Calcium-activated potassium channel subunit beta-4

Details

Name
Calcium-activated potassium channel subunit beta-4
Kind
protein
Synonyms
  • BK channel subunit beta-4
  • BKbeta4
  • Calcium-activated potassium channel, subfamily M subunit beta-4
  • Charybdotoxin receptor subunit beta-4
  • Hbeta4
  • K(VCA)beta-4
  • Maxi K channel subunit beta-4
  • Slo-beta-4
Gene Name
KCNMB4
UniProtKB Entry
Q86W47Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0013100|Calcium-activated potassium channel subunit beta-4
MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQ
QIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCK
RENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVT
FVVGVLIVVLTICAKSLAVKAEAMKKRKFS
Number of residues
210
Molecular Weight
23948.465
Theoretical pI
6.75
GO Classification
Functions
voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential
Processes
chemical synaptic transmission
Components
synapse
General Function
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations
Specific Function
Calcium-activated potassium channel activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
20-40 168-188
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0013101|Calcium-activated potassium channel subunit beta-4 (KCNMB4)
ATGGCGAAGCTCCGGGTGGCTTACGAGTACACGGAAGCCGAGGACAAGAGCATCCGGCTC
GGCTTGTTTCTCATCATCTCCGGCGTCGTGTCGCTCTTCATCTTCGGCTTCTGCTGGCTG
AGTCCCGCGCTGCAGGATCTGCAAGCCACGGAGGCCAATTGCACGGTGCTGTCGGTGCAG
CAGATCGGCGAGGTGTTCGAGTGCACCTTCACCTGTGGCGCCGACTGCAGGGGCACCTCG
CAGTACCCCTGCGTCCAGGTCTACGTGAACAACTCTGAGTCCAACTCTAGGGCGCTGCTG
CACAGCGACGAGCACCAGCTCCTGACCAACCCCAAGTGCTCCTATATCCCTCCCTGTAAG
AGAGAAAATCAGAAGAATTTGGAAAGTGTCATGAATTGGCAACAGTACTGGAAAGATGAG
ATTGGTTCCCAGCCATTTACTTGCTATTTTAATCAACATCAAAGACCAGATGATGTGCTT
CTGCATCGCACTCATGATGAGATTGTCCTCCTGCATTGCTTCCTCTGGCCCCTGGTGACA
TTTGTGGTGGGCGTTCTCATTGTGGTCCTGACCATCTGTGCCAAGAGCTTGGCGGTCAAG
GCGGAAGCCATGAAGAAGCGCAAGTTCTCTTAA
Chromosome Location
12
Locus
12q15
External Identifiers
ResourceLink
UniProtKB IDQ86W47
UniProtKB Entry NameKCMB4_HUMAN
GenBank Protein ID7799988
GenBank Gene IDAF160967
GeneCard IDKCNMB4
HGNC IDHGNC:6289
PDB ID(s)5Y7L, 6V22, 6V35
KEGG IDhsa:27345
NCBI Gene ID27345
General References
  1. Meera P, Wallner M, Toro L: 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. 2000 May 9;97(10):5562-7. [Article]
  2. Behrens R, Nolting A, Reimann F, Schwarz M, Waldschutz R, Pongs O: hKCNMB3 and hKCNMB4, cloning and characterization of two members of the large-conductance calcium-activated potassium channel beta subunit family. FEBS Lett. 2000 May 26;474(1):99-106. [Article]
  3. Brenner R, Jegla TJ, Wickenden A, Liu Y, Aldrich RW: Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4. J Biol Chem. 2000 Mar 3;275(9):6453-61. [Article]
  4. Weiger TM, Holmqvist MH, Levitan IB, Clark FT, Sprague S, Huang WJ, Ge P, Wang C, Lawson D, Jurman ME, Glucksmann MA, Silos-Santiago I, DiStefano PS, Curtis R: A novel nervous system beta subunit that downregulates human large conductance calcium-dependent potassium channels. J Neurosci. 2000 May 15;20(10):3563-70. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Jin P, Weiger TM, Wu Y, Levitan IB: Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit. J Biol Chem. 2002 Mar 22;277(12):10014-20. Epub 2002 Jan 14. [Article]
  7. Jin P, Weiger TM, Levitan IB: Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels. J Biol Chem. 2002 Nov 15;277(46):43724-9. Epub 2002 Sep 9. [Article]
  8. Orio P, Rojas P, Ferreira G, Latorre R: New disguises for an old channel: MaxiK channel beta-subunits. News Physiol Sci. 2002 Aug;17:156-61. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Tetraethylammoniumexperimental, investigationalyestargetinhibitorDetails