ID   GP132_MOUSE             Reviewed;         382 AA.
AC   Q9Z282; Q0VBS4; Q3U5A4;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Probable G-protein coupled receptor 132;
DE   AltName: Full=G2 accumulation protein;
GN   Name=Gpr132; Synonyms=G2a;
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].
RC   TISSUE=Spleen;
RX   PubMed=9770487; DOI=10.1073/pnas.95.21.12334;
RA   Weng Z., Fluckiger A.-C., Nisitani S., Wahl M.I., Le L.Q., Hunter C.A.,
RA   Fernal A.A., Le Beau M.M., Witte O.N.;
RT   "A DNA damage and stress inducible G protein-coupled receptor blocks cells
RT   in G2/M.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12334-12339(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12482833; DOI=10.1161/01.atv.0000040598.18570.54;
RA   Rikitake Y., Hirata K., Yamashita T., Iwai K., Kobayashi S., Itoh H.,
RA   Ozaki M., Ejiri J., Shiomi M., Inoue N., Kawashima S., Yokoyama M.;
RT   "Expression of G2A, a receptor for lysophosphatidylcholine, by macrophages
RT   in murine, rabbit, and human atherosclerotic plaques.";
RL   Arterioscler. Thromb. Vasc. Biol. 22:2049-2053(2002).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-137.
RX   PubMed=15728718; DOI=10.1091/mbc.e04-12-1044;
RA   Wang L., Radu C.G., Yang L.V., Bentolila L.A., Riedinger M., Witte O.N.;
RT   "Lysophosphatidylcholine-induced surface redistribution regulates signaling
RT   of the murine G protein-coupled receptor G2A.";
RL   Mol. Biol. Cell 16:2234-2247(2005).
CC   -!- FUNCTION: May be a receptor for oxidized free fatty acids derived from
CC       linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid
CC       (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be
CC       involved in apoptosis. Functions at the G2/M checkpoint to delay
CC       mitosis. May function as a sensor that monitors the oxidative states
CC       and mediates appropriate cellular responses such as secretion of
CC       paracrine signals and attenuation of proliferation. May mediate ths
CC       accumulation of intracellular inositol phosphates at acidic pH through
CC       proton-sensing activity (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:15728718}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15728718};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:15728718}.
CC       Note=Internalized and accumulated in endosomal compartments. LPC
CC       triggers the relocalization from the endosomal compartment to the cell
CC       surface.
CC   -!- TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues rich in
CC       lymphocytes like spleen and thymus. Weakly expressed in heart and lung.
CC       Highly expressed in infiltrating macrophages within atherosclerotic
CC       lesions. {ECO:0000269|PubMed:12482833}.
CC   -!- INDUCTION: By DNA-damaging agents.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF083442; AAC67542.1; -; mRNA.
DR   EMBL; AK089866; BAC40980.1; -; mRNA.
DR   EMBL; AK153765; BAE32176.1; -; mRNA.
DR   EMBL; BC120522; AAI20523.1; -; mRNA.
DR   EMBL; BC120524; AAI20525.1; -; mRNA.
DR   CCDS; CCDS26199.1; -.
DR   RefSeq; NP_064309.1; NM_019925.4.
DR   RefSeq; XP_006516165.1; XM_006516102.2.
DR   RefSeq; XP_006516166.1; XM_006516103.2.
DR   AlphaFoldDB; Q9Z282; -.
DR   SMR; Q9Z282; -.
DR   STRING; 10090.ENSMUSP00000021729; -.
DR   GlyCosmos; Q9Z282; 1 site, No reported glycans.
DR   GlyGen; Q9Z282; 1 site.
DR   PhosphoSitePlus; Q9Z282; -.
DR   EPD; Q9Z282; -.
DR   MaxQB; Q9Z282; -.
DR   PaxDb; 10090-ENSMUSP00000021729; -.
DR   ProteomicsDB; 271133; -.
DR   DNASU; 56696; -.
DR   Ensembl; ENSMUST00000021729.9; ENSMUSP00000021729.8; ENSMUSG00000021298.9.
DR   GeneID; 56696; -.
DR   KEGG; mmu:56696; -.
DR   UCSC; uc007pfk.1; mouse.
DR   AGR; MGI:1890220; -.
DR   CTD; 29933; -.
DR   MGI; MGI:1890220; Gpr132.
DR   VEuPathDB; HostDB:ENSMUSG00000021298; -.
DR   eggNOG; ENOG502QQC1; Eukaryota.
DR   GeneTree; ENSGT01100000263537; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q9Z282; -.
DR   OMA; CKLTGYI; -.
DR   OrthoDB; 4132231at2759; -.
DR   PhylomeDB; Q9Z282; -.
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; 56696; 3 hits in 77 CRISPR screens.
DR   PRO; PR:Q9Z282; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9Z282; Protein.
DR   Bgee; ENSMUSG00000021298; Expressed in thymus and 50 other cell types or tissues.
DR   ExpressionAtlas; Q9Z282; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:MGI.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IDA:CACAO.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR005388; G2A_lysphc_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24234:SF7; G-PROTEIN COUPLED RECEPTOR 132-RELATED; 1.
DR   PANTHER; PTHR24234; LYSOPHOSPHATIDIC ACID RECEPTOR 5/SPHINGOSYLPHOSPHORYLCHOLINE RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01563; G2ARECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; Q9Z282; MM.
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..382
FT                   /note="Probable G-protein coupled receptor 132"
FT                   /id="PRO_0000069462"
FT   TOPO_DOM        1..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..99
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..135
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..261
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..309
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        112..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   MUTAGEN         137
FT                   /note="R->A: Enhanced surface expression and a lower
FT                   localization to endosomal vesicles."
FT                   /evidence="ECO:0000269|PubMed:15728718"
SQ   SEQUENCE   382 AA;  42653 MW;  D4F8CE0370CCD610 CRC64;
     MRSEPTNAAG NTTLGVTSVL QSTSVPSSET CHVSYEESRV VLVVVYSAVC LLGLPANCLT
     AWLTLLQVLQ RNVLAVYLFC LSLCELLYIS TVPLWIIYIQ NQHKWNLGPQ ACKVTAYIFF
     CNIYISILLL CCISCDRYMA VVYALESRGH RHQRTAVTIS ACVILLVGLV NYPVFDMKVE
     KSFCFEPLRM NSKIAGYHYL RFTFGFAIPL GILAFTNHQI FRSIKLSDSL SAAQKNKVKR
     SAIAVVTIFL VCFAPYHVVL LVKAASFSFY QGDMDAVCAF ESRLYTVSMV FLCLSTVNSV
     ADPIIYVLGT DHSRQEVSRI HTGWKKWSTK TYVTCSKDSE ETHLPTELSN TYTFPNPAHP
     PGSQPAKLGL LCSPERLPEE LC
//