LPAR1_HUMAN
ID LPAR1_HUMAN Reviewed; 364 AA.
AC Q92633; B4DK36; O00656; O00722; P78351;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Lysophosphatidic acid receptor 1;
DE Short=LPA receptor 1;
DE Short=LPA-1;
DE AltName: Full=Lysophosphatidic acid receptor Edg-2 {ECO:0000303|PubMed:9070858};
GN Name=LPAR1; Synonyms=EDG2, LPA1;
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, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9070858; DOI=10.1006/bbrc.1997.6150;
RA An S., Dickens M.A., Bleu T., Hallmark O.G., Goetzl E.J.;
RT "Molecular cloning of the human Edg2 protein and its identification as a
RT functional cellular receptor for lysophosphatidic acid.";
RL Biochem. Biophys. Res. Commun. 231:619-622(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND REVIEW.
RX PubMed=9069262; DOI=10.1016/s0955-0674(97)80059-2;
RA Moolenaar W.H., Kranenburg O., Postma F.R., Zondag G.C.M.;
RT "Lysophosphatidic acid: G-protein signalling and cellular responses.";
RL Curr. Opin. Cell Biol. 9:168-173(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus, and Testis;
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 [7]
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).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18066075; DOI=10.1038/nm1685;
RA Tager A.M., LaCamera P., Shea B.S., Campanella G.S., Selman M., Zhao Z.,
RA Polosukhin V., Wain J., Karimi-Shah B.A., Kim N.D., Hart W.K., Pardo A.,
RA Blackwell T.S., Xu Y., Chun J., Luster A.D.;
RT "The lysophosphatidic acid receptor LPA1 links pulmonary fibrosis to lung
RT injury by mediating fibroblast recruitment and vascular leak.";
RL Nat. Med. 14:45-54(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RALA AND GRK2.
RX PubMed=19306925; DOI=10.1016/j.cellsig.2009.03.011;
RA Aziziyeh A.I., Li T.T., Pape C., Pampillo M., Chidiac P., Possmayer F.,
RA Babwah A.V., Bhattacharya M.;
RT "Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral
RT and GRK.";
RL Cell. Signal. 21:1207-1217(2009).
RN [10]
RP FUNCTION.
RX PubMed=19656035; DOI=10.1902/jop.2009.080624;
RA George J., Headen K.V., Ogunleye A.O., Perry G.A., Wilwerding T.M.,
RA Parrish L.C., McVaney T.P., Mattson J.S., Cerutis D.R.;
RT "Lysophosphatidic acid signals through specific lysophosphatidic acid
RT receptor subtypes to control key regenerative responses of human gingival
RT and periodontal ligament fibroblasts.";
RL J. Periodontology 80:1338-1347(2009).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19733258; DOI=10.1016/j.bbalip.2009.08.011;
RA Song H.Y., Lee M.J., Kim M.Y., Kim K.H., Lee I.H., Shin S.H., Lee J.S.,
RA Kim J.H.;
RT "Lysophosphatidic acid mediates migration of human mesenchymal stem cells
RT stimulated by synovial fluid of patients with rheumatoid arthritis.";
RL Biochim. Biophys. Acta 1801:23-30(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-85; LEU-87 AND
RP 325-ILE-LEU-326, AND GLYCOSYLATION.
RX PubMed=25025571; DOI=10.1016/j.cellsig.2014.07.005;
RA Zhao J., Wei J., Bowser R.K., Dong S., Xiao S., Zhao Y.;
RT "Molecular regulation of lysophosphatidic acid receptor 1 trafficking to
RT the cell surface.";
RL Cell. Signal. 26:2406-2411(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP REVIEW.
