P2RY3_MELGA
ID P2RY3_MELGA Reviewed; 328 AA.
AC O93361;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=P2Y purinoceptor 3;
DE Short=P2Y3;
DE AltName: Full=Nucleoside diphosphate receptor;
GN Name=P2RY3;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9730913; DOI=10.1124/mol.54.3.541;
RA Li Q., Olesky M., Palmer R.K., Harden T.K., Nicholas R.A.;
RT "Evidence that the p2y3 receptor is the avian homologue of the mammalian
RT P2Y6 receptor.";
RL Mol. Pharmacol. 54:541-546(1998).
CC -!- FUNCTION: Receptor for extracellular UDP > ADP = UTP. The activity of
CC 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; AF069555; AAC23863.1; -; Genomic_DNA.
DR AlphaFoldDB; O93361; -.
DR SMR; O93361; -.
DR InParanoid; O93361; -.
DR Proteomes; UP000001645; Unplaced.
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:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IEA:InterPro.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
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 3: Inferred from homology;
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_0000070018"
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; 37595 MW; B74D49B99C7164A5 CRC64;
MSMANFTAGR NSCTFQEEFK QVLLPLVYSV VFLLGLPLNA VVIGQIWLAR KALTRTTIYM
LNLATADLLY VCSLPLLIYN YTQKDYWPFG DFTCKFVRFQ FYTNLHGSIL FLTCISVQRY
MGICHPLASW HKKKGKKLTW LVCAAVWFIV IAQCLPTFVF ASTGTQRNRT VCYDLSPPDR
SASYFPYGIT LTITGFLLPF AAILACYCSM ARILCQKDEL IGLAVHKKKD KAVRMIIIVV
IVFSISFFPF HLTKTIYLIV RSSPTLPCPT LQAFAIAYKC TRPFASMNSV LDPILFYFTQ
RKFRESTRYL LDKMSSKWRH DHCITYGS