##gff-version 3 O00180 UniProtKB Chain 1 336 . . . ID=PRO_0000101740;Note=Potassium channel subfamily K member 1 O00180 UniProtKB Topological domain 1 20 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 42 103 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:22282804,ECO:0000305|PubMed:8978667;Dbxref=PMID:22282804,PMID:8978667 O00180 UniProtKB Intramembrane 104 116 . . . Note=Helical%3B Name%3DPore helix 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Intramembrane 117 122 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 123 132 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Transmembrane 133 156 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 157 181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 203 211 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Intramembrane 212 224 . . . Note=Helical%3B Name%3DPore helix 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Intramembrane 225 231 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 232 243 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Transmembrane 244 267 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Topological domain 268 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Region 117 122 . . . Note=Selectivity filter 1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:22282804,ECO:0000305|PubMed:21653227;Dbxref=PMID:21653227,PMID:22282804 O00180 UniProtKB Region 225 230 . . . Note=Selectivity filter 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22282804;Dbxref=PMID:22282804 O00180 UniProtKB Region 293 299 . . . Note=Important for intracellular retention in recycling endosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19959478;Dbxref=PMID:19959478 O00180 UniProtKB Site 118 118 . . . Note=Important for increased permeability to Na(+) when K(+) levels are subphysiological;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21653227;Dbxref=PMID:21653227 O00180 UniProtKB Site 146 146 . . . Note=Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22431633,ECO:0000269|PubMed:25001086;Dbxref=PMID:22431633,PMID:25001086 O00180 UniProtKB Site 261 261 . . . Note=Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z2T2 O00180 UniProtKB Glycosylation 95 95 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8978667;Dbxref=PMID:8978667 O00180 UniProtKB Disulfide bond 69 69 . . . Note=Interchain;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22282804,ECO:0000269|PubMed:8978667;Dbxref=PMID:22282804,PMID:8978667 O00180 UniProtKB Cross-link 274 274 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15820677,ECO:0000269|PubMed:20498050;Dbxref=PMID:15820677,PMID:20498050 O00180 UniProtKB Mutagenesis 69 69 . . . Note=Abolishes channel activity and formation of disulfide-linked homodimers. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8978667;Dbxref=PMID:8978667 O00180 UniProtKB Mutagenesis 95 95 . . . Note=Abolishes N-glycosylation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8978667;Dbxref=PMID:8978667 O00180 UniProtKB Mutagenesis 108 109 . . . Note=Impairs selectivity for K(+) ions and increases permeability to Na(+) ions%2C both at pH 7.4 and at pH 6. LF->FY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22431633;Dbxref=PMID:22431633 O00180 UniProtKB Mutagenesis 118 118 . . . Note=Abolishes change in ion selectivity in the presence of subphysiological K(+) levels. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21653227;Dbxref=PMID:21653227 O00180 UniProtKB Mutagenesis 122 122 . . . Note=Increases channel activity%2C and has only a minor effect on the inhibition by acidification of the extracellular medium. H->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22431633;Dbxref=PMID:22431633 O00180 UniProtKB Mutagenesis 122 122 . . . Note=Decreases channel activity and abolishes inhibition by acidification of the extracellular medium. H->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15820677,ECO:0000269|PubMed:20498050,ECO:0000269|PubMed:22431633;Dbxref=PMID:15820677,PMID:20498050,PMID:22431633 O00180 UniProtKB Mutagenesis 146 146 . . . Note=Does not increase the low intrinsic channel activity. L->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Mutagenesis 146 146 . . . Note=Increases channel activity. L->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22431633,ECO:0000269|PubMed:25001086;Dbxref=PMID:22431633,PMID:25001086 O00180 UniProtKB Mutagenesis 146 146 . . . Note=Increases channel activity. L->N%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Mutagenesis 146 146 . . . Note=Increases channel activity. Strongly increases channel activity%3B when associated with S-261. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Mutagenesis 161 161 . . . Note=No effect on channel activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605869;Dbxref=PMID:8605869 O00180 UniProtKB Mutagenesis 228 228 . . . Note=No effect on selectivity for K(+) ions. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22431633;Dbxref=PMID:22431633 O00180 UniProtKB Mutagenesis 231 231 . . . Note=Strongly decreases activity of homodimeric channels and of heterodimeric channels formed with KCNK3 and with KCNK9. No effect on location at the cell membrane. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23169818;Dbxref=PMID:23169818 O00180 UniProtKB Mutagenesis 250 250 . . . Note=Slightly decreases the increased permeability to Na(+) ions at pH 6. T->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22431633;Dbxref=PMID:22431633 O00180 UniProtKB Mutagenesis 261 261 . . . Note=Increases channel activity. L->D%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Mutagenesis 261 261 . . . Note=Increases channel activity. Strongly increases channel activity%3B when associated with S-146. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25001086;Dbxref=PMID:25001086 O00180 UniProtKB Mutagenesis 274 274 . . . Note=Converts the electrically silent channel that is present at the cell membrane to an active channel. K->A%2CC%2CD%2CQ%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20498050;Dbxref=PMID:20498050 O00180 UniProtKB Mutagenesis 274 274 . . . Note=Converts the electrically silent channel that is present at the cell membrane to an active channel. No effect on retention in recycling endosomes. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15820677,ECO:0000269|PubMed:17693262,ECO:0000269|PubMed:19959478,ECO:0000269|PubMed:20498050,ECO:0000269|PubMed:21653227,ECO:0000269|PubMed:22431633;Dbxref=PMID:15820677,PMID:17693262,PMID:19959478,PMID:20498050,PMID:21653227,PMID:22431633 O00180 UniProtKB Mutagenesis 293 294 . . . Note=Strongly increases location at the cell membrane. II->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19959478;Dbxref=PMID:19959478 O00180 UniProtKB Mutagenesis 299 336 . . . Note=No effect on intracellular retention in recycling endosomes. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19959478;Dbxref=PMID:19959478 O00180 UniProtKB Helix 19 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 72 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 104 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 128 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Turn 163 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 177 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 197 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 212 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 242 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM O00180 UniProtKB Helix 271 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UKM