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Potassium voltage-gated channel, shaker-related subfamily, member 5
Identifiers
Symbols KCNA5; HK2; HCK1; HPCN1; KV1.5; MGC117058; MGC117059; PCN1
External IDs OMIM176267 MGI96662 HomoloGene1683 IUPHAR: Kv1.5 GeneCards: KCNA5 Gene
RNA expression pattern
PBB GE KCNA5 206762 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3741 16493
Ensembl ENSG00000130037 ENSMUSG00000045534
UniProt P22460 Q9Z1R6
RefSeq (mRNA) NM_002234 NM_145983
RefSeq (protein) NP_002225 NP_666095
Location (UCSC) Chr 12:
5.02 - 5.03 Mb
Chr 6:
126.5 - 126.5 Mb
PubMed search [1] [2]

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

Contents

Function

Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila melanogaster, and each has been shown to have human homolog(s). This gene 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 and thereby contribute to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.[1]

Interactions

KCNA5 has been shown to interact with DLG4[2][3] and Actinin, alpha 2.[2][4]

See also

References

  1. ^ a b "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741.  
  2. ^ a b Eldstrom, Jodene; Choi Woo Sung, Steele David F, Fedida David (Jul. 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1-3): 205–11. ISSN 0014-5793. PMID 12860415.  
  3. ^ Eldstrom, Jodene; Doerksen Kyle W, Steele David F, Fedida David (Nov. 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. (Netherlands) 531 (3): 529–37. ISSN 0014-5793. PMID 12435606.  
  4. ^ 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. ISSN 0014-5793. PMID 10812072.  

Further reading

  • Gutman GA, Chandy KG, Grissmer S, et al. (2006). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels.". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104.  
  • Curran ME, Landes GM, Keating MT (1992). "Molecular cloning, characterization, and genomic localization of a human potassium channel gene.". Genomics 12 (4): 729–37. doi:10.1016/0888-7543(92)90302-9. PMID 1349297.  
  • Philipson LH, Hice RE, Schaefer K, et al. (1991). "Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel.". Proc. Natl. Acad. Sci. U.S.A. 88 (1): 53–7. doi:10.1073/pnas.88.1.53. PMID 1986382.  
  • Tamkun MM, Knoth KM, Walbridge JA, et al. (1991). "Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle.". FASEB J. 5 (3): 331–7. PMID 2001794.  
  • Mays DJ, Foose JM, Philipson LH, Tamkun MM (1995). "Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue.". J. Clin. Invest. 96 (1): 282–92. doi:10.1172/JCI118032. PMID 7615797.  
  • Crumb WJ, Wible B, Arnold DJ, et al. (1995). "Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity.". Mol. Pharmacol. 47 (1): 181–90. PMID 7838127.  
  • Phromchotikul T, Browne DL, Curran ME, et al. (1993). "Dinucleotide repeat polymorphism at the KCNA5 locus.". Hum. Mol. Genet. 2 (9): 1512. doi:10.1093/hmg/2.9.1512-a. PMID 8242092.  
  • Albrecht B, Weber K, Pongs O (1996). "Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13.". Recept. Channels 3 (3): 213–20. PMID 8821794.  
  • Holmes TC, Fadool DA, Ren R, Levitan IB (1997). "Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain.". Science 274 (5295): 2089–91. doi:10.1126/science.274.5295.2089. PMID 8953041.  
  • Lacerda AE, Roy ML, Lewis EW, Rampe D (1997). "Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart.". Mol. Pharmacol. 52 (2): 314–22. PMID 9271355.  
  • Kääb S, Dixon J, Duc J, et al. (1998). "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): 1383–93. PMID 9760292.  
  • Maruoka ND, Steele DF, Au BP, et al. (2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells.". FEBS Lett. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072.  
  • Peretz A, Gil-Henn H, Sobko A, et al. (2000). "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon.". EMBO J. 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. PMID 10921884.  
  • Nitabach MN, Llamas DA, Araneda RC, et al. (2001). "A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.". Proc. Natl. Acad. Sci. U.S.A. 98 (2): 705–10. doi:10.1073/pnas.031446198. PMID 11149959.  
  • Cukovic D, Lu GW, Wible B, et al. (2001). "A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2.". FEBS Lett. 498 (1): 87–92. doi:10.1016/S0014-5793(01)02505-4. PMID 11389904.  
  • Kurata HT, Soon GS, Eldstrom JR, et al. (2002). "Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels.". J. Biol. Chem. 277 (32): 29045–53. doi:10.1074/jbc.M111470200. PMID 12021261.  
  • Williams CP, Hu N, Shen W, et al. (2002). "Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit.". J. Pharmacol. Exp. Ther. 302 (2): 545–50. doi:10.1124/jpet.102.033357. PMID 12130714.  
  • Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). "N-terminal PDZ-binding domain in Kv1 potassium channels.". FEBS Lett. 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  
  • Zhang S, Kurata HT, Kehl SJ, Fedida D (2003). "Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition.". J. Gen. Physiol. 121 (3): 215–25. doi:10.1085/jgp.20028760. PMID 12601085.  

External links

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

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