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Protein

Calcium-activated potassium channel subunit beta-1

Gene

Kcnmb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca2+/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.1 Publication

GO - Molecular functioni

  • calcium-activated potassium channel activity Source: MGI

GO - Biological processi

  • potassium ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-activated potassium channel subunit beta-1
Alternative name(s):
BK channel subunit beta-1
Short name:
BKbeta
Short name:
BKbeta1
Calcium-activated potassium channel, subfamily M subunit beta-1
Short name:
Calcium-activated potassium channel subunit beta
Charybdotoxin receptor subunit beta-1
K(VCA)beta-1
Maxi K channel subunit beta-1
Slo-beta-1
Short name:
Slo-beta
Gene namesi
Name:Kcnmb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1334203. Kcnmb1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1817CytoplasmicSequence analysisAdd
BLAST
Transmembranei19 – 3921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini40 – 155116ExtracellularSequence analysisAdd
BLAST
Transmembranei156 – 17621Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini177 – 19115CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: MGI
  • voltage-gated potassium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 191190Calcium-activated potassium channel subunit beta-1PRO_0000187047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence analysis
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8CAE3.
PRIDEiQ8CAE3.

PTM databases

iPTMnetiQ8CAE3.
PhosphoSiteiQ8CAE3.

Expressioni

Tissue specificityi

Expressed in many tissues containing smooth muscles. In brain and heart, it is not expressed except in the vasculature, such as cerebral arteries, aorta and corona arteries.1 Publication

Interactioni

Subunit structurei

Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB1 per KCNMA1 tetramer (By similarity).By similarity

Protein-protein interaction databases

BioGridi200915. 1 interaction.
DIPiDIP-46326N.
STRINGi10090.ENSMUSP00000020362.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWME. Eukaryota.
ENOG41116AX. LUCA.
HOGENOMiHOG000290180.
HOVERGENiHBG052223.
InParanoidiQ8CAE3.
KOiK04937.
PhylomeDBiQ8CAE3.

Family and domain databases

InterProiIPR003930. K_chnl_Ca-activ_BK_bsu.
[Graphical view]
PANTHERiPTHR10258. PTHR10258. 1 hit.
PfamiPF03185. CaKB. 1 hit.
[Graphical view]
PRINTSiPR01450. BKCHANNELB.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CAE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKLVMAQK RGETRALCLG VAMVVCAAIT YYVLGTTVLP LYQKSVWTQE
60 70 80 90 100
SICHLIETNI KDQEELEGKK VPQYPCLWVN VSAVGRWAML YHTEDTRDQN
110 120 130 140 150
QQCSYIPRNL DNYQTALADV KKVRANFYKH HEFYCLSAPQ VNETSVVYQR
160 170 180 190
LYGPQVLLFS FFWPTFLLTG GLLLIAMVKL NRSLSILAAQ K
Length:191
Mass (Da):21,846
Last modified:January 23, 2007 - v3
Checksum:iABDD46528EA74AB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931T → A in AAD11857 (PubMed:9888999).Curated
Sequence conflicti173 – 1731L → I (PubMed:9888999).Curated
Sequence conflicti173 – 1731L → I (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020711 mRNA. Translation: AAD11857.1.
AJ001291 mRNA. Translation: CAA04651.1.
AK038987 mRNA. Translation: BAC30193.1.
BC013338 mRNA. Translation: AAH13338.1.
CCDSiCCDS24538.1.
RefSeqiNP_112446.2. NM_031169.4.
XP_006514604.1. XM_006514541.2.
UniGeneiMm.6206.

Genome annotation databases

GeneIDi16533.
KEGGimmu:16533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020711 mRNA. Translation: AAD11857.1.
AJ001291 mRNA. Translation: CAA04651.1.
AK038987 mRNA. Translation: BAC30193.1.
BC013338 mRNA. Translation: AAH13338.1.
CCDSiCCDS24538.1.
RefSeqiNP_112446.2. NM_031169.4.
XP_006514604.1. XM_006514541.2.
UniGeneiMm.6206.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200915. 1 interaction.
DIPiDIP-46326N.
STRINGi10090.ENSMUSP00000020362.

PTM databases

iPTMnetiQ8CAE3.
PhosphoSiteiQ8CAE3.

Proteomic databases

PaxDbiQ8CAE3.
PRIDEiQ8CAE3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16533.
KEGGimmu:16533.

Organism-specific databases

CTDi3779.
MGIiMGI:1334203. Kcnmb1.

Phylogenomic databases

eggNOGiENOG410IWME. Eukaryota.
ENOG41116AX. LUCA.
HOGENOMiHOG000290180.
HOVERGENiHBG052223.
InParanoidiQ8CAE3.
KOiK04937.
PhylomeDBiQ8CAE3.

Miscellaneous databases

NextBioi289953.
PROiQ8CAE3.
SOURCEiSearch...

Family and domain databases

InterProiIPR003930. K_chnl_Ca-activ_BK_bsu.
[Graphical view]
PANTHERiPTHR10258. PTHR10258. 1 hit.
PfamiPF03185. CaKB. 1 hit.
[Graphical view]
PRINTSiPR01450. BKCHANNELB.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human and rodent MaxiK channel beta-subunit genes: cloning and characterization."
    Jiang Z., Wallner M., Meera P., Toro L.
    Genomics 55:57-67(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Intestinal smooth muscle.
  2. "Cloning and functional analysis of a calcium activated potassium channel beta-subunit from murine heart muscle."
    Metzler M.H.F., Repp R., Zibuschka C., Dreyer F., Repp H.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Heart muscle.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hypothalamus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  5. "Vasoregulation by the beta1 subunit of the calcium-activated potassium channel."
    Brenner R., Perez G.J., Bonev A.D., Eckman D.M., Kosek J.C., Wiler S.W., Patterson A.J., Nelson M.T., Aldrich R.W.
    Nature 407:870-876(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiKCMB1_MOUSE
AccessioniPrimary (citable) accession number: Q8CAE3
Secondary accession number(s): O35336, O35645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.