RX PubMed=25732591; DOI=10.1007/s00018-015-1872-8;
RA Fukushima N., Ishii S., Tsujiuchi T., Kagawa N., Katoh K.;
RT "Comparative analyses of lysophosphatidic acid receptor-mediated
RT signaling.";
RL Cell. Mol. Life Sci. 72:2377-2394(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-326 IN COMPLEXES WITH SYNTHETIC
RP ANTAGONISTS, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=26091040; DOI=10.1016/j.cell.2015.06.002;
RA Chrencik J.E., Roth C.B., Terakado M., Kurata H., Omi R., Kihara Y.,
RA Warshaviak D., Nakade S., Asmar-Rovira G., Mileni M., Mizuno H.,
RA Griffith M.T., Rodgers C., Han G.W., Velasquez J., Chun J., Stevens R.C.,
RA Hanson M.A.;
RT "Crystal structure of antagonist bound human lysophosphatidic acid receptor
RT 1.";
RL Cell 161:1633-1643(2015).
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA) (PubMed:9070858,
CC PubMed:19306925, PubMed:25025571, PubMed:26091040). Plays a role in the
CC reorganization of the actin cytoskeleton, cell migration,
CC differentiation and proliferation, and thereby contributes to the
CC responses to tissue damage and infectious agents. Activates downstream
CC signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of
CC heteromeric G proteins. Signaling inhibits adenylyl cyclase activity
CC and decreases cellular cAMP levels (PubMed:26091040). Signaling
CC triggers an increase of cytoplasmic Ca(2+) levels (PubMed:19656035,
CC PubMed:19733258, PubMed:26091040). Activates RALA; this leads to the
CC activation of phospholipase C (PLC) and the formation of inositol
CC 1,4,5-trisphosphate (PubMed:19306925). Signaling mediates activation of
CC down-stream MAP kinases (By similarity). Contributes to the regulation
CC of cell shape. Promotes Rho-dependent reorganization of the actin
CC cytoskeleton in neuronal cells and neurite retraction
CC (PubMed:26091040). Promotes the activation of Rho and the formation of
CC actin stress fibers (PubMed:26091040). Promotes formation of
CC lamellipodia at the leading edge of migrating cells via activation of
CC RAC1 (By similarity). Through its function as lysophosphatidic acid
CC receptor, plays a role in chemotaxis and cell migration, including
CC responses to injury and wounding (PubMed:18066075, PubMed:19656035,
CC PubMed:19733258). Plays a role in triggering inflammation in response
CC to bacterial lipopolysaccharide (LPS) via its interaction with CD14.
CC Promotes cell proliferation in response to lysophosphatidic acid.
CC Required for normal skeleton development. May play a role in osteoblast
CC differentiation. Required for normal brain development. Required for
CC normal proliferation, survival and maturation of newly formed neurons
CC in the adult dentate gyrus. Plays a role in pain perception and in the
CC initiation of neuropathic pain (By similarity).
CC {ECO:0000250|UniProtKB:P61793, ECO:0000269|PubMed:18066075,
CC ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:19656035,
CC ECO:0000269|PubMed:19733258, ECO:0000269|PubMed:25025571,
CC ECO:0000269|PubMed:26091040, ECO:0000269|PubMed:9070858,
CC ECO:0000305|PubMed:11093753, ECO:0000305|PubMed:9069262}.
CC -!- SUBUNIT: Interacts with RALA and GRK2 (PubMed:19306925). Interacts with
CC GNAQ and GNA13. Interacts with CD14; the interaction is enhanced by
CC exposure to bacterial lipopolysaccharide (LPS) (By similarity).
CC {ECO:0000250|UniProtKB:P61793, ECO:0000269|PubMed:19306925}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:19306925,
CC ECO:0000269|PubMed:25025571}. Cell membrane
CC {ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:25025571,
CC ECO:0000269|PubMed:26091040, ECO:0000269|PubMed:9070858}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19306925,
CC ECO:0000269|PubMed:26091040}. Endosome {ECO:0000269|PubMed:19306925}.
CC Note=Prior to LPA treatment found predominantly at the cell surface.
