KCNMB2

From Wikipedia, the free encyclopedia

Potassium large conductance calcium-activated channel, subfamily M, beta member 2

PDB rendering based on 1jo6.

Available structures: 1jo6

Identifiers

Symbol(s)

KCNMB2; MGC22431

External IDs

OMIM: 605214 MGI: 1919663 HomoloGene: 4257

Gene ontology
Molecular Function:	• ion channel activity • ion channel inhibitor activity • calcium-activated potassium channel activity • potassium channel regulator activity
Cellular Component:	• voltage-gated potassium channel complex • membrane
Biological Process:	• regulation of action potential • detection of calcium ion • ion transport • potassium ion transport • smooth muscle contraction • generation of action potential • regulation of vasoconstriction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005832 (mRNA)
NP_005823 (protein)

NM_028231 (mRNA)
NP_082507 (protein)

Location

Chr 3: 180.01 - 180.04 Mb

Chr 3: 32.3 - 32.39 Mb

Pubmed search

[1]

[2]

Potassium large conductance calcium-activated channel, subfamily M, beta member 2, also known as KCNMB2, 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 and the modulatory beta subunit. The protein encoded by this gene is an auxiliary beta subunit which decreases the activation time of MaxiK alpha subunit currents. Two variants encoding the same protein have been found for this gene.^[1]

[edit] See also

[edit] References

^ ^a ^b Entrez Gene: KCNMB2 potassium large conductance calcium-activated channel, subfamily M, beta member 2.

[edit] Further reading

Orio P, Rojas P, Ferreira G, Latorre R (2002). "New disguises for an old channel: MaxiK channel beta-subunits.". News Physiol. Sci. 17: 156–61. PMID 12136044.
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.
Xia XM, Ding JP, Lingle CJ (1999). "Molecular basis for the inactivation of Ca2+- and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells.". J. Neurosci. 19 (13): 5255–64. PMID 10377337.
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.
Uebele VN, Lagrutta A, Wade T, et al. (2000). "Cloning and functional expression of two families of beta-subunits of the large conductance calcium-activated K+ channel.". J. Biol. Chem. 275 (30): 23211–8. doi:10.1074/jbc.M910187199. PMID 10766764.
Meera P, Wallner M, Toro L (2000). "A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin.". Proc. Natl. Acad. Sci. U.S.A. 97 (10): 5562–7. doi:10.1073/pnas.100118597. PMID 10792058.
Bentrop D, Beyermann M, Wissmann R, Fakler B (2001). "NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels.". J. Biol. Chem. 276 (45): 42116–21. doi:10.1074/jbc.M107118200. PMID 11517232.
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.
Xia XM, Ding JP, Lingle CJ (2003). "Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues.". J. Gen. Physiol. 121 (2): 125–48. PMID 12566540.
Hartness ME, Brazier SP, Peers C, et al. (2004). "Post-transcriptional control of human maxiK potassium channel activity and acute oxygen sensitivity by chronic hypoxia.". J. Biol. Chem. 278 (51): 51422–32. doi:10.1074/jbc.M309463200. PMID 14522958.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Orio P, Torres Y, Rojas P, et al. (2006). "Structural determinants for functional coupling between the beta and alpha subunits in the Ca2+-activated K+ (BK) channel.". J. Gen. Physiol. 127 (2): 191–204. doi:10.1085/jgp.200509370. PMID 16446507.
Zeng XH, Benzinger GR, Xia XM, Lingle CJ (2007). "BK channels with beta3a subunits generate use-dependent slow afterhyperpolarizing currents by an inactivation-coupled mechanism.". J. Neurosci. 27 (17): 4707–15. doi:10.1523/JNEUROSCI.0758-07.2007. PMID 17460083.
Zarei MM, Song M, Wilson RJ, et al. (2007). "Endocytic trafficking signals in KCNMB2 regulate surface expression of a large conductance voltage and Ca(2+)-activated K+ channel.". Neuroscience 147 (1): 80–9. doi:10.1016/j.neuroscience.2007.04.019. PMID 17521822.

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

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

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KCNMB2

From Wikipedia, the free encyclopedia

[edit] See also

[edit] References

[edit] Further reading

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