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   12-OCT-2022, entry version 120.
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; 175 antibodies from 24 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
//