GP132_HUMAN
ID GP132_HUMAN Reviewed; 380 AA.
AC Q9UNW8; A8K7X7; B4E144; Q9BSU2;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable G-protein coupled receptor 132;
DE AltName: Full=G2 accumulation protein;
GN Name=GPR132; Synonyms=G2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION.
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 [MRNA] (ISOFORMS 1 AND 3), FUNCTION, ALTERNATIVE
RP SPLICING, AND MUTAGENESIS OF LYS-7; LYS-31 AND ARG-42.
RX PubMed=19855098; DOI=10.1124/jpet.109.158758;
RA Ogawa A., Obinata H., Hattori T., Kishi M., Tatei K., Ishikawa O.,
RA Izumi T.;
RT "Identification and analysis of two splice variants of human G2A generated
RT by alternative splicing.";
RL J. Pharmacol. Exp. Ther. 332:469-478(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Synovium, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and 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 [9]
RP PRELIMINARY FUNCTION.
RX PubMed=11474113; DOI=10.1126/science.1061781;
RA Kabarowski J.H.S., Zhu K., Le L.Q., Witte O.N., Xu Y.;
RT "Lysophosphatidylcholine as a ligand for the immunoregulatory receptor
RT G2A.";
RL Science 293:702-705(2001).
RN [10]
RP ERRATUM OF PUBMED:11474113, AND RETRACTION NOTICE OF PUBMED:11474113.
RX PubMed=15653487; DOI=10.1126/science.307.5707.206b;
RA Witte O.N., Kabarowski J.H., Xu Y., Le L.Q., Zhu K.;
RL Science 307:206-206(2005).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=12586833; DOI=10.1074/jbc.m209101200;
RA Lin P., Ye R.D.;
RT "The lysophospholipid receptor G2A activates a specific combination of G
RT proteins and promotes apoptosis.";
RL J. Biol. Chem. 278:14379-14386(2003).
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. {ECO:0000269|PubMed:12586833,
CC ECO:0000269|PubMed:19855098, ECO:0000269|PubMed:9770487}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Internalized and accumulated in endosomal
CC compartments. LPC triggers the relocalization from the endosomal
CC compartment to the cell surface (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=G2A-a;
CC IsoId=Q9UNW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNW8-2; Sequence=VSP_008404;
CC Name=3; Synonyms=G2A-b;
CC IsoId=Q9UNW8-3; Sequence=VSP_054592;
CC -!- TISSUE SPECIFICITY: Highly expressed in macrophages and hematopoietic
CC tissues rich in lymphocytes, like spleen and thymus. Weakly expressed
CC in heart and lung. In atherosclerotic plaques, expression is observed
CC around the lipid core and at the shoulder region.
CC {ECO:0000269|PubMed:12482833}.
CC -!- INDUCTION: By stress and DNA-damaging agents.
CC {ECO:0000269|PubMed:9770487}.
CC -!- MISCELLANEOUS: [Isoform 3]: More abundant than isoform 1 in leukocytes
CC by approximately 3-fold. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be a receptor for
CC lysophosphatidylcholine (LPC) and sphingosylphosphorylcholine (SPC),
CC However, this work has been retracted. {ECO:0000305|PubMed:11474113}.
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DR EMBL; AF083955; AAD47380.1; -; mRNA.
DR EMBL; AB465599; BAG84609.1; -; mRNA.
DR EMBL; AB465600; BAG84610.1; -; mRNA.
DR EMBL; EU432121; ABY87920.1; -; mRNA.
DR EMBL; BT007257; AAP35921.1; -; mRNA.
DR EMBL; AK292142; BAF84831.1; -; mRNA.
DR EMBL; AK303654; BAG64656.1; -; mRNA.
DR EMBL; AL512356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81898.1; -; Genomic_DNA.
DR EMBL; BC004555; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC084546; AAH84546.1; -; mRNA.
DR CCDS; CCDS61567.1; -. [Q9UNW8-3]
DR CCDS; CCDS9997.1; -. [Q9UNW8-1]
DR RefSeq; NP_001265623.1; NM_001278694.1. [Q9UNW8-1]
DR RefSeq; NP_001265624.1; NM_001278695.1. [Q9UNW8-3]
DR RefSeq; NP_001265625.1; NM_001278696.1. [Q9UNW8-2]
DR RefSeq; NP_037477.1; NM_013345.3. [Q9UNW8-1]
DR AlphaFoldDB; Q9UNW8; -.
DR SMR; Q9UNW8; -.
DR STRING; 9606.ENSP00000328818; -.
