ID LPAR1_RAT Reviewed; 364 AA.
AC P61794; O88584; P56487; P70420; Q5FWS2; Q61130;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Lysophosphatidic acid receptor 1;
DE Short=LPA receptor 1;
DE Short=LPA-1;
DE AltName: Full=Lysophosphatidic acid receptor Edg-2;
GN Name=Lpar1; Synonyms=Edg2 {ECO:0000303|PubMed:9753172}, Gpcr91, Lpa1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=9753172; DOI=10.1046/j.1460-9568.1998.00117.x;
RA Allard J., Barron S., Diaz J., Lubetzki C., Zalc B., Schwartz J.-C.,
RA Sokoloff P.;
RT "A rat G protein-coupled receptor selectively expressed in myelin-forming
RT cells.";
RL Eur. J. Neurosci. 10:1045-1053(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Carroll S.L., Miller M.L., Benedict-Hamilton H.M.;
RT "Identification and characterization of novel G-protein coupled receptors
RT expressed in regenerating peripheral nerve.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA). 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. Signaling triggers an increase of
CC cytoplasmic Ca(2+) levels. Activates RALA; this leads to the activation
CC of phospholipase C (PLC) and the formation of inositol 1,4,5-
CC trisphosphate. Signaling mediates activation of down-stream MAP
CC kinases. Contributes to the regulation of cell shape. Promotes Rho-
CC dependent reorganization of the actin cytoskeleton in neuronal cells
CC and neurite retraction. Promotes the activation of Rho and the
CC formation of actin stress fibers. Promotes formation of lamellipodia at
CC the leading edge of migrating cells via activation of RAC1. Through its
CC function as LPA receptor, plays a role in chemotaxis and cell
CC migration, including responses to injury and wounding. Plays a role in
CC triggering inflammation in response to bacterial lipopolysaccharide
CC (LPS) via its interaction with CD14. Promotes cell proliferation in
CC response to LPA. Inhibits the intracellular ciliogenesis pathway in
CC response to LPA and through AKT1 activation (By similarity). Required
CC 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. {ECO:0000250|UniProtKB:P61793,
CC ECO:0000250|UniProtKB:Q92633}.
CC -!- SUBUNIT: Interacts with RALA and GRK2 (By similarity). 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:0000250|UniProtKB:Q92633}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P61793}. Cell
CC membrane {ECO:0000250|UniProtKB:P61793}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q92633}. Endosome {ECO:0000250|UniProtKB:P61793,
CC ECO:0000250|UniProtKB:Q92633}. Note=Prior to LPA treatment found
CC predominantly at the cell surface. Internalized after LPA treatment.
CC Colocalizes with RALA in endocytic vesicles after LPA treatment.
CC {ECO:0000250|UniProtKB:P61793, ECO:0000250|UniProtKB:Q92633}.
CC -!- TISSUE SPECIFICITY: Detected in brain corpus callosum, medulla
CC oblongata, cerebellum and sciatic nerve. Detected in heart.
CC {ECO:0000269|PubMed:9753172}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92633}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF014418; AAB86381.1; -; mRNA.
DR EMBL; AF090347; AAG24469.1; -; mRNA.
DR EMBL; BC089227; AAH89227.1; -; mRNA.
DR RefSeq; NP_446388.1; NM_053936.3.
DR RefSeq; XP_006238257.1; XM_006238195.3.
DR RefSeq; XP_006238259.1; XM_006238197.3.
DR RefSeq; XP_006238262.1; XM_006238200.3.
DR RefSeq; XP_006238263.1; XM_006238201.3.
DR RefSeq; XP_017448614.1; XM_017593125.1.
DR RefSeq; XP_017448615.1; XM_017593126.1.
DR RefSeq; XP_017448616.1; XM_017593127.1.
DR RefSeq; XP_017448617.1; XM_017593128.1.
DR AlphaFoldDB; P61794; -.
DR SMR; P61794; -.
DR STRING; 10116.ENSRNOP00000043652; -.
DR BindingDB; P61794; -.
DR ChEMBL; CHEMBL4595; -.
DR GlyCosmos; P61794; 2 sites, No reported glycans.
DR GlyGen; P61794; 2 sites.
DR PhosphoSitePlus; P61794; -.
DR SwissPalm; P61794; -.
DR PaxDb; 10116-ENSRNOP00000043652; -.
DR Ensembl; ENSRNOT00000044348.3; ENSRNOP00000043652.2; ENSRNOG00000013656.7.
DR Ensembl; ENSRNOT00055030839; ENSRNOP00055024825; ENSRNOG00055018195.
DR Ensembl; ENSRNOT00060018646; ENSRNOP00060014518; ENSRNOG00060011025.
DR Ensembl; ENSRNOT00065026842; ENSRNOP00065021086; ENSRNOG00065016138.
DR GeneID; 116744; -.
DR KEGG; rno:116744; -.
DR UCSC; RGD:620563; rat.
DR AGR; RGD:620563; -.
DR CTD; 1902; -.
DR RGD; 620563; Lpar1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244941; -.
DR HOGENOM; CLU_047979_0_0_1; -.
DR InParanoid; P61794; -.
DR OMA; CQRSENA; -.
DR OrthoDB; 5349764at2759; -.
DR PhylomeDB; P61794; -.
DR TreeFam; TF330052; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:P61794; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013656; Expressed in Ammon's horn and 19 other cell types or tissues.
DR Genevisible; P61794; RN.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IMP:RGD.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISO:RGD.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IMP:RGD.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS: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; ISO:RGD.
DR GO; GO:0099004; P:calmodulin dependent kinase signaling pathway; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:1904566; P:cellular response to 1-oleoyl-sn-glycerol 3-phosphate; IDA:RGD.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEP:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0022038; P:corpus callosum development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0042552; P:myelination; IEP:RGD.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:RGD.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0022008; P:neurogenesis; IEP:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0021554; P:optic nerve development; IEP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:RGD.
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; IMP:RGD.
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 GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR CDD; cd15344; 7tmA_LPAR1_Edg2; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004065; LPA_rcpt.
DR InterPro; IPR002277; LPA_rcpt_EDG2.
DR PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR22750:SF22; LYSOPHOSPHATIDIC ACID RECEPTOR 1; 1.
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 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.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="Lysophosphatidic acid receptor 1"
FT /id="PRO_0000069419"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 51..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 76..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 84..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 108..121
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 122..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 145..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 185..204
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 226..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 256..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 281..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 316..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 39
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 124..129
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 210
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
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:0000250|UniProtKB:Q92633"
FT DISULFID 188..195
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT DISULFID 284..287
FT /evidence="ECO:0000250|UniProtKB:Q92633"
SQ SEQUENCE 364 AA; 41119 MW; B0FA6265AA6688B7 CRC64;
MAAASTSSPV ISQPQFTAMN EQQCFYNESI AFFYNRSGKY LATEWNTVSK LVMGLGITVC
VFIMLANLLV MVAIYVNRRF HFPIYYLMAN LAAADFFAGL AYFYLMFNTG PNTRRLTVST
WLLRQGLIDT SLTASVANLL AIAIERHITV FRMQLHTRMS NRRVVVVIVV IWTMAIVMGA
IPSVGWNCIC DIDHCSNMAP LYSDSYLVFW AIFNLVTFVV MVVLYAHIFG YVRQRTMRMS
RHSSGPRRNR DTMMSLLKTV VIVLGAFIVC WTPGLVLLLL DVCCPQCDVL AYEKFFLLLA
EFNSAMNPII YSYRDKEMSA TFRQILCCQR NENPNGPTEG SDRSASSLNH TILAGVHSND
HSVV
//