CC Internalized after LPA treatment. Colocalizes with RALA in endocytic
CC vesicles after LPA treatment. {ECO:0000269|PubMed:19306925}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92633-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92633-2; Sequence=VSP_057046;
CC -!- TISSUE SPECIFICITY: Expressed in many adult organs, including brain,
CC heart, colon, small intestine, placenta, prostate, ovary, pancreas,
CC testes, spleen, skeletal muscle, and kidney. Little or no expression in
CC liver, lung, thymus, or peripheral blood leukocytes (PubMed:9070858).
CC Detected in lung fibroblasts from bronchoalveolar fluid from patients
CC with idiopathic pulmonary fibrosis (PubMed:18066075). Detected in bone
CC marrow-derived mesenchymal stem cells (PubMed:19733258).
CC {ECO:0000269|PubMed:18066075, ECO:0000269|PubMed:19733258,
CC ECO:0000269|PubMed:9070858}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25025571}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LPAR1ID40405ch9q31.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U80811; AAC51139.1; -; mRNA.
DR EMBL; Y09479; CAA70686.1; -; mRNA.
DR EMBL; Y09479; CAA70687.1; -; mRNA.
DR EMBL; U78192; AAC00530.1; -; mRNA.
DR EMBL; AY322546; AAP84359.1; -; mRNA.
DR EMBL; AK296374; BAG59048.1; -; mRNA.
DR EMBL; AC007157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030615; AAH30615.1; -; mRNA.
DR EMBL; BC036034; AAH36034.1; -; mRNA.
DR CCDS; CCDS6777.1; -. [Q92633-1]
DR PIR; JC5293; JC5293.
DR RefSeq; NP_001392.2; NM_001401.3. [Q92633-1]
DR RefSeq; NP_476500.1; NM_057159.2. [Q92633-1]
DR RefSeq; XP_005251838.1; XM_005251781.3.
DR RefSeq; XP_005251839.1; XM_005251782.3. [Q92633-1]
DR RefSeq; XP_016869872.1; XM_017014383.1.
DR RefSeq; XP_016869873.1; XM_017014384.1.
DR RefSeq; XP_016869874.1; XM_017014385.1.
DR RefSeq; XP_016869875.1; XM_017014386.1.
DR RefSeq; XP_016869876.1; XM_017014387.1.
DR RefSeq; XP_016869877.1; XM_017014388.1.
DR RefSeq; XP_016869878.1; XM_017014389.1.
DR RefSeq; XP_016869879.1; XM_017014390.1.
DR RefSeq; XP_016869880.1; XM_017014391.1.
DR RefSeq; XP_016869881.1; XM_017014392.1.
DR RefSeq; XP_016869882.1; XM_017014393.1.
DR RefSeq; XP_016869883.1; XM_017014394.1.
DR RefSeq; XP_016869884.1; XM_017014395.1.
DR RefSeq; XP_016869885.1; XM_017014396.1.
DR RefSeq; XP_016869886.1; XM_017014397.1.
DR RefSeq; XP_016869887.1; XM_017014398.1.
DR RefSeq; XP_016869888.1; XM_017014399.1.
DR RefSeq; XP_016869889.1; XM_017014400.1.
DR RefSeq; XP_016869890.1; XM_017014401.1.
DR RefSeq; XP_016869891.1; XM_017014402.1.
DR RefSeq; XP_016869892.1; XM_017014403.1.
DR RefSeq; XP_016869893.1; XM_017014404.1. [Q92633-1]
DR RefSeq; XP_016869894.1; XM_017014405.1.
DR RefSeq; XP_016869895.1; XM_017014406.1.
DR RefSeq; XP_016869896.1; XM_017014407.1.
DR PDB; 4Z34; X-ray; 3.00 A; A=2-232, A=248-326.
DR PDB; 4Z35; X-ray; 2.90 A; A=2-232, A=248-326.
DR PDB; 4Z36; X-ray; 2.90 A; A=2-232, A=249-327.
