Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P97678 (KCMB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Slowpoke-beta
Gene names
Name:Kcnmb1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

Tissue specificity

Weakly expressed. In brain, it is expressed in a few discrete populations of neurons that also express KCNMA1. Ref.1

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P97678-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P97678-2)

Also known as: 1b;

The sequence of this isoform differs from the canonical sequence as follows:
     123-146: VRANFYKHHNFYCFSAPQVNETSV → LRSRPISSAQQHGVTRNGRGPGQA
     147-191: Missing.
Isoform 3 (identifier: P97678-3)

Also known as: 1c;

The sequence of this isoform differs from the canonical sequence as follows:
     103-122: Missing.
     123-146: VRANFYKHHNFYCFSAPQVNETSV → LRSRPISSAQQHGVTRNGRGPGQA
     147-191: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 191190Calcium-activated potassium channel subunit beta-1
PRO_0000187049

Regions

Topological domain2 – 1817Cytoplasmic Potential
Transmembrane19 – 3921Helical; Name=1; Potential
Topological domain40 – 155116Extracellular Potential
Transmembrane156 – 17621Helical; Name=2; Potential
Topological domain177 – 19115Cytoplasmic Potential

Amino acid modifications

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

Natural variations

Alternative sequence103 – 12220Missing in isoform 3.
VSP_009824
Alternative sequence123 – 14624VRANF…NETSV → LRSRPISSAQQHGVTRNGRG PGQA in isoform 2 and isoform 3.
VSP_009825
Alternative sequence147 – 19145Missing in isoform 2 and isoform 3.
VSP_009826

Experimental info

Sequence conflict141T → A in AAB38413. Ref.2
Sequence conflict28 – 303AIT → VVA in AAB38413. Ref.2
Sequence conflict381V → M in AAB38413. Ref.2
Sequence conflict56 – 616VETNIK → IESNIR in AAB38413. Ref.2
Sequence conflict691R → K in AAB38413. Ref.2
Sequence conflict891M → V in AAB38413. Ref.2
Sequence conflict1051Y → H in AAD11548. Ref.1
Sequence conflict109 – 1113NLD → SLE in AAB38413. Ref.2
Sequence conflict115 – 1217TALVDVK → VARADVE in AAB38413. Ref.2
Sequence conflict1251A → T in AAB38413. Ref.2
Sequence conflict128 – 1325YKHHN → HEHRI in AAB38413. Ref.2
Sequence conflict138 – 1414APQV → TTRE in AAB38413. Ref.2
Sequence conflict145 – 1495SVVYQ → TVLYR in AAB38413. Ref.2
Sequence conflict1561I → T in AAB38413. Ref.2
Sequence conflict1611F → L in AAB38413. Ref.2
Sequence conflict1771M → I in AAD11548. Ref.1
Sequence conflict180 – 1823LNR → INQ in AAB38413. Ref.2
Sequence conflict186 – 1872VL → IP in AAD11548. Ref.1
Sequence conflict1861V → I in AAB38413. Ref.2
Sequence conflict1911K → R Ref.1
Sequence conflict1911K → R Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D39F2FE4D69D7662

FASTA19121,909
        10         20         30         40         50         60 
MGKKLVMAQK RGETRALCLG VAMVVCAAIT YYILGTTVLP LYQKSVWTQE STCHLVETNI 

        70         80         90        100        110        120 
KDQEELEGRK VPQYPCLWVN VSAVGRWAML YHTEDTRDQN QQCSYIPRNL DNYQTALVDV 

       130        140        150        160        170        180 
KKVRANFYKH HNFYCFSAPQ VNETSVVYQR LYGPQILLFS FFWPTFLLTG GLLIIAMVKL 

       190 
NRSLSVLAAQ K 

« Hide

Isoform 2 (1b) [UniParc].

Checksum: 6EF4D5EA24D68E57
Show »

FASTA14616,470
Isoform 3 (1c) [UniParc].

Checksum: 8B319BB95CE4E8CC
Show »

FASTA12614,147

References

[1]"Differential expression of the alpha and beta subunits of the large-conductance calcium-activated potassium channel: implication for channel diversity."
Chang C.-P., Dworetzky S.I., Wang J., Goldstein M.E.
Brain Res. Mol. Brain Res. 45:33-40(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
[2]"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] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Uterus.
[3]Lange A.R., Gebremedhin D., Aebly M., Harder D.R.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Vascular smooth muscle.
[4]Reimann F.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Uterus.
[5]"Molecular cloning of a novel spliced variant of calcium activated potassium channel beta subunit in rat smooth muscle."
Ohya S., Watanabe M., Imaizumi Y.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Aorta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U54498 mRNA. Translation: AAD11548.1.
AF020712 mRNA. Translation: AAD11858.1.
U79661 mRNA. Translation: AAB38413.1.
U40602 mRNA. Translation: AAB96355.1.
AB010963 mRNA. Translation: BAA33448.1.
AB050745 mRNA. Translation: BAB17678.1.
RefSeqNP_062146.1. NM_019273.1. [P97678-1]
NP_071539.1. NM_022203.1.
XP_006246151.1. XM_006246089.1. [P97678-1]
XP_006246152.1. XM_006246090.1. [P97678-1]
XP_006246153.1. XM_006246091.1. [P97678-2]
UniGeneRn.10820.
Rn.127785.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007408.

Chemistry

BindingDBP97678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007393; ENSRNOP00000007393; ENSRNOG00000005465. [P97678-2]
ENSRNOT00000007408; ENSRNOP00000007408; ENSRNOG00000005465. [P97678-1]
GeneID29747.
60591.
KEGGrno:29747.
rno:60591.
UCSCRGD:2961. rat. [P97678-1]

Organism-specific databases

CTD3779.
RGD2961. Kcnmb1.

Phylogenomic databases

eggNOGNOG40171.
GeneTreeENSGT00390000015997.
HOGENOMHOG000290180.
HOVERGENHBG052223.
KOK04937.
OMAIIAMVKI.
OrthoDBEOG77WWDC.
PhylomeDBP97678.
TreeFamTF328589.

Gene expression databases

GenevestigatorP97678.

Family and domain databases

InterProIPR003930. K_chnl_Ca-activ_BK_bsu.
[Graphical view]
PANTHERPTHR10258. PTHR10258. 1 hit.
PfamPF03185. CaKB. 1 hit.
[Graphical view]
PRINTSPR01450. BKCHANNELB.
ProtoNetSearch...

Other

NextBio610265.
PROP97678.

Entry information

Entry nameKCMB1_RAT
AccessionPrimary (citable) accession number: P97678
Secondary accession number(s): O35337 expand/collapse secondary AC list , O88805, Q9ESK7, Q9QWI7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 92 of the entry and version 4 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