P2Y12_HUMAN
ID P2Y12_HUMAN Reviewed; 342 AA.
AC Q9H244; D3DNJ5; Q546J7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=P2Y purinoceptor 12;
DE Short=P2Y12;
DE AltName: Full=ADP-glucose receptor;
DE Short=ADPG-R;
DE AltName: Full=P2T(AC);
DE AltName: Full=P2Y(AC);
DE AltName: Full=P2Y(cyc);
DE AltName: Full=P2Y12 platelet ADP receptor;
DE Short=P2Y(ADP);
DE AltName: Full=SP1999;
GN Name=P2RY12; Synonyms=HORK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INVOLVEMENT IN BDPLT8.
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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=11104774; DOI=10.1074/jbc.m009718200;
RA Zhang F.L., Luo L., Gustafson E., Lachowicz J., Smith M., Qiao X.,
RA Liu Y.-H., Chen G., Pramanik B., Laz T.M., Palmer K., Bayne M.,
RA Monsma F.J. Jr.;
RT "ADP is the cognate ligand for the orphan G protein-coupled receptor
RT SP1999.";
RL J. Biol. Chem. 276:8608-8615(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11502873;
RA Takasaki J., Kamohara M., Saito T., Matsumoto M., Matsumoto S., Ohishi T.,
RA Soga T., Matsushime H., Furuichi K.;
RT "Molecular cloning of the platelet P2T(AC) ADP receptor: pharmacological
RT comparison with another ADP receptor, the P2Y1 receptor.";
RL Mol. Pharmacol. 60:432-439(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reinscheid R.K., Nothacker H.-P., Wang Z., Zeng J., Ehlert F.J.,
RA Civelli O.;
RT "ADP-glucose activates a G-protein coupled receptor and inhibits smooth
RT muscle contractions.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Bruess M., von Kugelgen I., Bonisch H.;
RT "Cloning and characterization of a human platelet ADP-receptor.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT "Identification of G protein-coupled receptor genes from the human genome
RT sequence.";
RL FEBS Lett. 520:97-101(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH THE AGONIST AZD1283,
RP FUNCTION, DISULFIDE BOND, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-80;
RP SER-156; ASN-159; LYS-280 AND GLU-281.
RX PubMed=24670650; DOI=10.1038/nature13083;
RA Zhang K., Zhang J., Gao Z.G., Zhang D., Zhu L., Han G.W., Moss S.M.,
RA Paoletta S., Kiselev E., Lu W., Fenalti G., Zhang W., Mueller C.E.,
RA Yang H., Jiang H., Cherezov V., Katritch V., Jacobson K.A., Stevens R.C.,
RA Wu B., Zhao Q.;
RT "Structure of the human P2Y12 receptor in complex with an antithrombotic
RT drug.";
RL Nature 509:115-118(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-342 IN COMPLEX WITH THE ADP
RP ANALOG 2-(METHYLSULFANYL)ADENOSINE 5'-(TRIHYDROGEN DIPHOSPHATE), FUNCTION,
RP SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF SER-83; CYS-97;
RP CYS-175; ARG-256 AND LYS-280.
RX PubMed=24784220; DOI=10.1038/nature13288;
RA Zhang J., Zhang K., Gao Z.G., Paoletta S., Zhang D., Han G.W., Li T.,
RA Ma L., Zhang W., Mueller C.E., Yang H., Jiang H., Cherezov V., Katritch V.,
RA Jacobson K.A., Stevens R.C., Wu B., Zhao Q.;
RT "Agonist-bound structure of the human P2Y12 receptor.";
RL Nature 509:119-122(2014).
RN [12]
RP VARIANTS BDPLT8 GLN-256 AND TRP-265, INVOLVEMENT IN BDPLT8, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12578987; DOI=10.1073/pnas.0437879100;
RA Cattaneo M., Zighetti M.L., Lombardi R., Martinez C., Lecchi A.,
RA Conley P.B., Ware J., Ruggeri Z.M.;
RT "Molecular bases of defective signal transduction in the platelet P2Y12
RT receptor of a patient with congenital bleeding.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1978-1983(2003).
