P2Y12_RAT
ID P2Y12_RAT Reviewed; 343 AA.
AC Q9EPX4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=P2Y purinoceptor 12;
DE Short=P2Y12;
DE AltName: Full=P2Y12 platelet ADP receptor;
GN Name=P2ry12; Synonyms=P2y12;
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 STRAIN=Sprague-Dawley;
RX PubMed=11196645; DOI=10.1038/35051599;
RA Hollopeter G., Jantzen H.-M., Vincent D., Li G., England L.,
RA Ramakrishnan V., Yang R.-B., Nurden P., Nurden A., Julius D.J.,
RA Conley P.B.;
RT "Identification of the platelet ADP receptor targeted by antithrombotic
RT drugs.";
RL Nature 409:202-207(2001).
RN [2]
RP PROTEIN SEQUENCE OF 129-137, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Receptor for ADP and ATP coupled to G-proteins that inhibit
CC the adenylyl cyclase second messenger system. Required for normal
CC platelet aggregation and blood coagulation.
CC {ECO:0000269|PubMed:11196645}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11196645};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11196645}.
CC -!- DOMAIN: The transmembrane domain is composed of seven transmembrane
CC helices; most of these are not strictly perpendicular to the plane of
CC the membrane, but are tilted and/or kinked. Agonist binding promotes a
CC conformation change in the extracellular loops that leads to an inward
CC movement of the transmembrane helices. Antagonists can bind to an
CC overlapping site, but block the inward movement of the transmembrane
CC helices (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF313450; AAG48945.1; -; mRNA.
DR RefSeq; NP_073637.1; NM_022800.1.
DR RefSeq; XP_006232468.1; XM_006232406.3.
DR RefSeq; XP_006232469.1; XM_006232407.3.
DR RefSeq; XP_006232470.1; XM_006232408.3.
DR AlphaFoldDB; Q9EPX4; -.
DR SMR; Q9EPX4; -.
DR BioGRID; 249199; 1.
DR STRING; 10116.ENSRNOP00000018600; -.
DR BindingDB; Q9EPX4; -.
DR ChEMBL; CHEMBL2188; -.
DR DrugCentral; Q9EPX4; -.
DR GlyGen; Q9EPX4; 2 sites.
DR iPTMnet; Q9EPX4; -.
DR PhosphoSitePlus; Q9EPX4; -.
DR PaxDb; Q9EPX4; -.
DR PRIDE; Q9EPX4; -.
DR Ensembl; ENSRNOT00000018600; ENSRNOP00000018600; ENSRNOG00000013902.
DR Ensembl; ENSRNOT00000116463; ENSRNOP00000086953; ENSRNOG00000013902.
DR GeneID; 64803; -.
DR KEGG; rno:64803; -.
DR UCSC; RGD:621681; rat.
DR CTD; 64805; -.
DR RGD; 621681; P2ry12.
DR eggNOG; ENOG502QUS2; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9EPX4; -.
DR OMA; YKSYKRT; -.
DR OrthoDB; 971778at2759; -.
DR PhylomeDB; Q9EPX4; -.
DR TreeFam; TF330969; -.
DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-RNO-417957; P2Y receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9EPX4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013902; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q9EPX4; RN.
DR GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0044298; C:cell body membrane; ISO:RGD.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; ISO:RGD.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IDA:RGD.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:ARUK-UCL.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; IMP:ARUK-UCL.
DR GO; GO:0030030; P:cell projection organization; IMP:RGD.
DR GO; GO:0071318; P:cellular response to ATP; IMP:ARUK-UCL.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0021808; P:cytosolic calcium signaling involved in initiation of cell movement in glial-mediated radial cell migration; IMP:ARUK-UCL.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0008347; P:glial cell migration; IMP:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:ARUK-UCL.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:RGD.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IMP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; IMP:RGD.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IGI:ARUK-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:ARUK-UCL.
DR GO; GO:0033626; P:positive regulation of integrin activation by cell surface receptor linked signal transduction; IDA:ARUK-UCL.
DR GO; GO:0043270; P:positive regulation of ion transport; ISO:RGD.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; IMP:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:ARUK-UCL.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IMP:ARUK-UCL.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:ARUK-UCL.
DR GO; GO:1904139; P:regulation of microglial cell migration; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048678; P:response to axon injury; IDA:ARUK-UCL.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:ParkinsonsUK-UCL.
DR GO; GO:0150063; P:visual system development; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005394; P2Y12_rcpt.
DR PANTHER; PTHR24233:SF0; PTHR24233:SF0; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01569; P2Y12PRNCPTR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell membrane; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Hemostasis;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="P2Y purinoceptor 12"
FT /id="PRO_0000070039"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..103
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 240..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 266..284
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 285..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 305..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 162..165
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 262..265
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 103..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 343 AA; 39047 MW; 7AE0AFCE66674136 CRC64;
MEVPGANATS ANTTSIPGTS TLCSRDYKIT QVLFPLLYTV LFFAGLITNS LAMRIFFQIR
SKSNFIIFLK NTVISDLLMI LTFPFKILSD AKLGAGHLRT LVCQVTSVTF YFTMYISISF
LGLITIDRYL KTTRPFKTSS PSNLLGAKIL SVAIWAFMFL LSLPNMILTN RRPKDKDITK
CSFLKSEFGL VWHEIVNYIC QVIFWINFLI VIVCYSLITK ELYRSYVRTR GSAKAPKKRV
NIKVFIIIAV FFICFVPFHF ARIPYTLSQT RAVFDCNAEN TLFYVKESTL WLTSLNACLD
PFIYFFLCKS FRNSLMSMLR CSTSGANKKK GQEGGDPSEE TPM
