##gff-version 3 Q9UL51 UniProtKB Chain 1 889 . . . ID=PRO_0000054111;Note=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 Q9UL51 UniProtKB Topological domain 1 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 216 236 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 237 240 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 241 261 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 262 288 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 289 309 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 310 317 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 318 338 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 339 369 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 370 390 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 391 413 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Intramembrane 414 435 . . . Note=Pore-forming%3B Name%3DSegment H5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 436 440 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Transmembrane 441 461 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Topological domain 462 889 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Region 1 159 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UL51 UniProtKB Region 158 209 . . . Note=Involved in subunit assembly;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9UL51 UniProtKB Region 754 889 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UL51 UniProtKB Compositional bias 15 59 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UL51 UniProtKB Compositional bias 756 788 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UL51 UniProtKB Binding site 608 611 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22006928;Dbxref=PMID:22006928 Q9UL51 UniProtKB Binding site 618 619 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22006928;Dbxref=PMID:22006928 Q9UL51 UniProtKB Binding site 659 662 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22006928;Dbxref=PMID:22006928 Q9UL51 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JKA9 Q9UL51 UniProtKB Modified residue 668 668 . . . Note=Phosphoserine%3B by PKG/PRKG2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 754 754 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JKA9 Q9UL51 UniProtKB Modified residue 756 756 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 779 779 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 786 786 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Modified residue 868 868 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88703 Q9UL51 UniProtKB Glycosylation 407 407 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9UL51 UniProtKB Natural variant 126 126 . . . ID=VAR_086190;Note=In FEB2%3B affects channel activity resulting in faster kinetics and increased current density at higher temperature compared to wild type. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24324597;Dbxref=PMID:24324597 Q9UL51 UniProtKB Natural variant 246 246 . . . ID=VAR_086191;Note=In EIG17%3B gain-of-function variant%3B affects channel activity resulting in a depolarizing shift in activation and faster activation kinetics compared to controls. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29064616;Dbxref=PMID:29064616 Q9UL51 UniProtKB Natural variant 280 280 . . . ID=VAR_086192;Note=Does not affect channel activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29064616;Dbxref=dbSNP:rs114790896,PMID:29064616 Q9UL51 UniProtKB Natural variant 418 418 . . . ID=VAR_081530;Note=Found in a patient with childhood apraxia of speech%3B uncertain significance. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29463886;Dbxref=PMID:29463886 Q9UL51 UniProtKB Natural variant 515 515 . . . ID=VAR_086193;Note=In EIG17%3B causes a large negative shift of the activation curve%3B homomeric mutant channels transfected into rat cortical neurons lower the threshold of action potential firing and strongly increase cell excitability when compared with wild-type channels. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22131395;Dbxref=PMID:22131395 Q9UL51 UniProtKB Natural variant 527 527 . . . ID=VAR_061106;Note=R->Q;Dbxref=dbSNP:rs55687900 Q9UL51 UniProtKB Natural variant 632 632 . . . ID=VAR_086194;Note=In EIG17%3B gain-of-function variant%3B affects channel activity resulting in a depolarizing shift in activation and faster activation kinetics compared to controls. S->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29064616;Dbxref=PMID:29064616 Q9UL51 UniProtKB Natural variant 705 705 . . . ID=VAR_086195;Note=Does not affect channel activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29064616;Dbxref=dbSNP:rs200188844,PMID:29064616 Q9UL51 UniProtKB Natural variant 756 756 . . . ID=VAR_086196;Note=In EIG17%3B uncertain significance%3B does not affect channel activity. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29064616;Dbxref=dbSNP:rs1230549709,PMID:29064616 Q9UL51 UniProtKB Sequence conflict 17 20 . . . Note=TPAP->SPTT;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Sequence conflict 29 29 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Sequence conflict 32 32 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Sequence conflict 294 294 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Sequence conflict 713 713 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Sequence conflict 849 849 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UL51 UniProtKB Helix 471 489 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 494 508 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 515 520 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 524 534 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 536 540 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Turn 543 547 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 550 557 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 561 565 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 570 572 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 576 578 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MPF Q9UL51 UniProtKB Beta strand 580 586 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 589 592 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 598 601 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 606 608 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 610 614 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 619 626 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Beta strand 628 634 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 635 644 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 646 661 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Turn 662 664 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10 Q9UL51 UniProtKB Helix 668 670 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U10