P2RY1_CHICK
ID P2RY1_CHICK Reviewed; 362 AA.
AC P34996;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ATP receptor {ECO:0000303|PubMed:8508924};
DE AltName: Full=Purinergic receptor;
GN Name=P2RY1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=8508924; DOI=10.1016/0014-5793(93)81397-i;
RA Webb T.E., Simon J., Krishek B.J., Bateson A.N., Smart T.G., King B.F.,
RA Burnstock G., Barnard E.A.;
RT "Cloning and functional expression of a brain G-protein-coupled ATP
RT receptor.";
RL FEBS Lett. 324:219-225(1993).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=8872457;
RA van Rhee A.M., Fischer B., van Galen P.J.M., Jacobson K.A.;
RT "Modelling the P2Y purinoceptor using rhodopsin as template.";
RL Drug Des. Discov. 13:133-154(1995).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP
CC (PubMed:8508924). 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:8508924}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8508924};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
CC -!- TISSUE SPECIFICITY: Brain, spinal cord, gastrointestinal tract, spleen
CC and leg muscle. Is not detected in the heart, liver, stomach, lung and
CC kidney.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X73268; CAA51716.1; -; mRNA.
DR PIR; S33733; S33733.
DR RefSeq; NP_990664.1; NM_205333.1.
DR AlphaFoldDB; P34996; -.
DR SMR; P34996; -.
DR STRING; 9031.ENSGALP00000016845; -.
DR PaxDb; P34996; -.
DR Ensembl; ENSGALT00000016864; ENSGALP00000016845; ENSGALG00000010357.
DR GeneID; 396275; -.
DR KEGG; gga:396275; -.
DR CTD; 5028; -.
DR VEuPathDB; HostDB:geneid_396275; -.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P34996; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR PhylomeDB; P34996; -.
DR Reactome; R-GGA-416476; G alpha (q) signalling events.
DR Reactome; R-GGA-417957; P2Y receptors.
DR Reactome; R-GGA-418592; ADP signalling through P2Y purinoceptor 1.
DR PRO; PR:P34996; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000010357; Expressed in skeletal muscle tissue and 10 other tissues.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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: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_0000070009"
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; 41194 MW; A806C88FB9514761 CRC64;
MTEALISAAL NGTQPELLAG GWAAGNATTK 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
