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Probable G-protein coupled receptor 132 (G2 accumulation protein)

 GP132_HUMAN             Reviewed;         380 AA.
Q9UNW8; A8K7X7; B4E144; Q9BSU2;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 146.
RecName: Full=Probable G-protein coupled receptor 132;
AltName: Full=G2 accumulation protein;
Name=GPR132; Synonyms=G2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION.
TISSUE=Spleen;
PubMed=9770487; DOI=10.1073/pnas.95.21.12334;
Weng Z., Fluckiger A.-C., Nisitani S., Wahl M.I., Le L.Q.,
Hunter C.A., Fernal A.A., Le Beau M.M., Witte O.N.;
"A DNA damage and stress inducible G protein-coupled receptor blocks
cells in G2/M.";
Proc. Natl. Acad. Sci. U.S.A. 95:12334-12339(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, ALTERNATIVE
SPLICING, AND MUTAGENESIS OF LYS-7; LYS-31 AND ARG-42.
PubMed=19855098; DOI=10.1124/jpet.109.158758;
Ogawa A., Obinata H., Hattori T., Kishi M., Tatei K., Ishikawa O.,
Izumi T.;
"Identification and analysis of two splice variants of human G2A
generated by alternative splicing.";
J. Pharmacol. Exp. Ther. 332:469-478(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
Kaighin V.A., Martin A.L., Aronstam R.S.;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Synovium, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=B-cell, and Brain;
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).
[9]
PRELIMINARY FUNCTION.
PubMed=11474113; DOI=10.1126/science.1061781;
Kabarowski J.H.S., Zhu K., Le L.Q., Witte O.N., Xu Y.;
"Lysophosphatidylcholine as a ligand for the immunoregulatory receptor
G2A.";
Science 293:702-705(2001).
[10]
ERRATUM, AND RETRACTION.
PubMed=15653487; DOI=10.1126/science.307.5707.206b;
Witte O.N., Kabarowski J.H., Xu Y., Le L.Q., Zhu K.;
Science 307:206-206(2005).
[11]
TISSUE SPECIFICITY.
PubMed=12482833; DOI=10.1161/01.ATV.0000040598.18570.54;
Rikitake Y., Hirata K., Yamashita T., Iwai K., Kobayashi S., Itoh H.,
Ozaki M., Ejiri J., Shiomi M., Inoue N., Kawashima S., Yokoyama M.;
"Expression of G2A, a receptor for lysophosphatidylcholine, by
macrophages in murine, rabbit, and human atherosclerotic plaques.";
Arterioscler. Thromb. Vasc. Biol. 22:2049-2053(2002).
[12]
FUNCTION.
PubMed=12586833; DOI=10.1074/jbc.M209101200;
Lin P., Ye R.D.;
"The lysophospholipid receptor G2A activates a specific combination of
G proteins and promotes apoptosis.";
J. Biol. Chem. 278:14379-14386(2003).
-!- FUNCTION: May be a receptor for oxidized free fatty acids derived
from linoleic and arachidonic acids such as 9-
hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein,
most likely G alpha(q). May be involved in apoptosis. Functions at
the G2/M checkpoint to delay mitosis. May function as a sensor
that monitors the oxidative states and mediates appropriate
cellular responses such as secretion of paracrine signals and
attenuation of proliferation. May mediate ths accumulation of
intracellular inositol phosphates at acidic pH through proton-
sensing activity. {ECO:0000269|PubMed:12586833,
ECO:0000269|PubMed:19855098, ECO:0000269|PubMed:9770487}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Note=Internalized and accumulated
in endosomal compartments. LPC triggers the relocalization from
the endosomal compartment to the cell surface (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=G2A-a;
IsoId=Q9UNW8-1; Sequence=Displayed;
Name=2;
IsoId=Q9UNW8-2; Sequence=VSP_008404;
Name=3; Synonyms=G2A-b;
IsoId=Q9UNW8-3; Sequence=VSP_054592;
Note=More abundant than isoform 1 in leukocytes by approximately
3-fold.;
-!- TISSUE SPECIFICITY: Highly expressed in macrophages and
hematopoietic tissues rich in lymphocytes, like spleen and thymus.
Weakly expressed in heart and lung. In atherosclerotic plaques,
expression is observed around the lipid core and at the shoulder
region. {ECO:0000269|PubMed:12482833}.
-!- INDUCTION: By stress and DNA-damaging agents.
{ECO:0000269|PubMed:9770487}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- CAUTION: Was originally thought to be a receptor for
lysophosphatidylcholine (LPC) and sphingosylphosphorylcholine
(SPC), However, this work has been retracted.
{ECO:0000305|PubMed:11474113}.
-----------------------------------------------------------------------
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EMBL; AF083955; AAD47380.1; -; mRNA.
