KCNN4

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Potassium intermediate/small conductance calcium-activated channel, subfamily N, member 4
Identifiers
Symbols KCNN4 ; IK1; IKCA1; KCA4; KCa3.1; SK4; hIKCa1; hKCa4; hSK4
External IDs Template:OMIM5 Template:MGI HomoloGene1696
RNA expression pattern
File:PBB GE KCNN4 204401 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Potassium intermediate/small conductance calcium-activated channel, subfamily N, member 4, also known as KCNN4, is a human gene.[1]

The protein encoded by this gene is part of a potentially heterotetrameric voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization, which promotes calcium influx. The encoded protein may be part of the predominant calcium-activated potassium channel in T-lymphocytes. This gene is similar to other KCNN family potassium channel genes, but it differs enough to possibly be considered as part of a new subfamily.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: KCNN4 potassium intermediate/small conductance calcium-activated channel, subfamily N, member 4".

Further reading

  • Wei AD, Gutman GA, Aldrich R; et al. (2006). "International Union of Pharmacology. LII. Nomenclature and molecular relationships of calcium-activated potassium channels". Pharmacol. Rev. 57 (4): 463–72. doi:10.1124/pr.57.4.9. PMID 16382103.
  • Ishii TM, Silvia C, Hirschberg B; et al. (1997). "A human intermediate conductance calcium-activated potassium channel". Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11651–6. PMID 9326665.
  • Joiner WJ, Wang LY, Tang MD, Kaczmarek LK (1997). "hSK4, a member of a novel subfamily of calcium-activated potassium channels". Proc. Natl. Acad. Sci. U.S.A. 94 (20): 11013–8. PMID 9380751.
  • Logsdon NJ, Kang J, Togo JA; et al. (1998). "A novel gene, hKCa4, encodes the calcium-activated potassium channel in human T lymphocytes". J. Biol. Chem. 272 (52): 32723–6. PMID 9407042.
  • Ghanshani S, Coleman M, Gustavsson P; et al. (1998). "Human calcium-activated potassium channel gene KCNN4 maps to chromosome 19q13.2 in the region deleted in diamond-blackfan anemia". Genomics. 51 (1): 160–1. doi:10.1006/geno.1998.5333. PMID 9693050.
  • Fanger CM, Ghanshani S, Logsdon NJ; et al. (1999). "Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1". J. Biol. Chem. 274 (9): 5746–54. PMID 10026195.
  • Liu QH, Williams DA, McManus C; et al. (2000). "HIV-1 gp120 and chemokines activate ion channels in primary macrophages through CCR5 and CXCR4 stimulation". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4832–7. doi:10.1073/pnas.090521697. PMID 10758170.
  • Ghanshani S, Wulff H, Miller MJ; et al. (2001). "Up-regulation of the IKCa1 potassium channel during T-cell activation. Molecular mechanism and functional consequences". J. Biol. Chem. 275 (47): 37137–49. doi:10.1074/jbc.M003941200. PMID 10961988.
  • Wulff H, Gutman GA, Cahalan MD, Chandy KG (2001). "Delineation of the clotrimazole/TRAM-34 binding site on the intermediate conductance calcium-activated potassium channel, IKCa1". J. Biol. Chem. 276 (34): 32040–5. doi:10.1074/jbc.M105231200. PMID 11425865.
  • Koegel H, Kaesler S, Burgstahler R; et al. (2003). "Unexpected down-regulation of the hIK1 Ca2+-activated K+ channel by its opener 1-ethyl-2-benzimidazolinone in HaCaT keratinocytes. Inverse effects on cell growth and proliferation". J. Biol. Chem. 278 (5): 3323–30. doi:10.1074/jbc.M208914200. PMID 12421833.
  • Mazzone JN, Kaiser RA, Buxton IL (2003). "Calcium-activated potassium channel expression in human myometrium: effect of pregnancy". Proc. West. Pharmacol. Soc. 45: 184–6. PMID 12434576.
  • 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.
  • Syme CA, Hamilton KL, Jones HM; et al. (2003). "Trafficking of the Ca2+-activated K+ channel, hIK1, is dependent upon a C-terminal leucine zipper". J. Biol. Chem. 278 (10): 8476–86. doi:10.1074/jbc.M210072200. PMID 12493744.
  • Hamilton KL, Syme CA, Devor DC (2003). "Molecular localization of the inhibitory arachidonic acid binding site to the pore of hIK1". J. Biol. Chem. 278 (19): 16690–7. doi:10.1074/jbc.M212959200. PMID 12609997.
  • Mall M, Gonska T, Thomas J; et al. (2003). "Modulation of Ca2+-activated Cl- secretion by basolateral K+ channels in human normal and cystic fibrosis airway epithelia". Pediatr. Res. 53 (4): 608–18. doi:10.1203/01.PDR.0000057204.51420.DC. PMID 12612194.
  • Hoffman JF, Joiner W, Nehrke K; et al. (2003). "The hSK4 (KCNN4) isoform is the Ca2+-activated K+ channel (Gardos channel) in human red blood cells". Proc. Natl. Acad. Sci. U.S.A. 100 (12): 7366–71. doi:10.1073/pnas.1232342100. PMID 12773623.
  • Bernard K, Bogliolo S, Soriani O, Ehrenfeld J (2004). "Modulation of calcium-dependent chloride secretion by basolateral SK4-like channels in a human bronchial cell line". J. Membr. Biol. 196 (1): 15–31. doi:10.1007/s00232-003-0621-3. PMID 14724753.
  • Jones HM, Hamilton KL, Papworth GD; et al. (2004). "Role of the NH2 terminus in the assembly and trafficking of the intermediate conductance Ca2+-activated K+ channel hIK1". J. Biol. Chem. 279 (15): 15531–40. doi:10.1074/jbc.M400069200. PMID 14754884.
  • Gibson JS, Muzyamba MC (2005). "Modulation of Gardos channel activity by oxidants and oxygen tension: effects of 1-chloro-2,4-dinitrobenzene and phenazine methosulphate". Bioelectrochemistry (Amsterdam, Netherlands). 62 (2): 147–52. doi:10.1016/j.bioelechem.2003.07.008. PMID 15039018.
  • Lew VL, Tiffert T, Etzion Z; et al. (2005). "Distribution of dehydration rates generated by maximal Gardos-channel activation in normal and sickle red blood cells". Blood. 105 (1): 361–7. doi:10.1182/blood-2004-01-0125. PMID 15339840.

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

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