Swiss-Prot entry

ID   KCMB4_RAT      STANDARD;      PRT;   210 AA.
AC   Q9ESK8;
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 4 (Calcium-activated
DE   potassium channel, subfamily M, beta subunit 4) (Maxi K channel beta
DE   subunit 4) (BK channel beta subunit 4) (Slo-beta 4) (K(VCA)beta 4)
DE   (Charybdotoxin receptor beta subunit 4) (BKbeta4).
GN   Name=Kcnmb4;
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   TISSUE=Brain;
RA   Ohya S., Ohi Y., Imaizumi Y.;
RT   "rat calcium activated potassium channel beta 4 subunit (KCNMB4).";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Ha T.S., Park C.-S.;
RT   "Molecular cloning of large-conductance calcium-activated potassium
RT   channel beta 4 subunit from rat brain.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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. Decreases the gating kinetics and calcium sensitivity
CC       of the KCNMA1 channel, but with fast deactivation kinetics. May
CC       decrease KCNMA1 channel openings at low calcium concentrations but
CC       increases channel openings at high calcium concentrations. Makes
CC       KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin
CC       concentrations (By similarity).
CC   -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4
CC       molecules of KCMNB4 per KCNMA1 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein (By similarity).
CC   -!- DOMAIN: Resistance to charybdotoxin (CTX) toxin is mediated by the
CC       extracellular domain (By similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation modulates its effect on
CC       KCNMA1 activation kinetics (By similarity).
CC   -!- PTM: N-glycosylated. A highly glycosylated form is promoted by
CC       KCNMA1. Glycosylation, which is not required for the interaction
CC       with KCNMA1 and subcellular location, increases protection against
CC       charybdotoxin (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; AB050637; BAB17595.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AY028605; AAK21964.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   Ensembl; ENSRNOG00000022297; Rattus_norvegicus
DR   RGD; 620728; Kcnmb4.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; ISS.
DR   GO; GO:0005515; F:protein binding; ISS.
DR   GO; GO:0005513; P:calcium ion sensing; ISS.
DR   GO; GO:0019228; P:generation of action potential; ISS.
DR   GO; GO:0006813; P:potassium ion transport; ISS.
DR   GO; GO:0001508; P:regulation of action potential; ISS.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS.
DR   GO; GO:0019229; P:regulation of vasoconstriction; ISS.
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   CMR; Q9ESK8.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q9ESK8.
DR   ProtoNet; Q9ESK8.
DR   ProtoMap; Q9ESK8.
DR   PRESAGE; Q9ESK8.
DR   DIP; Q9ESK8.
DR   ModBase; Q9ESK8.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; Ion transport; Ionic channel; Phosphorylation;
KW   Transmembrane; Transport.
FT   TOPO_DOM      1     19       Cytoplasmic (Potential).
FT   TRANSMEM     20     40       1 (Potential).
FT   TOPO_DOM     41    167       Extracellular (Potential).
FT   TRANSMEM    168    188       2 (Potential).
FT   TOPO_DOM    189    210       Cytoplasmic (Potential).
FT   CARBOHYD     53     53       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (By similarity).
SQ   SEQUENCE   210 AA;  23885 MW;  11D49F58F9C6F1D4 CRC64;
     MAKLRVSYEY TEAEDKSIRL GLFLIVSGIL SLFIFGFCWL SPALQDLQAT AANCTVLSVQ
     QIGEVFECTF TCGTDCRGTS QYPCVQVYVN NSESNSRALL HSDQHQLLTN PKCSYIPPCK
     RENQKNSESV MNWQQYWKDE IGSQPFTCYF NQHQRPEDVL LQRTHDEIVL LHCFLWPVVA
     FVVGVLIVVL TICAKSLAVK AEAMKKRKFS
//