KCMB2_MOUSE
ID KCMB2_MOUSE Reviewed; 235 AA.
AC Q9CZM9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Calcium-activated potassium channel subunit beta-2;
DE AltName: Full=BK channel subunit beta-2;
DE Short=BKbeta2;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-2;
DE AltName: Full=Charybdotoxin receptor subunit beta-2;
DE AltName: Full=K(VCA)beta-2;
DE AltName: Full=Maxi K channel subunit beta-2;
DE AltName: Full=Slo-beta-2;
GN Name=Kcnmb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Garcia-Valdes J., Eghbali M., Stefani E., Toro L.;
RT "Mouse kcnmb2 subunit of the large conductance calcium-activated K channel
RT (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 PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1
CC (maxiK) channel. Modulates the calcium sensitivity and gating kinetics
CC of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a
CC negative regulator that confers rapid and complete inactivation of
CC KCNMA1 channel complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB2 per KCNMA1 tetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The ball and chain domain mediates the inactivation of KCNMA1.
CC It occludes the conduction pathway of KCNMA1 channels, and comprises
CC the pore-blocking ball domain (residues 1-17) and the chain domain
CC (residues 20-45) linking it to the transmembrane segment. The ball
CC domain is made up of a flexible N-terminus anchored at a well ordered
CC loop-helix motif. The chain domain consists of a 4-turn helix with an
CC unfolded linker at its C-terminus (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB2
CC subfamily. {ECO:0000305}.
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DR EMBL; AY062429; AAL38982.1; -; mRNA.
DR EMBL; AK012400; BAB28216.1; -; mRNA.
DR EMBL; BC046227; AAH46227.1; -; mRNA.
DR EMBL; BC058957; AAH58957.1; -; mRNA.
DR CCDS; CCDS17292.1; -.
DR RefSeq; NP_082507.1; NM_028231.2.
DR RefSeq; XP_006535612.1; XM_006535549.3.
DR RefSeq; XP_006535613.1; XM_006535550.1.
DR RefSeq; XP_006535614.1; XM_006535551.3.
DR RefSeq; XP_017175231.1; XM_017319742.1.
DR AlphaFoldDB; Q9CZM9; -.
DR BMRB; Q9CZM9; -.
DR SMR; Q9CZM9; -.
DR STRING; 10090.ENSMUSP00000113234; -.
DR GlyGen; Q9CZM9; 3 sites.
DR PhosphoSitePlus; Q9CZM9; -.
DR PaxDb; Q9CZM9; -.
DR PRIDE; Q9CZM9; -.
DR ProteomicsDB; 263591; -.
DR ABCD; Q9CZM9; 1 sequenced antibody.
DR DNASU; 72413; -.
DR Ensembl; ENSMUST00000119310; ENSMUSP00000112531; ENSMUSG00000037610.
DR Ensembl; ENSMUST00000119970; ENSMUSP00000113234; ENSMUSG00000037610.
DR Ensembl; ENSMUST00000178668; ENSMUSP00000136596; ENSMUSG00000037610.
DR Ensembl; ENSMUST00000192429; ENSMUSP00000141656; ENSMUSG00000037610.
DR GeneID; 72413; -.
DR KEGG; mmu:72413; -.
DR UCSC; uc008owa.1; mouse.
DR CTD; 10242; -.
DR MGI; MGI:1919663; Kcnmb2.
DR VEuPathDB; HostDB:ENSMUSG00000037610; -.
DR eggNOG; ENOG502QSCP; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR HOGENOM; CLU_085739_1_1_1; -.
DR InParanoid; Q9CZM9; -.
DR OMA; FACYSDP; -.
DR OrthoDB; 1178937at2759; -.
DR PhylomeDB; Q9CZM9; -.
DR TreeFam; TF328589; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 72413; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnmb2; mouse.
DR PRO; PR:Q9CZM9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CZM9; protein.
DR Bgee; ENSMUSG00000037610; Expressed in trigeminal ganglion and 96 other tissues.
DR ExpressionAtlas; Q9CZM9; baseline and differential.
DR Genevisible; Q9CZM9; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; ISO:MGI.
DR GO; GO:0005513; P:detection of calcium ion; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR Gene3D; 4.10.81.20; -; 1.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR InterPro; IPR037096; KCNMB2_ball/chain_dom_sf.
DR InterPro; IPR015382; KCNMB2_ball_chain_dom.
DR PANTHER; PTHR10258; PTHR10258; 1.
DR Pfam; PF03185; CaKB; 1.
DR Pfam; PF09303; KcnmB2_inactiv; 1.
DR PRINTS; PR01450; BKCHANNELB.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="Calcium-activated potassium channel subunit beta-2"
FT /id="PRO_0000187052"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Ball and chain"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
