P2RY1_BOVIN
ID P2RY1_BOVIN Reviewed; 373 AA.
AC P48042;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RY1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Aortic endothelium;
RX PubMed=7626079; DOI=10.1006/bbrc.1995.2018;
RA Henderson D.J., Elliot D.G., Smith G.M., Webb T.E., Dainty I.A.;
RT "Cloning and characterisation of a bovine P2Y receptor.";
RL Biochem. Biophys. Res. Commun. 212:648-656(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus callosum;
RX PubMed=9848096; DOI=10.1006/nbdi.1998.0197;
RA Deng G., Matute C., Kumar C.K., Fogarty D.J., Miledi R.;
RT "Cloning and expression of a P2y purinoceptor from the adult bovine corpus
RT callosum.";
RL Neurobiol. Dis. 5:259-270(1998).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP
CC (PubMed:7626079). 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:7626079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7626079};
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; X87628; CAA60958.1; -; mRNA.
DR EMBL; U34041; AAC78275.1; -; mRNA.
DR PIR; JC4162; JC4162.
DR RefSeq; NP_776835.1; NM_174410.3.
DR AlphaFoldDB; P48042; -.
DR SMR; P48042; -.
DR STRING; 9913.ENSBTAP00000001919; -.
DR PaxDb; P48042; -.
DR Ensembl; ENSBTAT00000001919; ENSBTAP00000001919; ENSBTAG00000001465.
DR GeneID; 281963; -.
DR KEGG; bta:281963; -.
DR CTD; 5028; -.
DR VEuPathDB; HostDB:ENSBTAG00000001465; -.
DR VGNC; VGNC:32523; P2RY1.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P48042; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR TreeFam; TF350009; -.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Reactome; R-BTA-417957; P2Y receptors.
DR Reactome; R-BTA-418592; ADP signalling through P2Y purinoceptor 1.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000001465; Expressed in longissimus thoracis muscle and 98 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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031686; F:A1 adenosine receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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..373
FT /note="P2Y purinoceptor 1"
FT /id="PRO_0000070004"
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; 42288 MW; 9270A7175C0BDA76 CRC64;
MTEVLWPAVP NGTDTAFLAD PGSPWGNSTV TSTAAVASPF KCALTKTGFQ FYYLPAVYIL
VFIIGFLGNS VAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTDWIFG
DAMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAVY ISVLVWLIVV
VGISPILFYS GTGIRKNKTI TCYDTTSDEY LRSYFIYSMC TTVAMFCVPL VLILGCYGLI
VRALIYKDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPEMCAFND
RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEDMTLN
ILSEFKQNGD TSL
