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Proteins/UNIPROT:O43526
Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability. M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers. The native M-current has 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. KCNQ2-KCNQ3 M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+). Suppressed by activation of the muscarinic acetylcholine receptor CHRM1..
Function from UniProtKB (O43526), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 2 · transported by
2 compounds
2 compounds.
0 reported routes2 assembled routes
10 rows
89 statements
89 statements · 6 reference databases · Subject: KCNQ2 · Sources: Bgee, Hetionet, Human Protein Atlas, Reactome, Rhea, WikiPathways
4 reactions
3 names
Resolves to: KCNQ2
Transported by ANO9 or HTR3E or TMEM150C or KCNK1 or KCNK3 or GRIN2D or GRID2 or KCNQ3 or KCNQ2 or GRIN3B or HCN1 or TRPA1 and 98 more alternatives
Reaction pageRight to leftBalanced
Rhea RHEA:34963CC BY 4.0Reference data
Transported by KCNK1 or KCNQ3 or KCNQ2 or KCNK2 or CNGA1 or CLDN15 or CLDN2 or KCNK10 or CLDN10 or CNGB1 or CNGA2 or CNGA3 and 8 more alternatives
Reaction pageDirection not assertedBalanced
Rhea RHEA:78547CC BY 4.0Reference data