ID A0A091DYY0_FUKDA Unreviewed; 200 AA.
AC A0A091DYY0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Calcium-activated potassium channel subunit beta {ECO:0000256|RuleBase:RU368097};
DE Short=BKbeta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=BK channel subunit beta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=Charybdotoxin receptor subunit beta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=K(VCA)beta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=Maxi K channel subunit beta {ECO:0000256|RuleBase:RU368097};
DE AltName: Full=Slo-beta {ECO:0000256|RuleBase:RU368097};
DE Flags: Fragment;
GN ORFNames=H920_02324 {ECO:0000313|EMBL:KFO36262.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO36262.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36262.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36262.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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.
CC {ECO:0000256|RuleBase:RU368097}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB per KCNMA1 tetramer. {ECO:0000256|RuleBase:RU368097}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU368097}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368097}.
CC -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU368097}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family.
CC {ECO:0000256|RuleBase:RU368097}.
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DR EMBL; KN121518; KFO36262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DYY0; -.
DR STRING; 885580.ENSFDAP00000007502; -.
DR eggNOG; ENOG502QR4Z; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005513; P:detection of calcium ion; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|RuleBase:RU368097};
KW Ion channel {ECO:0000256|RuleBase:RU368097, ECO:0000313|EMBL:KFO36262.1};
KW Ion transport {ECO:0000256|RuleBase:RU368097};
KW Membrane {ECO:0000256|RuleBase:RU368097};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transmembrane {ECO:0000256|RuleBase:RU368097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU368097};
KW Transport {ECO:0000256|RuleBase:RU368097}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368097"
FT TRANSMEM 164..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368097"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO36262.1"
SQ SEQUENCE 200 AA; 22691 MW; 326168F31A449B5A CRC64;
TEAEDKSIRL GLFLIISGVV SLFIFGFCWL SPALQDLQAT AANCTVLSVQ QIGEVFECTF
TCGADCRGTS QYPCVQVYVN NSESNSRALL HSDEHQLLTN PKCSYIPPCK RENQKNLESV
MNWQQYWKDE IGSQPFTCYF NQYQRPDDVL LHRTHDEIVL LHCFLWPLVT FVVGVLIVVL
TICAKSLAVK AEAMKKRKFS
//