RN [13]
RP VARIANT BDPLT8 GLN-187.
RX PubMed=25428217; DOI=10.1182/blood-2013-07-517896;
RA Lecchi A., Razzari C., Paoletta S., Dupuis A., Nakamura L., Ohlmann P.,
RA Gachet C., Jacobson K.A., Zieger B., Cattaneo M.;
RT "Identification of a new dysfunctional platelet P2Y12 receptor variant
RT associated with bleeding diathesis.";
RL Blood 125:1006-1013(2015).
CC -!- FUNCTION: Receptor for ADP and ATP coupled to G-proteins that inhibit
CC the adenylyl cyclase second messenger system. Not activated by UDP and
CC UTP. Required for normal platelet aggregation and blood coagulation.
CC {ECO:0000269|PubMed:11104774, ECO:0000269|PubMed:11196645,
CC ECO:0000269|PubMed:11502873, ECO:0000269|PubMed:12578987,
CC ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11196645,
CC ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:24670650,
CC ECO:0000269|PubMed:24784220}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987,
CC ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the platelets, lower levels in
CC the brain. Lowest levels in the lung, appendix, pituitary and adrenal
CC gland. Expressed in the spinal cord and in the fetal brain.
CC {ECO:0000269|PubMed:11104774, ECO:0000269|PubMed:11196645,
CC ECO:0000269|PubMed:11502873}.
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 such as AZD1283 can
CC bind to an overlapping site, but block the inward movement of the
CC transmembrane helices (PubMed:24670650, PubMed:24784220).
CC {ECO:0000269|PubMed:24670650, ECO:0000269|PubMed:24784220}.
CC -!- DISEASE: Bleeding disorder, platelet-type, 8 (BDPLT8) [MIM:609821]: A
CC condition characterized by mild to moderate mucocutaneous bleeding, and
CC excessive bleeding after surgery or trauma. The defect is due to severe
CC impairment of platelet response to ADP resulting in defective platelet
CC aggregation. {ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987,
CC ECO:0000269|PubMed:25428217}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF313449; AAG48944.1; -; mRNA.
DR EMBL; AF321815; AAK00948.1; -; mRNA.
DR EMBL; AB052684; BAB60824.1; -; mRNA.
DR EMBL; AF310685; AAL32292.1; -; Genomic_DNA.
DR EMBL; AJ320495; CAC87144.1; -; mRNA.
DR EMBL; AB083596; BAB89309.1; -; Genomic_DNA.
DR EMBL; AY136754; AAN01280.1; -; mRNA.
DR EMBL; CH471052; EAW78803.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78804.1; -; Genomic_DNA.
DR EMBL; BC017898; AAH17898.1; -; mRNA.
DR CCDS; CCDS3159.1; -.
DR RefSeq; NP_073625.1; NM_022788.4.
DR RefSeq; NP_795345.1; NM_176876.2.
DR RefSeq; XP_016862558.1; XM_017007069.1.
DR PDB; 4NTJ; X-ray; 2.62 A; A=2-342.
DR PDB; 4PXZ; X-ray; 2.50 A; A=2-342.
DR PDB; 4PY0; X-ray; 3.10 A; A=2-342.
DR PDBsum; 4NTJ; -.
DR PDBsum; 4PXZ; -.
DR PDBsum; 4PY0; -.
DR AlphaFoldDB; Q9H244; -.
DR SMR; Q9H244; -.
DR BioGRID; 122309; 69.
DR DIP; DIP-61226N; -.
DR IntAct; Q9H244; 47.
DR STRING; 9606.ENSP00000307259; -.
DR BindingDB; Q9H244; -.
DR ChEMBL; CHEMBL2001; -.
DR DrugBank; DB06441; Cangrelor.
DR DrugBank; DB00758; Clopidogrel.
DR DrugBank; DB06350; Elinogrel.
DR DrugBank; DB01240; Epoprostenol.
DR DrugBank; DB06209; Prasugrel.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB05553; Regrelor.
