Biology:KCNA5

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Short description: Protein-coding gene in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Potassium voltage-gated channel, shaker-related subfamily, member 5, also known as KCNA5 or Kv1.5, is a protein that in humans is encoded by the KCNA5 gene.[1]

Function

Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. KCNA5 encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, the function of which could restore the resting membrane potential of beta cells after depolarization, thereby contributing to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.[1] Mutations in this gene have been related to both atrial fibrillation[2] and sudden cardiac death.[3] KCNA5 are also key players in pulmonary vascular function, where they play a role in setting the resting membrane potential and its involvement during hypoxic pulmonary vasoconstriction.

Interactions

KCNA5 has been shown to interact with DLG4,[4][5] PDZ domain-containing proteins such as SAP97,[6] and Actinin, alpha 2.[4][7]

See also

References

  1. 1.0 1.1 "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741. 
  2. "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Human Molecular Genetics 15 (14): 2185–91. Jul 2006. doi:10.1093/hmg/ddl143. PMID 16772329. 
  3. "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochemical and Biophysical Research Communications 354 (3): 776–82. Mar 2007. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934. 
  4. 4.0 4.1 "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Letters 547 (1–3): 205–11. Jul 2003. doi:10.1016/S0014-5793(03)00668-9. PMID 12860415. 
  5. "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters 531 (3): 529–37. Nov 2002. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. 
  6. Murata, Mitsunobu; Buckett, Peter D.; Zhou, Jun; Brunner, Michael; Folco, Eduardo; Koren, Gideon (2001-12-01). "SAP97 interacts with Kv1.5 in heterologous expression systems" (in en). American Journal of Physiology. Heart and Circulatory Physiology 281 (6): H2575–H2584. doi:10.1152/ajpheart.2001.281.6.H2575. ISSN 0363-6135. PMID 11709425. 
  7. "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters 473 (2): 188–94. May 2000. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.