P2RY1_CAVPO
ID P2RY1_CAVPO Reviewed; 373 AA.
AC P59902;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RY1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Small intestine;
RA Gao N., Hu H., Zhu M.X., Wood J.D.;
RT "A novel P2Y1 receptor in the guinea pig submucous plexus.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P49650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47900};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY048684; AAL05953.1; -; mRNA.
DR RefSeq; NP_001166465.1; NM_001172994.1.
DR RefSeq; XP_005006594.1; XM_005006537.2.
DR AlphaFoldDB; P59902; -.
DR SMR; P59902; -.
DR STRING; 10141.ENSCPOP00000014399; -.
DR Ensembl; ENSCPOT00000015697; ENSCPOP00000014399; ENSCPOG00000015545.
DR GeneID; 100135592; -.
DR KEGG; cpoc:100135592; -.
DR CTD; 5028; -.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P59902; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR TreeFam; TF350009; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000015545; Expressed in heart and 12 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:0045031; F:G protein-coupled ATP receptor activity; IMP:BHF-UCL.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IMP:BHF-UCL.
DR GO; GO:0071318; P:cellular response to ATP; IMP:BHF-UCL.
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:0023041; P:neuronal signal transduction; IMP:BHF-UCL.
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; IMP:BHF-UCL.
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_0000070005"
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; 42301 MW; 2BD66543FFE3F341 CRC64;
MTEVLWPAAP NGTDAAFLAS PGFHWGNSTA TSTAAAAAPF RCALTKTGFQ FYYLPAVYIV
VFIIGFLGNS IAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTNWIFG
DAMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAVY ISVLVWLIVV
VAISPILFYS GTGIRKNKTI TCYDTTSDEY LRSYFIYSMC TTVAMFCVPL VLILGCYGLI
VRALIYKDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPEMCTFND
RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEDMTLN
ILSEFKQNGD TSL