DR DrugBank; DB08816; Ticagrelor.
DR DrugBank; DB00208; Ticlopidine.
DR DrugBank; DB00374; Treprostinil.
DR DrugBank; DB16349; Vicagrel.
DR DrugCentral; Q9H244; -.
DR GuidetoPHARMACOLOGY; 328; -.
DR TCDB; 9.A.14.13.31; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9H244; 2 sites.
DR iPTMnet; Q9H244; -.
DR PhosphoSitePlus; Q9H244; -.
DR BioMuta; P2RY12; -.
DR DMDM; 21263835; -.
DR jPOST; Q9H244; -.
DR MassIVE; Q9H244; -.
DR PaxDb; Q9H244; -.
DR PeptideAtlas; Q9H244; -.
DR PRIDE; Q9H244; -.
DR ProteomicsDB; 80487; -.
DR Antibodypedia; 2951; 205 antibodies from 31 providers.
DR DNASU; 64805; -.
DR Ensembl; ENST00000302632.4; ENSP00000307259.4; ENSG00000169313.10.
DR GeneID; 64805; -.
DR KEGG; hsa:64805; -.
DR MANE-Select; ENST00000302632.4; ENSP00000307259.4; NM_022788.5; NP_073625.1.
DR UCSC; uc003eyx.3; human.
DR CTD; 64805; -.
DR DisGeNET; 64805; -.
DR GeneCards; P2RY12; -.
DR HGNC; HGNC:18124; P2RY12.
DR HPA; ENSG00000169313; Tissue enhanced (brain, lymphoid tissue).
DR MalaCards; P2RY12; -.
DR MIM; 600515; gene.
DR MIM; 609821; phenotype.
DR neXtProt; NX_Q9H244; -.
DR OpenTargets; ENSG00000169313; -.
DR Orphanet; 36355; Bleeding disorder due to P2Y12 defect.
DR Orphanet; 240935; Prediction of resistance to clopidogrel.
DR PharmGKB; PA134971947; -.
DR VEuPathDB; HostDB:ENSG00000169313; -.
DR eggNOG; ENOG502QUS2; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9H244; -.
DR OMA; YKSYKRT; -.
DR OrthoDB; 15873at2759; -.
DR PhylomeDB; Q9H244; -.
DR TreeFam; TF330969; -.
DR PathwayCommons; Q9H244; -.
DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-HSA-417957; P2Y receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q9H244; -.
DR SIGNOR; Q9H244; -.
DR BioGRID-ORCS; 64805; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; P2RY12; human.
DR GeneWiki; P2Y12; -.
DR GenomeRNAi; 64805; -.
DR Pharos; Q9H244; Tclin.
DR PRO; PR:Q9H244; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H244; protein.
DR Bgee; ENSG00000169313; Expressed in inferior vagus X ganglion and 143 other tissues.
DR Genevisible; Q9H244; HS.
DR GO; GO:0044298; C:cell body membrane; IEA:Ensembl.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; IEA:Ensembl.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IDA:UniProtKB.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:ARUK-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:ARUK-UCL.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; ISS:ARUK-UCL.
DR GO; GO:0030030; P:cell projection organization; ISS:ARUK-UCL.
DR GO; GO:0071318; P:cellular response to ATP; ISS:ARUK-UCL.
DR GO; GO:0021808; P:cytosolic calcium signaling involved in initiation of cell movement in glial-mediated radial cell migration; ISS:ARUK-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007599; P:hemostasis; NAS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:ARUK-UCL.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:ARUK-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:ARUK-UCL.
DR GO; GO:0033626; P:positive regulation of integrin activation by cell surface receptor linked signal transduction; ISS:ARUK-UCL.
DR GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISS:ARUK-UCL.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; TAS:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:ARUK-UCL.
DR GO; GO:0050920; P:regulation of chemotaxis; ISS:ARUK-UCL.
DR GO; GO:1904139; P:regulation of microglial cell migration; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048678; P:response to axon injury; ISS:ARUK-UCL.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:ParkinsonsUK-UCL.
