##gff-version 3 Q61423 UniProtKB Chain 1 654 . . . ID=PRO_0000053982;Note=Potassium voltage-gated channel subfamily A member 4 Q61423 UniProtKB Topological domain 1 305 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 306 327 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 328 371 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 372 393 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 394 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 405 425 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 426 440 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 441 461 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 462 476 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 477 498 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 499 512 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Intramembrane 513 524 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Intramembrane 525 532 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 533 539 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Transmembrane 540 568 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Topological domain 569 654 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Region 24 145 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61423 UniProtKB Region 463 476 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Region 630 654 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61423 UniProtKB Motif 525 530 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q61423 UniProtKB Motif 652 654 . . . Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q61423 UniProtKB Compositional bias 80 99 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61423 UniProtKB Compositional bias 120 140 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61423 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q61423 UniProtKB Modified residue 600 600 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61423 UniProtKB Glycosylation 353 353 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61423 UniProtKB Sequence conflict 160 160 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61423 UniProtKB Sequence conflict 395 395 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61423 UniProtKB Sequence conflict 636 636 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305