LPA11_XENLA
ID LPA11_XENLA Reviewed; 366 AA.
AC Q9PU17; Q5D097;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Lysophosphatidic acid receptor 1-A;
DE Short=LPA receptor 1-A;
DE Short=LPA-1-A {ECO:0000303|PubMed:11278944};
DE AltName: Full=Lysophosphatidic acid receptor LPA1 homolog 1;
DE Short=xLPA1-1;
GN Name=lpar1-a; Synonyms=lpa1r, lpa1r1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11278944; DOI=10.1074/jbc.m011588200;
RA Kimura Y., Schmitt A., Fukushima N., Ishii I., Kimura H., Nebreda A.R.,
RA Chun J.;
RT "Two novel Xenopus homologs of mammalian LPA1/EDG-2 function as
RT lysophosphatidic acid receptors in Xenopus oocytes and mammalian cells.";
RL J. Biol. Chem. 276:15208-15215(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA)(PubMed:11278944).
CC Plays a role in the reorganization of the actin cytoskeleton, cell
CC migration, differentiation and proliferation, and thereby contributes
CC to the responses to tissue damage and infectious agents. Activates
CC downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q)
CC families of heteromeric G proteins. Signaling inhibits adenylyl cyclase
CC activity and decreases cellular cAMP levels (PubMed:11278944).
CC Signaling triggers an increase of cytoplasmic Ca(2+) levels. Signaling
CC leads to the activation of phospholipase C (PLC) and the formation of
CC inositol 1,4,5-trisphosphate. Signaling mediates activation of down-
CC stream MAP kinases (By similarity). Contributes to the regulation of
CC cell shape (PubMed:11278944). Promotes Rho-dependent reorganization of
CC the actin cytoskeleton in neuronal cells and neurite retraction.
CC Promotes the activation of Rho and the formation of actin stress
CC fibers. Promotes formation of lamellipodia at the leading edge of
CC migrating cells via activation of Rac. Through its function as
CC lysophosphatidic acid receptor, plays a role in chemotaxis and cell
CC migration, including responses to injury and wounding. Promotes cell
CC proliferation in response to lysophosphatidic acid (By similarity).
CC {ECO:0000250|UniProtKB:P61793, ECO:0000269|PubMed:11278944}.
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
CC {ECO:0000250|UniProtKB:Q92633}. Note=Prior to LPA treatment found
CC predominantly at the cell surface. Internalized after LPA treatment.
CC {ECO:0000250|UniProtKB:Q92633}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in oocytes and at lower
CC levels in brain and spinal cord. Below detection level in lung, heart,
CC kidney, liver, muscle, stomach, and intestine.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ249843; CAB62282.1; -; mRNA.
DR EMBL; BC049389; AAH49389.1; -; mRNA.
DR RefSeq; XP_018099224.1; XM_018243735.1.
DR RefSeq; XP_018099225.1; XM_018243736.1.
DR AlphaFoldDB; Q9PU17; -.
DR SMR; Q9PU17; -.
DR DNASU; 379403; -.
DR GeneID; 379403; -.
DR KEGG; xla:379403; -.
DR CTD; 379403; -.
DR Xenbase; XB-GENE-6255824; lpar1.S.
DR OMA; CITANCT; -.
DR OrthoDB; 989859at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 379403; Expressed in blastula and 19 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..366
FT /note="Lysophosphatidic acid receptor 1-A"
FT /id="PRO_0000069704"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 53..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 78..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 86..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 110..123
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 124..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 147..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 187..206
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 207..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 228..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 258..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 283..296
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TRANSMEM 297..317
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT TOPO_DOM 318..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 41
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 126..131
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT BINDING 212
FT /ligand="a 1-acyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57970"
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..192
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT DISULFID 190..197
FT /evidence="ECO:0000250|UniProtKB:Q92633"
FT DISULFID 286..289
FT /evidence="ECO:0000250|UniProtKB:Q92633"
SQ SEQUENCE 366 AA; 41364 MW; 2F5661B0D13DCAEE CRC64;
MASLSEFVSE PISMMSQTSA ASESQCYYNE TIAFFYNRSG KYLATEWNAV SKLVMGLGIT
VCIFIMLANL LVMVAIYVNR RFHFPIYYLM ANLAAADFFA GLAYFYLMFN TGPNTRRLTV
STWLLRQGLI DTSLTASVAN LLAIAIERHI TVFRMQLHTR MSNRRVVVVI VVIWTVAIVM
GAIPSVGWNC ICDLEQCSNM APLYSDSYLI FWTIFNLVTF VVMVVLYAHI FVYVRQKTMR
MSRHSSGPRR NRDTMMSLLK TVVIVLGAFI VCWTPGLVLL LLDICCPQCN ILAYEKFFLL
LAEFNSAMNP IIYSYRDKEM SATFKQILCC QRTENVNGPT EGSDRSASSL NHTILAGVHS
NDHSVV
