KCMB1_MOUSE
ID KCMB1_MOUSE Reviewed; 191 AA.
AC Q8CAE3; O35336; O35645;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Calcium-activated potassium channel subunit beta-1;
DE AltName: Full=BK channel subunit beta-1;
DE Short=BKbeta;
DE Short=BKbeta1;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-1;
DE Short=Calcium-activated potassium channel subunit beta;
DE AltName: Full=Charybdotoxin receptor subunit beta-1;
DE AltName: Full=K(VCA)beta-1;
DE AltName: Full=Maxi K channel subunit beta-1;
DE AltName: Full=Slo-beta-1;
DE Short=Slo-beta;
GN Name=Kcnmb1;
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=Intestinal smooth muscle;
RX PubMed=9888999; 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 [MRNA].
RC STRAIN=BALB/cJ; 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 channel
RT 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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11057658; DOI=10.1038/35038011;
RA Brenner R., Perez G.J., Bonev A.D., Eckman D.M., Kosek J.C., Wiler S.W.,
RA Patterson A.J., Nelson M.T., Aldrich R.W.;
RT "Vasoregulation by the beta1 subunit of the calcium-activated potassium
RT channel.";
RL Nature 407:870-876(2000).
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. Increases
CC the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also
CC modifies KCNMA1 channel kinetics and alters its pharmacological
CC properties. It slows down the activation and the deactivation kinetics
CC of the channel. Acts as a negative regulator of smooth muscle
CC contraction by enhancing the calcium sensitivity to KCNMA1. Its
CC presence is also a requirement for internal binding of the KCNMA1
CC channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and
CC for external binding of the agonist hormone 17-beta-estradiol (E2).
CC Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1
CC peptide blocker by increasing the CTX association rate and decreasing
CC the dissociation rate. {ECO:0000269|PubMed:11057658}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB1 per KCNMA1 tetramer (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CAE3; Q08460-4: Kcnma1; NbExp=2; IntAct=EBI-15575793, EBI-15575817;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues containing smooth
CC muscles. In brain and heart, it is not expressed except in the
CC vasculature, such as cerebral arteries, aorta and corona arteries.
CC {ECO:0000269|PubMed:11057658}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF020711; AAD11857.1; -; mRNA.
DR EMBL; AJ001291; CAA04651.1; -; mRNA.
DR EMBL; AK038987; BAC30193.1; -; mRNA.
DR EMBL; BC013338; AAH13338.1; -; mRNA.
DR CCDS; CCDS24538.1; -.
DR RefSeq; NP_112446.2; NM_031169.4.
DR RefSeq; XP_006514604.1; XM_006514541.3.
DR AlphaFoldDB; Q8CAE3; -.
DR SMR; Q8CAE3; -.
DR BioGRID; 200915; 1.
DR DIP; DIP-46326N; -.
DR IntAct; Q8CAE3; 1.
DR STRING; 10090.ENSMUSP00000020362; -.
DR GlyGen; Q8CAE3; 2 sites.
DR iPTMnet; Q8CAE3; -.
DR PhosphoSitePlus; Q8CAE3; -.
DR PaxDb; Q8CAE3; -.
DR PRIDE; Q8CAE3; -.
DR ProteomicsDB; 269254; -.
DR DNASU; 16533; -.
DR GeneID; 16533; -.
DR KEGG; mmu:16533; -.
DR CTD; 3779; -.
DR MGI; MGI:1334203; Kcnmb1.
DR eggNOG; ENOG502RZA0; Eukaryota.
DR InParanoid; Q8CAE3; -.
DR OrthoDB; 1178937at2759; -.
DR PhylomeDB; Q8CAE3; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 16533; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8CAE3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CAE3; protein.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IGI:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:1903413; P:cellular response to bile acid; ISO:MGI.
DR GO; GO:0071361; P:cellular response to ethanol; ISO:MGI.
DR GO; GO:0005513; P:detection of calcium ion; IBA:GO_Central.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR PANTHER; PTHR10258; PTHR10258; 1.
DR Pfam; PF03185; CaKB; 1.
DR PRINTS; PR01450; BKCHANNELB.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..191
FT /note="Calcium-activated potassium channel subunit beta-1"
FT /id="PRO_0000187047"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="T -> A (in Ref. 1; AAD11857)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="L -> I (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21846 MW; ABDD46528EA74AB7 CRC64;
MGKKLVMAQK RGETRALCLG VAMVVCAAIT YYVLGTTVLP LYQKSVWTQE SICHLIETNI
KDQEELEGKK VPQYPCLWVN VSAVGRWAML YHTEDTRDQN QQCSYIPRNL DNYQTALADV
KKVRANFYKH HEFYCLSAPQ VNETSVVYQR LYGPQVLLFS FFWPTFLLTG GLLLIAMVKL
NRSLSILAAQ K
