Domain:The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. ,Domain:The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. ,Function:Mediates the voltage-dependent potassium ion permeability of excitable membranes. Channels open or close in response to the voltage difference across the membrane , letting potassium ions pass in accordance with their electrochemical gradient. ,PTM:Highly phosphorylated on serine residues in the C-terminal. Differential phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating. Phosphorylation on Ser-457 , Ser-541 , Ser-567 , Ser-607 , Ser-656 and Ser-720 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation. Particularly , Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/ dephosphorylation activities. Tyr-128 can be dephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylation levels on Ser-607 are supersensitive to neuronal activity. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5. Levels then increase to reach adult levels by P14. Phosphorylation levels on Ser-564 and Ser-607 are greatly reduced during seizures , by 40% and 85% respectively. ,similarity:Belongs to the potassium channel family. B (Shab) subfamily. ,subunit:Heteromultimer with KCNG2 , KCNG3 , KCNG4 , KCNS1 , KCNS2 , KCNS3 and KCNV2. ,
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