P2RY1_MELGA
ID P2RY1_MELGA Reviewed; 362 AA.
AC P49652;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=6H1 orphan receptor;
DE AltName: Full=ADP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RY1;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8058061;
RA Filtz T.M., Li Q., Boyer J.L., Nicholas R.A., Harden T.K.;
RT "Expression of a cloned P2Y purinergic receptor that couples to
RT phospholipase C.";
RL Mol. Pharmacol. 46:8-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9240460; DOI=10.1006/bbrc.1997.6984;
RA Li Q., Schachter J.B., Harden T.K., Nicholas R.A.;
RT "The 6H1 orphan receptor, claimed to be the p2y5 receptor, does not mediate
RT nucleotide-promoted second messenger responses.";
RL Biochem. Biophys. Res. Commun. 236:455-460(1997).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP
CC (PubMed:8058061). In platelets, binding to ADP leads to mobilization of
CC intracellular calcium ions via activation of phospholipase C, a change
CC in platelet shape, and ultimately platelet aggregation (By similarity).
CC {ECO:0000250|UniProtKB:P49650, ECO:0000269|PubMed:8058061}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8058061};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
CC -!- TISSUE SPECIFICITY: Mainly found in blood, brain, and lung. To a lesser
CC extent in stomach, gut and skeletal muscle.
CC {ECO:0000269|PubMed:8058061}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U09842; AAA18784.1; -; mRNA.
DR EMBL; AF012103; AAB65428.1; -; mRNA.
DR RefSeq; NP_001290126.1; NM_001303197.1.
DR AlphaFoldDB; P49652; -.
DR SMR; P49652; -.
DR BindingDB; P49652; -.
DR ChEMBL; CHEMBL5720; -.
DR DrugCentral; P49652; -.
DR Ensembl; ENSMGAT00000017999; ENSMGAP00000017025; ENSMGAG00000016075.
DR GeneID; 100303708; -.
DR KEGG; mgp:100303708; -.
DR CTD; 5028; -.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P49652; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR TreeFam; TF350009; -.
DR PRO; PR:P49652; -.
DR Proteomes; UP000001645; Chromosome 11.
DR Bgee; ENSMGAG00000016075; Expressed in brain and 17 other tissues.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; ISS:UniProtKB.
DR GO; GO:0071415; P:cellular response to purine-containing compound; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0090075; P:relaxation of muscle; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000142; P2Y1_rcpt.
DR PANTHER; PTHR24231:SF2; PTHR24231:SF2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00595; P2Y1PRNOCPTR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="P2Y purinoceptor 1"
FT /id="PRO_0000070010"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 64..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 77..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 99..114
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 137..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 178..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 227..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 274..292
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 315..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 35
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 192..194
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 272..276
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 292..295
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 299
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..285
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT DISULFID 113..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 362 AA; 41180 MW; 3E128AB9EB64349C CRC64;
MTEALISAAL NGTQPELLAG GWAAGNASTK CSLTKTGFQF YYLPTVYILV FITGFLGNSV
AIWMFVFHMR PWSGISVYMF NLALADFLYV LTLPALIFYY FNKTDWIFGD VMCKLQRFIF
HVNLYGSILF LTCISVHRYT GVVHPLKSLG RLKKKNAVYV SSLVWALVVA VIAPILFYSG
TGVRRNKTIT CYDTTADEYL RSYFVYSMCT TVFMFCIPFI VILGCYGLIV KALIYKDLDN
SPLRRKSIYL VIIVLTVFAV SYLPFHVMKT LNLRARLDFQ TPQMCAFNDK VYATYQVTRG
LASLNSCVDP ILYFLAGDTF RRRLSRATRK SSRRSEPNVQ SKSEEMTLNI LTEYKQNGDT
SL
