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LPAR6_CHICK
ID   LPAR6_CHICK             Reviewed;         308 AA.
AC   P32250;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Lysophosphatidic acid receptor 6;
DE            Short=LPA receptor 6;
DE            Short=LPA-6;
DE   AltName: Full=Oleoyl-L-alpha-lysophosphatidic acid receptor;
DE   AltName: Full=P2Y purinoceptor 5;
DE            Short=P2Y5;
DE   AltName: Full=Purinergic receptor 5;
GN   Name=LPAR6; Synonyms=P2RY5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   PubMed=8393036;
RA   Kaplan M.H., Smith D.I., Sundick R.S.;
RT   "Identification of a G protein coupled receptor induced in activated T
RT   cells.";
RL   J. Immunol. 151:628-636(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8619790; DOI=10.1006/bbrc.1996.0189;
RA   Webb T.E., Kaplan M.G., Barnard E.A.;
RT   "Identification of 6H1 as a P2Y purinoceptor: P2Y5.";
RL   Biochem. Biophys. Res. Commun. 219:105-110(1996).
CC   -!- FUNCTION: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA).
CC       Intracellular cAMP is involved in the receptor activation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Induced in activated T-cells.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L06109; AAB06587.1; -; mRNA.
DR   PIR; I50241; I50241.
DR   AlphaFoldDB; P32250; -.
DR   SMR; P32250; -.
DR   VEuPathDB; HostDB:geneid_396118; -.
DR   InParanoid; P32250; -.
DR   PhylomeDB; P32250; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0070915; F:lysophosphatidic acid receptor activity; IBA:GO_Central.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..308
FT                   /note="Lysophosphatidic acid receptor 6"
FT                   /id="PRO_0000070027"
FT   TOPO_DOM        1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..109
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..206
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..250
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..289
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..308
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           281
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        86..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   308 AA;  35597 MW;  4214E969633B6F7D CRC64;
     MVSSNCSTED SFKYTLYGCV FSMVFVLGLI ANCVAIYIFT FTLKVRNETT TYMLNLAISD
     LLFVFTLPFR IYYFVVRNWP FGDVLCKISV TLFYTNMYGS ILFLTCISVD RFLAIVHPFR
     SKTLRTKRNA RIVCVAVWIT VLAGSTPASF FQSTNRQNNT EQRTCFENFP ESTWKTYLSR
     IVIFIEIVGF FIPLILNVTC STMVLRTLNK PLTLSRNKLS KKKVLKMIFV HLVIFCFCFV
     PYNITLILYS LMRTQTWINC SVVTAVRTMY PVTLCIAVSN CCFDPIVYYF TSDTNSELDK
     KQQVHQNT
 
 
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