OGR1_MOUSE
ID OGR1_MOUSE Reviewed; 365 AA.
AC Q8BFQ3; Q148P7; Q3U1L3; Q80T34;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ovarian cancer G-protein coupled receptor 1;
DE AltName: Full=G-protein coupled receptor 68;
DE AltName: Full=Sphingosylphosphorylcholine receptor;
GN Name=Gpr68; Synonyms=Ogr1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-224.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [4]
RP FUNCTION.
RX PubMed=17728215; DOI=10.1093/jnci/djm107;
RA Singh L.S., Berk M., Oates R., Zhao Z., Tan H., Jiang Y., Zhou A.,
RA Kirmani K., Steinmetz R., Lindner D., Xu Y.;
RT "Ovarian cancer G protein-coupled receptor 1, a new metastasis suppressor
RT gene in prostate cancer.";
RL J. Natl. Cancer Inst. 99:1313-1327(2007).
RN [5]
RP FUNCTION.
RX PubMed=18847331; DOI=10.1359/jbmr.081015;
RA Frick K.K., Krieger N.S., Nehrke K., Bushinsky D.A.;
RT "Metabolic acidosis increases intracellular calcium in bone cells through
RT activation of the proton receptor OGR1.";
RL J. Bone Miner. Res. 24:305-313(2009).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19479052; DOI=10.1371/journal.pone.0005705;
RA Li H., Wang D., Singh L.S., Berk M., Tan H., Zhao Z., Steinmetz R.,
RA Kirmani K., Wei G., Xu Y.;
RT "Abnormalities in osteoclastogenesis and decreased tumorigenesis in mice
RT deficient for ovarian cancer G protein-coupled receptor 1.";
RL PLoS ONE 4:E5705-E5705(2009).
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. Also functions as a metastasis suppressor gene in
CC prostate cancer. {ECO:0000269|PubMed:17728215,
CC ECO:0000269|PubMed:18847331}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the lung, testis, heart, brain,
CC spleen, thymus, brown fat, small intestine, colon, peripheral blood
CC leukocytes, macrophages, stomach, ovary and white fat but not in the
CC liver, kidney, and skeletal muscle. Expression in the prostate is weak
CC but detectable. {ECO:0000269|PubMed:19479052}.
CC -!- DISRUPTION PHENOTYPE: Mice have reduced osteoclasts derived from bone
CC marrow cells, a pH-dependent osteoclast survival effect is also
CC detected. However, the overall bone structures of the mice are not
CC affected. In addition melanoma cell tumorigenesis is significantly
CC inhibited. {ECO:0000269|PubMed:19479052}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18035.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI18045.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC29521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE33483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK036659; BAC29521.1; ALT_INIT; mRNA.
DR EMBL; AK087410; BAC39863.1; ALT_INIT; mRNA.
DR EMBL; AK155886; BAE33483.1; ALT_INIT; mRNA.
DR EMBL; BC118034; AAI18035.2; ALT_INIT; mRNA.
DR EMBL; BC118044; AAI18045.2; ALT_INIT; mRNA.
DR EMBL; AY255616; AAO85128.1; -; mRNA.
DR CCDS; CCDS26109.1; -.
DR RefSeq; NP_001171144.1; NM_001177673.1.
DR RefSeq; NP_001171145.1; NM_001177674.1.
DR RefSeq; NP_780702.1; NM_175493.4.
DR AlphaFoldDB; Q8BFQ3; -.
DR SMR; Q8BFQ3; -.
DR STRING; 10090.ENSMUSP00000105693; -.
DR ChEMBL; CHEMBL4523380; -.
DR GlyGen; Q8BFQ3; 2 sites.
DR iPTMnet; Q8BFQ3; -.
DR PhosphoSitePlus; Q8BFQ3; -.
DR EPD; Q8BFQ3; -.
DR PaxDb; Q8BFQ3; -.
DR PRIDE; Q8BFQ3; -.
DR ProteomicsDB; 294273; -.
DR Antibodypedia; 13584; 302 antibodies from 30 providers.
DR DNASU; 238377; -.
DR Ensembl; ENSMUST00000053668; ENSMUSP00000057510; ENSMUSG00000047415.
DR Ensembl; ENSMUST00000110065; ENSMUSP00000105692; ENSMUSG00000047415.
DR Ensembl; ENSMUST00000110066; ENSMUSP00000105693; ENSMUSG00000047415.
DR GeneID; 238377; -.
DR KEGG; mmu:238377; -.
DR UCSC; uc007ota.2; mouse.
DR CTD; 8111; -.
DR MGI; MGI:2441763; Gpr68.
DR VEuPathDB; HostDB:ENSMUSG00000047415; -.
DR eggNOG; ENOG502QQJA; Eukaryota.
DR GeneTree; ENSGT00950000183136; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q8BFQ3; -.
DR OMA; FLTCART; -.
DR OrthoDB; 716326at2759; -.
DR PhylomeDB; Q8BFQ3; -.
DR TreeFam; TF331803; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 238377; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gpr68; mouse.
DR PRO; PR:Q8BFQ3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BFQ3; protein.
DR Bgee; ENSMUSG00000047415; Expressed in animal zygote and 125 other tissues.
DR Genevisible; Q8BFQ3; MM.
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; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IMP:MGI.
DR GO; GO:0036035; P:osteoclast development; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IMP:MGI.
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..365
FT /note="Ovarian cancer G-protein coupled receptor 1"
FT /id="PRO_0000070114"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..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..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 365 AA; 41209 MW; FD36FFB064D9E349 CRC64;
MGNITTENSS LSCPIDHTIH QTLAPVVYVT VLVVGFPANC LSLYFGYLQI KARNELGVYL
CNLTIADLFY ICSLPFWLQY VLQHDDWSHG DLSCQVCGIL LYENIYISVG FLCCISIDRY
LAVAHPFRFH QFRTLKAAVG VSVLIWAKEL LTSIYFLNHK EVIEDEDQHR VCFEHYPIQA
WQRSINYYRF LVGFLFPICL LLASYQGILR AVRRSHGTQK SRKDQIQRLV LSTVVIFLAC
FLPYHVLLLV RSLWERNCEF AKSIFNVYHF SLLLTSFNCV ADPVLYCFVS ETTHRDLARL
RGACLAVLTC SRTSRAREAY PLGAPEASGK SGAQGEEPEL LTKLHSAFQT PSSLGVGGPS
TVGLA
