KCNMB3

Identifiers

KCNMB3, BKBETA3, HBETA3, K(VCA)BETA-3, KCNMB2, KCNMBL, SLO-BETA-3, SLOBETA3, potassium calcium-activated channel subfamily M regulatory beta subunit 3

External IDs

MGI: 3612244 HomoloGene: 18141 GeneCards: KCNMB3

Gene ontology
Molecular function	• calcium-activated potassium channel activity • potassium channel regulator activity
Cellular component	• integral component of membrane • voltage-gated potassium channel complex • plasma membrane • integral component of plasma membrane • membrane
Biological process	• detection of calcium ion • action potential • ion transport • neuronal action potential • transport • potassium ion transport • potassium ion transmembrane transport • chemical synaptic transmission
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


27094


100502876

Ensembl


ENSG00000171121


ENSMUSG00000091091

UniProt


Q9NPA1


n/a

RefSeq (mRNA)


NM_001163677 NM_014407 NM_171828 NM_171829 NM_171830


NM_001195074

RefSeq (protein)


NP_001157149.1 NP_055222.3 NP_741979.1 NP_741980.1 NP_741981.1


n/a

Location (UCSC)

Chr 3: 179.24 – 179.27 Mb

Chr 3: 32.47 – 32.49 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Calcium-activated potassium channel subunit beta-3 is a protein that in humans is encoded by the KCNMB3 gene.^[3]^[4]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: KCNMB3 potassium large conductance calcium-activated channel, subfamily M beta member 3".

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. doi:10.1152/nips.01387.2002. 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.
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.
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.
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.
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.
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

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

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

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

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 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

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

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

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

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: 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

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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KCNMB3

See also

References

Further reading