Swiss-Prot entry
ID KCMB2_MOUSE STANDARD; PRT; 235 AA.
AC Q9CZM9;
DT 05-JUL-2004 (Rel. 44, Created)
DT 05-JUL-2004 (Rel. 44, Last sequence update)
DT 13-SEP-2005 (Rel. 48, 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).
GN Name=Kcnmb2;
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=Kidney;
RA Garcia-Valdes J., Eghbali M., Stefani E., Toro L.;
RT "Mouse kcnmb2 subunit of the large conductance calcium-activated K
RT channel (MaxiK, BK).";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain;
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).
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 -!- 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; AY062429; AAL38982.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK012400; BAB28216.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC046227; AAH46227.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC058957; AAH58957.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; Q9Y691; 1JO6. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9CZM9; 1-45.
DR Ensembl; ENSMUSG00000037610; Mus_musculus
DR MGI; MGI:1919663; Kcnmb2.
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; Q9CZM9.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9CZM9.
DR ProtoNet; Q9CZM9.
DR ProtoMap; Q9CZM9.
DR PRESAGE; Q9CZM9.
DR DIP; Q9CZM9.
DR ModBase; Q9CZM9.
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).
SQ SEQUENCE 235 AA; 27120 MW; F87D3D91C22BBDF2 CRC64;
MFIWTSGRTS SSYRQDEKRN IYQKIRDHDL LDKRKTVTAL KAGEDRAILL GLAMMVCSIM
MYFLLGITLL RSYMQSVWTE EAQCALLNVS ITETFNCSFS CGPDCWKLSQ YPCLQVYVNL
TSSGERLLLY HTEETMKINQ KCSYIPKCGN NFEESMSLVS VVMENFRRHQ HFPCYSDPEG
NQKSVILTKL YSSNVLFHSL FWPTCMMAGG VAIVAMVKLT QYLSLLCERI QRINR
//