BSND_RAT
ID BSND_RAT Reviewed; 308 AA.
AC Q8R2H3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Barttin;
GN Name=Bsnd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=12111250; DOI=10.1007/s00424-002-0819-8;
RA Waldegger S., Jeck N., Barth P., Peters M., Vitzthum H., Wolf K., Kurtz A.,
RA Konrad M., Seyberth H.W.;
RT "Barttin increases surface expression and changes current properties of
RT ClC-K channels.";
RL Pflugers Arch. 444:411-418(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DOWN-REGULATION BY FUROSEMIDE.
RX PubMed=12759757; DOI=10.1007/s00424-003-1098-8;
RA Wolf K., Meier-Meitinger M., Bergler T., Castrop H., Vitzthum H.,
RA Riegger G.A.J., Kurtz A., Kraemer B.K.;
RT "Parallel down-regulation of chloride channel CLC-K1 and barttin mRNA in
RT the thin ascending limb of the rat nephron by furosemide.";
RL Pflugers Arch. 446:665-671(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a beta-subunit for CLCNKA and CLCNKB chloride
CC channels. In the kidney CLCNK/BSND heteromers mediate chloride
CC reabsorption by facilitating its basolateral efflux. In the stria,
CC CLCNK/BSND channels drive potassium secretion by recycling chloride for
CC the basolateral SLC12A2 cotransporter. {ECO:0000269|PubMed:12111250}.
CC -!- SUBUNIT: Interacts with CLCNK channels. Forms probably heteromers with
CC CLCNKA and CLCNKB. {ECO:0000269|PubMed:12111250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Staining in membranes of the renal tubule
CC and of potassium-secreting epithelia of the inner ear is basolateral.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed along the distal nephron.
CC {ECO:0000269|PubMed:12111250}.
CC -!- INDUCTION: Regulated in parallel with CLCNKA under furosemide
CC treatment. A significant decrease occurred after furosemide treatment
CC in inner medulla (0.5 fold), whereas cortical and outer medulla levels
CC remained unaffected. Regulation with CLCNKA in inner medulla is limited
CC to the thin limb; levels in collecting ducts were not affected by
CC furosemide treatment. During furosemide treatment selective down-
CC regulation with CLCNKA in thin limb plays a role in maintaining salt
CC and water homeostasis.
CC -!- PTM: Palmitoylation is necessary for activation of plasma membrane-
CC inserted CLC-K/barttin channels. {ECO:0000250|UniProtKB:Q8WZ55}.
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DR EMBL; AJ421029; CAD12871.1; -; mRNA.
DR EMBL; BC081725; AAH81725.1; -; mRNA.
DR RefSeq; NP_620435.1; NM_138979.2.
DR AlphaFoldDB; Q8R2H3; -.
DR STRING; 10116.ENSRNOP00000008739; -.
DR iPTMnet; Q8R2H3; -.
DR PhosphoSitePlus; Q8R2H3; -.
DR PaxDb; Q8R2H3; -.
DR PRIDE; Q8R2H3; -.
DR Ensembl; ENSRNOT00000008739; ENSRNOP00000008739; ENSRNOG00000006543.
DR GeneID; 192675; -.
DR KEGG; rno:192675; -.
DR UCSC; RGD:621139; rat.
DR CTD; 7809; -.
DR RGD; 621139; Bsnd.
DR eggNOG; ENOG502S3DP; Eukaryota.
DR GeneTree; ENSGT00390000008549; -.
DR HOGENOM; CLU_078815_0_0_1; -.
DR InParanoid; Q8R2H3; -.
DR OMA; FYAMGSV; -.
DR OrthoDB; 1577809at2759; -.
DR PhylomeDB; Q8R2H3; -.
DR TreeFam; TF335975; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:Q8R2H3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000006543; Expressed in kidney and 3 other tissues.
DR Genevisible; Q8R2H3; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IEA:Ensembl.
DR GO; GO:0017081; F:chloride channel regulator activity; IMP:RGD.
DR GO; GO:0006821; P:chloride transport; IMP:RGD.
DR InterPro; IPR029181; Barttin.
DR PANTHER; PTHR28399; PTHR28399; 1.
DR Pfam; PF15462; Barttin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Barttin"
FT /id="PRO_0000065001"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 127..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM4"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM4"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 54
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ55"
FT LIPID 56
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ55"
SQ SEQUENCE 308 AA; 33895 MW; FD96B807CABC3173 CRC64;
MADEKTFRIG FIVLGLFLLS LGTFLMSHDR PQVYGTFYAM GSIMVIGGVL WSMCQCYPKI
TFVPADSDFQ GMLSPKALSL LETGLSEVKS PQPPYVRLWE EAAYDQSLPD FTHIQMKVMG
YSEDPRPLLA PELKTGTSSA KEGEPHSAQT WMEAAVVVHR ELDEKEGEKS RSQSSPPACS
QGSAPLASFH DDLDVGSSEG RSPQPSPPDR DEAHLQVPWA SRGPLDRFGD FALIDDTPIS
EDMGLEGQAQ EEALPSKQPW SLRMKEETVQ AGAEEPEQEE EDLYYGLPDS PGDPLPDKEL
GFEPDVQG
