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Lysophosphatidic acid receptor 1 (LPA receptor 1) (LPA-1) (Lysophosphatidic acid receptor Edg-2)

 LPAR1_RAT               Reviewed;         364 AA.
P61794; O88584; P56487; P70420; Q5FWS2; Q61130;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
22-NOV-2017, entry version 116.
RecName: Full=Lysophosphatidic acid receptor 1;
Short=LPA receptor 1;
Short=LPA-1;
AltName: Full=Lysophosphatidic acid receptor Edg-2;
Name=Lpar1; Synonyms=Edg2 {ECO:0000303|PubMed:9753172}, Gpcr91, Lpa1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
PubMed=9753172; DOI=10.1046/j.1460-9568.1998.00117.x;
Allard J., Barron S., Diaz J., Lubetzki C., Zalc B., Schwartz J.-C.,
Sokoloff P.;
"A rat G protein-coupled receptor selectively expressed in myelin-
forming cells.";
Eur. J. Neurosci. 10:1045-1053(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Carroll S.L., Miller M.L., Benedict-Hamilton H.M.;
"Identification and characterization of novel G-protein coupled
receptors expressed in regenerating peripheral nerve.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Receptor for lysophosphatidic acid (LPA). Plays a role
in the reorganization of the actin cytoskeleton, cell migration,
differentiation and proliferation, and thereby contributes to the
responses to tissue damage and infectious agents. Activates
downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and
G(q) families of heteromeric G proteins. Signaling inhibits
adenylyl cyclase activity and decreases cellular cAMP levels.
Signaling triggers an increase of cytoplasmic Ca(2+) levels.
Activates RALA; this leads to the activation of phospholipase C
(PLC) and the formation of inositol 1,4,5-trisphosphate. Signaling
mediates activation of down-stream MAP kinases. Contributes to the
regulation of cell shape. Promotes Rho-dependent reorganization of
the actin cytoskeleton in neuronal cells and neurite retraction.
Promotes the activation of Rho and the formation of actin stress
fibers. Promotes formation of lamellipodia at the leading edge of
migrating cells via activation of RAC1. Through its function as
lysophosphatidic acid receptor, plays a role in chemotaxis and
cell migration, including responses to injury and wounding. Plays
a role in triggering inflammation in response to bacterial
lipopolysaccharide (LPS) via its interaction with CD14. Promotes
cell proliferation in response to lysophosphatidic acid. Required
for normal skeleton development. May play a role in osteoblast
differentiation. Required for normal brain development. Required
for normal proliferation, survival and maturation of newly formed
neurons in the adult dentate gyrus. Plays a role in pain
perception and in the initiation of neuropathic pain.
{ECO:0000250|UniProtKB:P61793}.
-!- SUBUNIT: Interacts with RALA and GRK2 (By similarity). Interacts
with GNAQ and GNA13. Interacts with CD14; the interaction is
enhanced by exposure to bacterial lipopolysaccharide (LPS) (By
similarity). {ECO:0000250|UniProtKB:P61793,
ECO:0000250|UniProtKB:Q92633}.
-!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P61793}.
Cell membrane {ECO:0000250|UniProtKB:P61793}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:Q92633}. Endosome
{ECO:0000250|UniProtKB:P61793, ECO:0000250|UniProtKB:Q92633}.
Note=Prior to LPA treatment found predominantly at the cell
surface. Internalized after LPA treatment. Colocalizes with RALA
in endocytic vesicles after LPA treatment.
{ECO:0000250|UniProtKB:P61793, ECO:0000250|UniProtKB:Q92633}.
-!- TISSUE SPECIFICITY: Detected in brain corpus callosum, medulla
oblongata, cerebellum and sciatic nerve. Detected in heart.
{ECO:0000269|PubMed:9753172}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92633}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AF014418; AAB86381.1; -; mRNA.
EMBL; AF090347; AAG24469.1; -; mRNA.
EMBL; BC089227; AAH89227.1; -; mRNA.
RefSeq; NP_446388.1; NM_053936.3.
RefSeq; XP_006238257.1; XM_006238195.3.
RefSeq; XP_006238259.1; XM_006238197.3.
