Aliases for KCNC3 Gene
- Potassium Voltage-Gated Channel Subfamily C Member 3 2 3
- Potassium Channel, Voltage Gated Shaw Related Subfamily C, Member 3 2 3 5
- Potassium Voltage-Gated Channel, Shaw-Related Subfamily, Member 3 2 3
- Voltage-Gated Potassium Channel Subunit Kv3.3 3 4
- KSHIIID 3 4
- Shaw-Related Voltage-Gated Potassium Channel Protein 3 3
External Ids for KCNC3 Gene
Previous HGNC Symbols for KCNC3 Gene
Previous GeneCards Identifiers for KCNC3 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 one of these subfamilies, namely 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. Alternate splicing results in several transcript variants. [provided by RefSeq, Mar 2014]
GeneCards Summary for KCNC3 Gene
KCNC3 (Potassium Voltage-Gated Channel Subfamily C Member 3) is a Protein Coding gene. Diseases associated with KCNC3 include spinocerebellar ataxia 13 and spinocerebellar ataxia type13. Among its related pathways are Transmission across Chemical Synapses and Potassium Channels. GO annotations related to this gene include ion channel activity and delayed rectifier potassium channel activity. An important paralog of this gene is KCNA10.
UniProtKB/Swiss-Prot for KCNC3 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.