Swiss-Prot entry
ID KCMB1_CANFA STANDARD; PRT; 190 AA.
AC Q28266;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Calcium-activated potassium channel beta subunit 1 (Calcium-activated
DE potassium channel, subfamily M, beta subunit 1) (Maxi K channel beta
DE subunit 1) (BK channel beta subunit 1) (Slo-beta 1) (K(VCA)beta 1)
DE (Charybdotoxin receptor beta subunit 1) (BKbeta1) (Calcium-activated
DE potassium channel beta-subunit) (BKbeta) (Slo-beta).
GN Name=KCNMB1;
OS Canis familiaris (Dog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Fissipedia; Canidae;
OC Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=97053370; PubMed=8897882 [NCBI, ExPASy, EBI, Israel, Japan];
RA Vogalis F., Vincent T., Qureshi I., Schmalz F.M., Ward M.W.,
RA Sanders K.M., Horowitz B.;
RT "Cloning and expression of the large-conductance Ca(2+)-activated K+
RT channel from colonic smooth muscle.";
RL Am. J. Physiol. 271:G629-G639(1996).
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. Increases the apparent Ca(2+)/voltage sensitivity of
CC the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and
CC alters its pharmacological properties. It slows down the
CC activation and the deactivation kinetics of the channel. Acts as a
CC negative regulator of smooth muscle contraction by enhancing the
CC calcium sensitivity to KCNMA1. Its presence is also a requirement
CC for internal binding of the KCNMA1 channel opener
CC dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external
CC binding of the agonist hormone 17-beta-estradiol (E2). Increases
CC the binding activity of charybdotoxin (CTX) toxin to KCNMA1
CC peptide blocker by increasing the CTX association rate and
CC decreasing the dissociation rate (By similarity).
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4
CC molecules of KCMNB1 per KCNMA1 tetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Integral membrane protein (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; U41002; AAA84001.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR Ensembl; ENSCAFG00000016956; Canis_familiaris
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 ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q28266.
DR ProtoNet; Q28266.
DR ProtoMap; Q28266.
DR PRESAGE; Q28266.
DR DIP; Q28266.
DR ModBase; Q28266.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Glycoprotein; Ion transport; Ionic channel; Transmembrane; Transport.
FT INIT_MET 0 0 By similarity.
FT TOPO_DOM 1 14 Cytoplasmic (Potential).
FT TRANSMEM 15 35 1 (Potential).
FT TOPO_DOM 36 156 Extracellular (Potential).
FT TRANSMEM 157 177 2 (Potential).
FT TOPO_DOM 178 190 Cytoplasmic (Potential).
FT CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 190 AA; 21803 MW; 087715070A35D3C8 CRC64;
GKKLVMAQKR GETRALCLGV AMVMCAVIAY YILGTTMLPL YQKSVWTQKS TCHLIETNIR
EQEELEGKKV PQYPCLWVNV SAVGRWAVLY HTEDTRDQNH QCSYIPGSLE NYQVARADVE
KVKAKFHEQQ IFYCFSTTRE NETTVLYRRL YGPQTLLFSL FWPTFLLTGG LLIIAMVKIN
QSLSILAAQR
//