KCNQ4

The protein encoded by this gene forms a potassium channel that is thought to play a critical role in the regulation of neuronal excitability, particularly in sensory cells of the cochlea. The current generated by this channel is inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. The encoded protein can form a homomultimeric potassium channel or possibly a heteromultimeric channel in association with the protein encoded by the KCNQ3 gene. Defects in this gene are a cause of nonsyndromic sensorineural deafness type 2 (DFNA2), an autosomal dominant form of progressive hearing loss. Two transcript variants encoding different isoforms have been found for this gene.

Full Name

potassium voltage-gated channel subfamily Q member 4

Function

Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors.

Biological Process

Inner ear morphogenesisIEA:Ensembl
Potassium ion transmembrane transportManual Assertion Based On ExperimentIBA:GO_Central
Potassium ion transportManual Assertion Based On ExperimentTAS:ProtInc
Regulation of ion transmembrane transportIEA:UniProtKB-KW
Sensory perception of soundManual Assertion Based On ExperimentTAS:ProtInc

Cellular Location

Basal cell membrane. Situated at the basal membrane of cochlear outer hair cells.

Involvement in disease

Deafness, autosomal dominant, 2A (DFNA2A):
A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.

Topology

Cytoplasmic: 1-97
Helical: 98-118
Extracellular: 119-131
Helical: 132-152
Cytoplasmic: 153-172
Helical: 173-193
Extracellular: 194-201
Helical: 202-224
Cytoplasmic: 225-237
Helical: 238-258
Extracellular: 259-270
Pore-forming: 271-292
Extracellular: 293-296
Helical: 297-317
Cytoplasmic: 318-695