LPAR1_SHEEP
ID LPAR1_SHEEP Reviewed; 393 AA.
AC P46628;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=EDG-2 {ECO:0000303|PubMed:8833998}, EDG2, LPA1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary pars tuberalis;
RX PubMed=8833998;
RA Masana M.I., Brown R.C., Pu H., Gurney M.E., Dubocovich M.L.;
RT "Cloning and characterization of a new member of the G-protein coupled
RT receptor EDG family.";
RL Recept. Channels 3:255-262(1995).
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 lysophosphatidic acid receptor, plays a role in chemotaxis
CC and cell migration, including responses to injury and wounding. Plays a
CC role in triggering inflammation in response to bacterial
CC lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell
CC proliferation in response to lysophosphatidic acid. Required for normal
CC skeleton development. May play a role in osteoblast differentiation.
CC Required for normal brain development. Required for normal
CC proliferation, survival and maturation of newly formed neurons in the
CC adult dentate gyrus. Plays a role in pain perception and in the
CC initiation of neuropathic pain. {ECO:0000250|UniProtKB:P61793}.
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 cortex and in pituitary pars
CC tuberalis. {ECO:0000269|PubMed:8833998}.
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}.
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; U18405; AAB52368.1; -; mRNA.
DR RefSeq; NP_001009332.1; NM_001009332.1.
DR AlphaFoldDB; P46628; -.
DR SMR; P46628; -.
DR STRING; 9940.ENSOARP00000007239; -.
DR GeneID; 443346; -.
DR KEGG; oas:443346; -.
DR CTD; 1902; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 989859at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; ISS:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS: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:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
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 2: Evidence at transcript 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..393
FT /note="Lysophosphatidic acid receptor 1"
FT /id="PRO_0000069420"
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..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT REGION 369..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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
