LPAR2_MOUSE
ID LPAR2_MOUSE Reviewed; 348 AA.
AC Q9JL06; Q6P290;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Lysophosphatidic acid receptor 2 {ECO:0000305};
DE Short=LPA receptor 2;
DE Short=LPA-2;
DE AltName: Full=Lysophosphatidic acid receptor Edg-4;
GN Name=Lpar2 {ECO:0000312|MGI:MGI:1858422}; Synonyms=Edg4, Lpa2;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10729222; DOI=10.1006/geno.2000.6122;
RA Contos J.J.A., Chun J.;
RT "Genomic characterization of the lysophosphatidic acid receptor gene,
RT lp(A2)/Edg4, and identification of a frameshift mutation in a previously
RT characterized cDNA.";
RL Genomics 64:155-169(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [5]
RP REVIEW.
RX PubMed=11093753; DOI=10.1124/mol.58.6.1188;
RA Contos J.J.A., Ishii I., Chun J.;
RT "Lysophosphatidic acid receptors.";
RL Mol. Pharmacol. 58:1188-1196(2000).
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of
CC diverse cellular activities. Seems to be coupled to the G(i)/G(o),
CC G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key
CC role in phospholipase C-beta (PLC-beta) signaling pathway Stimulates
CC phospholipase C (PLC) activity in a manner that is independent of RALA
CC activation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLC9A3R2/NHERF2, MAGI3 and PLCB3. Interacts
CC with RALA and GRK2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Prior to
CC LPA treatment found predominantly at the cell surface but in the
CC presence of LPA colocalizes with RALA in the endocytic vesicles.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in testes, kidney, and
CC embryonic brain. Other organs also express the transcript, including
CC heart, lung, spleen, thymus, stomach, and adult brain. Several have
CC little or no expression, including liver, small intestine, and skeletal
CC muscle.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF65684.1; Type=Frameshift; Note=Several.; Evidence={ECO:0000305};
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DR EMBL; AF218844; AAF65684.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AK144861; BAE26107.1; -; mRNA.
DR EMBL; BC060131; AAH60131.1; -; mRNA.
DR EMBL; BC064676; AAH64676.1; -; mRNA.
DR CCDS; CCDS40362.1; -.
DR RefSeq; NP_064412.2; NM_020028.3.
DR AlphaFoldDB; Q9JL06; -.
DR SMR; Q9JL06; -.
DR IntAct; Q9JL06; 2.
DR MINT; Q9JL06; -.
DR STRING; 10090.ENSMUSP00000128261; -.
DR ChEMBL; CHEMBL4523464; -.
DR GuidetoPHARMACOLOGY; 273; -.
DR GlyGen; Q9JL06; 2 sites.
DR PhosphoSitePlus; Q9JL06; -.
DR PRIDE; Q9JL06; -.
DR ProteomicsDB; 291960; -.
DR ProteomicsDB; 333080; -.
DR Antibodypedia; 15391; 347 antibodies from 32 providers.
DR Ensembl; ENSMUST00000034325; ENSMUSP00000034325; ENSMUSG00000031861.
DR Ensembl; ENSMUST00000164890; ENSMUSP00000128261; ENSMUSG00000031861.
DR GeneID; 53978; -.
DR KEGG; mmu:53978; -.
DR UCSC; uc009lxv.1; mouse.
DR CTD; 9170; -.
DR MGI; MGI:1858422; Lpar2.
DR VEuPathDB; HostDB:ENSMUSG00000031861; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244941; -.
DR HOGENOM; CLU_047979_0_0_1; -.
DR InParanoid; Q9JL06; -.
DR OMA; TRMSKHT; -.
DR OrthoDB; 968418at2759; -.
DR PhylomeDB; Q9JL06; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 53978; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9JL06; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JL06; protein.
DR Bgee; ENSMUSG00000031861; Expressed in remnant of Rathke's pouch and 128 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IEA:InterPro.
DR GO; GO:0030165; F:PDZ domain binding; IPI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004065; LPA_rcpt.
DR InterPro; IPR004066; LPA_rcpt_EDG4.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01528; EDG4RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01527; LPARECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..348
FT /note="Lysophosphatidic acid receptor 2"
FT /id="PRO_0000069426"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 345..348
FT /note="PDZ-binding"
FT LIPID 308
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 267
FT /note="S -> T (in Ref. 1; AAF65684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39003 MW; 22F98C271AAF1233 CRC64;
MGQCYYNETI GFFYNNSGKE LSLHWRPKDV VVVALGLTVS VLVLLTNLLV IAAIASNRRF
HQPIYYLLGN LAAADLFAGM AYLFLMFHTG PRTARLSIKG WFLRQGLLDT SLTASVATLL
AIAVERHRSV MAVQLHSRLP RGRVVTLIVG VWAAALGLGL LPAHFWHCLC DLDSCSRMVP
LFSRSYLAAW ALSSLLVFLL MVAVYTRIFF YVRRRVERMA EHVSCHPRYR ETTLSLVKTV
VIILGAFVVC WTPGQVVLLL DGLDCKSCNV LAVEKYFLLL AEANSLVNAV VYSCRDAEMR
RTFRRLLCCM CLRWSSHKSA RYSASAQTGA STRIMLPENG RPLMDSTL
