BSND_MOUSE
ID BSND_MOUSE Reviewed; 307 AA.
AC Q8VIM4; B1AZI5; Q8C740; Q8CHY0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Barttin;
GN Name=Bsnd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11687798; DOI=10.1038/ng752;
RA Birkenhaeger R., Otto E., Schuermann M.J., Vollmer M., Ruf E.-M.,
RA Maier-Lutz I., Beekmann F., Fekete A., Omran H., Feldmann D., Milford D.V.,
RA Jeck N., Konrad M., Landau D., Knoers N.V.A.M., Antignac C., Sudbrak R.,
RA Kispert A., Hildebrandt F.;
RT "Mutation of BSND causes Bartter syndrome with sensorineural deafness and
RT kidney failure.";
RL Nat. Genet. 29:310-314(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RA Nie L., Feng W., Dinglasan J.N., Yamoah E.N.;
RT "Functional phenotype of inner ear-specific chloride channel ClC-K and its
RT accessory subunit.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11734858; DOI=10.1038/35107099;
RA Estevez R., Boettger T., Stein V., Birkenhaeger R., Otto E.,
RA Hildebrandt F., Jentsch T.J.;
RT "Barttin is a Cl- channel beta-subunit crucial for renal Cl-reabsorption
RT and inner ear K+ secretion.";
RL Nature 414:558-561(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-107; SER-162 AND
RP SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SUBUNIT: Interacts with CLCNK channels. Forms probably heteromers with
CC CLCNKA in the thin ascending limb of Henle and with CLCNKB in the thick
CC ascending limb and more distal segments. {ECO:0000269|PubMed:11734858}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:11734858}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11734858}. Note=Staining in membranes of the renal
CC tubule is basolateral. Also detected in basolateral membranes of
CC intercalated cells of the collecting duct, which are known to express
CC CLCNKB as well. Both acid-secreting alpha-intercalated cells and base-
CC secreting beta-intercalated cells express this protein basolaterally,
CC but intervening AQP2-expressing principal cells appear devoid of
CC protein expression. In the inner ear, colocalizes with CLCNK in K(+)-
CC secreting marginal cells of the stria vascularis. The basolateral
CC staining contrasts with the apical localization of the KCNQ1 K(+)
CC channel. Also found in K(+)-secreting vestibular dark cells, where it
CC colocalized in basolateral membranes with CLCNK below apical membranes
CC that expressed KCNQ1.
CC -!- TISSUE SPECIFICITY: Expression is evident in inner and outer stripes of
CC the outer medulla of the kidney, most probably representing thin limbs
CC of Henle's loop together with some collecting duct coursing through the
CC outer stripe. In situ hybridization in fetal kidney at 18.5 dpc
CC revealed a clear continuity between hybridization signals from the thin
CC limb of Henle's loop and the distal convoluted tubule, suggesting that
CC part of the expression pattern may result from expression in the thick
CC ascending limb of Henle's loop. In addition, strong signals are present
CC in a subset of cortical tubules, representing distal convoluted tubules
CC or cortical collecting duct. Strong expression is also observed in the
CC inner medulla of the kidney. This expression does not extend all the
CC way to the tip of the papilla. Thus this signal most probably
CC represents cells of the thin ascending limbs. In the inner ear, strong
CC and exclusive expression is detected in marginal cells of the stria
CC vascularis. In addition to cochlear signal, expression is observed in
CC dark cells localized at the base of the crista ampullaris of the
CC vestibular organ. {ECO:0000269|PubMed:11687798,
CC ECO:0000269|PubMed:11734858}.
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; AF391088; AAL33907.1; -; mRNA.
DR EMBL; AY373833; AAQ81629.1; -; mRNA.
DR EMBL; AK052587; BAC35049.1; -; mRNA.
DR EMBL; AL954352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038287; AAH38287.1; -; mRNA.
DR CCDS; CCDS18419.1; -.
DR RefSeq; NP_536706.2; NM_080458.2.
DR AlphaFoldDB; Q8VIM4; -.
DR STRING; 10090.ENSMUSP00000049563; -.
DR iPTMnet; Q8VIM4; -.
DR PhosphoSitePlus; Q8VIM4; -.
DR SwissPalm; Q8VIM4; -.
DR jPOST; Q8VIM4; -.
DR MaxQB; Q8VIM4; -.
DR PaxDb; Q8VIM4; -.
DR PRIDE; Q8VIM4; -.
DR ProteomicsDB; 273846; -.
DR Antibodypedia; 33230; 176 antibodies from 25 providers.
DR DNASU; 140475; -.
DR Ensembl; ENSMUST00000054472; ENSMUSP00000049563; ENSMUSG00000025418.
DR GeneID; 140475; -.
DR KEGG; mmu:140475; -.
DR UCSC; uc008tyj.1; mouse.
DR CTD; 7809; -.
DR MGI; MGI:2153465; Bsnd.
DR VEuPathDB; HostDB:ENSMUSG00000025418; -.
DR eggNOG; ENOG502S3DP; Eukaryota.
DR GeneTree; ENSGT00390000008549; -.
DR HOGENOM; CLU_078815_0_0_1; -.
DR InParanoid; Q8VIM4; -.
DR OMA; FYAMGSV; -.
DR OrthoDB; 1577809at2759; -.
DR TreeFam; TF335975; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 140475; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8VIM4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VIM4; protein.
DR Bgee; ENSMUSG00000025418; Expressed in inner renal medulla loop of Henle and 44 other tissues.
DR Genevisible; Q8VIM4; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0017081; F:chloride channel regulator activity; ISO:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; NAS:UniProtKB.
DR GO; GO:0006873; P:cellular ion homeostasis; ISO:MGI.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; NAS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IEA:GOC.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; NAS:UniProtKB.
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..307
FT /note="Barttin"
FT /id="PRO_0000065000"
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..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R2H3"
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"
FT CONFLICT 83
FT /note="T -> A (in Ref. 1; AAL33907)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="N -> D (in Ref. 2; AAQ81629 and 5; AAH38287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33813 MW; BB837B92EC39F2CF CRC64;
MADEKTFRIG FIVLGLFLLS LGTFLMSHDR PQVYGTFYAM GSVMVIGGVI WSMCQCYPKI
TFVPADSDFQ GILSPKALSL LETGLSEVKS PQPPYVRLWE EAAYDQSLPD FTHIQMKVMG
YSEDPRPLLA PELKTGASSV REGEPRTAQA WMEAPVVVHR GSDENEGEKS HSQSSPSVGP
QGSAPLASFH DDLDVGSSEG SSLQPSPNRD EPHRQVPWAS RGPLDRFSDF ALIDDTPTSE
DTVLDGQARE AALPRKQQWS LRMKGETVQA RAEEPEQEEE DLYYGLPDSP GNPLPDKELG
FEPDIQG
