Aliases for KCNC4 Gene
- Potassium Voltage-Gated Channel Subfamily C Member 4 2 3 5
- Potassium Channel, Voltage Gated Shaw Related Subfamily C, Member 4 2 3
- Potassium Voltage-Gated Channel, Shaw-Related Subfamily, Member 4 2 3
- KSHIIIC 3 4
- Voltage-Gated Potassium Channel Subunit KV3.4 3
- Voltage-Gated Potassium Channel Subunit Kv3.4 4
External Ids for KCNC4 Gene
Previous HGNC Symbols for KCNC4 Gene
Previous GeneCards Identifiers for KCNC4 Gene
The Shaker gene family of Drosophila encodes components of voltage-gated potassium channels and is comprised of four subfamilies. Based on sequence similarity, this gene is similar to the Shaw subfamily. The protein encoded by this gene belongs to the delayed rectifier class of channel proteins and is an integral membrane protein that mediates the voltage-dependent potassium ion permeability of excitable membranes. It generates atypical voltage-dependent transient current that may be important for neuronal excitability. Multiple transcript variants have been found for this gene. [provided by RefSeq, Jul 2010]
GeneCards Summary for KCNC4 Gene
KCNC4 (Potassium Voltage-Gated Channel Subfamily C Member 4) is a Protein Coding gene. Diseases associated with KCNC4 include Spinocerebellar Ataxia 13. Among its related pathways are Potassium Channels and Transmission across Chemical Synapses. GO annotations related to this gene include ion channel activity and potassium channel activity. An important paralog of this gene is KCNC2.
UniProtKB/Swiss-Prot for KCNC4 Gene
This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Voltage-gated potassium channels (KV) belong to the 6-TM family of potassium channel that also comprises the Ca2+-activated Slo (actually 7-TM) and the Ca2+-activated SK subfamilies. The alpha-subunits contain a single pore-forming region and combine to form tetramers.