KCMB4_MOUSE
ID KCMB4_MOUSE Reviewed; 210 AA.
AC Q9JIN6; Q149I1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Calcium-activated potassium channel subunit beta-4;
DE AltName: Full=BK channel subunit beta-4;
DE Short=BKbeta4;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-4;
DE AltName: Full=Charybdotoxin receptor subunit beta-4;
DE AltName: Full=K(VCA)beta-4;
DE AltName: Full=Maxi K channel subunit beta-4;
DE AltName: Full=Slo-beta-4;
GN Name=Kcnmb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH KCNMA1.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10804197; DOI=10.1523/jneurosci.20-10-03563.2000;
RA Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S.,
RA Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A.,
RA Silos-Santiago I., DiStefano P.S., Curtis R.;
RT "A novel nervous system beta subunit that downregulates human large
RT conductance calcium-dependent potassium channels.";
RL J. Neurosci. 20:3563-3570(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH FMR1.
RX PubMed=25561520; DOI=10.1073/pnas.1423094112;
RA Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J.,
RA Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T.,
RA Klyachko V.A.;
RT "Independent role for presynaptic FMRP revealed by an FMR1 missense
RT mutation associated with intellectual disability and seizures.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015).
CC -!- FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1
CC (maxiK) channel. Modulates the calcium sensitivity and gating kinetics
CC of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases
CC the gating kinetics and calcium sensitivity of the KCNMA1 channel, but
CC with fast deactivation kinetics. May decrease KCNMA1 channel openings
CC at low calcium concentrations but increases channel openings at high
CC calcium concentrations. Makes KCNMA1 channel resistant to 100 nM
CC charybdotoxin (CTX) toxin concentrations (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer (PubMed:10804197). There are
CC probably 4 molecules of KCMNB4 per KCNMA1 tetramer (PubMed:10804197).
CC Interacts with FMR1 (via N-terminus) (PubMed:25561520).
CC {ECO:0000269|PubMed:10804197, ECO:0000269|PubMed:25561520}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: Resistance to charybdotoxin (CTX) toxin is mediated by the
CC extracellular domain. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation modulates its effect on KCNMA1
CC activation kinetics (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. A highly glycosylated form is promoted by KCNMA1.
CC Glycosylation, which is not required for the interaction with KCNMA1
CC and subcellular location, increases protection against charybdotoxin
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB4
CC subfamily. {ECO:0000305}.
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DR EMBL; AF215892; AAF75597.1; -; mRNA.
DR EMBL; BC117779; AAI17780.1; -; mRNA.
DR CCDS; CCDS24184.1; -.
DR RefSeq; NP_067427.1; NM_021452.1.
DR AlphaFoldDB; Q9JIN6; -.
DR SMR; Q9JIN6; -.
DR BioGRID; 208440; 1.
DR IntAct; Q9JIN6; 1.
DR STRING; 10090.ENSMUSP00000065384; -.
DR TCDB; 8.A.14.1.1; the ca(2+)-activated k(+) channel auxiliary subunit slowpoke-Beta (sloBeta) family.
DR GlyGen; Q9JIN6; 2 sites.
DR PhosphoSitePlus; Q9JIN6; -.
DR PaxDb; Q9JIN6; -.
DR PRIDE; Q9JIN6; -.
DR ProteomicsDB; 269255; -.
DR ABCD; Q9JIN6; 1 sequenced antibody.
DR Antibodypedia; 29474; 181 antibodies from 30 providers.
DR DNASU; 58802; -.
DR Ensembl; ENSMUST00000068233; ENSMUSP00000065384; ENSMUSG00000054934.
DR GeneID; 58802; -.
DR KEGG; mmu:58802; -.
DR UCSC; uc007hbw.1; mouse.
DR CTD; 27345; -.
DR MGI; MGI:1913272; Kcnmb4.
DR VEuPathDB; HostDB:ENSMUSG00000054934; -.
DR eggNOG; ENOG502QR4Z; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR HOGENOM; CLU_085739_0_0_1; -.
DR InParanoid; Q9JIN6; -.
DR OMA; PDDVLWQ; -.
DR OrthoDB; 1178937at2759; -.
DR PhylomeDB; Q9JIN6; -.
DR TreeFam; TF328589; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 58802; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnmb4; mouse.
DR PRO; PR:Q9JIN6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JIN6; protein.
DR Bgee; ENSMUSG00000054934; Expressed in primary motor cortex and 223 other tissues.
DR Genevisible; Q9JIN6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IGI:MGI.
DR GO; GO:0005267; F:potassium channel activity; ISS:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; ISS:UniProtKB.
DR GO; GO:0005513; P:detection of calcium ion; ISS:UniProtKB.
DR GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR PANTHER; PTHR10258; PTHR10258; 1.
DR Pfam; PF03185; CaKB; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..210
FT /note="Calcium-activated potassium channel subunit beta-4"
FT /id="PRO_0000187056"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23857 MW; 11C73DD2C2C6F1D4 CRC64;
MAKLRVSYEY TEAEDKSIRL GLFLIVSGIL SLFIFGFCWL SPALQDLQAT AANCTVLSVQ
QIGEVFECTF TCGTDCRGTS QYPCVQVYVN NSESNSRALL HSDQHQLLTN PKCSYIPPCK
RENQKNSESV MNWQQYWKDE IGSQPFTCYF NQHQRPEDVL LQRTHDEIAL LHCFLWPVVA
FVVGVLIVVL TICAKSLAVK AEAMKKRKFS
