##gff-version 3 P16388 UniProtKB Chain 1 495 . . . ID=PRO_0000053969;Note=Potassium voltage-gated channel subfamily A member 1 P16388 UniProtKB Topological domain 1 164 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 165 186 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 187 220 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 221 242 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 243 253 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 254 274 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 275 287 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 288 308 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 309 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 324 345 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 346 359 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Intramembrane 360 371 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Intramembrane 372 379 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 380 386 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Transmembrane 387 415 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Topological domain 416 495 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Region 1 128 . . . Note=Tetramerization domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 P16388 UniProtKB Region 1 30 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16388 UniProtKB Region 310 323 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Motif 372 377 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P16388 UniProtKB Motif 493 495 . . . Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P16388 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 P16388 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16388 UniProtKB Modified residue 437 437 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 P16388 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10499 P16388 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q09470 P16388 UniProtKB Lipidation 243 243 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q09470 P16388 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16388 UniProtKB Natural variant 400 400 . . . Note=In RNA edited version. I->V