##gff-version 3 Q09470 UniProtKB Chain 1 495 . . . ID=PRO_0000053968;Note=Potassium voltage-gated channel subfamily A member 1 Q09470 UniProtKB Topological domain 1 164 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 165 186 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 187 220 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 221 242 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 243 253 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 254 274 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 275 287 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 288 308 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 309 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 324 345 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 346 359 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Intramembrane 360 371 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Intramembrane 372 379 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 380 386 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Transmembrane 387 415 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Topological domain 416 495 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Region 1 128 . . . Note=Tetramerization domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 Q09470 UniProtKB Region 1 30 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q09470 UniProtKB Region 310 323 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Motif 372 377 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q09470 UniProtKB Motif 493 495 . . . Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q09470 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 Q09470 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q09470 UniProtKB Modified residue 437 437 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 Q09470 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 Q09470 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23774215;Dbxref=PMID:23774215 Q09470 UniProtKB Lipidation 243 243 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15837928;Dbxref=PMID:15837928 Q09470 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q09470 UniProtKB Natural variant 174 174 . . . ID=VAR_001508;Note=In EA1. V->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7842011,ECO:0000269|PubMed:8541859;Dbxref=dbSNP:rs104894349,PMID:7842011,PMID:8541859 Q09470 UniProtKB Natural variant 177 177 . . . ID=VAR_001509;Note=In EA1. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9600245;Dbxref=PMID:9600245 Q09470 UniProtKB Natural variant 184 184 . . . ID=VAR_020830;Note=In EA1%3B alters voltage dependence and kinetics of activation though not of C-type inactivation. F->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8541859,ECO:0000269|PubMed:8845167;Dbxref=dbSNP:rs104894357,PMID:8541859,PMID:8845167 Q09470 UniProtKB Natural variant 204 204 . . . ID=VAR_020051;Note=R->H;Dbxref=dbSNP:rs2229000 Q09470 UniProtKB Natural variant 226 226 . . . ID=VAR_001510;Note=In EA1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9600245;Dbxref=dbSNP:rs104894354,PMID:9600245 Q09470 UniProtKB Natural variant 226 226 . . . ID=VAR_037100;Note=In MK1%3B induces a reduced efflux of potassium ions during depolarization which results in increased muscle cell activity%3B coexpression studies of the mutant protein with the wild-type protein produces significantly reduced currents suggesting a severe effect of the mutation. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17136396;Dbxref=dbSNP:rs28933383,PMID:17136396 Q09470 UniProtKB Natural variant 226 226 . . . ID=VAR_020831;Note=In EA1. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8871592;Dbxref=dbSNP:rs28933383,PMID:8871592 Q09470 UniProtKB Natural variant 226 226 . . . ID=VAR_037101;Note=In EA1%3B yields currents with a largely reduced amplitude. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10355668;Dbxref=dbSNP:rs28933383,PMID:10355668 Q09470 UniProtKB Natural variant 239 239 . . . ID=VAR_001511;Note=In EA1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7842011;Dbxref=dbSNP:rs104894348,PMID:7842011 Q09470 UniProtKB Natural variant 242 242 . . . ID=VAR_037102;Note=In MK1%3B 10%25 reduction of mean peak current amplitudes compared to wil-dtype%3B mutant and wild-type expression together is consistent with a loss-of-function effect of the mutation. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11026449;Dbxref=dbSNP:rs28933381,PMID:11026449 Q09470 UniProtKB Natural variant 244 244 . . . ID=VAR_037103;Note=In MK1%3B does not affect channel activity. