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KCND2
Protein-coding gene in the species Homo sapiens
Protein-coding gene in the species Homo sapiens
Potassium voltage-gated channel subfamily D member 2 is a protein that in humans is encoded by the KCND2 gene. It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.
Description
Voltage-gated potassium (Kv) 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. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.
Interactions
KCND2 has been shown to interact with FLNC.
References
References
- (December 1999). "Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current". Receptors Channels.
- (December 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol Rev.
- "Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2".
- (May 2001). "The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium". J. Mol. Cell. Cardiol..
- Petrecca, K. (December 2000). "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin". J. Neurosci..
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