Aliases for KCNIP4 Gene
External Ids for KCNIP4 Gene
Previous GeneCards Identifiers for KCNIP4 Gene
This gene encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins (KCNIPs), which belong to the recoverin branch of the EF-hand superfamily. Members of the KCNIP family are small calcium binding proteins. They all have EF-hand-like domains, and differ from each other in the N-terminus. They are integral subunit components of native Kv4 channel complexes. They may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. This protein member also interacts with presenilin. Multiple alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for KCNIP4 Gene
KCNIP4 (Potassium Voltage-Gated Channel Interacting Protein 4) is a Protein Coding gene. Diseases associated with KCNIP4 include Visceral Myopathy. Among its related pathways are Cardiac conduction and Regulation of Wnt-mediated beta catenin signaling and target gene transcription. GO annotations related to this gene include calcium ion binding and potassium channel regulator activity. An important paralog of this gene is KCNIP2.
UniProtKB/Swiss-Prot for KCNIP4 Gene
Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates KCND2 channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner (PubMed:11847232, PubMed:18957440, PubMed:23576435). Modulates KCND3/Kv4.3 currents (PubMed:23576435). Isoform 4 does not increase KCND2 expression at the cell membrane (PubMed:18957440). Isoform 4 retains KCND3 in the endoplasmic reticulum and negatively regulates its expression at the cell membrane.
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.