ID KCMB3_RAT Reviewed; 239 AA.
AC A7VL23;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Calcium-activated potassium channel subunit beta-3;
DE AltName: Full=Calcium-activated potassium channel subfamily M subunit beta-3;
DE AltName: Full=Maxi K channel subunit beta-3;
GN Name=Kcnmb3 {ECO:0000312|EMBL:BAF79924.1};
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] {ECO:0000312|EMBL:BAF79924.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA Ishii H., Usui S., Sakuma Y.;
RT "Potassium large conductance calcium-activated channel, subfamily M, beta
RT member 3 (Kcnmb3).";
RL Submitted (MAR-2007) 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. Alters the
CC functional properties of the current expressed by the KCNMA1 channel.
CC May partially inactivate the current of KCNBMA. Two or more subunits of
CC KCNMB3 are required to block the KCNMA1 tetramer (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB3 per KCNMA1 tetramer (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NPA1}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- DOMAIN: The extracellular domain forms gates to block ion permeation,
CC providing a mechanism by which current can be rapidly diminished upon
CC cellular repolarization. {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- PTM: The extracellular domain contains disulfide bond essential for the
CC gating mechanism. {ECO:0000250|UniProtKB:Q9NPA1}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB3
CC subfamily. {ECO:0000305}.
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DR EMBL; AB297662; BAF79924.1; -; mRNA.
DR RefSeq; NP_001098030.1; NM_001104560.2.
DR AlphaFoldDB; A7VL23; -.
DR SMR; A7VL23; -.
DR STRING; 10116.ENSRNOP00000055650; -.
DR GlyCosmos; A7VL23; 3 sites, No reported glycans.
DR GlyGen; A7VL23; 3 sites.
DR PaxDb; 10116-ENSRNOP00000055650; -.
DR ABCD; A7VL23; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000058860.3; ENSRNOP00000055650.2; ENSRNOG00000027836.5.
DR GeneID; 310303; -.
DR KEGG; rno:310303; -.
DR UCSC; RGD:1311852; rat.
DR AGR; RGD:1311852; -.
DR CTD; 27094; -.
DR RGD; 1311852; Kcnmb3.
DR eggNOG; ENOG502QR4Z; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR HOGENOM; CLU_085739_1_0_1; -.
DR InParanoid; A7VL23; -.
DR OMA; KYSTAVR; -.
DR OrthoDB; 4267391at2759; -.
DR PhylomeDB; A7VL23; -.
DR TreeFam; TF328589; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:A7VL23; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000027836; Expressed in testis.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0005513; P:detection of calcium ion; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR PANTHER; PTHR10258; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA; 1.
DR PANTHER; PTHR10258:SF4; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA-3; 1.
DR Pfam; PF03185; CaKB; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..239
FT /note="Calcium-activated potassium channel subunit beta-3"
FT /id="PRO_0000312595"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 26447 MW; 090A87142030B2FC CRC64;
MQPFSIPVQI TLQGGRRRQG RTALPASGIS NGDPLKVHPK LPSSAGEDRA TLLGIAMMAS
SVLMFFLLGT TVLKPFMLSS PREESNCTTV HTHIADDWLD FAFTCEGSCQ GQGTYPCLQV
FVNLSHSGQK VLLHYDEEAI RTNPKCFYTP KCHGDRDHLL NSALDIKEFF DHNNGTFPCF
YSPDGPLGVV LRKSGHKVVF HCLFWPLLTL LGGALIVGLV RLTQHLSFQC EKYRAVVRA
//