EMBL; AB465599; BAG84609.1; -; mRNA.
EMBL; AB465600; BAG84610.1; -; mRNA.
EMBL; EU432121; ABY87920.1; -; mRNA.
EMBL; BT007257; AAP35921.1; -; mRNA.
EMBL; AK292142; BAF84831.1; -; mRNA.
EMBL; AK303654; BAG64656.1; -; mRNA.
EMBL; AL512356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81898.1; -; Genomic_DNA.
EMBL; BC004555; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC084546; AAH84546.1; -; mRNA.
CCDS; CCDS61567.1; -. [Q9UNW8-3]
CCDS; CCDS9997.1; -. [Q9UNW8-1]
RefSeq; NP_001265623.1; NM_001278694.1. [Q9UNW8-1]
RefSeq; NP_001265624.1; NM_001278695.1. [Q9UNW8-3]
RefSeq; NP_001265625.1; NM_001278696.1. [Q9UNW8-2]
RefSeq; NP_037477.1; NM_013345.3. [Q9UNW8-1]
UniGene; Hs.532504; -.
ProteinModelPortal; Q9UNW8; -.
STRING; 9606.ENSP00000328818; -.
ChEMBL; CHEMBL3085618; -.
GuidetoPHARMACOLOGY; 128; -.
iPTMnet; Q9UNW8; -.
PhosphoSitePlus; Q9UNW8; -.
DMDM; 37537754; -.
PaxDb; Q9UNW8; -.
PeptideAtlas; Q9UNW8; -.
PRIDE; Q9UNW8; -.
DNASU; 29933; -.
Ensembl; ENST00000329797; ENSP00000328818; ENSG00000183484. [Q9UNW8-1]
Ensembl; ENST00000392585; ENSP00000376364; ENSG00000183484. [Q9UNW8-3]
Ensembl; ENST00000539291; ENSP00000438094; ENSG00000183484. [Q9UNW8-1]
GeneID; 29933; -.
KEGG; hsa:29933; -.
UCSC; uc001yqd.5; human. [Q9UNW8-1]
CTD; 29933; -.
DisGeNET; 29933; -.
EuPathDB; HostDB:ENSG00000183484.11; -.
GeneCards; GPR132; -.
HGNC; HGNC:17482; GPR132.
HPA; HPA029694; -.
HPA; HPA029695; -.
MIM; 606167; gene.
neXtProt; NX_Q9UNW8; -.
OpenTargets; ENSG00000183484; -.
PharmGKB; PA134940832; -.
eggNOG; ENOG410IKDS; Eukaryota.
eggNOG; ENOG4111F3F; LUCA.
GeneTree; ENSGT00910000143980; -.
HOGENOM; HOG000013146; -.
HOVERGEN; HBG104029; -.
InParanoid; Q9UNW8; -.
KO; K08426; -.
OMA; NSVADPI; -.
OrthoDB; EOG091G0BBZ; -.
PhylomeDB; Q9UNW8; -.
TreeFam; TF331803; -.
Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-HSA-416476; G alpha (q) signalling events.
GeneWiki; GPR132; -.
GenomeRNAi; 29933; -.
PRO; PR:Q9UNW8; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000183484; -.
CleanEx; HS_GPR132; -.
ExpressionAtlas; Q9UNW8; baseline and differential.
Genevisible; Q9UNW8; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
InterPro; IPR005388; G2A_lysphc_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01563; G2ARECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Receptor; Reference proteome; Stress response; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 380 Probable G-protein coupled receptor 132.
/FTId=PRO_0000069461.
TOPO_DOM 1 45 Extracellular. {ECO:0000255}.
TRANSMEM 46 68 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 69 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 102 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 103 116 Extracellular. {ECO:0000255}.
TRANSMEM 117 138 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 139 158 Cytoplasmic. {ECO:0000255}.
TRANSMEM 159 178 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 179 197 Extracellular. {ECO:0000255}.
TRANSMEM 198 220 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 221 246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 247 269 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 270 288 Extracellular. {ECO:0000255}.
TRANSMEM 289 311 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 312 380 Cytoplasmic. {ECO:0000255}.
COMPBIAS 151 157 Poly-Arg.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 115 186 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 188 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_008404.
VAR_SEQ 1 11 MCPMLLKNGYN -> MP (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:19855098}.
/FTId=VSP_054592.
MUTAGEN 7 7 K->A: No change in basal activity.
{ECO:0000269|PubMed:19855098}.
MUTAGEN 31 31 K->A: Decreased IP1 accumulation at any
pH. {ECO:0000269|PubMed:19855098}.
MUTAGEN 42 42 R->A: Decreased basal activity at
alkaline pH and loss of proton-sensing
activity at low pH.
{ECO:0000269|PubMed:19855098}.
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


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