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Calcium-activated potassium channel subunit beta-4 (BK channel subunit beta-4) (BKbeta4) (Hbeta4) (Calcium-activated potassium channel, subfamily M subunit beta-4) (Charybdotoxin receptor subunit beta-4) (K(VCA)beta-4) (Maxi K channel subunit beta-4) (Slo-beta-4)

 KCMB4_HUMAN             Reviewed;         210 AA.
Q86W47; Q8IVR3; Q9NPA4; Q9P0G5;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
18-JUL-2018, entry version 118.
RecName: Full=Calcium-activated potassium channel subunit beta-4;
AltName: Full=BK channel subunit beta-4;
Short=BKbeta4;
Short=Hbeta4;
AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-4;
AltName: Full=Charybdotoxin receptor subunit beta-4;
AltName: Full=K(VCA)beta-4;
AltName: Full=Maxi K channel subunit beta-4;
AltName: Full=Slo-beta-4;
Name=KCNMB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, AND VARIANT
ILE-199.
PubMed=10792058; DOI=10.1073/pnas.100118597;
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. 97:5562-5567(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10828459; DOI=10.1016/S0014-5793(00)01584-2;
Behrens R., Nolting A., Reimann F., Schwarz M., Waldschuetz 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. 474:99-106(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KCNMA1, AND
TISSUE SPECIFICITY.
PubMed=10692449; DOI=10.1074/jbc.275.9.6453;
Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W.;
"Cloning and functional characterization of novel large conductance
calcium-activated potassium channel beta subunits, hKCNMB3 and
hKCNMB4.";
J. Biol. Chem. 275:6453-6461(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH KCNMA1.
TISSUE=CNS;
PubMed=10804197;
Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S.,
Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A.,
Silos-Santiago I., DiStefano P.S., Curtis R.;
"A novel nervous system beta subunit that downregulates human large
conductance calcium-dependent potassium channels.";
J. Neurosci. 20:3563-3570(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION, AND MUTAGENESIS OF THR-11; SER-17 AND SER-210.
PubMed=11790768; DOI=10.1074/jbc.M107682200;
Jin P., Weiger T.M., Wu Y., Levitan I.B.;
"Phosphorylation-dependent functional coupling of hSlo calcium-
dependent potassium channel and its hbeta 4 subunit.";
J. Biol. Chem. 277:10014-10020(2002).
[7]
GLYCOSYLATION, AND MUTAGENESIS OF ASN-53 AND ASN-90.
PubMed=12223479; DOI=10.1074/jbc.M205795200;
Jin P., Weiger T.M., Levitan I.B.;
"Reciprocal modulation between the alpha and beta 4 subunits of hSlo
calcium-dependent potassium channels.";
J. Biol. Chem. 277:43724-43729(2002).
[8]
REVIEW.
PubMed=12136044; DOI=10.1152/nips.01387.2002;
Orio P., Rojas P., Ferreira G., Latorre R.;
"New disguises for an old channel: MaxiK channel beta-subunits.";
News Physiol. Sci. 17:156-161(2002).
[9]
INTERACTION WITH FMR1.
PubMed=25561520; DOI=10.1073/pnas.1423094112;
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J.,
Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T.,
Klyachko V.A.;
"Independent role for presynaptic FMRP revealed by an FMR1 missense
mutation associated with intellectual disability and seizures.";
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015).
-!- 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. {ECO:0000269|PubMed:10692449,
ECO:0000269|PubMed:10792058, ECO:0000269|PubMed:10828459}.
-!- SUBUNIT: Interacts with KCNMA1 tetramer (PubMed:10692449,
PubMed:10804197). There are probably 4 molecules of KCMNB4 per
KCNMA1 tetramer (PubMed:10692449, PubMed:10804197). Interacts with
FMR1 (via N-terminus) (PubMed:25561520).
{ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:10804197,
ECO:0000269|PubMed:25561520}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Predominantly expressed in brain. In brain, it
is expressed in the cerebellum, cerebral cortex, medulla, spinal
cord, occipital pole, frontal lobe, temporal lobe, putamen,
amygdala, caudate nucleus, corpus callosum, hippocampus,
substantia nigra and thalamus. Weakly or not expressed in other
tissues. {ECO:0000269|PubMed:10692449,
ECO:0000269|PubMed:10828459}.
-!- DOMAIN: Resistance to charybdotoxin (CTX) toxin is mediated by the
extracellular domain.
-!- PTM: Phosphorylated. Phosphorylation modulates its effect on
KCNMA1 activation kinetics. {ECO:0000269|PubMed:11790768}.
-!- PTM: N-glycosylated. A highly glycosylated form is promoted by
KCNMA1. Glycosylation, which is not required for the interaction
with KCNMA1 and subcellular location, increases protection against
charybdotoxin. {ECO:0000269|PubMed:10792058,
ECO:0000269|PubMed:12223479}.
-!- MISCELLANEOUS: Treatment with okadaic acid reduces its effect on
KCNMA1.
-!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB4
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF160967; AAF69805.1; -; mRNA.
EMBL; AF170917; AAF89699.1; -; mRNA.
EMBL; AF207992; AAF28333.1; -; mRNA.
EMBL; AF215891; AAF75596.1; -; mRNA.
