P2RY1_MOUSE
ID P2RY1_MOUSE Reviewed; 373 AA.
AC P49650;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ADP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2ry1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=10606627; DOI=10.1172/jci8399;
RA Leon C., Hechler B., Freund M., Eckly A., Vial C., Ohlmann P., Dierich A.,
RA LeMeur M., Cazenave J.-P., Gachet C.;
RT "Defective platelet aggregation and increased resistance to thrombosis in
RT purinergic P2Y(1) receptor-null mice.";
RL J. Clin. Invest. 104:1731-1737(1999).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP.
CC In platelets, binding to ADP leads to mobilization of intracellular
CC calcium ions via activation of phospholipase C, a change in platelet
CC shape, and ultimately platelet aggregation.
CC {ECO:0000269|PubMed:10606627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47900};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
CC -!- DISRUPTION PHENOTYPE: Platelets from mutant mice are defective in ADP-
CC mediated platelet aggregation, leading to prolonged bleeding time.
CC Otherwise, mice have no visible phenotype and do not display
CC spontaneous bleeding. {ECO:0000269|PubMed:10606627}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U22829; AAA91302.1; -; mRNA.
DR EMBL; AJ245636; CAB57317.1; -; Genomic_DNA.
DR CCDS; CCDS17377.1; -.
DR RefSeq; NP_001268945.1; NM_001282016.1.
DR RefSeq; NP_032798.1; NM_008772.5.
DR AlphaFoldDB; P49650; -.
DR SMR; P49650; -.
DR STRING; 10090.ENSMUSP00000029331; -.
DR GlyGen; P49650; 4 sites.
DR iPTMnet; P49650; -.
DR PhosphoSitePlus; P49650; -.
DR PaxDb; P49650; -.
DR PRIDE; P49650; -.
DR ProteomicsDB; 294088; -.
DR Antibodypedia; 2952; 400 antibodies from 36 providers.
DR DNASU; 18441; -.
DR Ensembl; ENSMUST00000029331; ENSMUSP00000029331; ENSMUSG00000027765.
DR Ensembl; ENSMUST00000193201; ENSMUSP00000142006; ENSMUSG00000027765.
DR Ensembl; ENSMUST00000193943; ENSMUSP00000141371; ENSMUSG00000027765.
DR GeneID; 18441; -.
DR KEGG; mmu:18441; -.
DR UCSC; uc008pjj.2; mouse.
DR CTD; 5028; -.
DR MGI; MGI:105049; P2ry1.
DR VEuPathDB; HostDB:ENSMUSG00000027765; -.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P49650; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR PhylomeDB; P49650; -.
DR TreeFam; TF350009; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-417957; P2Y receptors.
DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR BioGRID-ORCS; 18441; 2 hits in 71 CRISPR screens.
DR PRO; PR:P49650; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P49650; protein.
DR Bgee; ENSMUSG00000027765; Expressed in lumbar dorsal root ganglion and 84 other tissues.
DR ExpressionAtlas; P49650; baseline and differential.
DR Genevisible; P49650; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0031686; F:A1 adenosine receptor binding; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
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:0045031; F:G protein-coupled ATP receptor activity; ISO:MGI.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISO:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0071415; P:cellular response to purine-containing compound; ISS:UniProtKB.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; ISO:MGI.
DR GO; GO:0035589; P:G protein-coupled purinergic nucleotide receptor signaling pathway; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IMP:MGI.
DR GO; GO:0051100; P:negative regulation of binding; ISO:MGI.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0043270; P:positive regulation of ion transport; IMP:MGI.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0090075; P:relaxation of muscle; IEA:InterPro.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:MGI.
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_0000070007"
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; 42213 MW; 944125E9F4560BB3 CRC64;
MTEVPWSVVP NGTDAAFLAG LGSLWGNSTV ASTAAVSSSF QCALTKTGFQ FYYLPAVYIL
VFIIGFLGNS VAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTDWIFG
DAMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAIY VSVLVWLIVV
VAISPILFYS GTGTRKNKTV TCYDTTSNDY LRSYFIYSMC TTVAMFCIPL VLILGCYGLI
VKALIYNDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPEMCDFND
RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEEMTLN
ILSEFKQNGD TSL
