##gff-version 3 Q920E3 UniProtKB Chain 1 988 . . . ID=PRO_0000054011;Note=Potassium voltage-gated channel subfamily H member 5 Q920E3 UniProtKB Topological domain 1 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 218 238 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 239 243 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 244 264 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 265 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 292 312 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 313 319 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 320 340 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 341 346 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 347 367 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 368 419 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Intramembrane 420 440 . . . Note=Pore-forming%3B Name%3DSegment H5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 441 446 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Transmembrane 447 467 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Topological domain 468 988 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Domain 14 86 . . . Note=PAS Q920E3 UniProtKB Domain 91 143 . . . Note=PAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00141 Q920E3 UniProtKB Region 704 715 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Region 721 741 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q920E3 UniProtKB Region 838 893 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q920E3 UniProtKB Region 909 948 . . . Note=CAD (involved in subunit assembly);Ontology_term=ECO:0000250;evidence=ECO:0000250 Q920E3 UniProtKB Motif 432 437 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q920E3 UniProtKB Compositional bias 845 864 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q920E3 UniProtKB Compositional bias 865 883 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q920E3 UniProtKB Binding site 550 668 . . . . Q920E3 UniProtKB Modified residue 883 883 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q920E3 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q920E3 UniProtKB Cross-link 785 785 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NCM2 Q920E3 UniProtKB Sequence conflict 552 552 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305