Aliases for KCNG3 Gene
- Potassium Channel, Voltage Gated Modifier Subfamily G, Member 3 2 3
- Potassium Voltage-Gated Channel, Subfamily G, Member 3 2 3
- Voltage-Gated Potassium Channel Subunit Kv10.1 3 4
- Voltage-Gated Potassium Channel Subunit Kv6.3 3 4
- Voltage-Gated Potassium Channel Subunit Kv6.4 3
- Voltage-Gated Potassium Channel Kv10.1 3
- Voltage-Gated Potassium Channel 6.3 3
- Kv10.1 3
- KV6.3 3
External Ids for KCNG3 Gene
Previous GeneCards Identifiers for KCNG3 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 channel, voltage-gated, subfamily G. This member is a gamma subunit functioning as a modulatory molecule. Alternative splicing results in two transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008]
GeneCards Summary for KCNG3 Gene
KCNG3 (Potassium Channel, Voltage Gated Modifier Subfamily G, Member 3) is a Protein Coding gene. Among its related pathways are Transmission across Chemical Synapses and Dopamine-DARPP32 Feedback onto cAMP Pathway. GO annotations related to this gene include ion channel activity and delayed rectifier potassium channel activity. An important paralog of this gene is KCNB2.
UniProtKB/Swiss-Prot for KCNG3 Gene
Potassium channel subunit that does not form functional channels by itself (PubMed:11852086). Can form functional heterotetrameric channels with KCNB1; this promotes a reduction in the rate of activation and inactivation of the delayed rectifier voltage-gated potassium channel KCNB1 (PubMed:11852086, PubMed:19074135).
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.