KCNA5

Potassium channel, voltage gated shaker related subfamily A, member 5
Identifiers
Symbols KCNA5 ; ATFB7; HCK1; HK2; HPCN1; KV1.5; PCN1
External IDs OMIM: 176267 MGI: 96662 HomoloGene: 1683 IUPHAR: 542 ChEMBL: 4306 GeneCards: KCNA5 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 3741 16493
Ensembl ENSG00000130037 ENSMUSG00000045534
UniProt P22460 Q61762
RefSeq (mRNA) NM_002234 NM_145983
RefSeq (protein) NP_002225 NP_666095
Location (UCSC) Chr 12:
5.04 – 5.05 Mb
Chr 6:
126.53 – 126.7 Mb
PubMed search

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] and Actinin, alpha 2.[4][6]

See also

References

  1. 1 2 "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
  2. Olson TM, Alekseev AE, Liu XK, Park S, Zingman LV, Bienengraeber M, Sattiraju S, Ballew JD, Jahangir A, Terzic A (Jul 2006). "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Human Molecular Genetics 15 (14): 2185–91. doi:10.1093/hmg/ddl143. PMID 16772329.
  3. Nielsen NH, Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, Bentzen BH, Sigurd B, Larsen LA, Andersen PS, Haunsø S, Kjeldsen K, Grunnet M, Christiansen M, Olesen SP (Mar 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochemical and Biophysical Research Communications 354 (3): 776–82. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934.
  4. 1 2 Eldstrom J, Choi WS, Steele DF, Fedida D (Jul 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Letters 547 (1-3): 205–11. doi:10.1016/S0014-5793(03)00668-9. PMID 12860415.
  5. Eldstrom J, Doerksen KW, Steele DF, Fedida D (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606.
  6. Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D (May 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters 473 (2): 188–94. 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.

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