KCND2

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Potassium voltage-gated channel, Shal-related subfamily, member 2
PDB rendering based on 1nn7.
Available structures: 1nn7, 1s6c
Identifiers
Symbol(s) KCND2; KIAA1044; KV4.2; MGC119702; MGC119703; RK5
External IDs OMIM: 605410 MGI: 102663 HomoloGene: 40828
Orthologs
Human Mouse
Entrez 3751 16508
Ensembl ENSG00000184408 ENSMUSG00000060882
Uniprot Q9NZV8 Q9Z0V2
Refseq NM_012281 (mRNA)
NP_036413 (protein)		 NM_019697 (mRNA)
NP_062671 (protein)
Location Chr 7: 119.7 - 120.18 Mb Chr 6: 21.17 - 21.68 Mb
Pubmed search [1] [2]

Potassium voltage-gated channel, Shal-related subfamily, member 2, also known as KCND2 or Kv4.2, is a human gene.[1]

Voltage-gated potassium (Kv) 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, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.[1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2.

[edit] 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. 
  • Kong W, Po S, Yamagishi T, et al. (1999). "Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing.". Am. J. Physiol. 275 (6 Pt 2): H1963-70. PMID 9843794. 
  • Kikuno R, Nagase T, Ishikawa K, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 6 (3): 197-205. PMID 10470851. 
  • Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein.". J. Neurosci. 19 (18): 7770-80. PMID 10479680. 
  • Zhu XR, Wulf A, Schwarz M, et al. (1999). "Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current.". Recept. Channels 6 (5): 387-400. PMID 10551270. 
  • An WF, Bowlby MR, Betty M, et al. (2000). "Modulation of A-type potassium channels by a family of calcium sensors.". Nature 403 (6769): 553-6. doi:10.1038/35000592. PMID 10676964. 
  • Isbrandt D, Leicher T, Waldschütz R, et al. (2000). "Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA).". Genomics 64 (2): 144-54. doi:10.1006/geno.2000.6117. PMID 10729221. 
  • Postma AV, Bezzina CR, de Vries JF, et al. (2000). "Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3.". Hum. Genet. 106 (6): 614-9. PMID 10942109. 
  • Petrecca K, Miller DM, Shrier A (2001). "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin.". J. Neurosci. 20 (23): 8736-44. PMID 11102480. 
  • Bähring R, Dannenberg J, Peters HC, et al. (2001). "Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating.". J. Biol. Chem. 276 (26): 23888-94. doi:10.1074/jbc.M101320200. PMID 11287421. 
  • Nakamura TY, Pountney DJ, Ozaita A, et al. (2001). "A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents.". Proc. Natl. Acad. Sci. U.S.A. 98 (22): 12808-13. doi:10.1073/pnas.221168498. PMID 11606724. 
  • Morohashi Y, Hatano N, Ohya S, et al. (2002). "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4.". J. Biol. Chem. 277 (17): 14965-75. doi:10.1074/jbc.M200897200. PMID 11847232. 
  • Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). "N-terminal PDZ-binding domain in Kv1 potassium channels.". FEBS Lett. 531 (3): 529-37. PMID 12435606. 
  • Schrader LA, Anderson AE, Mayne A, et al. (2002). "PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex.". J. Neurosci. 22 (23): 10123-33. PMID 12451113. 
  • 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. 
  • Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function.". J. Biol. Chem. 278 (9): 7607-16. doi:10.1074/jbc.M210455200. PMID 12493773. 
  • Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767-72. doi:10.1126/science.1083423. PMID 12690205. 
  • Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7.". Nature 424 (6945): 157-64. doi:10.1038/nature01782. PMID 12853948. 
  • Wong W, Schlichter LC (2004). "Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95.". J. Biol. Chem. 279 (1): 444-52. doi:10.1074/jbc.M304675200. PMID 14559911. 
  • Kim LA, Furst J, Butler MH, et al. (2004). "Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2.". J. Biol. Chem. 279 (7): 5549-54. doi:10.1074/jbc.M311332200. PMID 14623880. 

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