KCNT1

Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a sodium-activated potassium channel subunit which is thought to function in ion conductance and developmental signaling pathways. Mutations in this gene cause the early-onset epileptic disorders, malignant migrating partial seizures of infancy and autosomal dominant nocturnal frontal lobe epilepsy. Alternative splicing results in multiple transcript variants.

potassium sodium-activated channel subfamily T member 1

Outwardly rectifying potassium channel subunit that may coassemble with other Slo-type channel subunits. Activated by high intracellular sodium or chloride levels. Activated upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated by calcium in the absence of sodium ions (in vitro) (By similarity).

Cell membrane

Developmental and epileptic encephalopathy 14 (DEE14):
A rare epileptic encephalopathy of infancy that combines pharmacoresistant seizures with developmental delay. This severe neurologic disorder is characterized by onset in the first 6 months of life of refractory focal seizures and arrest of psychomotor development. Ictal EEG shows discharges that arise randomly from various areas of both hemispheres and migrate from one brain region to another.
Epilepsy, nocturnal frontal lobe, 5 (ENFL5):
An autosomal dominant focal epilepsy syndrome characterized by childhood onset of clusters of motor seizures during sleep. Some patients may develop behavioral or psychiatric manifestations and/or intellectual disability. The phenotype is more severe than observed in other genetic forms of nocturnal frontal lobe epilepsy.

Cytoplasmic: 1-97
Helical: 98-118
Extracellular: 119-155
Helical: 156-176
Cytoplasmic: 177-187
Helical: 188-208
Extracellular: 209-213
Helical: 214-226
Cytoplasmic: 227-251
Helical: 252-272
Extracellular: 273-281
Pore-forming: 282-302
Extracellular: 303-304
Helical: 305-325
Cytoplasmic: 326-1230

Phosphorylated by protein kinase C. Phosphorylation of the C-terminal domain increases channel activity (By similarity).