeRNAi; 2837; -.
DR Pharos; Q9UKP6; Tchem.
DR PRO; PR:Q9UKP6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UKP6; protein.
DR Bgee; ENSG00000181408; Expressed in right testis and 49 other tissues.
DR Genevisible; Q9UKP6; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0001604; F:urotensin II receptor activity; IBA:GO_Central.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="Urotensin-2 receptor"
FT /id="PRO_0000070193"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 70
FT /note="A -> P (in dbSNP:rs34442190)"
FT /id="VAR_049451"
FT VARIANT 146
FT /note="S -> R (in a breast cancer sample; somatic mutation;
FT dbSNP:rs770047242)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035768"
FT TURN 155..159
FT /evidence="ECO:0007829|PDB:6HVK"
SQ SEQUENCE 389 AA; 42130 MW; 6D6A88DBF78400CE CRC64;
MALTPESPSS FPGLAATGSS VPEPPGGPNA TLNSSWASPT EPSSLEDLVA TGTIGTLLSA
MGVVGVVGNA YTLVVTCRSL RAVASMYVYV VNLALADLLY LLSIPFIVAT YVTKEWHFGD
VGCRVLFGLD FLTMHASIFT LTVMSSERYA AVLRPLDTVQ RPKGYRKLLA LGTWLLALLL
TLPVMLAMRL VRRGPKSLCL PAWGPRAHRA YLTLLFATSI AGPGLLIGLL YARLARAYRR
SQRASFKRAR RPGARALRLV LGIVLLFWAC FLPFWLWQLL AQYHQAPLAP RTARIVNYLT
TCLTYGNSCA NPFLYTLLTR NYRDHLRGRV RGPGSGGGRG PVPSLQPRAR FQRCSGRSLS
SCSPQPTDSL VLAPAAPARP APEGPRAPA
