Biology:KCNA5
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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]
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
- ↑ 1.0 1.1 "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3741.
- ↑ "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Human Molecular Genetics 15 (14): 2185–2191. July 2006. doi:10.1093/hmg/ddl143. PMID 16772329.
- ↑ "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochemical and Biophysical Research Communications 354 (3): 776–782. March 2007. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934.
- ↑ 4.0 4.1 "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Letters 547 (1–3): 205–211. July 2003. doi:10.1016/S0014-5793(03)00668-9. PMID 12860415. Bibcode: 2003FEBSL.547..205E.
- ↑ "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters 531 (3): 529–537. November 2002. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. Bibcode: 2002FEBSL.531..529E.
- ↑ "SAP97 interacts with Kv1.5 in heterologous expression systems". American Journal of Physiology. Heart and Circulatory Physiology 281 (6): H2575–H2584. December 2001. doi:10.1152/ajpheart.2001.281.6.H2575. PMID 11709425.
- ↑ "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters 473 (2): 188–194. May 2000. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072. Bibcode: 2000FEBSL.473..188M.
Further reading
- "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacological Reviews 57 (4): 473–508. December 2005. doi:10.1124/pr.57.4.10. PMID 16382104.
- "Molecular cloning, characterization, and genomic localization of a human potassium channel gene". Genomics 12 (4): 729–737. April 1992. doi:10.1016/0888-7543(92)90302-9. PMID 1349297.
- "Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel". Proceedings of the National Academy of Sciences of the United States of America 88 (1): 53–57. January 1991. doi:10.1073/pnas.88.1.53. PMID 1986382. Bibcode: 1991PNAS...88...53P.
- "Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle". FASEB Journal 5 (3): 331–337. March 1991. doi:10.1096/fasebj.5.3.2001794. PMID 2001794.
- "Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue". The Journal of Clinical Investigation 96 (1): 282–292. July 1995. doi:10.1172/JCI118032. PMID 7615797.
- "Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity". Molecular Pharmacology 47 (1): 181–190. January 1995. doi:10.1016/S0026-895X(25)08517-7. PMID 7838127.
- "Dinucleotide repeat polymorphism at the KCNA5 locus". Human Molecular Genetics 2 (9): 1512. September 1993. doi:10.1093/hmg/2.9.1512-a. PMID 8242092.
- "Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13". Receptors & Channels 3 (3): 213–220. 1996. PMID 8821794.
- "Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain". Science 274 (5295): 2089–2091. December 1996. doi:10.1126/science.274.5295.2089. PMID 8953041. Bibcode: 1996Sci...274.2089H.
- "Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart". Molecular Pharmacology 52 (2): 314–322. August 1997. doi:10.1124/mol.52.2.314. PMID 9271355.
- "Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density". Circulation 98 (14): 1383–1393. October 1998. doi:10.1161/01.cir.98.14.1383. PMID 9760292.
- "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters 473 (2): 188–194. May 2000. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072. Bibcode: 2000FEBSL.473..188M.
- "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon". The EMBO Journal 19 (15): 4036–4045. August 2000. doi:10.1093/emboj/19.15.4036. PMID 10921884.
- "A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors". Proceedings of the National Academy of Sciences of the United States of America 98 (2): 705–710. January 2001. doi:10.1073/pnas.031446198. PMID 11149959.
- "A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2". FEBS Letters 498 (1): 87–92. June 2001. doi:10.1016/S0014-5793(01)02505-4. PMID 11389904. Bibcode: 2001FEBSL.498...87C.
- "Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels". The Journal of Biological Chemistry 277 (32): 29045–29053. August 2002. doi:10.1074/jbc.M111470200. PMID 12021261.
- "Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit". The Journal of Pharmacology and Experimental Therapeutics 302 (2): 545–550. August 2002. doi:10.1124/jpet.102.033357. PMID 12130714.
- "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters 531 (3): 529–537. November 2002. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. Bibcode: 2002FEBSL.531..529E.
- "Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition". The Journal of General Physiology 121 (3): 215–225. March 2003. doi:10.1085/jgp.20028760. PMID 12601085.
External links
- Kv1.5+Potassium+Channel at the US National Library of Medicine Medical Subject Headings (MeSH)
- KCNA5+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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