Aliases for KCNV2 Gene
- Potassium Voltage-Gated Channel Modifier Subfamily V Member 2 2 3 5
- Potassium Channel, Voltage Gated Modifier Subfamily V, Member 2 2 3
- Voltage-Gated Potassium Channel Subunit Kv8.2 3 4
- Potassium Channel, Subfamily V, Member 2 2 3
- Potassium Voltage-Gated Channel Subfamily V Member 2 3
- Kv11.1 3
- Kv8.2 3
- RCD3B 3
External Ids for KCNV2 Gene
Previous GeneCards Identifiers for KCNV2 Gene
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. This gene encodes a member of the potassium voltage-gated channel subfamily V. This member is identified as a 'silent subunit', and it does not form homomultimers, but forms heteromultimers with several other subfamily members. Through obligatory heteromerization, it exerts a function-altering effect on other potassium channel subunits. This protein is strongly expressed in pancreas and has a weaker expression in several other tissues. [provided by RefSeq, Jul 2008]
GeneCards Summary for KCNV2 Gene
KCNV2 (Potassium Voltage-Gated Channel Modifier Subfamily V Member 2) is a Protein Coding gene. Diseases associated with KCNV2 include Retinal Cone Dystrophy 3B and Cone Dystrophy. Among its related pathways are Sweet Taste Signaling 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 KCNB1.
UniProtKB/Swiss-Prot for KCNV2 Gene
Potassium channel subunit. Modulates channel activity by shifting the threshold and the half-maximal activation to more negative values.
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.