DR PDB; 7TD0; EM; 2.83 A; R=2-340.
DR PDB; 7TD1; EM; 3.08 A; R=2-340.
DR PDB; 7TD2; EM; 3.11 A; R=2-340.
DR PDBsum; 4Z34; -.
DR PDBsum; 4Z35; -.
DR PDBsum; 4Z36; -.
DR PDBsum; 7TD0; -.
DR PDBsum; 7TD1; -.
DR PDBsum; 7TD2; -.
DR AlphaFoldDB; Q92633; -.
DR SMR; Q92633; -.
DR BioGRID; 108226; 235.
DR IntAct; Q92633; 104.
DR MINT; Q92633; -.
DR STRING; 9606.ENSP00000363553; -.
DR BindingDB; Q92633; -.
DR ChEMBL; CHEMBL3819; -.
DR GuidetoPHARMACOLOGY; 272; -.
DR SwissLipids; SLP:000001567; -.
DR GlyGen; Q92633; 2 sites.
DR iPTMnet; Q92633; -.
DR PhosphoSitePlus; Q92633; -.
DR SwissPalm; Q92633; -.
DR BioMuta; LPAR1; -.
DR DMDM; 26454626; -.
DR jPOST; Q92633; -.
DR MassIVE; Q92633; -.
DR MaxQB; Q92633; -.
DR PaxDb; Q92633; -.
DR PeptideAtlas; Q92633; -.
DR PRIDE; Q92633; -.
DR ProteomicsDB; 4425; -.
DR ProteomicsDB; 75389; -. [Q92633-1]
DR Antibodypedia; 15104; 406 antibodies from 35 providers.
DR DNASU; 1902; -.
DR Ensembl; ENST00000358883.8; ENSP00000351755.4; ENSG00000198121.15. [Q92633-1]
DR Ensembl; ENST00000374430.6; ENSP00000363552.1; ENSG00000198121.15. [Q92633-1]
DR Ensembl; ENST00000374431.7; ENSP00000363553.3; ENSG00000198121.15. [Q92633-1]
DR Ensembl; ENST00000683809.1; ENSP00000506912.1; ENSG00000198121.15. [Q92633-1]
DR GeneID; 1902; -.
DR KEGG; hsa:1902; -.
DR MANE-Select; ENST00000683809.1; ENSP00000506912.1; NM_001351411.2; NP_001338340.1.
DR UCSC; uc004bfa.4; human. [Q92633-1]
DR CTD; 1902; -.
DR DisGeNET; 1902; -.
DR GeneCards; LPAR1; -.
DR HGNC; HGNC:3166; LPAR1.
DR HPA; ENSG00000198121; Group enriched (brain, choroid plexus).
DR MIM; 602282; gene.
DR neXtProt; NX_Q92633; -.
DR OpenTargets; ENSG00000198121; -.
DR PharmGKB; PA162394187; -.
DR VEuPathDB; HostDB:ENSG00000198121; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244941; -.
DR InParanoid; Q92633; -.
DR OMA; TNCSNMA; -.
DR PhylomeDB; Q92633; -.
DR TreeFam; TF330052; -.
DR PathwayCommons; Q92633; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR SignaLink; Q92633; -.
DR SIGNOR; Q92633; -.
DR BioGRID-ORCS; 1902; 28 hits in 1065 CRISPR screens.
DR ChiTaRS; LPAR1; human.
DR GeneWiki; LPAR1; -.
DR GenomeRNAi; 1902; -.
DR Pharos; Q92633; Tchem.
DR PRO; PR:Q92633; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q92633; protein.
DR Bgee; ENSG00000198121; Expressed in medial globus pallidus and 203 other tissues.
DR ExpressionAtlas; Q92633; baseline and differential.
DR Genevisible; Q92633; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0035727; F:lysophosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:1904566; P:cellular response to 1-oleoyl-sn-glycerol 3-phosphate; IEA:Ensembl.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR CDD; cd15344; 7tmA_LPAR1_Edg2; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004065; LPA_rcpt.
