Swiss-Prot entry

ID   KCMB2_RAT      STANDARD;      PRT;   235 AA.
AC   Q811Q0; Q8CF83;
DT   05-JUL-2004 (Rel. 44, Created)
DT   05-JUL-2004 (Rel. 44, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Calcium-activated potassium channel beta subunit 2 (Calcium-activated
DE   potassium channel, subfamily M, beta subunit 2) (Maxi K channel beta
DE   subunit 2) (BK channel beta subunit 2) (Slo-beta 2) (K(VCA)beta 2)
DE   (Charybdotoxin receptor beta subunit 2) (BKbeta2) (Rbeta3).
GN   Name=Kcnmb2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Rattus. 
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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
RT   K+ channel (KCNMB2, rSlo beta 2 subunit).";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 40-201.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   MEDLINE=22342043; PubMed=12454985 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1002/cne.10471;
RA   Langer P., Gruender S., Ruesch A.;
RT   "Expression of a Ca2+-activated BK channel mRNA and its splice
RT   variants in the rat cochlea.";
RL   J. Comp. Neurol. 455:198-209(2003).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=10377337 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Xia X.-M., Ding J.-P., Lingle C.J.;
RT   "Molecular basis for the inactivation of Ca2+- and voltage-dependent
RT   BK channels in adrenal chromaffin cells and rat insulinoma tumor
RT   cells.";
RL   J. Neurosci. 19:5255-5264(1999).
CC   -!- FUNCTION: Regulatory subunit of the calcium activated potassium
CC       KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and
CC       gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel
CC       diversity. Acts as a negative regulator that confers rapid and
CC       complete inactivation of KCNMA1 channel complex (By similarity).
CC   -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4
CC       molecules of KCMNB2 per KCNMA1 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and heart. Also
CC       expressed in lung.
CC   -!- DOMAIN: The ball and chain domain mediates the inactivation of
CC       KCNMA1. It occludes the conduction pathway of KCNMA1 channels, and
CC       comprises the pore-blocking ball domain (residues 1-17) and the
CC       chain domain (residues 20-45) linking it to the transmembrane
CC       segment. The ball domain is made up of a flexible N-terminus
CC       anchored at a well ordered loop-helix motif. The chain domain
CC       consists of a 4-turn helix with an unfolded linker at its C-
CC       terminus (By similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the KCNMB family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AY191836; AAO43501.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AJ517198; CAD56888.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; Q9Y691; 1JO6. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q811Q0; 1-45.
DR   Ensembl; ENSRNOG00000010094; Rattus_norvegicus
DR   InterPro; IPR003930; BK_channel_beta.
DR   InterPro; Graphical view of domain structure.
DR   PANTHER; PTHR10258; BK_channel_beta; 1.
DR   Pfam; PF03185; CaKB; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01450; BKCHANNELB.
DR   CMR; Q811Q0.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q811Q0.
DR   ProtoNet; Q811Q0.
DR   ProtoMap; Q811Q0.
DR   PRESAGE; Q811Q0.
DR   DIP; Q811Q0.
DR   ModBase; Q811Q0.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; Ion transport; Ionic channel; Transmembrane; Transport.
FT   TOPO_DOM      1     46       Cytoplasmic (Potential).
FT   TRANSMEM     47     67       1 (Potential).
FT   TOPO_DOM     68    194       Extracellular (Potential).
FT   TRANSMEM    195    215       2 (Potential).
FT   TOPO_DOM    216    235       Cytoplasmic (Potential).
FT   REGION        1     45       Ball and chain.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    119    119       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     84     84       R -> C (in Ref. 2).
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
//