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Proteins/UNIPROT:O43525
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. 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 M1 muscarinic acetylcholine receptors. KCNQ3 also associates with KCNQ5 to form a functional channel in vitro and may also contribute to the M-current in brain..
Function from UniProtKB (O43525), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
6 rows
24 statements
24 statements · 5 reference databases · Subject: KCNQ3 · Sources: Bgee, Hetionet, Reactome, Rhea, WikiPathways
4 reactions
3 names
Resolves to: KCNQ3
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