P2RY3_CHICK
ID P2RY3_CHICK Reviewed; 328 AA.
AC Q98907;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=P2Y purinoceptor 3;
DE Short=P2Y3;
DE AltName: Full=Nucleoside diphosphate receptor;
GN Name=P2RY3;
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=Brain;
RX PubMed=8700132;
RA Webb T.E., Henderson D., King B.F., Wang S., Simon J., Bateson A.N.,
RA Burnstock G., Barnard E.A.;
RT "A novel G protein-coupled P2 purinoceptor (P2Y3) activated preferentially
RT by nucleoside diphosphates.";
RL Mol. Pharmacol. 50:258-265(1996).
CC -!- FUNCTION: Receptor for extracellular ADP > UTP > ATP = UDP. The
CC activity of this receptor is mediated by G proteins which activate a
CC phosphatidylinositol-calcium second messenger system.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X98283; CAA66930.1; -; mRNA.
DR RefSeq; NP_990526.1; NM_205195.1.
DR AlphaFoldDB; Q98907; -.
DR SMR; Q98907; -.
DR STRING; 9031.ENSGALP00000027948; -.
DR PaxDb; Q98907; -.
DR Ensembl; ENSGALT00000028001; ENSGALP00000027948; ENSGALG00000017327.
DR Ensembl; ENSGALT00000100424; ENSGALP00000070498; ENSGALG00000017327.
DR GeneID; 396114; -.
DR KEGG; gga:396114; -.
DR CTD; 5031; -.
DR VEuPathDB; HostDB:geneid_396114; -.
DR eggNOG; ENOG502QRYJ; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q98907; -.
DR OMA; KWRHDHC; -.
DR OrthoDB; 925903at2759; -.
DR PhylomeDB; Q98907; -.
DR TreeFam; TF330775; -.
DR Reactome; R-GGA-416476; G alpha (q) signalling events.
DR Reactome; R-GGA-417957; P2Y receptors.
DR PRO; PR:Q98907; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017327; Expressed in spleen and 11 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IBA:GO_Central.
DR GO; GO:0045029; F:G protein-coupled UDP receptor activity; IBA:GO_Central.
DR GO; GO:0045030; F:G protein-coupled UTP receptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR GO; GO:0071415; P:cellular response to purine-containing compound; IEA:Ensembl.
DR GO; GO:1905835; P:cellular response to pyrimidine ribonucleotide; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030321; P:transepithelial chloride transport; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000371; P2Y3_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01065; P2Y3PRNOCPTR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..328
FT /note="P2Y purinoceptor 3"
FT /id="PRO_0000070017"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 328 AA; 37587 MW; 7A3BF1C91F54FAAB CRC64;
MSMANFTGGR NSCTFHEEFK QVLLPLVYSV VFLLGLPLNA VVIGQIWLAR KALTRTTIYM
LNLAMADLLY VCSLPLLIYN YTQKDYWPFG DFTCKFVRFQ FYTNLHGSIL FLTCISVQRY
MGICHPLASW HKKKGKKLTW LVCAAVWFIV IAQCLPTFVF ASTGTQRNRT VCYDLSPPDR
STSYFPYGIT LTITGFLLPF AAILACYCSM ARILCQKDEL IGLAVHKKKD KAVRMIIIVV
IVFSISFFPF HLTKTIYLIV RSSASLPCPT LQAFAIAYKC TRPFASMNSV LDPILFYFTQ
RKFRESTRYL LDKMSSKWRQ DHCISYGS
