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Q28067 (KCMB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:KCNMB1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB1 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIonic channel
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 191190Calcium-activated potassium channel subunit beta-1
PRO_0000187044

Regions

Topological domain2 – 1817Cytoplasmic Potential
Transmembrane19 – 3921Helical; Name=1; Potential
Topological domain40 – 157118Extracellular Potential
Transmembrane158 – 17821Helical; Name=2; Potential
Topological domain179 – 19113Cytoplasmic Potential

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q28067 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 111C15E4A2B6B545

FASTA19121,957
        10         20         30         40         50         60 
MGKKLVMAQR RGETRALCLG VAMVVGAVIT YYILGTTVLP LYQKSVWTQE STCHLIETNI 

        70         80         90        100        110        120 
RDQEELEGKR VPQYPCLWVN VSSVGRWAVL YHTEDTRDQN HQCSYIPSSL DNYQVARADV 

       130        140        150        160        170        180 
EKVRARFHEN QDFFCFSTTR ENETSVLYRR LYGPQSLLFS LFWPTFLLTG GLLIIVMVKI 

       190 
NQSLSILAAQ R 

« Hide

References

« Hide 'large scale' references
[1]"Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle."
Knaus H.-G., Folander K., Garcia-Calvo M., Garcia M.L., Kaczorowski G.J., Smith M., Swanson R.
J. Biol. Chem. 269:17274-17278(1994) [PubMed: 8006036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-29.
Tissue: Aorta and Trachea.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26101 mRNA. Translation: AAA21741.1.
BC147983 mRNA. Translation: AAI47984.1.
IPIIPI00697173.
PIRA54165.
RefSeqNP_001001141.1. NM_001001141.1.
UniGeneBt.62471.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ28067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000003886; ENSBTAP00000003886; ENSBTAG00000002985.
ENSBTAT00000056280; ENSBTAP00000049066; ENSBTAG00000002985.
GeneID407176.
KEGGbta:407176.

Organism-specific databases

CTD3779.

Phylogenomic databases

eggNOGmaNOG08126.
GeneTreeENSGT00390000015997.
HOVERGENHBG052223.
InParanoidQ28067.
OMAYQRLYGP.
OrthoDBEOG47SSFT.
PhylomeDBQ28067.

Family and domain databases

InterProIPR003930. K_chnl_Ca-activ_BK_bsu.
[Graphical view]
KOK04937.
PANTHERPTHR10258. BK_channel_beta. 1 hit.
PfamPF03185. CaKB. 1 hit.
[Graphical view]
PRINTSPR01450. BKCHANNELB.
ProtoNetSearch...

Entry information

Entry nameKCMB1_BOVIN
AccessionPrimary (citable) accession number: Q28067
Secondary accession number(s): A6QLJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families