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LPAR1_RAT
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   03-AUG-2022, entry version 138.
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 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 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   GlyGen; P61794; 2 sites.
DR   PhosphoSitePlus; P61794; -.
DR   PaxDb; P61794; -.
DR   PRIDE; P61794; -.
DR   Ensembl; ENSRNOT00000044348; ENSRNOP00000043652; ENSRNOG00000013656.
DR   GeneID; 116744; -.
DR   KEGG; rno:116744; -.
DR   UCSC; RGD:620563; rat.
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; TNCSNMA; -.
DR   OrthoDB; 989859at2759; -.
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 tissues.
DR   Genevisible; P61794; RN.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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; IDA: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:0007420; P:brain development; IEP: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: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:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:RGD.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:RGD.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO: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   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   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
 
 
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