KCNA5

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.[5]

KCNA5
Identifiers
AliasesKCNA5, ATFB7, HCK1, HK2, HPCN1, KV1.5, PCN1, potassium voltage-gated channel subfamily A member 5
External IDsOMIM: 176267 MGI: 96662 HomoloGene: 1683 GeneCards: KCNA5
Gene location (Human)
Chr.Chromosome 12 (human)[1]
Band12p13.32Start5,043,879 bp[1]
End5,046,788 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 6: 126.53 – 126.54 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5] Mutations in this gene have been related to both atrial fibrillation [6] and sudden cardiac death.[7] 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[8][9] and Actinin, alpha 2.[8][10]

See also

References
  1. GRCh38: Ensembl release 89: ENSG00000130037 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000045534 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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

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

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