KCNN4

From Wikipedia, the free encyclopedia

Potassium intermediate/small conductance calcium-activated channel, subfamily N, member 4

Identifiers

KCNN4; IK1; IKCA1; KCA4; KCa3.1; SK4; hIKCa1; hKCa4; hSK4

External IDs

OMIM: 602754 MGI: 1277957 HomoloGene: 1696

Gene ontology
Molecular Function:	• ion channel activity • voltage-gated potassium channel activity • calmodulin binding • calcium-activated potassium channel activity
Cellular Component:	• membrane fraction • voltage-gated potassium channel complex • membrane • integral to membrane
Biological Process:	• ion transport • potassium ion transport • defense response • positive regulation of protein secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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]

[edit] See also

[edit] References

^ ^a ^b Entrez Gene: KCNN4 potassium intermediate/small conductance calcium-activated channel, subfamily N, member 4.

[edit] 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.

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel