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Protein

Barttin

Gene

Bsnd

Organism
Rattus norvegicus (Rat)
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.1 Publication

GO - Molecular functioni

  • chloride channel activity Source: Ensembl
  • chloride channel regulator activity Source: RGD

GO - Biological processi

  • chloride transport Source: RGD
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Barttin
Gene namesi
Name:Bsnd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621139. Bsnd.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Staining in membranes of the renal tubule and of potassium-secreting epithelia of the inner ear is basolateral.By similarity

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 – 308255CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308BarttinPRO_0000065001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi54 – 541S-palmitoyl cysteineBy similarity
Lipidationi56 – 561S-palmitoyl cysteineBy similarity
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei107 – 1071PhosphoserineBy similarity
Modified residuei290 – 2901PhosphoserineCombined sources

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

PaxDbiQ8R2H3.
PRIDEiQ8R2H3.

PTM databases

PhosphoSiteiQ8R2H3.

Expressioni

Tissue specificityi

Expressed along the distal nephron.1 Publication

Inductioni

Regulated in parallel with CLCNKA under furosemide treatment. A significant decrease occurred after furosemide treatment in inner medulla (0.5 fold), whereas cortical and outer medulla levels remained unaffected. Regulation with CLCNKA in inner medulla is limited to the thin limb; levels in collecting ducts were not affected by furosemide treatment. During furosemide treatment selective down-regulation with CLCNKA in thin limb plays a role in maintaining salt and water homeostasis.

Gene expression databases

GenevisibleiQ8R2H3. RN.

Interactioni

Subunit structurei

Interacts with CLCNK channels. Forms probably heteromers with CLCNKA and CLCNKB.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008739.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J53T. Eukaryota.
ENOG410ZGZV. LUCA.
GeneTreeiENSGT00390000008549.
HOGENOMiHOG000049268.
HOVERGENiHBG050739.
InParanoidiQ8R2H3.
KOiK19331.
OMAiDFSHIQM.
OrthoDBiEOG7BS4BK.
PhylomeDBiQ8R2H3.
TreeFamiTF335975.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8R2H3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEKTFRIG FIVLGLFLLS LGTFLMSHDR PQVYGTFYAM GSIMVIGGVL
60 70 80 90 100
WSMCQCYPKI TFVPADSDFQ GMLSPKALSL LETGLSEVKS PQPPYVRLWE
110 120 130 140 150
EAAYDQSLPD FTHIQMKVMG YSEDPRPLLA PELKTGTSSA KEGEPHSAQT
160 170 180 190 200
WMEAAVVVHR ELDEKEGEKS RSQSSPPACS QGSAPLASFH DDLDVGSSEG
210 220 230 240 250
RSPQPSPPDR DEAHLQVPWA SRGPLDRFGD FALIDDTPIS EDMGLEGQAQ
260 270 280 290 300
EEALPSKQPW SLRMKEETVQ AGAEEPEQEE EDLYYGLPDS PGDPLPDKEL

GFEPDVQG
Length:308
Mass (Da):33,895
Last modified:June 1, 2002 - v1
Checksum:iFD96B807CABC3173
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421029 mRNA. Translation: CAD12871.1.
BC081725 mRNA. Translation: AAH81725.1.
RefSeqiNP_620435.1. NM_138979.2.
UniGeneiRn.22715.

Genome annotation databases

EnsembliENSRNOT00000008739; ENSRNOP00000008739; ENSRNOG00000006543.
GeneIDi192675.
KEGGirno:192675.
UCSCiRGD:621139. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421029 mRNA. Translation: CAD12871.1.
BC081725 mRNA. Translation: AAH81725.1.
RefSeqiNP_620435.1. NM_138979.2.
UniGeneiRn.22715.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008739.

PTM databases

PhosphoSiteiQ8R2H3.

Proteomic databases

PaxDbiQ8R2H3.
PRIDEiQ8R2H3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008739; ENSRNOP00000008739; ENSRNOG00000006543.
GeneIDi192675.
KEGGirno:192675.
UCSCiRGD:621139. rat.

Organism-specific databases

CTDi7809.
RGDi621139. Bsnd.

Phylogenomic databases

eggNOGiENOG410J53T. Eukaryota.
ENOG410ZGZV. LUCA.
GeneTreeiENSGT00390000008549.
HOGENOMiHOG000049268.
HOVERGENiHBG050739.
InParanoidiQ8R2H3.
KOiK19331.
OMAiDFSHIQM.
OrthoDBiEOG7BS4BK.
PhylomeDBiQ8R2H3.
TreeFamiTF335975.

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Miscellaneous databases

NextBioi623089.
PROiQ8R2H3.

Gene expression databases

GenevisibleiQ8R2H3. RN.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Barttin increases surface expression and changes current properties of ClC-K channels."
    Waldegger S., Jeck N., Barth P., Peters M., Vitzthum H., Wolf K., Kurtz A., Konrad M., Seyberth H.W.
    Pflugers Arch. 444:411-418(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    Strain: Wistar.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Parallel down-regulation of chloride channel CLC-K1 and barttin mRNA in the thin ascending limb of the rat nephron by furosemide."
    Wolf K., Meier-Meitinger M., Bergler T., Castrop H., Vitzthum H., Riegger G.A.J., Kurtz A., Kraemer B.K.
    Pflugers Arch. 446:665-671(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY FUROSEMIDE.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBSND_RAT
AccessioniPrimary (citable) accession number: Q8R2H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2002
Last modified: December 9, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.