KCNMB2

Protein-coding gene in the species Homo sapiens
KCNMB2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JO6

Identifiers
AliasesKCNMB2, potassium calcium-activated channel subfamily M regulatory beta subunit 2
External IDsOMIM: 605214; MGI: 1919663; HomoloGene: 4257; GeneCards: KCNMB2; OMA:KCNMB2 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for KCNMB2
Genomic location for KCNMB2
Band3q26.32Start178,272,932 bp[1]
End178,844,429 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for KCNMB2
Genomic location for KCNMB2
Band3|3 A3Start31,956,656 bp[2]
End32,254,329 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • right uterine tube

  • bronchial epithelial cell

  • caput epididymis

  • corpus epididymis

  • cingulate gyrus

  • prefrontal cortex

  • Brodmann area 23

  • Brodmann area 9

  • smooth muscle tissue
Top expressed in
  • trigeminal ganglion

  • islet of Langerhans

  • olfactory epithelium

  • superior cervical ganglion

  • secondary oocyte

  • carotid body

  • neural tube

  • pituitary gland

  • substantia nigra

  • lateral geniculate nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • potassium channel regulator activity
  • calcium-activated potassium channel activity
  • ion channel inhibitor 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
  • potassium ion transport
  • regulation of vasoconstriction
  • ion transport
  • neuronal action potential
  • chemical synaptic transmission
  • potassium ion transmembrane transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10242

72413

Ensembl

ENSG00000197584

ENSMUSG00000037610

UniProt

Q9Y691

Q9CZM9

RefSeq (mRNA)

NM_001278911
NM_005832
NM_181361

NM_028231

RefSeq (protein)

NP_001265840
NP_005823
NP_852006

NP_082507

Location (UCSC)Chr 3: 178.27 – 178.84 MbChr 3: 31.96 – 32.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
KCNMB2, ball and chain domain
solution structure of the cytoplasmic n-terminus of the bk beta-subunit kcnmb2
Identifiers
SymbolKcnmB2_inactiv
PfamPF09303
InterProIPR015382
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Calcium-activated potassium channel subunit beta-2 is a protein that in humans is encoded by the KCNMB2 gene.[5][6]

Big Potassium (BK) channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. BK channels can contain two distinct subunits: a pore-forming alpha subunit and a modulatory beta subunit. Each complete BK channel contains four copies of the pore-forming alpha subunit and up to four beta subunits. The protein encoded by the KCNMB2 gene is an auxiliary beta subunit which influences the calcium sensitivity of BK currents and, following activation of BK current, causes persistent inactivation. The subunit encoded by the KCNMB2 gene is expressed in various endocrine cells, including pancreas and adrenal chromaffin cells. It is also found in the brain, including the hippocampus. The KCNMB2 gene is homologous to three other genes found in mammalian genomes: KCNMB1 (found primarily in smooth muscle), KCNMB3, and KCNMB4 (the primary brain BK auxiliary subunit).[6]

Calcium-activated potassium channel subunit beta-2 comprises two domains. An N-terminal cytoplasmic domain, the ball and chain domain, which is responsible for the fast inactivation of these channels,[7] and a C-terminal calcium-activated potassium channel beta subunit domain. The N-terminal domain only occurs in calcium-activated potassium channel subunit beta-2, while the C-terminal domain is found in related proteins.

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197584 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037610 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wallner M, Meera P, Toro L (May 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. Bibcode:1999PNAS...96.4137W. doi:10.1073/pnas.96.7.4137. PMC 22433. PMID 10097176.
  6. ^ a b "Entrez Gene: KCNMB2 potassium large conductance calcium-activated channel, subfamily M, beta member 2".
  7. ^ Bentrop D, Beyermann M, Wissmann R, Fakler B (November 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.

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 (4): 156–61. doi:10.1152/nips.01387.2002. hdl:10533/173696. PMID 12136044.
  • 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. doi:10.1523/JNEUROSCI.19-13-05255.1999. PMC 6782330. 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. 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. Bibcode:2000PNAS...97.4832L. 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. Bibcode:2000PNAS...97.5562M. doi:10.1073/pnas.100118597. PMC 25868. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. doi:10.1085/jgp.20028667. PMC 2217327. 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. PMC 528928. 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. PMC 2151488. 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. PMC 6672991. 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. S2CID 24449192.

External links

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

  • v
  • t
  • e
  • 1jo6: Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2
    1jo6: Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2
  • v
  • t
  • e
Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl−: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders
This article incorporates text from the public domain Pfam and InterPro: IPR015382


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