ID   S4A11_MOUSE             Reviewed;         862 AA.
AC   A2AJN7; Q0VG86; Q3URQ1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Solute carrier family 4 member 11;
DE   AltName: Full=Sodium borate cotransporter 1;
DE            Short=NaBC1;
GN   Name=Slc4a11; Synonyms=BTR1;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-862.
RC   STRAIN=C57BL/6J;
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   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=20185830; DOI=10.1074/jbc.m109.094680;
RA   Groger N., Frohlich H., Maier H., Olbrich A., Kostin S., Braun T.,
RA   Boettger T.;
RT   "SLC4A11 prevents osmotic imbalance leading to corneal endothelial
RT   dystrophy, deafness, and polyuria.";
RL   J. Biol. Chem. 285:14467-14474(2010).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23813972; DOI=10.1093/hmg/ddt307;
RA   Vilas G.L., Loganathan S.K., Liu J., Riau A.K., Young J.D., Mehta J.S.,
RA   Vithana E.N., Casey J.R.;
RT   "Transmembrane water-flux through SLC4A11: a route defective in genetic
RT   corneal diseases.";
RL   Hum. Mol. Genet. 22:4579-4590(2013).
RN   [6]
RP   FUNCTION.
RX   PubMed=33247189; DOI=10.1038/s42003-020-01449-4;
RA   Rico P., Rodrigo-Navarro A., Sanchez Perez L., Salmeron-Sanchez M.;
RT   "Borax induces osteogenesis by stimulating NaBC1 transporter via activation
RT   of BMP pathway.";
RL   Commun. Biol. 3:717-717(2020).
CC   -!- FUNCTION: Multifunctional transporter with an impact in cell morphology
CC       and differentiation (PubMed:20185830). In the presence of borate
CC       B(OH)4(-), acts as a voltage-dependent electrogenic Na(+)-coupled
CC       B(OH)4(-) cotransporter controlling boron homeostasis (By similarity).
CC       At early stages of stem cell differentiation, participates in synergy
CC       with ITGA5-ITGB1 and ITGAV-ITGB3 integrins and BMPR1A to promote cell
CC       adhesion and contractility that drives differentiation toward
CC       osteogenic commitment while inhibiting adipogenesis (PubMed:33247189).
CC       In the absence of B(OH)4(-), acts as a Na(+)-coupled OH(-) or H(+)
CC       permeable channel with implications in cellular redox balance.
CC       Regulates the oxidative stress response in corneal endothelium by
CC       enhancing antioxidant defenses and protecting cells from reactive
CC       oxygen species. In response to hypo-osmotic challenge, also acts as
CC       water permeable channel at the basolateral cell membrane of corneal
CC       endothelial cells and facilitates transendothelial fluid reabsorption
CC       in the aqueous humor. In the presence of ammonia, acts as an
CC       electrogenic NH3/H(+) cotransporter and may play a role in ammonia
CC       transport and reabsorption in renal Henle's loop epithelium (By
CC       similarity). {ECO:0000250|UniProtKB:Q8NBS3,
CC       ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:33247189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Na(+)(in) + tetrahydroxoborate(in) = 2 Na(+)(out) +
CC         tetrahydroxoborate(out); Xref=Rhea:RHEA:66816, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:41132; Evidence={ECO:0000250|UniProtKB:Q8NBS3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66817;
CC         Evidence={ECO:0000250|UniProtKB:Q8NBS3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8NBS3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NBS3};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q8NBS3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in the endothelial cells of the cornea.
CC       In the inner ear, is located in fibrocytes underlying the stria
CC       vascularis. In the kidney, is expressed in the thin descending limb of
CC       Henle loop. {ECO:0000269|PubMed:20185830}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBS3}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice show corneal defects characterized by
CC       progressive thickening of the stroma and descement membrane concomitant
CC       with increased sodium chloride concentration in the stroma
CC       (PubMed:20185830, PubMed:23813972). They show impaired urinary
CC       concentration, increased urinary volume, and increased urinary sodium
CC       loss in the kidney. They also show stress-induced morphological changes
CC       of fibrocytes of the inner ear resulting in deafness.
CC       {ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:23813972}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
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DR   EMBL; AL772162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111884; AAI11885.1; -; mRNA.
DR   EMBL; AK141286; BAE24637.1; -; mRNA.
DR   CCDS; CCDS38244.1; -.
DR   RefSeq; NP_001074631.1; NM_001081162.1.
DR   AlphaFoldDB; A2AJN7; -.
DR   SMR; A2AJN7; -.
DR   STRING; 10090.ENSMUSP00000096963; -.