DR InterPro; IPR002277; LPA_rcpt_EDG2.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01148; EDG2RECEPTOR.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endosome; G-protein coupled receptor; Glycoprotein; Lipid-binding;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="Lysophosphatidic acid receptor 1"
FT /id="PRO_0000069417"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT TRANSMEM 51..75
FT /note="Helical; Name=1"
FT TOPO_DOM 76..83
FT /note="Cytoplasmic"
FT TRANSMEM 84..107
FT /note="Helical; Name=2"
FT TOPO_DOM 108..121
FT /note="Extracellular"
FT TRANSMEM 122..144
FT /note="Helical; Name=3"
FT TOPO_DOM 145..163
FT /note="Cytoplasmic"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT TOPO_DOM 185..204
FT /note="Extracellular"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT TOPO_DOM 226..255
FT /note="Cytoplasmic"
FT TRANSMEM 256..280
FT /note="Helical; Name=6"
FT TOPO_DOM 281..294
FT /note="Extracellular"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT TOPO_DOM 316..364
FT /note="Cytoplasmic"
FT BINDING 39
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000305|PubMed:26091040"
FT BINDING 124..129
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000305|PubMed:26091040"
FT BINDING 210
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000305|PubMed:26091040"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61793"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..190
FT /evidence="ECO:0007744|PDB:4Z34, ECO:0007744|PDB:4Z35,
FT ECO:0007744|PDB:4Z36"
FT DISULFID 188..195
FT /evidence="ECO:0007744|PDB:4Z34, ECO:0007744|PDB:4Z35,
FT ECO:0007744|PDB:4Z36"
FT DISULFID 284..287
FT /evidence="ECO:0007744|PDB:4Z34, ECO:0007744|PDB:4Z35,
FT ECO:0007744|PDB:4Z36"
FT VAR_SEQ 1..15
FT /note="MAAISTSIPVISQPQ -> MLLLLIPAHSSVLENE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057046"
FT VARIANT 77
FT /note="N -> S (in dbSNP:rs11542862)"
FT /id="VAR_049414"
FT MUTAGEN 85
FT /note="Y->A: Impairs localization at the cell membrane."
FT /evidence="ECO:0000269|PubMed:25025571"
FT MUTAGEN 87
FT /note="L->A: Impairs localization at the cell membrane."
FT /evidence="ECO:0000269|PubMed:25025571"
FT MUTAGEN 325..326
FT /note="IL->AA: Impairs localization at the cell membrane."
FT /evidence="ECO:0000269|PubMed:25025571"
FT CONFLICT 340
FT /note="G -> S (in Ref. 1; AAC51139)"
FT /evidence="ECO:0000305"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 47..76
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 83..106
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 118..151
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 158..178
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 204..232
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 248..283
FT /evidence="ECO:0007829|PDB:4Z35"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:4Z35"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:4Z35"
SQ SEQUENCE 364 AA; 41109 MW; 4CA6262FD00DFE74 CRC64;
MAAISTSIPV ISQPQFTAMN EPQCFYNESI AFFYNRSGKH LATEWNTVSK LVMGLGITVC
IFIMLANLLV MVAIYVNRRF HFPIYYLMAN LAAADFFAGL AYFYLMFNTG PNTRRLTVST
WLLRQGLIDT SLTASVANLL AIAIERHITV FRMQLHTRMS NRRVVVVIVV IWTMAIVMGA
IPSVGWNCIC DIENCSNMAP LYSDSYLVFW AIFNLVTFVV MVVLYAHIFG YVRQRTMRMS
RHSSGPRRNR DTMMSLLKTV VIVLGAFIIC WTPGLVLLLL DVCCPQCDVL AYEKFFLLLA
EFNSAMNPII YSYRDKEMSA TFRQILCCQR SENPTGPTEG SDRSASSLNH TILAGVHSND
HSVV
