KCNMB3

Potassium large conductance calcium-activated channel, subfamily M beta member 3

Identifiers

KCNMB3; BKBETA3; HBETA3; KCNMB2; KCNMBL; SLOBETA3

External IDs

OMIM: 605222 MGI: 3612244 HomoloGene: 18141 GeneCards: KCNMB3 Gene

Gene Ontology
Molecular function	• ion channel activity • calcium-activated potassium channel activity • potassium channel regulator activity
Cellular component	• integral to plasma membrane • voltage-gated potassium channel complex • membrane
Biological process	• regulation of action potential • detection of calcium ion • ion transport • potassium ion transport • blood coagulation • regulation of action potential in neuron • platelet activation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
178.96 – 178.98 Mb

Chr 3:
32.37 – 32.39 Mb

PubMed search

[1]

[2]

Calcium-activated potassium channel subunit beta-3 is a protein that in humans is encoded by the KCNMB3 gene.^[1]^[2]

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 may partially inactivate or slightly decrease the activation time of MaxiK alpha subunit currents. At least four transcript variants encoding four different isoforms have been found for this gene.^[2]

References

^ Riazi MA, Brinkman-Mills P, Johnson A, Naylor SL, Minoshima S, Shimizu N, Baldini A, McDermid HE (Feb 2000). "Identification of a putative regulatory subunit of a calcium-activated potassium channel in the dup(3q) syndrome region and a related sequence on 22q11.2". Genomics 62 (1): 90–4. doi:10.1006/geno.1999.5975. PMID 10585773.
^ ^a ^b "Entrez Gene: KCNMB3 potassium large conductance calcium-activated channel, subfamily M beta member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27094.

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.
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. doi:10.1074/jbc.275.9.6453. 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. PMC 18318. PMID 10758170. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18318.
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. PMC 25868. PMID 10792058. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25868.
Behrens R, Nolting A, Reimann F, et al. (2000). "hKCNMB3 and hKCNMB4, cloning and characterization of two members of the large-conductance calcium-activated potassium channel beta subunit family.". FEBS Lett. 474 (1): 99–106. doi:10.1016/S0014-5793(00)01584-2. PMID 10828459.
Xia XM, Ding JP, Zeng XH, et al. (2000). "Rectification and rapid activation at low Ca2+ of Ca2+-activated, voltage-dependent BK currents: consequences of rapid inactivation by a novel beta subunit.". J. Neurosci. 20 (13): 4890–903. PMID 10864947.
Lingle CJ, Zeng XH, Ding JP, Xia XM (2001). "Inactivation of BK channels mediated by the NH(2) terminus of the beta3b auxiliary subunit involves a two-step mechanism: possible separation of binding and blockade.". J. Gen. Physiol. 117 (6): 583–606. doi:10.1085/jgp.117.6.583. PMC 2232400. PMID 11382808. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2232400.
Zeng XH, Ding JP, Xia XM, Lingle CJ (2001). "Gating properties conferred on BK channels by the beta3b auxiliary subunit in the absence of its NH(2)- and COOH termini.". J. Gen. Physiol. 117 (6): 607–28. doi:10.1085/jgp.117.6.607. PMC 2232397. PMID 11382809. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2232397.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Zeng XH, Xia XM, Lingle CJ (2003). "Redox-sensitive extracellular gates formed by auxiliary beta subunits of calcium-activated potassium channels.". Nat. Struct. Biol. 10 (6): 448–54. doi:10.1038/nsb932. PMID 12740608.
Hu S, Labuda MZ, Pandolfo M, et al. (2003). "Variants of the KCNMB3 regulatory subunit of maxi BK channels affect channel inactivation.". Physiol. Genomics 15 (3): 191–8. doi:10.1152/physiolgenomics.00110.2003. PMID 14612589.
Lorenz S, Heils A, Kasper JM, Sander T (2007). "Allelic association of a truncation mutation of the KCNMB3 gene with idiopathic generalized epilepsy.". Am. J. Med. Genet. B Neuropsychiatr. Genet. 144 (1): 10–3. doi:10.1002/ajmg.b.30369. PMID 16958040.

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

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Voltage-gated	L-type/Ca_vα (1.1, 1.2, 1.3, 1.4) · N-type/Ca_vα2.2 · P-type/Ca_vα(2.1) · Q-type/Ca_vα2.1 · R-type/Ca_vα2.3 · T-type/Ca_vα(3.1, 3.2, 3.3) α₂δ-subunits (1, 2) · β-subunits (β1, β2, β3, β4) · γ-subunits (γ1, γ2, γ3, γ4) Cation channels of sperm (1, 2, 3, 4) · Two-pore channel (1, 2)

Ligand-gated	Inositol trisphosphate receptor (1, 2, 3) · Ryanodine receptor (1, 2, 3)

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel (α, β, γ, δ)

Proton gated	Amiloride-sensitive cation channel (1, 2, 3, 4)

Voltage-gated	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Na_vβ (1, 2, 3, 4)

K⁺: Potassium channel

Voltage-gated	K_vα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (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) K_vα7-12 (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) K_vβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene

Calcium-activated	BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3, SK4) · K_Ca (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1)

Inward-rectifier	K_ATP · K_ir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/K_ir (3.1, 3.2, 3.3, 3.4) · K_ir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)

Tandem pore domain	K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)

Other

Cl^-: Chloride channel	ANO1 · Bestrophin (1, 2) · 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)

H⁺: Voltage-gated	HVCN1

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) · TRPN · TRPP (1, 2) · TRPV (1, 2, 3, 4, 5, 6)

Cyclic nucleotide-gated (FC)	α (1, 2, 3, 4) · β (1, 2, 3) · HCN (1, 2, 3, 4)

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) · Voltage-dependent anion channel (1, 2, 3) · General bacterial porin family

Gap junction	Connexin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) · B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) · C (GJC1, GJC2, GJC3) · D (GJD2, GJD3, GJD4)) Innexin

General	Ligand-gated ion channel · Voltage-gated ion channel · Stretch-activated ion channel

see also disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

KCNMB3

See also

References

Further reading