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Ovarian cancer G-protein coupled receptor 1 (OGR-1) (G-protein coupled receptor 68) (GPR12A) (Sphingosylphosphorylcholine receptor)

 OGR1_HUMAN              Reviewed;         365 AA.
Q15743; Q13334; Q4VBB4; Q6IX34;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=Ovarian cancer G-protein coupled receptor 1;
Short=OGR-1;
AltName: Full=G-protein coupled receptor 68;
AltName: Full=GPR12A;
AltName: Full=Sphingosylphosphorylcholine receptor;
Name=GPR68; Synonyms=OGR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7498459; DOI=10.1016/0014-5793(95)01196-L;
An S., Tsai C., Goetzl E.J.;
"Cloning, sequencing and tissue distribution of two related G protein-
coupled receptor candidates expressed prominently in human lung
tissue.";
FEBS Lett. 375:121-124(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Ovarian carcinoma;
PubMed=8661159; DOI=10.1006/geno.1996.0377;
Xu Y., Casey G.;
"Identification of human OGR1, a novel G protein-coupled receptor that
maps to chromosome 14.";
Genomics 35:397-402(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Kaighin V.A., Martin A.L., Aronstam R.S.;
"Isolation of cDNA coding for human orphan G protein receptor 68.";
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
King M.M., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PRELIMINARY FUNCTION.
PubMed=10806476; DOI=10.1038/35010529;
Xu Y., Zhu K., Hong G., Wu W., Baudhuin L.M., Xiao Y.-J., Damron D.S.;
"Sphingosylphosphorylcholine is a ligand for ovarian cancer G-protein-
coupled receptor 1.";
Nat. Cell Biol. 2:261-267(2000).
[9]
ERRATUM, AND RETRACTION.
PubMed=16508674; DOI=10.1038/ncb1377;
Xu Y., Zhu K., Hong G., Wu W., Baudhuin L.M., Xiao Y.-J., Damron D.S.;
Nat. Cell Biol. 8:299-299(2006).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-17; HIS-20;
HIS-84; HIS-89; HIS-159; HIS-175; HIS-245 AND HIS-269.
PubMed=12955148; DOI=10.1038/nature01905;
Ludwig M.-G., Vanek M., Guerini D., Gasser J.A., Jones C.E.,
Junker U., Hofstetter H., Wolf R.M., Seuwen K.;
"Proton-sensing G-protein-coupled receptors.";
Nature 425:93-98(2003).
[11]
INVOLVEMENT IN AI2A6, AND VARIANT AI2A6 PRO-74.
PubMed=27693231; DOI=10.1016/j.ajhg.2016.08.020;
Parry D.A., Smith C.E., El-Sayed W., Poulter J.A., Shore R.C.,
Logan C.V., Mogi C., Sato K., Okajima F., Harada A., Zhang H.,
Koruyucu M., Seymen F., Hu J.C., Simmer J.P., Ahmed M., Jafri H.,
Johnson C.A., Inglehearn C.F., Mighell A.J.;
"Mutations in the pH-sensing G-protein-coupled receptor GPR68 cause
amelogenesis imperfecta.";
Am. J. Hum. Genet. 99:984-990(2016).
[12]
VARIANT SER-39.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Proton-sensing receptor involved in pH homeostasis. May
represents an osteoblastic pH sensor regulating cell-mediated
responses to acidosis in bone. Mediates its action by association
with G proteins that stimulates inositol phosphate (IP) production
or Ca(2+) mobilization. The receptor is almost silent at pH 7.8
but fully activated at pH 6.8. Function also as a metastasis
suppressor gene in prostate cancer (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12955148}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Found at low level in a wide range of tissues,
but significantly expressed in lung, kidney, bone and nervous
system. {ECO:0000269|PubMed:12955148}.
-!- DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A6 (AI2A6)
[MIM:617217]: A defect of enamel formation. The disorder involves
both primary and secondary dentitions. The teeth have a shiny agar
jelly appearance and the enamel is softer than normal. Brown
pigment is present in middle layers of enamel.
