KCMB4_RAT
ID KCMB4_RAT Reviewed; 210 AA.
AC Q9ESK8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Ohya S., Ohi Y., Imaizumi Y.;
RT "Rat calcium activated potassium channel beta 4 subunit (KCNMB4).";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ha T.S., Park C.-S.;
RT "Molecular cloning of large-conductance calcium-activated potassium channel
RT beta 4 subunit from rat brain.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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. There are probably 4 molecules
CC of KCMNB4 per KCNMA1 tetramer. Interacts with FMR1 (via N-terminus).
CC {ECO:0000250|UniProtKB:Q86W47, ECO:0000250|UniProtKB:Q9JIN6}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB050637; BAB17595.1; -; mRNA.
DR EMBL; AY028605; AAK21964.1; -; mRNA.
DR RefSeq; NP_076450.1; NM_023960.2.
DR AlphaFoldDB; Q9ESK8; -.
DR SMR; Q9ESK8; -.
DR STRING; 10116.ENSRNOP00000038834; -.
DR ChEMBL; CHEMBL4523667; -.
DR GlyGen; Q9ESK8; 2 sites.
DR PaxDb; Q9ESK8; -.
DR ABCD; Q9ESK8; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000085579; ENSRNOP00000075448; ENSRNOG00000054458.
DR GeneID; 66016; -.
DR KEGG; rno:66016; -.
DR UCSC; RGD:620728; rat.
DR CTD; 27345; -.
DR RGD; 620728; Kcnmb4.
DR eggNOG; ENOG502QR4Z; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR HOGENOM; CLU_085739_0_0_1; -.
DR InParanoid; Q9ESK8; -.
DR OMA; PDDVLWQ; -.
DR OrthoDB; 1178937at2759; -.
DR PhylomeDB; Q9ESK8; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:Q9ESK8; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000054458; Expressed in frontal cortex and 15 other tissues.
DR ExpressionAtlas; Q9ESK8; baseline and differential.
DR Genevisible; Q9ESK8; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000187057"
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; 23885 MW; 11D49F58F9C6F1D4 CRC64;
MAKLRVSYEY TEAEDKSIRL GLFLIVSGIL SLFIFGFCWL SPALQDLQAT AANCTVLSVQ
QIGEVFECTF TCGTDCRGTS QYPCVQVYVN NSESNSRALL HSDQHQLLTN PKCSYIPPCK
RENQKNSESV MNWQQYWKDE IGSQPFTCYF NQHQRPEDVL LQRTHDEIVL LHCFLWPVVA
FVVGVLIVVL TICAKSLAVK AEAMKKRKFS
