##gff-version 3 Q08460 UniProtKB Chain 1 1209 . . . ID=PRO_0000054134;Note=Calcium-activated potassium channel subunit alpha-1 Q08460 UniProtKB Topological domain 1 86 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 87 107 . . . Note=Helical%3B Name%3DSegment S0;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 108 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 200 214 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 215 235 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 236 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 240 260 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 261 264 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 265 285 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 286 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 301 321 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 322 335 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Intramembrane 336 358 . . . Note=Pore-forming%3B Name%3DP region;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 359 367 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Transmembrane 368 388 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Topological domain 389 1209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q08460 UniProtKB Domain 415 558 . . . Note=RCK N-terminal Q08460 UniProtKB Region 1 61 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Region 556 576 . . . Note=Segment S7 Q08460 UniProtKB Region 613 633 . . . Note=Segment S8 Q08460 UniProtKB Region 681 685 . . . Note=Heme-binding motif Q08460 UniProtKB Region 703 733 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Region 783 803 . . . Note=Segment S9 Q08460 UniProtKB Region 1005 1025 . . . Note=Segment S10 Q08460 UniProtKB Region 1159 1209 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Motif 352 355 . . . Note=Selectivity for potassium Q08460 UniProtKB Motif 976 998 . . . Note=Calcium bowl Q08460 UniProtKB Compositional bias 26 61 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Compositional bias 712 730 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Compositional bias 1159 1190 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Compositional bias 1191 1209 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q08460 UniProtKB Binding site 439 439 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Binding site 462 462 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Binding site 464 464 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Binding site 985 985 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B7ZC96 Q08460 UniProtKB Binding site 988 988 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B7ZC96 Q08460 UniProtKB Binding site 991 991 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B7ZC96 Q08460 UniProtKB Binding site 993 993 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B7ZC96 Q08460 UniProtKB Modified residue 709 709 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 711 711 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 724 724 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 728 728 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 916 916 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 924 924 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 928 928 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 1194 1194 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28204 Q08460 UniProtKB Modified residue 1197 1197 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28204 Q08460 UniProtKB Lipidation 118 118 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08460 UniProtKB Lipidation 119 119 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08460 UniProtKB Lipidation 121 121 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08460 UniProtKB Alternative sequence 1 65 . . . ID=VSP_009959;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7687074;Dbxref=PMID:7687074 Q08460 UniProtKB Alternative sequence 1 50 . . . ID=VSP_009960;Note=In isoform 2. MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSS->MELEHPKSPPYP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7687074;Dbxref=PMID:7687074 Q08460 UniProtKB Alternative sequence 643 646 . . . ID=VSP_009961;Note=In isoform 2%2C isoform 3 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10517674,ECO:0000303|PubMed:12388098,ECO:0000303|PubMed:7687074;Dbxref=PMID:10517674,PMID:12388098,PMID:7687074 Q08460 UniProtKB Alternative sequence 702 702 . . . ID=VSP_009962;Note=In isoform 2. L->LIYF;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7687074;Dbxref=PMID:7687074 Q08460 UniProtKB Alternative sequence 702 702 . . . ID=VSP_009963;Note=In isoform 4. L->PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERTFPLSSVSVNDCSTSFRAF;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10517674;Dbxref=PMID:10517674 Q08460 UniProtKB Alternative sequence 948 974 . . . ID=VSP_009964;Note=In isoform 2%2C isoform 3 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10517674,ECO:0000303|PubMed:12388098,ECO:0000303|PubMed:7687074;Dbxref=PMID:10517674,PMID:12388098,PMID:7687074 Q08460 UniProtKB Alternative sequence 1203 1209 . . . ID=VSP_009965;Note=In isoform 2. RKEMVYR->ATRMTRMGQAEKKWFTDEPDNAYPRNIQIKPMSTHMANQINQYKSTSSLIPPIREVEDEC;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7687074;Dbxref=PMID:7687074 Q08460 UniProtKB Mutagenesis 151 151 . . . Note=Loss of phosphorylation-independent activation of channel activity by ethanol. CaMK2-dependent phosphorylation leads to populations of partially phosphorylated tetramers with a range of responses to ethanol from activation to inhibition. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16341213;Dbxref=PMID:16341213 Q08460 UniProtKB Mutagenesis 272 272 . . . Note=Alters the voltage-dependent gating. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11112549;Dbxref=PMID:11112549 Q08460 UniProtKB Mutagenesis 278 278 . . . Note=Alters the voltage-dependent gating. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11112549;Dbxref=PMID:11112549 Q08460 UniProtKB Mutagenesis 284 284 . . . Note=Alters the voltage-dependent gating%3B when associated with R-287. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11112549;Dbxref=PMID:11112549 Q08460 UniProtKB Mutagenesis 287 287 . . . Note=Alters the voltage-dependent gating%3B when associated with K-284. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11112549;Dbxref=PMID:11112549 Q08460 UniProtKB Mutagenesis 427 427 . . . Note=Does not affect sensitivity to Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192411;Dbxref=PMID:12192411 Q08460 UniProtKB Mutagenesis 432 432 . . . Note=Reduced sensitivity to Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192411;Dbxref=PMID:12192411 Q08460 UniProtKB Mutagenesis 434 434 . . . Note=Does not affect sensitivity to Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192411;Dbxref=PMID:12192411 Q08460 UniProtKB Mutagenesis 439 439 . . . Note=Abolishes sensitivity to Mg(2+)%2C but not sensitivity to Ca(2+). E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Mutagenesis 444 444 . . . Note=Reduces sensitivity to Mg(2+)%2C but not sensitivity to Ca(2+). H->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Mutagenesis 461 461 . . . Note=Reduces sensitivity to Mg(2+)%2C but not sensitivity to Ca(2+). T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Mutagenesis 462 462 . . . Note=Reduces sensitivity to Mg(2+)%2C but not sensitivity to Ca(2+). Q->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12192410;Dbxref=PMID:12192410 Q08460 UniProtKB Mutagenesis 464 464 . . . Note=Remains sensitive to Mg(2+). E->D%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12192410,ECO:0000269|PubMed:12192411;Dbxref=PMID:12192410,PMID:12192411 Q08460 UniProtKB Mutagenesis 464 464 . . . Note=Abolishes sensitivity to Mg(2+)%2C but not sensitivity to Ca(2+). E->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12192410,ECO:0000269|PubMed:12192411;Dbxref=PMID:12192410,PMID:12192411 Q08460 UniProtKB Mutagenesis 992 996 . . . Note=Alters calcium binding. DDDPD->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12149279;Dbxref=PMID:12149279 Q08460 UniProtKB Modified residue 670 670 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q08460 UniProtKB Modified residue 672 672 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079