ID   GPR87_MOUSE             Reviewed;         358 AA.
AC   Q99MT7; Q8C4Y7;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=G-protein coupled receptor 87;
GN   Name=Gpr87;
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 [MRNA].
RX   PubMed=11273702; DOI=10.1006/jmbi.2001.4520;
RA   Wittenberger T., Schaller H.C., Hellebrand S.;
RT   "An expressed sequence tag (EST) data mining strategy succeeding in the
RT   discovery of new G-protein coupled receptors.";
RL   J. Mol. Biol. 307:799-813(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17905198; DOI=10.1016/j.bbrc.2007.09.063;
RA   Tabata K., Baba K., Shiraishi A., Ito M., Fujita N.;
RT   "The orphan GPCR GPR87 was deorphanized and shown to be a lysophosphatidic
RT   acid receptor.";
RL   Biochem. Biophys. Res. Commun. 363:861-866(2007).
CC   -!- FUNCTION: Receptor for lysophosphatidic acid (LPA). Necessary for
CC       p53/TP53-dependent survival in response to DNA damage (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in testis and brain and to
CC       a lesser extent placenta, ovary, prostate, and skeletal muscle but not
CC       in heart, lung, kidney, liver or intestine.
CC       {ECO:0000269|PubMed:17905198}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF295366; AAK01866.1; -; mRNA.
DR   EMBL; AK080394; BAC37905.1; -; mRNA.
DR   CCDS; CCDS79914.1; -.
DR   RefSeq; NP_001289132.1; NM_001302203.1.
DR   AlphaFoldDB; Q99MT7; -.
DR   SMR; Q99MT7; -.
DR   STRING; 10090.ENSMUSP00000143683; -.
DR   GlyCosmos; Q99MT7; 3 sites, No reported glycans.
DR   GlyGen; Q99MT7; 3 sites.
DR   PhosphoSitePlus; Q99MT7; -.
DR   PaxDb; 10090-ENSMUSP00000059272; -.
DR   Antibodypedia; 18298; 283 antibodies from 29 providers.
DR   DNASU; 84111; -.
DR   Ensembl; ENSMUST00000200095.2; ENSMUSP00000143683.2; ENSMUSG00000051431.8.
DR   GeneID; 84111; -.
DR   KEGG; mmu:84111; -.
DR   UCSC; uc008pip.2; mouse.
DR   AGR; MGI:1934133; -.
DR   CTD; 53836; -.
DR   MGI; MGI:1934133; Gpr87.
DR   VEuPathDB; HostDB:ENSMUSG00000051431; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01060000248592; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q99MT7; -.
DR   OMA; YINTCTF; -.
DR   OrthoDB; 5390357at2759; -.
DR   PhylomeDB; Q99MT7; -.
DR   BioGRID-ORCS; 84111; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q99MT7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q99MT7; Protein.
DR   Bgee; ENSMUSG00000051431; Expressed in esophagus and 38 other cell types or tissues.
DR   ExpressionAtlas; Q99MT7; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd15969; 7tmA_GPR87; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR008109; P2Y13_rcpt.
DR   PANTHER; PTHR24233:SF8; G-PROTEIN COUPLED RECEPTOR 87; 1.
DR   PANTHER; PTHR24233; P2Y PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01735; P2Y13PRNCPTR.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q99MT7; MM.
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.
FT   CHAIN           1..358
FT                   /note="G-protein coupled receptor 87"
FT                   /id="PRO_0000069596"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..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..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
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        114..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        1..11
FT                   /note="MGLNLTLTKLP -> MAVPNVNVSTFA (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  41414 MW;  6D258E98CB3BE4B9 CRC64;
     MGLNLTLTKL PGNELYSQAS HTANSTSEGH GKNSTLHNKF DTIILPVLYL VIFVASILLN
     GLAVWIFFHI RNKTSFIFYL KNIVVADLIM TLTFPFRIVR DAGFGPWYFE FILCRYTSVL
     FYANMYTSIV FLGLISVDRY LKVVKPFGDS RMYSITFTKV LSVCVWVIMA ILSLPNIILT
     NGQPTKENIH DCMKLKSPLG AKWHMAVTYV DSCLFVAVLV ILIGCYIAIS RYIHKSSRQF
     ISQSSRKRKH NQSIRVVVAV FFTCFLPYHL CRIPFTFSNL DRLLDESAHK ILYYCKEMTL
     FLSACNVCLD PIIYFFMCKS FSRRLFKKSN IRTRSESIRS LQSVRRSEVR IYYDYTDV
//