DR GO; GO:0150063; P:visual system development; IEA:Ensembl.
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 3D-structure; Blood coagulation; Cell membrane; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Hemostasis;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="P2Y purinoceptor 12"
FT /id="PRO_0000070036"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT TRANSMEM 28..50
FT /note="Helical; Name=1"
FT TOPO_DOM 51..61
FT /note="Cytoplasmic"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT TOPO_DOM 83..97
FT /note="Extracellular"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT TOPO_DOM 119..142
FT /note="Cytoplasmic"
FT TRANSMEM 143..162
FT /note="Helical; Name=4"
FT TOPO_DOM 163..185
FT /note="Extracellular"
FT TRANSMEM 186..207
FT /note="Helical; Name=5"
FT TOPO_DOM 208..233
FT /note="Cytoplasmic"
FT TRANSMEM 234..259
FT /note="Helical; Name=6"
FT TOPO_DOM 260..278
FT /note="Extracellular"
FT TRANSMEM 279..298
FT /note="Helical; Name=7"
FT TOPO_DOM 299..342
FT /note="Cytoplasmic"
FT REGION 319..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 97
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 105
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 156..159
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 175..179
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 191
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 256..259
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 263
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 280
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
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 DISULFID 97..175
FT VARIANT 187
FT /note="H -> Q (in BDPLT8)"
FT /evidence="ECO:0000269|PubMed:25428217"
FT /id="VAR_072802"
FT VARIANT 256
FT /note="R -> Q (in BDPLT8; dbSNP:rs121917885)"
FT /evidence="ECO:0000269|PubMed:12578987"
FT /id="VAR_025383"
FT VARIANT 265
FT /note="R -> W (in BDPLT8; dbSNP:rs121917886)"
FT /evidence="ECO:0000269|PubMed:12578987"
FT /id="VAR_025384"
FT VARIANT 330
FT /note="E -> G (in dbSNP:rs16846673)"
FT /id="VAR_049431"
FT MUTAGEN 80
FT /note="K->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24670650"
FT MUTAGEN 83
FT /note="S->A: No effect on ADP binding."
FT /evidence="ECO:0000269|PubMed:24784220"
FT MUTAGEN 97
FT /note="C->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24784220"
FT MUTAGEN 156
FT /note="S->A: Slightly decreases affinity for ADP."
FT /evidence="ECO:0000269|PubMed:24670650"
FT MUTAGEN 159
FT /note="N->A: Slightly decreases affinity for ADP."
FT /evidence="ECO:0000269|PubMed:24670650"
FT MUTAGEN 175
FT /note="C->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24784220"
FT MUTAGEN 256
FT /note="R->A: Decreases affinity for ADP."
FT /evidence="ECO:0000269|PubMed:24784220"
FT MUTAGEN 280
FT /note="K->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24670650,
FT ECO:0000269|PubMed:24784220"
FT MUTAGEN 281
FT /note="E->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24670650"
FT HELIX 24..50
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:4PXZ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 100..127
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 136..161
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 181..226
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 270..293
FT /evidence="ECO:0007829|PDB:4PXZ"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4PXZ"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:4PXZ"
SQ SEQUENCE 342 AA; 39439 MW; 8553D2746C89176D CRC64;
MQAVDNLTSA PGNTSLCTRD YKITQVLFPL LYTVLFFVGL ITNGLAMRIF FQIRSKSNFI
IFLKNTVISD LLMILTFPFK ILSDAKLGTG PLRTFVCQVT SVIFYFTMYI SISFLGLITI
DRYQKTTRPF KTSNPKNLLG AKILSVVIWA FMFLLSLPNM ILTNRQPRDK NVKKCSFLKS
EFGLVWHEIV NYICQVIFWI NFLIVIVCYT LITKELYRSY VRTRGVGKVP RKKVNVKVFI
IIAVFFICFV PFHFARIPYT LSQTRDVFDC TAENTLFYVK ESTLWLTSLN ACLDPFIYFF
LCKSFRNSLI SMLKCPNSAT SLSQDNRKKE QDGGDPNEET PM
