Bsnd
entrez
140475
canonical
uniprot
Q8VIM4
canonical
ensembl
ENSMUSG00000025418
resolver
ensp
ENSMUSP00000049563
resolver
enst
ENSMUST00000054472
resolver
genesymbol
Bsnd
resolver
uniprot
B1AZI5
resolver
uniprot
Q8C740
resolver
uniprot
Q8CHY0
resolver
uniprot_entry
BSND_MOUSE
resolver
uniprot_sec
B1AZI5
resolver
uniprot_sec
Q8C740
resolver
uniprot_sec
Q8CHY0
resolver
amino_acid_sequence
MADEKTFRIGFIVLGLFLLSLGTFLMSHDRPQVYGTFYAMGSVMVIGGVIWSMCQCYPKITFVPADSDFQGILSPKALSLLETGLSEVKSPQPPYVRLWEEAAYDQSLPDFTHIQMKVMGYSEDPRPLLAPELKTGASSVREGEPRTAQAWMEAPVVVHRGSDENEGEKSHSQSSPSVGPQGSAPLASFHDDLDVGSSEGSSLQPSPNRDEPHRQVPWASRGPLDRFSDFALIDDTPTSEDTVLDGQAREAALPRKQQWSLRMKGETVQARAEEPEQEEEDLYYGLPDSPGNPLPDKELGFEPDIQG
uniprot
proteins
function
FUNCTION: Regulatory subunit of anion-selective CLCNKA:BSND and CLCNKB:BSND heteromeric channels involved in basolateral chloride conductance along the nephron to achieve urine concentration and maintain systemic acid-base homeostasis, and in the stria vascularis of the inner ear to establish the endocochlear potential necessary for normal hearing (PubMed:11734858, PubMed:18833191, PubMed:21593186, PubMed:23791703). Most likely acts as a chaperone that allosterically regulates proper sorting of CLCNKA:BSND and CLCNKB:BSND channels at the basolateral plasma membrane domain and functional switch to ion conducting state. Mediates constitutive opening of channel common gates (PubMed:11734858, PubMed:18833191, PubMed:21593186, PubMed:23791703). {ECO:0000269|PubMed:11734858, ECO:0000269|PubMed:18833191, ECO:0000269|PubMed:21593186, ECO:0000269|PubMed:23791703}.
uniprot
proteins
mass_dalton
33813
uniprot
proteins
mutagenesis
MUTAGEN 95; /note="Y->A: Increases channel conductance."; /evidence="ECO:0000269|PubMed:23791703
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is necessary for activation of plasma membrane-inserted CLC-K/barttin channels. {ECO:0000250|UniProtKB:Q8WZ55}.
uniprot
proteins
pubmed
11687798
uniprot
proteins
pubmed
11734858
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18833191
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21593186
uniprot
proteins
pubmed
23791703
uniprot
proteins
sequence_length
307
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11734858}; Multi-pass membrane protein {ECO:0000255}. Note=Staining in membranes of the renal tubule is basolateral. Also detected in basolateral membranes of intercalated cells of the collecting duct, which are known to express CLCNKB as well. Both acid-secreting alpha-intercalated cells and base-secreting beta-intercalated cells express this protein basolaterally, but intervening AQP2-expressing principal cells appear devoid of protein expression. In the inner ear, colocalizes with CLCNK in K(+)-secreting marginal cells of the stria vascularis. The basolateral staining contrasts with the apical localization of the KCNQ1 K(+) channel. Also found in K(+)-secreting vestibular dark cells, where it colocalized in basolateral membranes with CLCNK below apical membranes that expressed KCNQ1.
uniprot
proteins
transmembrane_region
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 33..53; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins