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   27-MAR-2024, entry version 167.
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/jci17864;
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.ENSMUSP00000143036; -.
DR   GlyCosmos; Q9CPV9; 2 sites, No reported glycans.
DR   GlyGen; Q9CPV9; 2 sites.
DR   iPTMnet; Q9CPV9; -.
DR   PhosphoSitePlus; Q9CPV9; -.
DR   SwissPalm; Q9CPV9; -.
DR   MaxQB; Q9CPV9; -.
DR   PaxDb; 10090-ENSMUSP00000051353; -.
DR   ProteomicsDB; 294420; -.
DR   Antibodypedia; 2951; 251 antibodies from 31 providers.
DR   DNASU; 70839; -.
DR   Ensembl; ENSMUST00000050360.14; ENSMUSP00000051353.8; ENSMUSG00000036353.14.
DR   Ensembl; ENSMUST00000170388.6; ENSMUSP00000126819.2; ENSMUSG00000036353.14.
DR   Ensembl; ENSMUST00000196583.5; ENSMUSP00000143036.2; ENSMUSG00000036353.14.
DR   Ensembl; ENSMUST00000199609.2; ENSMUSP00000143521.2; ENSMUSG00000036353.14.
DR   GeneID; 70839; -.
DR   KEGG; mmu:70839; -.
DR   UCSC; uc008pir.2; mouse.
DR   AGR; MGI:1918089; -.
DR   CTD; 64805; -.
DR   MGI; MGI:1918089; P2ry12.
DR   VEuPathDB; HostDB:ENSMUSG00000036353; -.
DR   eggNOG; ENOG502QUS2; Eukaryota.
DR   GeneTree; ENSGT01060000248592; -.
DR   InParanoid; Q9CPV9; -.
DR   OMA; FVCQVTQ; -.
DR   OrthoDB; 5390357at2759; -.
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 76 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 121 other cell types or tissues.
DR   ExpressionAtlas; Q9CPV9; baseline and differential.
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:0016020; C:membrane; ISS:UniProtKB.
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:0021801; P:cerebral cortex radial glia-guided 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:0030032; P:lamellipodium assembly; ISO:MGI.
DR   GO; GO:0006811; P:monoatomic ion transport; IGI: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:1904141; P:positive regulation of microglial cell migration; ISO:MGI.
DR   GO; GO:0043270; P:positive regulation of monoatomic ion transport; IGI:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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: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   CDD; cd15150; 7tmA_P2Y12; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR005394; P2Y12_rcpt.
DR   PANTHER; PTHR24233:SF0; P2Y PURINOCEPTOR 12; 1.
DR   PANTHER; PTHR24233; P2Y PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01569; P2Y12PRNCPTR.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q9CPV9; MM.
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
//