KCNMA1

From Wikipedia, the free encyclopedia

Potassium large conductance calcium-activated channel, subfamily M, alpha member 1

Identifiers

KCNMA1; BKTM; DKFZp686K1437; KCa1.1; MGC71881; MaxiK; SAKCA; SLO; SLO-ALPHA

External IDs

OMIM: 600150 MGI: 99923 HomoloGene: 1693

Gene ontology
Molecular Function:	• magnesium ion binding • ion channel activity • voltage-gated potassium channel activity • calcium ion binding • protein binding • calcium-activated potassium channel activity • potassium ion binding
Cellular Component:	• voltage-gated potassium channel complex • membrane • integral to membrane
Biological Process:	• ion transport • potassium ion transport • muscle contraction • synaptic transmission • neurotransmitter secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001014797 (mRNA)
NP_001014797 (protein)

NM_010610 (mRNA)
NP_034740 (protein)

Location

Chr 10: 78.31 - 79.07 Mb

Chr 14: 22.08 - 22.79 Mb

Pubmed search

[1]

[2]

Potassium large conductance calcium-activated channel, subfamily M, alpha member 1, also known as KCNMA1, is a human gene.^[1]

MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit, which is the product of this gene, and the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.^[1]

[edit] See also

[edit] References

^ ^a ^b Entrez Gene: KCNMA1 potassium large conductance calcium-activated channel, subfamily M, alpha member 1.

[edit] Further reading

Magleby KL (2003). "Gating mechanism of BK (Slo1) channels: so near, yet so far.". J. Gen. Physiol. 121 (2): 81-96. PMID 12566537.
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.
McCobb DP, Fowler NL, Featherstone T, et al. (1995). "A human calcium-activated potassium channel gene expressed in vascular smooth muscle.". Am. J. Physiol. 269 (3 Pt 2): H767-77. PMID 7573516.
Butler A, Tsunoda S, McCobb DP, et al. (1993). "mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels.". Science 261 (5118): 221-4. PMID 7687074.
Dworetzky SI, Trojnacki JT, Gribkoff VK (1995). "Cloning and expression of a human large-conductance calcium-activated potassium channel.". Brain Res. Mol. Brain Res. 27 (1): 189-93. PMID 7877450.
Pallanck L, Ganetzky B (1995). "Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke.". Hum. Mol. Genet. 3 (8): 1239-43. PMID 7987297.
Tseng-Crank J, Foster CD, Krause JD, et al. (1995). "Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain.". Neuron 13 (6): 1315-30. PMID 7993625.
Knaus HG, Folander K, Garcia-Calvo M, et al. (1994). "Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle.". J. Biol. Chem. 269 (25): 17274-8. PMID 8006036.
Meera P, Wallner M, Jiang Z, Toro L (1996). "A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels.". FEBS Lett. 382 (1-2): 84-8. PMID 8612769.
Wallner M, Meera P, Ottolia M, et al. (1996). "Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium.". Recept. Channels 3 (3): 185-99. PMID 8821792.
Wallner M, Meera P, Toro L (1997). "Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus.". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14922-7. PMID 8962157.
Meera P, Wallner M, Song M, Toro L (1998). "Large conductance voltage- and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus.". Proc. Natl. Acad. Sci. U.S.A. 94 (25): 14066-71. PMID 9391153.
Díaz L, Meera P, Amigo J, et al. (1999). "Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel.". J. Biol. Chem. 273 (49): 32430-6. PMID 9829973.
Wallner M, Meera P, Toro L (1999). "Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog.". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 4137-42. PMID 10097176.
Valverde MA, Rojas P, Amigo J, et al. (1999). "Acute activation of Maxi-K channels (hSlo) by estradiol binding to the beta subunit.". Science 285 (5435): 1929-31. PMID 10489376.
Brenner R, Jegla TJ, Wickenden A, et al. (2000). "Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4.". J. Biol. Chem. 275 (9): 6453-61. PMID 10692449.
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.
Quirk JC, Reinhart PH (2001). "Identification of a novel tetramerization domain in large conductance K(ca) channels.". Neuron 32 (1): 13-23. PMID 11604135.
Soto MA, González C, Lissi E, et al. (2002). "Ca(2+)-activated K+ channel inhibition by reactive oxygen species.". Am. J. Physiol., Cell Physiol. 282 (3): C461-71. doi:10.1152/ajpcell.00167.2001. PMID 11832330.
Wang YW, Ding JP, Xia XM, Lingle CJ (2002). "Consequences of the stoichiometry of Slo1 alpha and auxiliary beta subunits on functional properties of large-conductance Ca2+-activated K+ channels.". J. Neurosci. 22 (5): 1550-61. PMID 11880485.

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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