Swiss-Prot entry
ID KCMB1_RAT STANDARD; PRT; 190 AA.
AC P97678; O35337; O88805; Q9ESK7; Q9QWI7;
DT 01-NOV-1997 (Rel. 35, 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 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) (Slowpoke-beta).
GN Name=Kcnmb1;
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 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX MEDLINE=97259567; PubMed=9105668 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0169-328X(96)00230-6;
RA Chang C.-P., Dworetzky S.I., Wang J., Goldstein M.E.;
RT "Differential expression of the alpha and beta subunits of the large-
RT conductance calcium-activated potassium channel: implication for
RT channel diversity.";
RL Brain Res. Mol. Brain Res. 45:33-40(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX MEDLINE=99107811; PubMed=9888999 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/geno.1998.5627;
RA Jiang Z., Wallner M., Meera P., Toro L.;
RT "Human and rodent MaxiK channel beta-subunit genes: cloning and
RT characterization.";
RL Genomics 55:57-67(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
RA Lange A.R., Gebremedhin D., Aebly M., Harder D.R.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RA Reimann F.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3).
RC TISSUE=Aorta;
RA Ohya S., Watanabe M., Imaizumi Y.;
RT "Molecular cloning of a novel spliced variant of calcium activated
RT potassium channel beta subunit in rat smooth muscle.";
RL Submitted (FEB-1998) 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. 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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97678-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=P97678-2; Sequence=VSP_009825, VSP_009826;
CC Name=3; Synonyms=1c;
CC IsoId=P97678-3; Sequence=VSP_009824, VSP_009825, VSP_009826;
CC -!- TISSUE SPECIFICITY: Weakly expressed. In brain, it is expressed in
CC a few discrete populations of neurons that also express KCNMA1.
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; U54498; AAD11548.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF020712; AAD11858.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U79661; AAB38413.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U40602; AAB96355.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB010963; BAA33448.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB050745; BAB17678.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR RGD; 2961; Kcnmb1.
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; P97678.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P97678.
DR ProtoNet; P97678.
DR ProtoMap; P97678.
DR PRESAGE; P97678.
DR DIP; P97678.
DR ModBase; P97678.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Alternative splicing; Glycoprotein; Ion transport; Ionic channel;
KW Transmembrane; Transport.
FT INIT_MET 0 0 By similarity.
FT TOPO_DOM 1 17 Cytoplasmic (Potential).
FT TRANSMEM 18 38 1 (Potential).
FT TOPO_DOM 39 154 Extracellular (Potential).
FT TRANSMEM 155 175 2 (Potential).
FT TOPO_DOM 176 190 Cytoplasmic (Potential).
FT CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
FT VARSPLIC 102 121 Missing (in isoform 3).
FT /FTId=VSP_009824.
FT VARSPLIC 122 145 VRANFYKHHNFYCFSAPQVNETSV -> LRSRPISSAQQHG
FT VTRNGRGPGQA (in isoform 2 and isoform 3).
FT /FTId=VSP_009825.
FT VARSPLIC 146 190 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_009826.
FT CONFLICT 13 13 T -> A (in Ref. 2).
FT CONFLICT 27 29 AIT -> VVA (in Ref. 2).
FT CONFLICT 37 37 V -> M (in Ref. 2).
FT CONFLICT 55 60 VETNIK -> IESNIR (in Ref. 2).
FT CONFLICT 68 68 R -> K (in Ref. 2).
FT CONFLICT 88 88 M -> V (in Ref. 2).
FT CONFLICT 104 104 Y -> H (in Ref. 1).
FT CONFLICT 108 110 NLD -> SLE (in Ref. 2).
FT CONFLICT 114 120 TALVDVK -> VARADVE (in Ref. 2).
FT CONFLICT 124 124 A -> T (in Ref. 2).
FT CONFLICT 127 131 YKHHN -> HEHRI (in Ref. 2).
FT CONFLICT 137 140 APQV -> TTRE (in Ref. 2).
FT CONFLICT 144 148 SVVYQ -> TVLYR (in Ref. 2).
FT CONFLICT 155 155 I -> T (in Ref. 2).
FT CONFLICT 160 160 F -> L (in Ref. 2).
FT CONFLICT 176 176 M -> I (in Ref. 1).
FT CONFLICT 179 181 LNR -> INQ (in Ref. 2).
FT CONFLICT 185 186 VL -> IP (in Ref. 1).
FT CONFLICT 185 185 V -> I (in Ref. 2).
FT CONFLICT 190 190 K -> R (in Ref. 1 and 2).
SQ SEQUENCE 190 AA; 21777 MW; EA092F4B26FBADDF CRC64;
GKKLVMAQKR GETRALCLGV AMVVCAAITY YILGTTVLPL YQKSVWTQES TCHLVETNIK
DQEELEGRKV PQYPCLWVNV SAVGRWAMLY HTEDTRDQNQ QCSYIPRNLD NYQTALVDVK
KVRANFYKHH NFYCFSAPQV NETSVVYQRL YGPQILLFSF FWPTFLLTGG LLIIAMVKLN
RSLSVLAAQK
//