##gff-version 3 Q63472 UniProtKB Chain 1 962 . . . ID=PRO_0000053996;Note=Potassium voltage-gated channel subfamily H member 1 Q63472 UniProtKB Topological domain 1 220 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 221 241 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 242 248 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 249 269 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 270 290 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 291 309 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 310 318 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 319 341 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 342 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 351 372 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 373 421 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Intramembrane 422 443 . . . Note=Pore-forming%3B Name%3DSegment H5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 444 450 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Transmembrane 451 471 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Topological domain 472 962 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Domain 14 94 . . . Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 Q63472 UniProtKB Domain 93 145 . . . Note=PAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00141 Q63472 UniProtKB Region 151 162 . . . Note=Required for phosphatidylinositol bisphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95259 Q63472 UniProtKB Region 646 743 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60603 Q63472 UniProtKB Region 672 674 . . . Note=Interaction with cyclic nucleotide-binding pocket;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60603 Q63472 UniProtKB Region 830 859 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63472 UniProtKB Region 897 937 . . . Note=CAD (involved in subunit assembly);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9400421;Dbxref=PMID:9400421 Q63472 UniProtKB Region 933 962 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63472 UniProtKB Motif 436 441 . . . Note=Selectivity filter;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Compositional bias 830 847 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63472 UniProtKB Compositional bias 933 948 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63472 UniProtKB Modified residue 947 947 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60603 Q63472 UniProtKB Modified residue 951 951 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60603 Q63472 UniProtKB Modified residue 954 954 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60603 Q63472 UniProtKB Glycosylation 388 388 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:27516594;Dbxref=PMID:27516594 Q63472 UniProtKB Glycosylation 406 406 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255