{ECO:0000269|PubMed:27693231}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- CAUTION: Was originally (PubMed:10806476) thought to be a receptor
for sphingosylphosphorylcholine (SPC). However, this work has been
retracted (PubMed:16508674). {ECO:0000305|PubMed:10806476,
ECO:0000305|PubMed:16508674}.
-!- SEQUENCE CAUTION:
Sequence=AAH96071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH96072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH96073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH96074.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH98567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAT38917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=ACG60649.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=EAW81447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GPR68ID40745ch14q32.html";
-----------------------------------------------------------------------
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EMBL; U35398; AAA79060.1; -; mRNA.
EMBL; U48405; AAC50596.1; -; Genomic_DNA.
EMBL; EU883575; ACG60649.1; ALT_INIT; mRNA.
EMBL; AY615372; AAT38917.1; ALT_INIT; mRNA.
EMBL; AL135818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81447.1; ALT_INIT; Genomic_DNA.
EMBL; BC067472; AAH67472.1; -; mRNA.
EMBL; BC069592; AAH69592.1; -; mRNA.
EMBL; BC096071; AAH96071.1; ALT_INIT; mRNA.
EMBL; BC096072; AAH96072.1; ALT_INIT; mRNA.
EMBL; BC096073; AAH96073.1; ALT_INIT; mRNA.
EMBL; BC096074; AAH96074.1; ALT_INIT; mRNA.
EMBL; BC098567; AAH98567.1; ALT_INIT; mRNA.
CCDS; CCDS9894.2; -.
PIR; S68208; S68208.
RefSeq; NP_001171147.1; NM_001177676.1.
RefSeq; NP_001335366.1; NM_001348437.1.
RefSeq; NP_003476.3; NM_003485.3.
RefSeq; XP_005268167.1; XM_005268110.4.
RefSeq; XP_005268168.1; XM_005268111.3.
RefSeq; XP_005268169.1; XM_005268112.3.
RefSeq; XP_006720325.1; XM_006720262.3.
RefSeq; XP_011535498.1; XM_011537196.2.
RefSeq; XP_011535499.1; XM_011537197.2.
RefSeq; XP_011535500.1; XM_011537198.2.
RefSeq; XP_011535501.1; XM_011537199.2.
UniGene; Hs.8882; -.
ProteinModelPortal; Q15743; -.
STRING; 9606.ENSP00000434045; -.
ChEMBL; CHEMBL3713916; -.
iPTMnet; Q15743; -.
PhosphoSitePlus; Q15743; -.
SwissPalm; Q15743; -.
BioMuta; GPR68; -.
DMDM; 3024266; -.
PaxDb; Q15743; -.
PeptideAtlas; Q15743; -.
PRIDE; Q15743; -.
DNASU; 8111; -.
Ensembl; ENST00000531499; ENSP00000434045; ENSG00000119714.
Ensembl; ENST00000535815; ENSP00000440797; ENSG00000119714.
GeneID; 8111; -.
KEGG; hsa:8111; -.
UCSC; uc001xzg.4; human.
CTD; 8111; -.
DisGeNET; 8111; -.
EuPathDB; HostDB:ENSG00000119714.10; -.
GeneCards; GPR68; -.
HGNC; HGNC:4519; GPR68.
MalaCards; GPR68; -.
MIM; 601404; gene.
MIM; 617217; phenotype.
neXtProt; NX_Q15743; -.
OpenTargets; ENSG00000119714; -.
PharmGKB; PA28911; -.
eggNOG; ENOG410IH5V; Eukaryota.
eggNOG; ENOG410Z8KI; LUCA.
GeneTree; ENSGT00900000140916; -.
HOGENOM; HOG000004801; -.
InParanoid; Q15743; -.
KO; K08408; -.
OMA; NCLSLYY; -.
OrthoDB; EOG091G06ZG; -.
PhylomeDB; Q15743; -.
TreeFam; TF331803; -.
Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-HSA-416476; G alpha (q) signalling events.