EMBL; BC042446; AAH42446.2; -; mRNA.
EMBL; BC050621; AAH50621.2; -; mRNA.
CCDS; CCDS8997.1; -.
RefSeq; NP_055320.4; NM_014505.5.
UniGene; Hs.525529; -.
ProteinModelPortal; Q86W47; -.
IntAct; Q86W47; 2.
STRING; 9606.ENSP00000258111; -.
DrugBank; DB01110; Miconazole.
DrugBank; DB00721; Procaine.
iPTMnet; Q86W47; -.
PhosphoSitePlus; Q86W47; -.
SwissPalm; Q86W47; -.
BioMuta; KCNMB4; -.
DMDM; 46395791; -.
EPD; Q86W47; -.
PaxDb; Q86W47; -.
PeptideAtlas; Q86W47; -.
PRIDE; Q86W47; -.
ProteomicsDB; 70115; -.
Ensembl; ENST00000258111; ENSP00000258111; ENSG00000135643.
GeneID; 27345; -.
KEGG; hsa:27345; -.
UCSC; uc001svx.4; human.
CTD; 27345; -.
DisGeNET; 27345; -.
EuPathDB; HostDB:ENSG00000135643.4; -.
GeneCards; KCNMB4; -.
HGNC; HGNC:6289; KCNMB4.
HPA; HPA072287; -.
MIM; 605223; gene.
neXtProt; NX_Q86W47; -.
OpenTargets; ENSG00000135643; -.
PharmGKB; PA30069; -.
eggNOG; ENOG410IJVB; Eukaryota.
eggNOG; ENOG410XSTD; LUCA.
GeneTree; ENSGT00390000015997; -.
HOGENOM; HOG000113205; -.
HOVERGEN; HBG052224; -.
InParanoid; Q86W47; -.
KO; K04941; -.
OMA; HEDERQL; -.
OrthoDB; EOG091G0MVO; -.
PhylomeDB; Q86W47; -.
TreeFam; TF328589; -.
Reactome; R-HSA-1296052; Ca2+ activated K+ channels.
Reactome; R-HSA-418457; cGMP effects.
ChiTaRS; KCNMB4; human.
GeneWiki; KCNMB4; -.
GenomeRNAi; 27345; -.
PRO; PR:Q86W47; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135643; -.
CleanEx; HS_KCNMB4; -.
ExpressionAtlas; Q86W47; baseline and differential.
Genevisible; Q86W47; HS.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
GO; GO:0001508; P:action potential; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0005513; P:detection of calcium ion; IDA:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:UniProtKB.
GO; GO:0019229; P:regulation of vasoconstriction; TAS:UniProtKB.
InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
PANTHER; PTHR10258; PTHR10258; 1.
Pfam; PF03185; CaKB; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 210 Calcium-activated potassium channel
subunit beta-4.
/FTId=PRO_0000187055.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 41 167 Extracellular. {ECO:0000255}.
TRANSMEM 168 188 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 189 210 Cytoplasmic. {ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
VARIANT 199 199 V -> I. {ECO:0000269|PubMed:10792058}.
/FTId=VAR_018178.
MUTAGEN 11 11 T->A: Suppresses the effect of okadaic
acid and increases activation time
constant; when associated with A-17 and
A-210. {ECO:0000269|PubMed:11790768}.
MUTAGEN 11 11 T->D: Suppresses its effect on KCNMA1
channel activation and on deactivation
kinetics; when associated with E-17 and
E-210. {ECO:0000269|PubMed:11790768}.
MUTAGEN 17 17 S->A: Suppresses the effect of okadaic
acid and increases activation time
constant; when associated with A-11 and
A-210. {ECO:0000269|PubMed:11790768}.
MUTAGEN 17 17 S->E: Suppresses its effect on KCNMA1
channel activation and on deactivation
kinetics; when associated with D-11 and
E-210. {ECO:0000269|PubMed:11790768}.
MUTAGEN 53 53 N->A: Loss of N-glycosylation and reduced
protection against charybdotoxin; when
associated with A-90.
{ECO:0000269|PubMed:12223479}.
MUTAGEN 90 90 N->A: Loss of N-glycosylation and reduced
protection against charybdotoxin; when
associated with A-53.
{ECO:0000269|PubMed:12223479}.
MUTAGEN 210 210 S->A: Suppresses the effect of okadaic
acid and increases activation time
constant; when associated with A-11 and
A-17. {ECO:0000269|PubMed:11790768}.
MUTAGEN 210 210 S->E: Suppresses its effect on KCNMA1
channel activation and on deactivation
kinetics; when associated with D-11 and
E-17. {ECO:0000269|PubMed:11790768}.
SEQUENCE 210 AA; 23949 MW; A59D56DD034F027A CRC64;
MAKLRVAYEY TEAEDKSIRL GLFLIISGVV SLFIFGFCWL SPALQDLQAT EANCTVLSVQ
QIGEVFECTF TCGADCRGTS QYPCVQVYVN NSESNSRALL HSDEHQLLTN PKCSYIPPCK
RENQKNLESV MNWQQYWKDE IGSQPFTCYF NQHQRPDDVL LHRTHDEIVL LHCFLWPLVT
FVVGVLIVVL TICAKSLAVK AEAMKKRKFS


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