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 OMIM: 602754 MGI: 1277957 HomoloGene: 1696
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3783 16534
Ensembl ENSG00000104783 ENSMUSG00000054342
Uniprot O15554 Q8C2E0
Refseq NM_002250 (mRNA)
NP_002241 (protein)		 NM_008433 (mRNA)
NP_032459 (protein)
Location Chr 19: 48.96 - 48.98 Mb Chr 7: 24.08 - 24.09 Mb
Pubmed search [1] [2]

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. ^ a b "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 membrane protein-related article is a stub. You can help Wikipedia by expanding it.

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v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channel
L-type/Cavα (1.1, 1.2, 1.3, 1.4) • N-type/Cavα2.2 • P-type/Cavα(2.1) • Q-type/Cavα2.1 • R-type/Cavα2.3 • T-type/Cavα(3.2)
α2δ-subunits (1, 2) • β-subunits (β1, β2, β3, β4) • γ-subunits (γ1, γ2, γ3, γ4)
Cation channels of sperm • Two-pore channel (1, 2)
Ligand-gated
Na+: Sodium channel
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) • Navβ (1, 2, 3, 4)
Other
K+: Potassium channel
Kvα (1-6) (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.10, 2.1, 2.2, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 4.3, 5.1, 6.1, 6.2, 6.3, 6.4)
Kvα (7-12) (7.1, 7.2, 7.3, 7.4, 7.5, 8.1, 8.2, 9.1, 9.2, 9.3, 10.1, 10.2, 11.1/hERG, 11.2, 11.3, 12.1, 12.2, 12.3)
Kvβ (1, 2, 3) • KCNIP (1, 2, 3, 4) • minK/ISK • MiRP (1, 2, 3) • Shaker gene
Kir (1.1, 2.1, 2.2, 2.3, 2.4) • GIRK/Kir (3.1, 3.2, 3.3, 3.4) • Kir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)
K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)
M+: TRP cation channel
TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (1, 2, 3) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)
Cl-: Chloride channel
CFTR • CLCA (1, 2, 3, 4) • CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) • CLIC (1, 2, 3, 4, 5, 6, L1) • CLNS (1A, 1B)
Cyclic nucleotide-gated
α1, α2, α3, α4, β1, β3, H1, H2, H3, H4
Porin
Other/general

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