BSND
entrez
7809
canonical
uniprot
Q8WZ55
canonical
ensembl
ENSG00000162399
resolver
ensp
ENSP00000498282
resolver
enst
ENST00000651561
resolver
genesymbol
BSND
resolver
genesymbol_syn
BART
resolver
hgnc
HGNC:16512
resolver
uniprot
Q5VU50
resolver
uniprot
Q6NT28
resolver
uniprot_entry
BSND_HUMAN
resolver
uniprot_entry
Q5VU50_HUMAN
resolver
uniprot_sec
Q6NT28
resolver
amino_acid_sequence
MADEKTFRIGFIVLGLFLLALGTFLMSHDRPQVYGTFYAMGSVMVIGGIIWSMCQCYPKITFVPADSDFQGILSPKAMGLLENGLAAEMKSPSPQPPYVRLWEEAAYDQSLPDFSHIQMKVMSYSEDHRSLLAPEMGQPKLGTSDGGEGGPGDVQAWMEAAVVIHKGSDESEGERRLTQSWPGPLACPQGPAPLASFQDDLDMDSSEGSSPNASPHDREEACSPQQEPQGCRCPLDRFQDFALIDAPTLEDEPQEGQQWEIALPNNWQRYPRTKVEEKEASDTGGEEPEKEEEDLYYGLPDGAGDLLPDKELGFEPDTQG
uniprot
proteins
disease_involvement
DISEASE: Bartter syndrome 4A, neonatal, with sensorineural deafness (BARTS4A) [MIM:602522]: A form of Bartter syndrome, an autosomal recessive disorder characterized by impaired salt reabsorption in the thick ascending loop of Henle with pronounced salt wasting, hypokalemic metabolic alkalosis, and varying degrees of hypercalciuria. BARTS4A is associated with sensorineural deafness. {ECO:0000269|PubMed:11687798, ECO:0000269|PubMed:11734858, ECO:0000269|PubMed:12111250, ECO:0000269|PubMed:12574213, ECO:0000269|PubMed:12761627, ECO:0000269|PubMed:16328537, ECO:0000269|PubMed:16773427, ECO:0000269|PubMed:18776122, ECO:0000269|PubMed:19646679}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:12111250, PubMed:12574213, PubMed:16849430, PubMed:18776122, PubMed:19646679, PubMed:20538786, PubMed:26013830). 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:12111250, PubMed:12574213, PubMed:16849430, PubMed:18776122, PubMed:19646679, PubMed:20538786, PubMed:26013830). {ECO:0000269|PubMed:11734858, ECO:0000269|PubMed:12111250, ECO:0000269|PubMed:12574213, ECO:0000269|PubMed:16849430, ECO:0000269|PubMed:18776122, ECO:0000269|PubMed:19646679, ECO:0000269|PubMed:20538786, ECO:0000269|PubMed:26013830}.
uniprot
proteins
mass_dalton
35197
uniprot
proteins
mutagenesis
MUTAGEN 54..320; /note="Missing: Abolishes CLCNKB channel conductance."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 54; /note="C->S: 38% reduction in palmitoylation. Abolishes palmitoylation; when associated with S-56."; /evidence="ECO:0000269|PubMed:26013830"; MUTAGEN 56; /note="C->S: 74% reduction in palmitoylation. Abolishes palmitoylation; when associated with S-54."; /evidence="ECO:0000269|PubMed:26013830"; MUTAGEN 57..320; /note="Missing: Abolishes CLCNKB channel conductance."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 61..320; /note="Missing: Abolishes CLCNKB channel conductance."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 72..320; /note="Missing: Decreases the amplitude of CLCNKB channel current but does not affect the open probability."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 85..320; /note="Missing: Decreases the amplitude of CLCNKB channel current but does not affect the open probability."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 98; /note="Y->A: Stimulation of CLCNKA and CLCNKB currents enhanced; intense localization in the plasma membrane with no intracellular localization observed."; /evidence="ECO:0000269|PubMed:11734858, ECO:0000269|PubMed:12761627"; MUTAGEN 115..320; /note="Missing: No effect on CLCNKB channel conductance."; /evidence="ECO:0000269|PubMed:16849430"; MUTAGEN 243..320; /note="Missing: No effect on CLCNKB channel conductance."; /evidence="ECO:0000269|PubMed:16849430
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is necessary for activation of plasma membrane-inserted CLC-K/barttin channels. {ECO:0000269|PubMed:26013830}.
uniprot
proteins
pubmed
11687798
uniprot
proteins
pubmed
11734858
uniprot
proteins
pubmed
12111250
uniprot
proteins
pubmed
12574213
uniprot
proteins
pubmed
12761627
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16328537
uniprot
proteins
pubmed
16773427
uniprot
proteins
pubmed
16849430
uniprot
proteins
pubmed
18776122
uniprot
proteins
pubmed
19646679
uniprot
proteins
pubmed
20538786
uniprot
proteins
pubmed
26013830
uniprot
proteins
sequence_length
320
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:18776122}; Multi-pass membrane protein {ECO:0000255}. Note=Mostly sorted at the basolateral membrane. A significant amount also observed intracellularly. Staining in membranes of the renal tubule and of potassium-secreting epithelia of the inner ear is basolateral (By similarity). {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 33..53; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins