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Ca+2-activated K+ channel subunit beta-1; BK channel subunit beta-1; BKbeta; BKbeta1; Hbeta1; Ca+2-activated K+ channel, subfamily M subunit beta-1; Ca+2-activated K+ channel subunit beta; charybdotoxin receptor subunit beta-1; K(VCA)beta-1; Maxi K channel subunit beta-1; Slo-beta-1; Slo-beta (KCNMB1)
Function:
- regulatory subunit of the Ca+2-activated K+ channel KCNMA1
- modulates the Ca+2 sensitivity & gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity
- increases the apparent Ca+2/voltage sensitivity of the KCNMA1 channel
- modifies KCNMA1 channel kinetics & alters its pharmacological properties
- slows down the activation & the deactivation kinetics of the channel
- acts as a negative regulator of smooth muscle contraction by enhancing the Ca+2 sensitivity of KCNMA1
- required for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside & for external binding of the agonist hormone 17-beta-estradiol
- increases binding of charybdotoxin (CTX) toxin to KCNMA1
- interacts with KCNMA1 tetramer
- probably 4 molecules of KCMNB1 per KCNMA1 tetramer
Structure:
- N-glycosylated
- belongs to the KCNMB (TC 8.A.14.1) family, KCNMB1 subfamily
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- abundantly expressed in smooth muscle
- low levels of expression in most other tissues
- within the brain, relatively high levels found in hippocampus & corpus callosum
Polymorphism:
- genetic variation in KCNMB1 can influence the severity of diastolic hypertension
General
glycoprotein
K+ channel subfamily M
transmembrane 2 protein
Properties
SIZE: entity length = 191 aa
MW = 22 kD
COMPARTMENT: plasma membrane
MOTIF: cytoplasmic domain {2-18}
transmembrane domain {19-39}
exoplasmic loop {40-157}
MOTIF: N-glycosylation site {N80}
N-glycosylation site {N142}
transmembrane domain {158-178}
cytoplasmic domain {179-191}
ION-PERMEABILITY: K+
Database Correlations
OMIM correlations
MORBIDMAP 603951
UniProt Q16558
Pfam PF03185
Entrez Gene 3779
Kegg hsa:3779
References
UniProt :accession Q16558