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   24-JAN-2024, entry version 113.
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}.
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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.ENSRNOP00000075448; -.
DR   ChEMBL; CHEMBL4523667; -.
DR   GlyCosmos; Q9ESK8; 2 sites, No reported glycans.
DR   GlyGen; Q9ESK8; 2 sites.
DR   PhosphoSitePlus; Q9ESK8; -.
DR   PaxDb; 10116-ENSRNOP00000038834; -.
DR   ABCD; Q9ESK8; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000085579.2; ENSRNOP00000075448.1; ENSRNOG00000054458.2.
DR   Ensembl; ENSRNOT00055021384; ENSRNOP00055017299; ENSRNOG00055012546.
DR   Ensembl; ENSRNOT00060016179; ENSRNOP00060012652; ENSRNOG00060009578.
DR   Ensembl; ENSRNOT00065022427; ENSRNOP00065017386; ENSRNOG00065013632.
DR   GeneID; 66016; -.
DR   KEGG; rno:66016; -.
DR   UCSC; RGD:620728; rat.
DR   AGR; RGD:620728; -.
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; 3976732at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q9ESK8; baseline and differential.
DR   GO; GO:0005886; C: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:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
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; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA; 1.
DR   PANTHER; PTHR10258:SF3; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA-4; 1.
DR   Pfam; PF03185; CaKB; 1.
DR   Genevisible; Q9ESK8; RN.
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
//