##gff-version 3
Q02280	UniProtKB	Chain	1	1174	.	.	.	ID=PRO_0000053964;Note=Potassium voltage-gated channel protein eag	
Q02280	UniProtKB	Topological domain	1	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	227	246	.	.	.	Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	247	268	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	269	291	.	.	.	Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	292	313	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	314	335	.	.	.	Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	336	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	343	369	.	.	.	Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	370	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	372	393	.	.	.	Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	394	441	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Intramembrane	442	467	.	.	.	Note=Pore-forming%3B Name%3DSegment H5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	468	470	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Transmembrane	471	493	.	.	.	Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Topological domain	494	1174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Domain	43	97	.	.	.	Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140	
Q02280	UniProtKB	Domain	113	165	.	.	.	Note=PAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00141	
Q02280	UniProtKB	Region	742	763	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Region	778	842	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Region	865	884	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Region	930	977	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Region	1022	1097	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Region	1115	1174	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Motif	453	458	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q02280	UniProtKB	Compositional bias	818	832	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Compositional bias	867	883	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Compositional bias	1071	1095	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Compositional bias	1115	1166	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q02280	UniProtKB	Binding site	571	688	.	.	.	.	
Q02280	UniProtKB	Modified residue	787	787	.	.	.	Note=Phosphothreonine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980904;Dbxref=PMID:11980904	
Q02280	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Glycosylation	412	412	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Glycosylation	424	424	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q02280	UniProtKB	Mutagenesis	787	787	.	.	.	Note=Reduced eag channel amplitude and accelerated inactivation. Does not affect binding with CASK. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980904;Dbxref=PMID:11980904	
Q02280	UniProtKB	Sequence conflict	548	548	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	567	567	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	571	571	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	699	699	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	769	769	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	894	894	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	934	934	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	1015	1015	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	1042	1042	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	1049	1049	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	1088	1088	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Sequence conflict	1142	1142	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q02280	UniProtKB	Beta strand	788	791	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FG8