GeneWiki; GPR68; -.
GenomeRNAi; 8111; -.
PRO; PR:Q15743; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119714; -.
CleanEx; HS_GPR68; -.
ExpressionAtlas; Q15743; baseline and differential.
Genevisible; Q15743; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
CDD; cd15367; 7tmA_GPR68_OGR1; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR005389; OGR1_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01564; OGR1RECEPTOR.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Amelogenesis imperfecta; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Membrane; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix; Tumor suppressor.
CHAIN 1 365 Ovarian cancer G-protein coupled receptor
1.
/FTId=PRO_0000070113.
TOPO_DOM 1 21 Extracellular. {ECO:0000255}.
TRANSMEM 22 46 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 47 58 Cytoplasmic. {ECO:0000255}.
TRANSMEM 59 80 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 81 95 Extracellular. {ECO:0000255}.
TRANSMEM 96 117 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 118 136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 137 158 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 159 183 Extracellular. {ECO:0000255}.
TRANSMEM 184 205 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 206 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 249 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 250 263 Extracellular. {ECO:0000255}.
TRANSMEM 264 284 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 285 365 Cytoplasmic. {ECO:0000255}.
CARBOHYD 3 3 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 8 8 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 172 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 39 39 N -> S (found in a renal cell carcinoma
case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064716.
VARIANT 53 53 R -> Q (in dbSNP:rs2230339).
/FTId=VAR_058714.
VARIANT 74 74 L -> P (in AI2A6).
{ECO:0000269|PubMed:27693231}.
/FTId=VAR_077874.
MUTAGEN 17 17 H->F: Failed to stimulate IP formation at
pH 6.8, activity is restored at more acid
pH. {ECO:0000269|PubMed:12955148}.
MUTAGEN 20 20 H->F: Failed to stimulate IP formation at
pH 6.8, activity is restored at more acid
pH. {ECO:0000269|PubMed:12955148}.
MUTAGEN 84 84 H->F: Failed to stimulate IP formation at
pH 6.8, activity is restored at more acid
pH. {ECO:0000269|PubMed:12955148}.
MUTAGEN 89 89 H->F: No effect on pH-sensing activity.
{ECO:0000269|PubMed:12955148}.
MUTAGEN 159 159 H->F: No effect on pH-sensing activity.
{ECO:0000269|PubMed:12955148}.
MUTAGEN 169 169 H->F: Failed to stimulate IP formation at
pH 6.8, activity is restored at more acid
pH.
MUTAGEN 175 175 H->F: No effect on pH-sensing activity.
{ECO:0000269|PubMed:12955148}.
MUTAGEN 245 245 H->F: Severe loss pH-sensing activity.
{ECO:0000269|PubMed:12955148}.
MUTAGEN 269 269 H->F: Failed to stimulate IP formation at
pH 6.8, activity is restored at more acid
pH. {ECO:0000269|PubMed:12955148}.
CONFLICT 140 142 GVS -> RVT (in Ref. 1; AAA79060).
{ECO:0000305}.
SEQUENCE 365 AA; 41077 MW; 05919AFD5B842CCD CRC64;
MGNITADNSS MSCTIDHTIH QTLAPVVYVT VLVVGFPANC LSLYFGYLQI KARNELGVYL
CNLTVADLFY ICSLPFWLQY VLQHDNWSHG DLSCQVCGIL LYENIYISVG FLCCISVDRY
LAVAHPFRFH QFRTLKAAVG VSVVIWAKEL LTSIYFLMHE EVIEDENQHR VCFEHYPIQA
WQRAINYYRF LVGFLFPICL LLASYQGILR AVRRSHGTQK SRKDQIQRLV LSTVVIFLAC
FLPYHVLLLV RSVWEASCDF AKGVFNAYHF SLLLTSFNCV ADPVLYCFVS ETTHRDLARL
RGACLAFLTC SRTGRAREAY PLGAPEASGK SGAQGEEPEL LTKLHPAFQT PNSPGSGGFP
TGRLA


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