Protein Details: Potassium voltage-gated channel subfamily KQT member 2

Function

Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current; a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore; it is important in the regulation of neuronal excitability. KCNQ2 current is blocked by barium and tetraethylammonium whereas 4-aminopyridine and charybdotoxin have no effect on KCNQ2 current. Tyrosine kinase inhibitors genistein or herbimycin a markedly down-regulate KCNQ2 current. As the native M-channel; the potassium channel composed of KCNQ2 and KCNQ3 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1 . KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium; in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity; increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity)

Sequence

PDB Structures

Ligand Binding