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Protein

Barttin

Gene

Bsnd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter.

GO - Molecular functioni

GO - Biological processi

  • cellular chloride ion homeostasis Source: UniProtKB
  • cellular ion homeostasis Source: MGI
  • cellular potassium ion homeostasis Source: UniProtKB
  • chloride transmembrane transport Source: GOC
  • sensory perception of sound Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Barttin
Gene namesi
Name:Bsnd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2153465. Bsnd.

Subcellular locationi

  • Basolateral cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

  • 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 2621HelicalSequence analysisAdd
BLAST
Topological domaini27 – 326ExtracellularSequence analysis
Transmembranei33 – 5321HelicalSequence analysisAdd
BLAST
Topological domaini54 – 307254CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307BarttinPRO_0000065000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi54 – 541S-palmitoyl cysteineBy similarity
Lipidationi56 – 561S-palmitoyl cysteineBy similarity
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei107 – 1071PhosphoserineCombined sources
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei228 – 2281PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineBy similarity

Post-translational modificationi

Palmitoylation is necessary for activation of plasma membrane-inserted CLC-K/barttin channels.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ8VIM4.
PaxDbiQ8VIM4.
PRIDEiQ8VIM4.

PTM databases

iPTMnetiQ8VIM4.
PhosphoSiteiQ8VIM4.

Expressioni

Tissue specificityi

Expression is evident in inner and outer stripes of the outer medulla of the kidney, most probably representing thin limbs of Henle's loop together with some collecting duct coursing through the outer stripe. In situ hybridization in fetal kidney at 18.5 dpc revealed a clear continuity between hybridization signals from the thin limb of Henle's loop and the distal convoluted tubule, suggesting that part of the expression pattern may result from expression in the thick ascending limb of Henle's loop. In addition, strong signals are present in a subset of cortical tubules, representing distal convoluted tubules or cortical collecting duct. Strong expression is also observed in the inner medulla of the kidney. This expression does not extend all the way to the tip of the papilla. Thus this signal most probably represents cells of the thin ascending limbs. In the inner ear, strong and exclusive expression is detected in marginal cells of the stria vascularis. In addition to cochlear signal, expression is observed in dark cells localized at the base of the crista ampullaris of the vestibular organ.2 Publications

Gene expression databases

BgeeiENSMUSG00000025418.
GenevisibleiQ8VIM4. MM.

Interactioni

Subunit structurei

Interacts with CLCNK channels. Forms probably heteromers with CLCNKA in the thin ascending limb of Henle and with CLCNKB in the thick ascending limb and more distal segments.1 Publication

Protein-protein interaction databases

IntActiQ8VIM4. 1 interaction.
MINTiMINT-4089408.
STRINGi10090.ENSMUSP00000049563.

Structurei

3D structure databases

ProteinModelPortaliQ8VIM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J53T. Eukaryota.
ENOG410ZGZV. LUCA.
GeneTreeiENSGT00390000008549.
HOGENOMiHOG000049268.
HOVERGENiHBG050739.
InParanoidiQ8VIM4.
KOiK19331.
OMAiDFSHIQM.
OrthoDBiEOG091G0IJM.
TreeFamiTF335975.

Family and domain databases

InterProiIPR029181. Barttin_dom.
[Graphical view]
PfamiPF15462. Barttin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VIM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEKTFRIG FIVLGLFLLS LGTFLMSHDR PQVYGTFYAM GSVMVIGGVI
60 70 80 90 100
WSMCQCYPKI TFVPADSDFQ GILSPKALSL LETGLSEVKS PQPPYVRLWE
110 120 130 140 150
EAAYDQSLPD FTHIQMKVMG YSEDPRPLLA PELKTGASSV REGEPRTAQA
160 170 180 190 200
WMEAPVVVHR GSDENEGEKS HSQSSPSVGP QGSAPLASFH DDLDVGSSEG
210 220 230 240 250
SSLQPSPNRD EPHRQVPWAS RGPLDRFSDF ALIDDTPTSE DTVLDGQARE
260 270 280 290 300
AALPRKQQWS LRMKGETVQA RAEEPEQEEE DLYYGLPDSP GNPLPDKELG

FEPDIQG
Length:307
Mass (Da):33,813
Last modified:October 3, 2012 - v3
Checksum:iBB837B92EC39F2CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831T → A in AAL33907 (PubMed:11687798).Curated
Sequence conflicti292 – 2921N → D in AAQ81629 (Ref. 2) Curated
Sequence conflicti292 – 2921N → D in AAH38287 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF391088 mRNA. Translation: AAL33907.1.
AY373833 mRNA. Translation: AAQ81629.1.
AK052587 mRNA. Translation: BAC35049.1.
AL954352 Genomic DNA. Translation: CAM15752.1.
BC038287 mRNA. Translation: AAH38287.1.
CCDSiCCDS18419.1.
RefSeqiNP_536706.2. NM_080458.2.
UniGeneiMm.135448.

Genome annotation databases

EnsembliENSMUST00000054472; ENSMUSP00000049563; ENSMUSG00000025418.
GeneIDi140475.
KEGGimmu:140475.
UCSCiuc008tyj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF391088 mRNA. Translation: AAL33907.1.
AY373833 mRNA. Translation: AAQ81629.1.
AK052587 mRNA. Translation: BAC35049.1.
AL954352 Genomic DNA. Translation: CAM15752.1.
BC038287 mRNA. Translation: AAH38287.1.
CCDSiCCDS18419.1.
RefSeqiNP_536706.2. NM_080458.2.
UniGeneiMm.135448.

3D structure databases

ProteinModelPortaliQ8VIM4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VIM4. 1 interaction.
MINTiMINT-4089408.
STRINGi10090.ENSMUSP00000049563.

PTM databases

iPTMnetiQ8VIM4.
PhosphoSiteiQ8VIM4.

Proteomic databases

MaxQBiQ8VIM4.
PaxDbiQ8VIM4.
PRIDEiQ8VIM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054472; ENSMUSP00000049563; ENSMUSG00000025418.
GeneIDi140475.
KEGGimmu:140475.
UCSCiuc008tyj.1. mouse.

Organism-specific databases

CTDi7809.
MGIiMGI:2153465. Bsnd.

Phylogenomic databases

eggNOGiENOG410J53T. Eukaryota.
ENOG410ZGZV. LUCA.
GeneTreeiENSGT00390000008549.
HOGENOMiHOG000049268.
HOVERGENiHBG050739.
InParanoidiQ8VIM4.
KOiK19331.
OMAiDFSHIQM.
OrthoDBiEOG091G0IJM.
TreeFamiTF335975.

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Miscellaneous databases

PROiQ8VIM4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025418.
GenevisibleiQ8VIM4. MM.

Family and domain databases

InterProiIPR029181. Barttin_dom.
[Graphical view]
PfamiPF15462. Barttin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBSND_MOUSE
AccessioniPrimary (citable) accession number: Q8VIM4
Secondary accession number(s): B1AZI5, Q8C740, Q8CHY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 3, 2012
Last modified: September 7, 2016
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.