DR ChEMBL; CHEMBL3085618; -.
DR GuidetoPHARMACOLOGY; 128; -.
DR GlyGen; Q9UNW8; 1 site.
DR iPTMnet; Q9UNW8; -.
DR PhosphoSitePlus; Q9UNW8; -.
DR BioMuta; GPR132; -.
DR DMDM; 37537754; -.
DR PaxDb; Q9UNW8; -.
DR PeptideAtlas; Q9UNW8; -.
DR PRIDE; Q9UNW8; -.
DR ProteomicsDB; 85336; -. [Q9UNW8-1]
DR ProteomicsDB; 85337; -. [Q9UNW8-2]
DR Antibodypedia; 14925; 291 antibodies from 34 providers.
DR DNASU; 29933; -.
DR Ensembl; ENST00000329797.8; ENSP00000328818.3; ENSG00000183484.12. [Q9UNW8-1]
DR Ensembl; ENST00000392585.2; ENSP00000376364.2; ENSG00000183484.12. [Q9UNW8-3]
DR Ensembl; ENST00000539291.6; ENSP00000438094.2; ENSG00000183484.12. [Q9UNW8-1]
DR GeneID; 29933; -.
DR KEGG; hsa:29933; -.
DR MANE-Select; ENST00000329797.8; ENSP00000328818.3; NM_013345.4; NP_037477.1.
DR UCSC; uc001yqd.5; human. [Q9UNW8-1]
DR CTD; 29933; -.
DR DisGeNET; 29933; -.
DR GeneCards; GPR132; -.
DR HGNC; HGNC:17482; GPR132.
DR HPA; ENSG00000183484; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 606167; gene.
DR neXtProt; NX_Q9UNW8; -.
DR OpenTargets; ENSG00000183484; -.
DR PharmGKB; PA134940832; -.
DR VEuPathDB; HostDB:ENSG00000183484; -.
DR eggNOG; ENOG502QQC1; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9UNW8; -.
DR OMA; FAPYHVV; -.
DR OrthoDB; 985737at2759; -.
DR PhylomeDB; Q9UNW8; -.
DR TreeFam; TF331803; -.
DR PathwayCommons; Q9UNW8; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; Q9UNW8; -.
DR SIGNOR; Q9UNW8; -.
DR BioGRID-ORCS; 29933; 9 hits in 1076 CRISPR screens.
DR GeneWiki; GPR132; -.
DR GenomeRNAi; 29933; -.
DR Pharos; Q9UNW8; Tchem.
DR PRO; PR:Q9UNW8; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UNW8; protein.
DR Bgee; ENSG00000183484; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q9UNW8; baseline and differential.
DR Genevisible; Q9UNW8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR InterPro; IPR005388; G2A_lysphc_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01563; G2ARECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Stress response; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="Probable G-protein coupled receptor 132"
FT /id="PRO_0000069461"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_008404"
FT VAR_SEQ 1..11
FT /note="MCPMLLKNGYN -> MP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:19855098"
FT /id="VSP_054592"
FT MUTAGEN 7
FT /note="K->A: No change in basal activity."
FT /evidence="ECO:0000269|PubMed:19855098"
FT MUTAGEN 31
FT /note="K->A: Decreased IP1 accumulation at any pH."
FT /evidence="ECO:0000269|PubMed:19855098"
FT MUTAGEN 42
FT /note="R->A: Decreased basal activity at alkaline pH and
FT loss of proton-sensing activity at low pH."
FT /evidence="ECO:0000269|PubMed:19855098"
SQ SEQUENCE 380 AA; 42499 MW; 6DE63D17275ECD74 CRC64;
MCPMLLKNGY NGNATPVTTT APWASLGLSA KTCNNVSFEE SRIVLVVVYS AVCTLGVPAN
CLTAWLALLQ VLQGNVLAVY LLCLALCELL YTGTLPLWVI YIRNQHRWTL GLLACKVTAY
IFFCNIYVSI LFLCCISCDR FVAVVYALES RGRRRRRTAI LISACIFILV GIVHYPVFQT
EDKETCFDML QMDSRIAGYY YARFTVGFAI PLSIIAFTNH RIFRSIKQSM GLSAAQKAKV
KHSAIAVVVI FLVCFAPYHL VLLVKAAAFS YYRGDRNAMC GLEERLYTAS VVFLCLSTVN
GVADPIIYVL ATDHSRQEVS RIHKGWKEWS MKTDVTRLTH SRDTEELQSP VALADHYTFS
RPVHPPGSPC PAKRLIEESC
