##gff-version 3 O60706 UniProtKB Chain 1 1549 . . . ID=PRO_0000093402;Note=ATP-binding cassette sub-family C member 9 O60706 UniProtKB Topological domain 1 30 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 31 51 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 52 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 73 93 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 94 101 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 102 122 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 123 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 133 153 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 154 167 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 168 188 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 189 301 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 302 322 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 323 350 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 351 371 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 372 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 424 444 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 445 455 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 456 476 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 477 531 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 532 552 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 553 571 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 572 592 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 593 990 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 991 1011 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 1012 1034 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 1035 1055 . . . Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 1056 1127 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 1128 1148 . . . Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 1149 1245 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Transmembrane 1246 1266 . . . Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Topological domain 1267 1549 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Domain 297 597 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Domain 672 912 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O60706 UniProtKB Domain 994 1274 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O60706 UniProtKB Domain 1312 1546 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O60706 UniProtKB Region 944 967 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60706 UniProtKB Compositional bias 950 966 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60706 UniProtKB Binding site 705 712 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O60706 UniProtKB Binding site 1346 1353 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O60706 UniProtKB Glycosylation 9 9 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Glycosylation 326 326 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Glycosylation 330 330 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Glycosylation 334 334 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O60706 UniProtKB Alternative sequence 1508 1549 . . . ID=VSP_000058;Note=In isoform SUR2B. SSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK->HTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM;Ontology_term=ECO:0000305;evidence=ECO:0000305 O60706 UniProtKB Natural variant 60 60 . . . ID=VAR_068485;Note=In HTOCD. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907230,PMID:22610116 O60706 UniProtKB Natural variant 207 207 . . . ID=VAR_068486;Note=In HTOCD. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=PMID:22610116 O60706 UniProtKB Natural variant 380 380 . . . ID=VAR_068487;Note=In HTOCD. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs1165205076,PMID:22610116 O60706 UniProtKB Natural variant 432 432 . . . ID=VAR_068488;Note=In HTOCD%3B mutant channels show reduced ATP sensitivity%3B rat ABCC9 construct containing this mutation shows gain of function. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22610116,ECO:0000269|PubMed:26621776;Dbxref=PMID:22610116,PMID:26621776 O60706 UniProtKB Natural variant 478 478 . . . ID=VAR_068489;Note=In HTOCD%3B rat ABCC9 construct containing this mutation shows gain of function. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22608503,ECO:0000269|PubMed:26621776;Dbxref=dbSNP:rs387907211,PMID:22608503,PMID:26621776 O60706 UniProtKB Natural variant 1020 1020 . . . ID=VAR_068490;Note=In HTOCD. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907229,PMID:22610116 O60706 UniProtKB Natural variant 1039 1039 . . . ID=VAR_068491;Note=In HTOCD. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=PMID:22610116 O60706 UniProtKB Natural variant 1043 1043 . . . ID=VAR_068492;Note=In HTOCD%3B rat ABCC9 construct containing this mutation shows gain of function. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22608503,ECO:0000269|PubMed:26621776;Dbxref=dbSNP:rs387907210,PMID:22608503,PMID:26621776 O60706 UniProtKB Natural variant 1054 1054 . . . ID=VAR_068493;Note=In HTOCD. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=PMID:22610116 O60706 UniProtKB Natural variant 1108 1108 . . . ID=VAR_048143;Note=P->S;Dbxref=dbSNP:rs35404804 O60706 UniProtKB Natural variant 1116 1116 . . . ID=VAR_068494;Note=In HTOCD. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907228,PMID:22610116 O60706 UniProtKB Natural variant 1116 1116 . . . ID=VAR_068495;Note=In HTOCD%3B mutant channels show reduced ATP sensitivity. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907227,PMID:22610116 O60706 UniProtKB Natural variant 1154 1154 . . . ID=VAR_068496;Note=In HTOCD%3B mutant channels show reduced ATP sensitivity. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22608503,ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907209,PMID:22608503,PMID:22610116 O60706 UniProtKB Natural variant 1154 1154 . . . ID=VAR_068497;Note=In HTOCD. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22608503,ECO:0000269|PubMed:22610116;Dbxref=dbSNP:rs387907208,PMID:22608503,PMID:22610116 O60706 UniProtKB Natural variant 1160 1160 . . . ID=VAR_083082;Note=L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31303265;Dbxref=dbSNP:rs780799175,PMID:31303265 O60706 UniProtKB Natural variant 1513 1513 . . . ID=VAR_018483;Note=In CMD1O. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15034580;Dbxref=dbSNP:rs72559751,PMID:15034580 O60706 UniProtKB Natural variant 1547 1547 . . . ID=VAR_066210;Note=In ATFB12%3B compromises adenine nucleotide-dependent induction of KATP current%3B mutant ABCC9 that is coexpressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current%2C but shows a blunted response to ADP. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17245405;Dbxref=dbSNP:rs387906805,PMID:17245405 O60706 UniProtKB Sequence conflict 586 586 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O60706 UniProtKB Sequence conflict 589 589 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 O60706 UniProtKB Sequence conflict 1503 1503 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305