UR2R_RAT
ID UR2R_RAT Reviewed; 386 AA.
AC P49684; P48041;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Urotensin-2 receptor;
DE Short=UR-2-R;
DE AltName: Full=G-protein coupled receptor 14;
DE AltName: Full=G-protein coupled sensory epithelial neuropeptide-like receptor;
DE Short=SENR;
DE AltName: Full=Urotensin II receptor;
DE Short=UR-II-R;
GN Name=Uts2r; Synonyms=Gpr14, Senr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8666380; DOI=10.1006/geno.1995.9996;
RA Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R.,
RA Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F.,
RA Docherty J.M.;
RT "Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and
RT GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and
RT somatostatin receptors.";
RL Genomics 29:335-344(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Circumvallate papilla;
RX PubMed=7733947; DOI=10.1006/bbrc.1995.1563;
RA Tal M., Ammar D.A., Karpuj M., Krizhanovsky V., Naim M., Thompson D.A.;
RT "A novel putative neuropeptide receptor expressed in neural tissue,
RT including sensory epithelia.";
RL Biochem. Biophys. Res. Commun. 209:752-759(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Urinary bladder;
RA Suga H., Takao K.;
RT "Expression of the rat SENR in the urinary bladder tissues.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheochromocytoma;
RA Liu H., Zou M., Suga H., Takao K.;
RT "The SENR/GPR14 expresses in rat pheochromocytoma PC 12 cells.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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: Preferentially expressed in neural and sensory
CC tissues.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U32673; AAC52593.1; -; Genomic_DNA.
DR EMBL; U23483; AAA80111.1; -; Genomic_DNA.
DR EMBL; AB012210; BAA25251.1; -; mRNA.
DR EMBL; AB029611; BAA82357.1; -; mRNA.
DR PIR; I84612; I84612.
DR RefSeq; NP_065412.1; NM_020537.1.
DR AlphaFoldDB; P49684; -.
DR SMR; P49684; -.
DR BioGRID; 248616; 1.
DR STRING; 10116.ENSRNOP00000051809; -.
DR BindingDB; P49684; -.
DR ChEMBL; CHEMBL4921; -.
DR GuidetoPHARMACOLOGY; 365; -.
DR GlyGen; P49684; 2 sites.
DR PhosphoSitePlus; P49684; -.
DR PaxDb; P49684; -.
DR PRIDE; P49684; -.
DR Ensembl; ENSRNOT00000054926; ENSRNOP00000051809; ENSRNOG00000036669.
DR GeneID; 57305; -.
DR KEGG; rno:57305; -.
DR CTD; 2837; -.
DR RGD; 621884; Uts2r.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244811; -.
DR HOGENOM; CLU_009579_1_0_1; -.
DR InParanoid; P49684; -.
DR OMA; WGPRAHR; -.
DR OrthoDB; 1076228at2759; -.
DR PhylomeDB; P49684; -.
DR TreeFam; TF334200; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P49684; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036669; Expressed in skeletal muscle tissue and 2 other tissues.
DR Genevisible; P49684; RN.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0001604; F:urotensin II receptor activity; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0003105; P:negative regulation of glomerular filtration; IMP:RGD.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0035811; P:negative regulation of urine volume; IMP:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:0046005; P:positive regulation of circadian sleep/wake cycle, REM sleep; IMP:RGD.
DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..386
FT /note="Urotensin-2 receptor"
FT /id="PRO_0000070196"
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..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 CONFLICT 315
FT /note="F -> L (in Ref. 1; AAC52593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 42707 MW; FA4E95CC6A4CA27C CRC64;
MALSLESTTS FHMLTVSGST VTELPGDSNV SLNSSWSGPT DPSSLKDLVA TGVIGAVLSA
MGVVGMVGNV YTLVVMCRFL RASASMYVYV VNLALADLLY LLSIPFIIAT YVTKDWHFGD
VGCRVLFSLD FLTMHASIFT LTIMSSERYA AVLRPLDTVQ RSKGYRKLLV LGTWLLALLL
TLPMMLAIQL VRRGSKSLCL PAWGPRAHRT YLTLLFGTSI VGPGLVIGLL YVRLARAYWL
SQQASFKQTR RLPNPRVLYL ILGIVLLFWA CFLPFWLWQL LAQYHEAMPL TPETARIVNY
LTTCLTYGNS CINPFLYTLL TKNYREYLRG RQRSLGSSCH SPGSPGSFLP SRVHLQQDSG
RSLSSSSQQA TETLMLSPVP RNGALL
