##gff-version 3 Q9H244 UniProtKB Chain 1 342 . . . ID=PRO_0000070036;Note=P2Y purinoceptor 12 Q9H244 UniProtKB Topological domain 1 27 . . . Note=Extracellular Q9H244 UniProtKB Transmembrane 28 50 . . . Note=Helical%3B Name%3D1 Q9H244 UniProtKB Topological domain 51 61 . . . Note=Cytoplasmic Q9H244 UniProtKB Transmembrane 62 82 . . . Note=Helical%3B Name%3D2 Q9H244 UniProtKB Topological domain 83 97 . . . Note=Extracellular Q9H244 UniProtKB Transmembrane 98 118 . . . Note=Helical%3B Name%3D3 Q9H244 UniProtKB Topological domain 119 142 . . . Note=Cytoplasmic Q9H244 UniProtKB Transmembrane 143 162 . . . Note=Helical%3B Name%3D4 Q9H244 UniProtKB Topological domain 163 185 . . . Note=Extracellular Q9H244 UniProtKB Transmembrane 186 207 . . . Note=Helical%3B Name%3D5 Q9H244 UniProtKB Topological domain 208 233 . . . Note=Cytoplasmic Q9H244 UniProtKB Transmembrane 234 259 . . . Note=Helical%3B Name%3D6 Q9H244 UniProtKB Topological domain 260 278 . . . Note=Extracellular Q9H244 UniProtKB Transmembrane 279 298 . . . Note=Helical%3B Name%3D7 Q9H244 UniProtKB Topological domain 299 342 . . . Note=Cytoplasmic Q9H244 UniProtKB Region 319 342 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H244 UniProtKB Binding site 93 93 . . . . Q9H244 UniProtKB Binding site 97 97 . . . . Q9H244 UniProtKB Binding site 105 105 . . . . Q9H244 UniProtKB Binding site 156 159 . . . . Q9H244 UniProtKB Binding site 175 179 . . . . Q9H244 UniProtKB Binding site 187 187 . . . . Q9H244 UniProtKB Binding site 191 191 . . . . Q9H244 UniProtKB Binding site 256 259 . . . . Q9H244 UniProtKB Binding site 263 263 . . . . Q9H244 UniProtKB Binding site 280 280 . . . . Q9H244 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPX4 Q9H244 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPX4 Q9H244 UniProtKB Glycosylation 6 6 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H244 UniProtKB Glycosylation 13 13 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H244 UniProtKB Disulfide bond 17 270 . . . . Q9H244 UniProtKB Disulfide bond 97 175 . . . . Q9H244 UniProtKB Natural variant 187 187 . . . ID=VAR_072802;Note=In BDPLT8. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25428217;Dbxref=PMID:25428217 Q9H244 UniProtKB Natural variant 256 256 . . . ID=VAR_025383;Note=In BDPLT8. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12578987;Dbxref=dbSNP:rs121917885,PMID:12578987 Q9H244 UniProtKB Natural variant 265 265 . . . ID=VAR_025384;Note=In BDPLT8. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12578987;Dbxref=dbSNP:rs121917886,PMID:12578987 Q9H244 UniProtKB Natural variant 330 330 . . . ID=VAR_049431;Note=E->G;Dbxref=dbSNP:rs16846673 Q9H244 UniProtKB Mutagenesis 80 80 . . . Note=Abolishes ADP binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24670650;Dbxref=PMID:24670650 Q9H244 UniProtKB Mutagenesis 83 83 . . . Note=No effect on ADP binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24784220;Dbxref=PMID:24784220 Q9H244 UniProtKB Mutagenesis 97 97 . . . Note=Abolishes ADP binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24784220;Dbxref=PMID:24784220 Q9H244 UniProtKB Mutagenesis 156 156 . . . Note=Slightly decreases affinity for ADP. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24670650;Dbxref=PMID:24670650 Q9H244 UniProtKB Mutagenesis 159 159 . . . Note=Slightly decreases affinity for ADP. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24670650;Dbxref=PMID:24670650 Q9H244 UniProtKB Mutagenesis 175 175 . . . Note=Abolishes ADP binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24784220;Dbxref=PMID:24784220 Q9H244 UniProtKB Mutagenesis 256 256 . . . Note=Decreases affinity for ADP. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24784220;Dbxref=PMID:24784220 Q9H244 UniProtKB Mutagenesis 280 280 . . . Note=Abolishes ADP binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24670650,ECO:0000269|PubMed:24784220;Dbxref=PMID:24670650,PMID:24784220 Q9H244 UniProtKB Mutagenesis 281 281 . . . Note=Abolishes ADP binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24670650;Dbxref=PMID:24670650 Q9H244 UniProtKB Helix 24 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 58 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 77 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 91 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 100 127 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 136 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 175 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 181 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 236 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 250 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 270 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Helix 296 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ Q9H244 UniProtKB Turn 302 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXZ