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   03-AUG-2022, entry version 80.
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   GlyGen; A7VL23; 3 sites.
DR   PaxDb; A7VL23; -.
DR   ABCD; A7VL23; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000058860; ENSRNOP00000055650; ENSRNOG00000027836.
DR   GeneID; 310303; -.
DR   KEGG; rno:310303; -.
DR   UCSC; RGD:1311852; rat.
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; DDWMDCA; -.
DR   OrthoDB; 1178937at2759; -.
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:0005887; C:integral component of 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; PTHR10258; 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