RefSeq; XP_006238262.1; XM_006238200.3.
RefSeq; XP_006238263.1; XM_006238201.3.
RefSeq; XP_017448614.1; XM_017593125.1.
RefSeq; XP_017448615.1; XM_017593126.1.
RefSeq; XP_017448616.1; XM_017593127.1.
RefSeq; XP_017448617.1; XM_017593128.1.
UniGene; Rn.11200; -.
ProteinModelPortal; P61794; -.
SMR; P61794; -.
STRING; 10116.ENSRNOP00000043652; -.
BindingDB; P61794; -.
ChEMBL; CHEMBL4595; -.
PhosphoSitePlus; P61794; -.
PaxDb; P61794; -.
Ensembl; ENSRNOT00000044348; ENSRNOP00000043652; ENSRNOG00000013656.
GeneID; 116744; -.
KEGG; rno:116744; -.
UCSC; RGD:620563; rat.
CTD; 1902; -.
RGD; 620563; Lpar1.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118804; -.
HOGENOM; HOG000233501; -.
HOVERGEN; HBG103071; -.
InParanoid; P61794; -.
KO; K04289; -.
OMA; CCQRQEN; -.
OrthoDB; EOG091G0DD4; -.
PhylomeDB; P61794; -.
TreeFam; TF330052; -.
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-418594; G alpha (i) signalling events.
Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
PRO; PR:P61794; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000013656; -.
Genevisible; P61794; RN.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001965; F:G-protein alpha-subunit binding; IMP:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:RGD.
GO; GO:0035727; F:lysophosphatidic acid binding; ISO:RGD.
GO; GO:0070915; F:lysophosphatidic acid receptor activity; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
GO; GO:0005543; F:phospholipid binding; IDA:RGD.
GO; GO:0000187; P:activation of MAPK activity; ISO:RGD.
GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032060; P:bleb assembly; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
GO; GO:1904566; P:cellular response to 1-oleoyl-sn-glycerol 3-phosphate; IDA:RGD.
GO; GO:0071453; P:cellular response to oxygen levels; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0022038; P:corpus callosum development; IEP:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0042552; P:myelination; IEP:RGD.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0022008; P:neurogenesis; IEP:RGD.
GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
GO; GO:0021554; P:optic nerve development; IEP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; IDA:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IMP:RGD.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
CDD; cd15344; 7tmA_LPAR1_Edg2; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR004065; LPA_rcpt.
InterPro; IPR002277; LPA_rcpt_EDG2.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01148; EDG2RECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01527; LPARECEPTOR.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 364 Lysophosphatidic acid receptor 1.
/FTId=PRO_0000069419.
TOPO_DOM 1 50 Extracellular.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 51 75 Helical; Name=1.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 76 83 Cytoplasmic.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 84 107 Helical; Name=2.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 108 121 Extracellular.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 122 144 Helical; Name=3.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 145 163 Cytoplasmic.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 164 184 Helical; Name=4.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 185 204 Extracellular.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 205 225 Helical; Name=5.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 226 255 Cytoplasmic.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 256 280 Helical; Name=6.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 281 294 Extracellular.
{ECO:0000250|UniProtKB:Q92633}.
TRANSMEM 295 315 Helical; Name=7.
{ECO:0000250|UniProtKB:Q92633}.
TOPO_DOM 316 364 Cytoplasmic.
{ECO:0000250|UniProtKB:Q92633}.
REGION 124 129 Lysophosphatidic acid binding.
{ECO:0000250|UniProtKB:Q92633}.
BINDING 39 39 Lysophosphatidic acid.
{ECO:0000250|UniProtKB:Q92633}.
BINDING 210 210 Lysophosphatidic acid.
{ECO:0000250|UniProtKB:Q92633}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000250|UniProtKB:Q92633}.
MOD_RES 351 351 Phosphothreonine.
{ECO:0000250|UniProtKB:P61793}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 24 190 {ECO:0000250|UniProtKB:Q92633}.
DISULFID 188 195 {ECO:0000250|UniProtKB:Q92633}.
DISULFID 284 287 {ECO:0000250|UniProtKB:Q92633}.
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


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