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11026449;Dbxref=dbSNP:rs28933382,PMID:11026449 Q09470 UniProtKB Natural variant 249 249 . . . ID=VAR_001512;Note=In EA1. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7842011;Dbxref=dbSNP:rs104894356,PMID:7842011 Q09470 UniProtKB Natural variant 255 255 . . . ID=VAR_072397;Note=In MK1%3B strongly reduces the activity of homomeric channels with dominant negative effects on wild-type channels. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19307729;Dbxref=dbSNP:rs121918067,PMID:19307729 Q09470 UniProtKB Natural variant 325 325 . . . ID=VAR_020832;Note=In EA1%3B results in non-functional homomeric channels%3B accelerates recovery from N-type inactivation due to interaction with KCNAB1%3B slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. E->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077175,ECO:0000269|PubMed:17156368,ECO:0000269|PubMed:8541859,ECO:0000269|PubMed:8845167;Dbxref=dbSNP:rs104894353,PMID:12077175,PMID:17156368,PMID:8541859,PMID:8845167 Q09470 UniProtKB Natural variant 329 329 . . . ID=VAR_020833;Note=In EA1. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11013453;Dbxref=PMID:11013453 Q09470 UniProtKB Natural variant 342 342 . . . ID=VAR_020834;Note=In EA1%3B phenotype without myokymia. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15532032;Dbxref=PMID:15532032 Q09470 UniProtKB Natural variant 400 400 . . . ID=VAR_016805;Note=In RNA edited version. I->V Q09470 UniProtKB Natural variant 404 404 . . . ID=VAR_001513;Note=In EA1%3B results in slower channel activation compared to wild-type%3B slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. V->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11026449,ECO:0000269|PubMed:17156368,ECO:0000269|PubMed:9600245;Dbxref=dbSNP:rs104894355,PMID:11026449,PMID:17156368,PMID:9600245 Q09470 UniProtKB Natural variant 405 405 . . . ID=VAR_078205;Note=Found in a patient with neonatal onset epileptic encephalopathy%3B likely pathogenic. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864847;Dbxref=dbSNP:rs1555085798,PMID:27864847 Q09470 UniProtKB Natural variant 408 408 . . . ID=VAR_001514;Note=In EA1%3B channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation%3B accelerates recovery from N-type inactivation due to interaction with KCNAB1%3B slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. V->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077175,ECO:0000269|PubMed:17156368,ECO:0000269|PubMed:7842011,ECO:0000269|PubMed:8845167;Dbxref=dbSNP:rs104894352,PMID:12077175,PMID:17156368,PMID:7842011,PMID:8845167 Q09470 UniProtKB Mutagenesis 35 36 . . . Note=No effect on palmitoylation%2C no effect on current kinetics. CC->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15837928;Dbxref=PMID:15837928 Q09470 UniProtKB Mutagenesis 177 177 . . . Note=Slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17156368;Dbxref=PMID:17156368 Q09470 UniProtKB Mutagenesis 243 243 . . . Note=Strongly decreases palmitoylation and alters current kinetics. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15837928;Dbxref=PMID:15837928 Q09470 UniProtKB Mutagenesis 255 255 . . . Note=Slightly increases channel activity%2C but does not affect expression at the cell membrane. N->A%2CH%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19307729;Dbxref=PMID:19307729 Q09470 UniProtKB Mutagenesis 255 255 . . . Note=Abolishes channel activity%2C but does not affect expression at the cell membrane. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19307729;Dbxref=PMID:19307729 Q09470 UniProtKB Mutagenesis 255 255 . . . Note=Strongly reduces channel activity%2C but does not affect expression at the cell membrane. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19307729;Dbxref=PMID:19307729 Q09470 UniProtKB Mutagenesis 255 255 . . . Note=No effect on channel activity. N->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19307729;Dbxref=PMID:19307729 Q09470 UniProtKB Mutagenesis 446 446 . . . Note=Impairs phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23774215;Dbxref=PMID:23774215 Q09470 UniProtKB Mutagenesis 446 446 . . . Note=Impairs expression at the cell membrane. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23774215;Dbxref=PMID:23774215 Q09470 UniProtKB Sequence conflict 265 265 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q09470 UniProtKB Sequence conflict 315 315 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q09470 UniProtKB Sequence conflict 452 452 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305