KCMB2_RAT
ID KCMB2_RAT Reviewed; 235 AA.
AC Q811Q0; Q8CF83;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Calcium-activated potassium channel subunit beta-2;
DE AltName: Full=BK channel subunit beta-2;
DE Short=BKbeta2;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-2;
DE AltName: Full=Charybdotoxin receptor subunit beta-2;
DE AltName: Full=K(VCA)beta-2;
DE AltName: Full=Maxi K channel subunit beta-2;
DE AltName: Full=Rbeta3;
DE AltName: Full=Slo-beta-2;
GN Name=Kcnmb2;
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 STRAIN=Sprague-Dawley; TISSUE=Heart;
RA Eghbali M., Foroughi S., Toro L., Stefani E.;
RT "Rat inactivating beta 2 subunit of large conductance Ca2+-activated K+
RT channel (KCNMB2, rSlo beta 2 subunit).";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-201.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=12454985; DOI=10.1002/cne.10471;
RA Langer P., Gruender S., Ruesch A.;
RT "Expression of a Ca2+-activated BK channel mRNA and its splice variants in
RT the rat cochlea.";
RL J. Comp. Neurol. 455:198-209(2003).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10377337; DOI=10.1523/jneurosci.19-13-05255.1999;
RA Xia X.-M., Ding J.-P., Lingle C.J.;
RT "Molecular basis for the inactivation of Ca2+- and voltage-dependent BK
RT channels in adrenal chromaffin cells and rat insulinoma tumor cells.";
RL J. Neurosci. 19:5255-5264(1999).
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. Acts as a
CC negative regulator that confers rapid and complete inactivation of
CC KCNMA1 channel complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB2 per KCNMA1 tetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and heart. Also expressed
CC in lung. {ECO:0000269|PubMed:10377337}.
CC -!- DOMAIN: The ball and chain domain mediates the inactivation of KCNMA1.
CC It occludes the conduction pathway of KCNMA1 channels, and comprises
CC the pore-blocking ball domain (residues 1-17) and the chain domain
CC (residues 20-45) linking it to the transmembrane segment. The ball
CC domain is made up of a flexible N-terminus anchored at a well ordered
CC loop-helix motif. The chain domain consists of a 4-turn helix with an
CC unfolded linker at its C-terminus (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB2
CC subfamily. {ECO:0000305}.
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DR EMBL; AY191836; AAO43501.1; -; mRNA.
DR EMBL; AJ517198; CAD56888.1; -; mRNA.
DR RefSeq; NP_789831.1; NM_176861.1.
DR AlphaFoldDB; Q811Q0; -.
DR BMRB; Q811Q0; -.
DR SMR; Q811Q0; -.
DR STRING; 10116.ENSRNOP00000013410; -.
DR GlyGen; Q811Q0; 3 sites.
DR PaxDb; Q811Q0; -.
DR ABCD; Q811Q0; 1 sequenced antibody.
DR GeneID; 294961; -.
DR KEGG; rno:294961; -.
DR UCSC; RGD:631398; rat.
DR CTD; 10242; -.
DR RGD; 631398; Kcnmb2.
DR eggNOG; ENOG502QSCP; Eukaryota.
DR InParanoid; Q811Q0; -.
DR PhylomeDB; Q811Q0; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:Q811Q0; -.
DR Proteomes; UP000002494; Unplaced.
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:0005267; F:potassium channel activity; IDA: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 Gene3D; 4.10.81.20; -; 1.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR InterPro; IPR037096; KCNMB2_ball/chain_dom_sf.
DR InterPro; IPR015382; KCNMB2_ball_chain_dom.
DR PANTHER; PTHR10258; PTHR10258; 1.
DR Pfam; PF03185; CaKB; 1.
DR Pfam; PF09303; KcnmB2_inactiv; 1.
DR PRINTS; PR01450; BKCHANNELB.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="Calcium-activated potassium channel subunit beta-2"
FT /id="PRO_0000187053"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Ball and chain"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 84
FT /note="R -> C (in Ref. 2; CAD56888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 27154 MW; E111B041867A3F70 CRC64;
MFIWTSGRTS SSYRHDEKRN IYQKIRDHDL LDKRKTVTAL KAGEDRAILL GLAMMVCSIM
MYFLLGITLL RSYMQSVWTE EAQRALLNVS ITETFNCSFS CGPDCWKLSQ YPCLQVYVNL
TSSGEKLLLY HTEETMKINQ KCSYIPKCGN NFEESMSLVS VVMENFRRHQ HFPCYSDPEG
NQKSVILTKL YSSNVLFHSL FWPTCMMAGG VAIVAMVKLT QYLSLLCERI QRINR
