LPAR3_MOUSE
ID LPAR3_MOUSE Reviewed; 354 AA.
AC Q9EQ31;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lysophosphatidic acid receptor 3;
DE Short=LPA receptor 3;
DE Short=LPA-3;
DE AltName: Full=Lysophosphatidic acid receptor Edg-7;
GN Name=Lpar3; Synonyms=Edg7, Lpa3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and Swiss Webster / NIH;
RX PubMed=11313151; DOI=10.1016/s0378-1119(01)00410-3;
RA Contos J.J.A., Chun J.;
RT "The mouse lp(A3)/Edg7 lysophosphatidic acid receptor gene: genomic
RT structure, chromosomal localization, and expression pattern.";
RL Gene 267:243-253(2001).
RN [2]
RP ERRATUM OF PUBMED:11313151.
RA Contos J.J.A., Chun J.;
RL Gene 272:345-345(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of
CC diverse cellular activities. Seems to be coupled to the G(i)/G(o) and
CC G(q) families of heteromeric G proteins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in testes, kidney, and
CC lung, with moderate levels in small intestine, and low levels in heart,
CC stomach, spleen, and adult and perinatal brain. Little or no expression
CC in embryonic brain, liver, or thymus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF293845; AAG13674.1; -; mRNA.
DR EMBL; AF272365; AAK02017.1; -; Genomic_DNA.
DR EMBL; AF272364; AAK02017.1; JOINED; Genomic_DNA.
DR CCDS; CCDS17901.1; -.
DR RefSeq; NP_075359.1; NM_022983.4.
DR AlphaFoldDB; Q9EQ31; -.
DR SMR; Q9EQ31; -.
DR STRING; 10090.ENSMUSP00000037712; -.
DR GuidetoPHARMACOLOGY; 274; -.
DR GlyGen; Q9EQ31; 2 sites.
DR iPTMnet; Q9EQ31; -.
DR PhosphoSitePlus; Q9EQ31; -.
DR PaxDb; Q9EQ31; -.
DR PRIDE; Q9EQ31; -.
DR ProteomicsDB; 291961; -.
DR Antibodypedia; 2955; 339 antibodies from 35 providers.
DR DNASU; 65086; -.
DR Ensembl; ENSMUST00000039164; ENSMUSP00000037712; ENSMUSG00000036832.
DR GeneID; 65086; -.
DR KEGG; mmu:65086; -.
DR UCSC; uc008rra.2; mouse.
DR CTD; 23566; -.
DR MGI; MGI:1929469; Lpar3.
DR VEuPathDB; HostDB:ENSMUSG00000036832; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244941; -.
DR HOGENOM; CLU_047979_0_0_1; -.
DR InParanoid; Q9EQ31; -.
DR OMA; MKRMICC; -.
DR OrthoDB; 854783at2759; -.
DR PhylomeDB; Q9EQ31; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 65086; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9EQ31; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9EQ31; protein.
DR Bgee; ENSMUSG00000036832; Expressed in lumbar dorsal root ganglion and 114 other tissues.
DR ExpressionAtlas; Q9EQ31; baseline and differential.
DR Genevisible; Q9EQ31; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0032060; P:bleb assembly; IGI:MGI.
DR GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004065; LPA_rcpt.
DR InterPro; IPR005385; LPA_rcpt_EDG7.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01560; EDG7RECEPTOR.
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; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="Lysophosphatidic acid receptor 3"
FT /id="PRO_0000069434"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 315..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 309
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 40316 MW; 8B6F9A3CA9C1F062 CRC64;
MNECHYDKRM DFFYNRSNTD TADEWTGTKL VIVLCVGTFF CLFIFFSNSL VIAAVITNRK
FHFPFYYLLA NLAAADFFAG IAYVFLMFNT GPVSKTLTVN RWFLRQGLLD TSLTASLANL
LVIAVERHMS IMRMRVHSNL TKKRVTLLIL LVWAIAIFMG AVPTLGWNCL CNISACSSLA
PIYSRSYLIF WTVSNLLAFF IMVAVYVRIY MYVKRKTNVL SPHTSGSISR RRAPMKLMKT
VMTVLGAFVV CWTPGLVVLL LDGLNCKQCN VQHVKRWFLL LALLNSVMNP IIYSYKDEDM
YNTMRKMICC ALQDSNTERR PSRNPSTIHS RSETGSQYLE DSISQGPVCN KNGS
