OGR1_BOVIN
ID OGR1_BOVIN Reviewed; 361 AA.
AC O46685;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ovarian cancer G-protein coupled receptor 1;
DE AltName: Full=G protein-coupled receptor RGR1;
DE Short=bRGR1;
DE AltName: Full=G-protein coupled receptor 68;
GN Name=GPR68;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9299461; DOI=10.1006/bbrc.1997.7185;
RA Ferrer-Martinez A., Felipe A., Mata J.F., Casado F.J., Pastor-Anglada M.;
RT "Molecular cloning of a bovine renal G-protein coupled receptor gene
RT (bRGR): regulation of bRGR mRNA levels by amino acid availability.";
RL Biochem. Biophys. Res. Commun. 238:107-112(1997).
CC -!- FUNCTION: Proton-sensing receptor involved in pH homeostasis. May
CC represents an osteoblastic pH sensor regulating cell-mediated responses
CC to acidosis in bone. Mediates its action by association with G proteins
CC that stimulates inositol phosphate (IP) production or Ca(2+)
CC mobilization. The receptor is almost silent at pH 7.8 but fully
CC activated at pH 6.8 (By similarity). Also functions as a metastasis
CC suppressor gene in prostate cancer (By similarity). {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; U88366; AAC05611.1; -; mRNA.
DR EMBL; U88367; AAC05612.1; -; mRNA.
DR PIR; JC5653; JC5653.
DR RefSeq; NP_776754.1; NM_174329.2.
DR AlphaFoldDB; O46685; -.
DR SMR; O46685; -.
DR STRING; 9913.ENSBTAP00000008858; -.
DR PaxDb; O46685; -.
DR Ensembl; ENSBTAT00000008858; ENSBTAP00000008858; ENSBTAG00000006738.
DR GeneID; 281799; -.
DR KEGG; bta:281799; -.
DR CTD; 8111; -.
DR VEuPathDB; HostDB:ENSBTAG00000006738; -.
DR VGNC; VGNC:29597; GPR68.
DR eggNOG; ENOG502QQJA; Eukaryota.
DR GeneTree; ENSGT00950000183136; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; O46685; -.
DR OMA; FLTCART; -.
DR OrthoDB; 716326at2759; -.
DR TreeFam; TF331803; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000006738; Expressed in mammary gland and 86 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005389; OGR1_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01564; OGR1RECEPTOR.
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; Tumor suppressor.
FT CHAIN 1..361
FT /note="Ovarian cancer G-protein coupled receptor 1"
FT /id="PRO_0000383597"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 340..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 361 AA; 40906 MW; 4802E77C9A45DEE1 CRC64;
MGNITADNTS MNCDIDHTIH QTLAPVVYVM VLVVGFPANC LSLYYGYLQI KARNELGVYL
CNLTVADLFY ICSLPFWLQY VLQHDHWSHD DLSCQVCGIL LYENIYISVG FLCCISIDRY
LAVAHPFRFH QFRTLKAAMG VSALIWVKEL LTSIYFLMHE EVVEDADRHR VCFEHYPLEP
RQRGINYYRF LVGFLFPICL LLASYRGILR AVRRSHGTQK SRKDQIQRLV LSTVVIFLAC
FLPYHVLLLV RSLWESSCDF AKGIFNAYHF SLLLTSFNCV ADPVLYCFVS ETTHRDLARL
RGACLAFLTC ARTGRAREAY PLGAPEASGK SEDPEVLTRL HPAFQTPHPP GMGGSPAGGL
S
