Swiss-Prot entry
ID KCMB1_MOUSE STANDARD; PRT; 190 AA.
AC Q8CAE3; O35336; O35645;
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 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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6; TISSUE=Intestinal smooth muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/c; TISSUE=Heart muscle;
RA Metzler M.H.F., Repp R., Zibuschka C., Dreyer F., Repp H.;
RT "Cloning and functional analysis of a calcium activated potassium
RT channel beta-subunit from murine heart muscle.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX MEDLINE=22354683; PubMed=12466851 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J.,
RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W.,
RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S.,
RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S.,
RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J.,
RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D.,
RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L.,
RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A.,
RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H.,
RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G.,
RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S.,
RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M.,
RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M.,
RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C.,
RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L.,
RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N.,
RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K.,
RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S.,
RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I.,
RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A.,
RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J.,
RA Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11057658 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/35038011;
RA Brenner R., Perez G.J., Bonev A.D., Eckman D.M., Kosek J.C.,
RA Wiler S.W., Patterson A.J., Nelson M.T., Aldrich R.W.;
RT "Vasoregulation by the beta1 subunit of the calcium-activated
RT potassium channel.";
RL Nature 407:870-876(2000).
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.
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 -!- TISSUE SPECIFICITY: Expressed in many tissues containing smooth
CC muscles. In brain and heart, it is not expressed axcept in the
CC vasculature, such as cerebral arteries, aorta and corona arteries.
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; AF020711; AAD11857.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AJ001291; CAA04651.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK038987; BAC30193.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC013338; AAH13338.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR Ensembl; ENSMUSG00000020155; Mus_musculus
DR MGI; MGI:1334203; Kcnmb1.
DR GO; GO:0016021; C:integral to membrane; TAS.
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; Q8CAE3.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q8CAE3.
DR ProtoNet; Q8CAE3.
DR ProtoMap; Q8CAE3.
DR PRESAGE; Q8CAE3.
DR DIP; Q8CAE3.
DR ModBase; Q8CAE3.
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 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 CONFLICT 92 92 T -> A (in Ref. 1).
FT CONFLICT 172 172 L -> I (in Ref. 1 and 3).
SQ SEQUENCE 190 AA; 21714 MW; 924B46FD7EC1910A CRC64;
GKKLVMAQKR GETRALCLGV AMVVCAAITY YVLGTTVLPL YQKSVWTQES ICHLIETNIK
DQEELEGKKV PQYPCLWVNV SAVGRWAMLY HTEDTRDQNQ QCSYIPRNLD NYQTALADVK
KVRANFYKHH EFYCLSAPQV NETSVVYQRL YGPQVLLFSF FWPTFLLTGG LLLIAMVKLN
RSLSILAAQK
//