P2Y12_MOUSE
ID P2Y12_MOUSE Reviewed; 347 AA.
AC Q9CPV9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=P2Y purinoceptor 12;
DE Short=P2Y12;
GN Name=P2ry12;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12897207; DOI=10.1172/jci200317864;
RA Andre P., Delaney S.M., LaRocca T., Vincent D., DeGuzman F., Jurek M.,
RA Koller B., Phillips D.R., Conley P.B.;
RT "P2Y12 regulates platelet adhesion/activation, thrombus growth, and
RT thrombus stability in injured arteries.";
RL J. Clin. Invest. 112:398-406(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:12897207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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 -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but display impaired
CC blood coagulation, due to defects in platelet aggregation and thrombus
CC formation. {ECO:0000269|PubMed:12897207}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK013804; BAB29000.1; -; mRNA.
DR EMBL; AK014807; BAB29561.1; -; mRNA.
DR EMBL; BC027381; AAH27381.1; -; mRNA.
DR CCDS; CCDS17373.1; -.
DR RefSeq; NP_081847.3; NM_027571.3.
DR RefSeq; XP_006502146.1; XM_006502083.3.
DR RefSeq; XP_006502147.1; XM_006502084.3.
DR RefSeq; XP_006502148.1; XM_006502085.3.
DR AlphaFoldDB; Q9CPV9; -.
DR SMR; Q9CPV9; -.
DR STRING; 10090.ENSMUSP00000051353; -.
DR GlyGen; Q9CPV9; 2 sites.
DR iPTMnet; Q9CPV9; -.
DR PhosphoSitePlus; Q9CPV9; -.
DR SwissPalm; Q9CPV9; -.
DR MaxQB; Q9CPV9; -.
DR PaxDb; Q9CPV9; -.
DR PRIDE; Q9CPV9; -.
DR ProteomicsDB; 294420; -.
DR Antibodypedia; 2951; 205 antibodies from 31 providers.
DR DNASU; 70839; -.
DR Ensembl; ENSMUST00000050360; ENSMUSP00000051353; ENSMUSG00000036353.
DR Ensembl; ENSMUST00000170388; ENSMUSP00000126819; ENSMUSG00000036353.
DR Ensembl; ENSMUST00000196583; ENSMUSP00000143036; ENSMUSG00000036353.
DR Ensembl; ENSMUST00000199609; ENSMUSP00000143521; ENSMUSG00000036353.
DR GeneID; 70839; -.
DR KEGG; mmu:70839; -.
DR UCSC; uc008pir.2; mouse.
DR CTD; 64805; -.
DR MGI; MGI:1918089; P2ry12.
DR VEuPathDB; HostDB:ENSMUSG00000036353; -.
DR eggNOG; ENOG502QUS2; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR InParanoid; Q9CPV9; -.
DR OMA; YKSYKRT; -.
DR OrthoDB; 971778at2759; -.
DR PhylomeDB; Q9CPV9; -.
DR TreeFam; TF330969; -.
DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-MMU-417957; P2Y receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 70839; 0 hits in 71 CRISPR screens.
DR ChiTaRS; P2ry12; mouse.
DR PRO; PR:Q9CPV9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CPV9; protein.
DR Bgee; ENSMUSG00000036353; Expressed in globus pallidus and 119 other tissues.
DR ExpressionAtlas; Q9CPV9; baseline and differential.
DR Genevisible; Q9CPV9; MM.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0044298; C:cell body membrane; IGI:ARUK-UCL.
DR GO; GO:0031253; C:cell projection membrane; IGI:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IMP:MGI.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; ISO:MGI.
DR GO; GO:0071318; P:cellular response to ATP; IMP:ParkinsonsUK-UCL.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0021808; P:cytosolic calcium signaling involved in initiation of cell movement in glial-mediated radial cell migration; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0001973; P:G protein-coupled adenosine 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; IGI:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; 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; ISO:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR GO; GO:0033626; P:positive regulation of integrin activation by cell surface receptor linked signal transduction; ISO:MGI.
DR GO; GO:0043270; P:positive regulation of ion transport; IGI:MGI.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0050920; P:regulation of chemotaxis; ISO:MGI.
DR GO; GO:1904139; P:regulation of microglial cell migration; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048678; P:response to axon injury; ISO:MGI.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:ParkinsonsUK-UCL.
DR GO; GO:0150063; P:visual system development; IGI:ARUK-UCL.
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; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Hemostasis; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..347
FT /note="P2Y purinoceptor 12"
FT /id="PRO_0000070038"
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..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 321..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
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:0000250|UniProtKB:Q9EPX4"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX4"
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 347 AA; 39474 MW; F107488E57E025F1 CRC64;
MDVPGVNTTS ANTTFSPGTS TLCVRDYKIT QVLFPLLYTV LFFAGLITNS LAMRIFFQIR
SKSNFIIFLK NTVISDLLMI LTFPFKILSD AKLGAGPLRT LVCQVTSVTF YFTMYISISF
LGLITIDRYL KTTRPFKTSS PSNLLGAKIL SVVIWAFMFL ISLPNMILTN RRPKDKDVTK
CSFLKSEFGL VWHEIVNYIC QVIFWINFLI VIVCYSLITK ELYRSYVRTR GSAKVPKKKV
NVKVFIIIAV FFICFVPFHF ARIPYTLSQT RAVFDCSAEN TLFYVKESTL WLTSLNACLD
PFIYFFLCKS FRNSLTSMLR CSNSTSTSGT NKKKGQEGGE PSEETPM
