P2Y12_MACFA
ID P2Y12_MACFA Reviewed; 342 AA.
AC Q95KC3; Q9BGT8;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=P2Y purinoceptor 12;
DE Short=P2Y12;
GN Name=P2RY12; ORFNames=QflA-10912, QmoA-10634;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex, and Medulla oblongata;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB056385; BAB33041.1; -; mRNA.
DR EMBL; AB062981; BAB60747.1; -; mRNA.
DR AlphaFoldDB; Q95KC3; -.
DR SMR; Q95KC3; -.
DR STRING; 9541.XP_005546161.1; -.
DR eggNOG; ENOG502QUS2; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
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 2: Evidence at transcript 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..342
FT /note="P2Y purinoceptor 12"
FT /id="PRO_0000070037"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 28..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 51..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..97
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..185
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 208..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 234..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 260..278
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 279..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 299..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 317..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 175..179
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 256..259
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX4"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX4"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 97..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 49
FT /note="I -> T (in Ref. 1; BAB33041)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="A -> T (in Ref. 1; BAB33041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 39480 MW; E93FC26BBFF5EC4C CRC64;
MQAIDNLTSA PGNTSLCTRD YKITQVLFPL LYTVLFFVGL ITNSLAMRIF FQIRSKSNFI
IFLKNTVISD LLMILTFPFK ILSDAKLGAG PLRTFVCQVT SVIFYFTMYI SISFLGLITI
DRYQKTTRPF KTSNPKNLLG AKILSVLIWA FMFLLSLPNM ILTNRRPRDK NVKKCSFLKS
EFGLVWHEIV NYICQVIFWI NFLIVIVCYT LITKELYRSY VRTRGVGKVP RKKVNVKVFI
IIAVFFICFV PFHFARIPYT LSQTRDVFDC AAENTLFYVK ESTLWLTSLN ACLDPFIYFF
LCKSFRNSLI SMLKCPNSAT SQSQDNRKKE QDGGDPNEET PM
