LPAR2_MACFA
ID LPAR2_MACFA Reviewed; 348 AA.
AC Q95KH4;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Lysophosphatidic acid receptor 2 {ECO:0000250|UniProtKB:Q9HBW0};
DE Short=LPA receptor 2;
DE Short=LPA-2;
DE AltName: Full=Lysophosphatidic acid receptor Edg-4;
GN Name=LPAR2 {ECO:0000250|UniProtKB:Q9HBW0}; Synonyms=EDG4, LPA2;
GN ORFNames=QtrA-12246;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of
CC diverse cellular activities. Seems to be coupled to the G(i)/G(o),
CC G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key
CC role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates
CC phospholipase C (PLC) activity in a manner that is independent of RALA
CC activation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLC9A3R2/NHERF2, MAGI3 and PLCB3. Interacts
CC with RALA and GRK2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Prior to
CC LPA treatment found predominantly at the cell surface but in the
CC presence of LPA colocalizes with RALA in the endocytic vesicles.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB46883.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB060872; BAB46883.1; ALT_INIT; mRNA.
DR RefSeq; NP_001306445.1; NM_001319516.1.
DR AlphaFoldDB; Q95KH4; -.
DR STRING; 9541.XP_005588612.1; -.
DR GeneID; 102120852; -.
DR CTD; 9170; -.
DR eggNOG; KOG3656; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004065; LPA_rcpt.
DR InterPro; IPR004066; LPA_rcpt_EDG4.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01528; EDG4RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01527; LPARECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..348
FT /note="Lysophosphatidic acid receptor 2"
FT /id="PRO_0000069425"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 345..348
FT /note="PDZ-binding"
FT LIPID 308
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 38768 MW; 656E400D7358141E CRC64;
MGHCYYNETI GFFYNNSGKE LSSHWRPKDV VVVALGLTVS VLVLLTNLLV IAAIASNRRF
HQPIYYLLGN LAAADLFAGV AYLFLMFHTG PRTARLSLEG WFLRQGLLDT SLTASVATLL
AIAVERRRSV MAVQLHSRLP RGRVVMLIVG VWVAALGLGL LPAHSWHCLC ALDRCSRMAP
LLSRSYLAVW ALSSLLVFLL MVAVYTRIFF YVRRRVQRMA EHVSCHPRYR ETTLSLVKTV
VIILGAFVVC WTPGQVVLLL DGLGCKSCNV LAVEKYFLLL AEANSLVNAA VYSCRDAEMR
RTFRRLLCCA CLRRSTRESA HYTSSAQGGA STRIMLPENG HPLMDSTL
