KCNMB4
Potassium large conductance calcium-activated channel, subfamily M, beta member 4 | |||||||||||||
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Identifiers | |||||||||||||
Symbol | KCNMB4 | ||||||||||||
External IDs | OMIM: 605223 MGI: 1913272 HomoloGene: 8721 GeneCards: KCNMB4 Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 27345 | 58802 | |||||||||||
Ensembl | ENSG00000135643 | ENSMUSG00000054934 | |||||||||||
UniProt | Q86W47 | Q9JIN6 | |||||||||||
RefSeq (mRNA) | NM_014505 | NM_021452 | |||||||||||
RefSeq (protein) | NP_055320 | NP_067427 | |||||||||||
Location (UCSC) | Chr 12: 70.76 – 70.83 Mb | Chr 10: 116.42 – 116.47 Mb | |||||||||||
PubMed search | |||||||||||||
Calcium-activated potassium channel subunit beta-4 is a protein that in humans is encoded by the KCNMB4 gene.[1][2][3]
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 slows activation kinetics, leads to steeper calcium sensitivity, and shifts the voltage range of current activation to more negative potentials than does the beta 1 subunit.[3]
See also
References
- ↑ Brenner R, Jegla TJ, Wickenden A, Liu Y, Aldrich RW (Apr 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.
- ↑ Behrens R, Nolting A, Reimann F, Schwarz M, Waldschutz R, Pongs O (Jul 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.
- ↑ 3.0 3.1 "Entrez Gene: KCNMB4 potassium large conductance calcium-activated channel, subfamily M, beta member 4".
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.
- 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.
- Meera P, Wallner M, Toro L (2000). "A neuronal β 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.
- Weiger TM, Holmqvist MH, Levitan IB et al. (2000). "A novel nervous system beta subunit that downregulates human large conductance calcium-dependent potassium channels". J. Neurosci. 20 (10): 3563–70. PMID 10804197.
- Jin P, Weiger TM, Wu Y, Levitan IB (2002). "Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit". J. Biol. Chem. 277 (12): 10014–20. doi:10.1074/jbc.M107682200. PMID 11790768.
- Jin P, Weiger TM, Levitan IB (2003). "Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels". J. Biol. Chem. 277 (46): 43724–9. doi:10.1074/jbc.M205795200. PMID 12223479.
- 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.
- 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. PMC 528928. PMID 15489334.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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