P2RY1_RAT
ID P2RY1_RAT Reviewed; 373 AA.
AC P49651;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2ry1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Insulinoma;
RX PubMed=7779087; DOI=10.1006/bbrc.1995.1798;
RA Tokuyama Y., Hara M., Jones E.M.C., Fan Z., Bell G.I.;
RT "Cloning of rat and mouse P2Y purinoceptors.";
RL Biochem. Biophys. Res. Commun. 211:211-218(1995).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP
CC (PubMed:7779087). 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:7779087}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7779087};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle, heart, liver, kidney, lung,
CC brain, spleen, but not in testis.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U22830; AAA91303.1; -; mRNA.
DR RefSeq; NP_036932.1; NM_012800.1.
DR AlphaFoldDB; P49651; -.
DR SMR; P49651; -.
DR BioGRID; 247305; 2.
DR MINT; P49651; -.
DR STRING; 10116.ENSRNOP00000019304; -.
DR BindingDB; P49651; -.
DR ChEMBL; CHEMBL2497; -.
DR GuidetoPHARMACOLOGY; 323; -.
DR GlyGen; P49651; 4 sites.
DR PhosphoSitePlus; P49651; -.
DR PaxDb; P49651; -.
DR PRIDE; P49651; -.
DR Ensembl; ENSRNOT00000019305; ENSRNOP00000019304; ENSRNOG00000014232.
DR GeneID; 25265; -.
DR KEGG; rno:25265; -.
DR UCSC; RGD:3242; rat.
DR CTD; 5028; -.
DR RGD; 3242; P2ry1.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P49651; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR PhylomeDB; P49651; -.
DR TreeFam; TF350009; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-417957; P2Y receptors.
DR Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
DR PRO; PR:P49651; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014232; Expressed in quadriceps femoris and 18 other tissues.
DR Genevisible; P49651; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0044297; C:cell body; IDA:BHF-UCL.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0031686; F:A1 adenosine receptor binding; IPI:BHF-UCL.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IDA:BHF-UCL.
DR GO; GO:0045031; F:G protein-coupled ATP receptor activity; IDA:BHF-UCL.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0071415; P:cellular response to purine-containing compound; ISS:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035589; P:G protein-coupled purinergic nucleotide receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0008347; P:glial cell migration; IMP:RGD.
DR GO; GO:0006811; P:ion transport; IEA:Ensembl.
DR GO; GO:0051100; P:negative regulation of binding; IDA:BHF-UCL.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IDA:RGD.
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:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; TAS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IDA:RGD.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0043270; P:positive regulation of ion transport; ISO:RGD.
DR GO; GO:0060406; P:positive regulation of penile erection; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0090075; P:relaxation of muscle; IEA:InterPro.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IDA:RGD.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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..373
FT /note="P2Y purinoceptor 1"
FT /id="PRO_0000070008"
FT TOPO_DOM 1..51
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 110..125
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 148..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 167..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 189..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 238..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 285..303
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT TOPO_DOM 326..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 46
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 203..205
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 283..287
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 303..306
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT BINDING 310
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 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..296
FT /evidence="ECO:0000250|UniProtKB:P47900"
FT DISULFID 124..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 373 AA; 42322 MW; 6DDF676287B5E648 CRC64;
MTEVPWSAVP NGTDAAFLAG LGSLWGNSTI ASTAAVSSSF RCALIKTGFQ FYYLPAVYIL
VFIIGFLGNS VAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTDWIFG
DVMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAIY VSVLVWLIVV
VAISPILFYS GTGIRKNKTV TCYDSTSDEY LRSYFIYSMC TTVAMFCIPL VLILGCYGLI
VRALIYKDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPEMCDFND
RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEEMTLN
ILSEFKQNGD TSL
