Voltage-gated potassium channel subunit beta-1 (KCNAB1) is a protein that in humans is encoded by the KCNAB1 gene. Potassium channels are the most complex ion channels, influencing many physiological functions, including neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal families- have been identified, each of them has been shown to exist in human. KCNAB1 is characterized by six membrane-spanning domains with a shaker-type repeat in the fourth segment. There are three distinct isoforms encoded by three alternatively spliced transcript variants have been found. These three isoforms are all beta subunits, which form a heteromultimeric complex and modulate the activity of the pore-forming alpha subunits.
Basic Information of KCNAB1 | |
Protein Name | Voltage-gated potassium channel subunit beta-1 |
Gene Name | KCNAB1 |
Aliases | K(+) channel subunit beta-1, Kv-beta-1 |
Organism | Homo sapiens (Human) |
UniProt ID | Q14722 |
Transmembrane Times | / |
Length (aa) | 419 |
Sequence | MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGESQLRARQLALLREVEMNWYLKLCDLSSEHTTVCTTGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS |
KCNAB1 is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It also modulates action potentials via its effect on the pore-forming alpha subunits. Research shows that it can promote the expression of the pore-forming alpha subunits at the cell membrane, and thereby increase channel activity. KCNAB1 controls the closure of delayed rectifier potassium channels by obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members. It has the ability to promote the closure of KCNA1, KCNA2 and KCNA5 channels and accelerates KCNA4 channel closure, as well as the closure of heteromeric channels formed by KCNA1 and KCNA4. KCNAB1 protein can bind to NADPH, which is required for efficient down-regulation of potassium channel activity. Oxidation of the bound NADPH can strongly decrease N-type inactivation of potassium channel activity.
The authors support that KCNAB1 is a susceptibility gene for LTE, which is in agreement with previous studies showing that this gene may alter susceptibility to focal epilepsy.
This article demonstrates that KCNAB1 does not appear to play a role in the pathogenesis of rolandic epilepsy.
In this article, they find variants in CLCN2 and KCNAB have not previously been implicated in the causation of hypertension. These findings provide new insights into the pathophysiology of BP regulation and may point to novel drug targets for the treatment of hypertension.
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