Potassium voltage-gated channel, shaker-related subfamily, member 5
Symbols  ; ATFB7; HCK1; HK2; HPCN1; KV1.5; PCN1
External IDs IUPHAR: ChEMBL: GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
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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]


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.


KCNA5 has been shown to interact with DLG4[4][5] and Actinin, alpha 2.[4][6]

See also


  1. ^ a b "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 (July 2006). "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Hum Mol Genet 15 (14): 2185–91.  
  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 (March 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochem Biophys Res Commun 354 (3): 776–82.  
  4. ^ a b Eldstrom, Jodene; Choi Woo Sung; Steele David F; Fedida David (July 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1–3): 205–11.  
  5. ^ Eldstrom, Jodene; Doerksen Kyle W; Steele David F; Fedida David (November 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. (Netherlands) 531 (3): 529–37.  
  6. ^ Maruoka, N D; Steele D F; Au B P; Dan P; Zhang X; Moore E D; Fedida D (May 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. (NETHERLANDS) 473 (2): 188–94.  

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