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

 LPAR1_SHEEP             Reviewed;         393 AA.
P46628;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
30-AUG-2017, entry version 87.
RecName: Full=Lysophosphatidic acid receptor 1;
Short=LPA receptor 1;
Short=LPA-1;
AltName: Full=Lysophosphatidic acid receptor Edg-2;
Name=LPAR1; Synonyms=EDG-2 {ECO:0000303|PubMed:8833998}, EDG2, LPA1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Pituitary pars tuberalis;
PubMed=8833998;
Masana M.I., Brown R.C., Pu H., Gurney M.E., Dubocovich M.L.;
"Cloning and characterization of a new member of the G-protein coupled
receptor EDG family.";
Recept. Channels 3:255-262(1995).
-!- 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 cortex and in pituitary pars
tuberalis. {ECO:0000269|PubMed:8833998}.
-!- 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; U18405; AAB52368.1; -; mRNA.
RefSeq; NP_001009332.1; NM_001009332.1.
UniGene; Oar.533; -.
ProteinModelPortal; P46628; -.
SMR; P46628; -.
GeneID; 443346; -.
KEGG; oas:443346; -.
CTD; 1902; -.
HOVERGEN; HBG103071; -.
KO; K04289; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0070915; F:lysophosphatidic acid receptor activity; ISS:UniProtKB.
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:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
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: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.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 393 Lysophosphatidic acid receptor 1.
/FTId=PRO_0000069420.
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 316 393 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 393 AA; 44433 MW; 356E961153C345FC CRC64;
MAAASTSSPV VSQPQFTAMN EPQCFYNESI AFFYNRSGKY LATEWNTVSK LVMGLGITVC
IFIMLANLLV MVAIYVNRRF HFPIYYLMAN LAAADFFAGL AYFYLMFNTG PNTRRLTVST
WLLRQGLIDT TVTASVANLL AIAIERHITV FRMQLHTRMS NRRVVVVIVV IWTMAIVMGA
IPSVGWNCIC DIENCSNMAP LYSDSYLVFW AIFNLVTFVV MVVLYAHIFG YVRQRTMRMS
RHSSGPRRNR DTMMSLLKTV VIVLGAFIIC WTPGLVLLLL DVCCPQCDVL AYEKFFLLLA
EFNSAMNPII YSYRDKEMSA TFRQILCCQR SENTSGPTEG SDRSASSLNH TILAGVHSND
HSVFRKETKM RGGHHLLRDE QPPPPERPGQ GRV


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