DR   GlyCosmos; A2AJN7; 2 sites, No reported glycans.
DR   GlyGen; A2AJN7; 2 sites.
DR   iPTMnet; A2AJN7; -.
DR   PhosphoSitePlus; A2AJN7; -.
DR   EPD; A2AJN7; -.
DR   PaxDb; 10090-ENSMUSP00000096963; -.
DR   PeptideAtlas; A2AJN7; -.
DR   ProteomicsDB; 256825; -.
DR   Antibodypedia; 7351; 136 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000099362.11; ENSMUSP00000096963.5; ENSMUSG00000074796.11.
DR   GeneID; 269356; -.
DR   KEGG; mmu:269356; -.
DR   UCSC; uc008mjv.1; mouse.
DR   AGR; MGI:2138987; -.
DR   CTD; 83959; -.
DR   MGI; MGI:2138987; Slc4a11.
DR   VEuPathDB; HostDB:ENSMUSG00000074796; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000154894; -.
DR   HOGENOM; CLU_002289_6_0_1; -.
DR   InParanoid; A2AJN7; -.
DR   OMA; AIFHWIV; -.
DR   OrthoDB; 1013180at2759; -.
DR   PhylomeDB; A2AJN7; -.
DR   TreeFam; TF313630; -.
DR   BioGRID-ORCS; 269356; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Slc4a11; mouse.
DR   PRO; PR:A2AJN7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AJN7; Protein.
DR   Bgee; ENSMUSG00000074796; Expressed in vestibular membrane of cochlear duct and 84 other cell types or tissues.
DR   ExpressionAtlas; A2AJN7; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR   GO; GO:0046715; F:active borate transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0015252; F:proton channel activity; ISO:MGI.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005272; F:sodium channel activity; ISO:MGI.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005372; F:water transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015701; P:bicarbonate transport; ISO:MGI.
DR   GO; GO:0046713; P:borate transport; ISO:MGI.
DR   GO; GO:0071476; P:cellular hypotonic response; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0042044; P:fluid transport; IMP:UniProtKB.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; ISO:MGI.
DR   GO; GO:0006820; P:monoatomic anion transport; IEA:InterPro.
DR   GO; GO:0050801; P:monoatomic ion homeostasis; IMP:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; ISO:MGI.
DR   GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF82; SOLUTE CARRIER FAMILY 4 MEMBER 11; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   Genevisible; A2AJN7; MM.
PE   2: Evidence at transcript level;
KW   Anion exchange; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..862
FT                   /note="Solute carrier family 4 member 11"
FT                   /id="PRO_0000352350"
FT   TOPO_DOM        1..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        380..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        399..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..428
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        429..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        453..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..542
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        543..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        578..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        600..627
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        628..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        646..670
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        692..721
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        722..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..752
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        753..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        771..774
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        775..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        798..802
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        803..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        820..823
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   TRANSMEM        824..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        845..862
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBS3"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        151
FT                   /note="A -> T (in Ref. 2; AAI11885)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        850
FT                   /note="A -> S (in Ref. 2; AAI11885)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   862 AA;  96751 MW;  D8118D841B1B8D6A CRC64;
     MSQNEHCQDS GEYFSAGTQG YFKNNMEDNL EVREDSLGDE VFDTVNSSIV SGESIRFFVN
     VNLEVQPSKS DLEAATGGCV LLHTSRKYLK LKNFEEEVRA HRDLDGFLAQ ASIILNETAT
     SLDDVLRTML NRFALDPNHA EPDCDLDLLM AKLFTDAGAP MESKVHLLSD TIQGVTATVR
     GVQYEQSWLC IICTMKTLQK RHVCISRLVR PQNWGENSCE VRFVILVLAP PKMKSTKTAM
     EVARTFATMF SDITFRQKLL KTRTEEEFKE ALVHQRQLLT MMMPRAAGHS MSSLHTHRHP
     QPPKCKDFFP FGKGIWMDIM RRFPVYPMDF TDGIIGKSKS VGKYVTTTLF LYFACLLPTI
     AFGSLNDENT NGAIDVQKTI AGQSIGGLLY ALFSGQPLVI LLTTAPLAIY TQVIRVICDD
     YNLDFNAFYA WTGLWNSFFL ALYAFLNLSL LMNLFKRSTE EIIALFISIT FVLDAVKGMV
     KIFGKYYYGH HYHTKRTSSL VSLLGIGRSP NSSLHTALNA SLLASPVEMA TTSSPGSTHS
     GQATAVLSLL IMLGTLWLGY TLYQFKKSPY LHPCVRETLS DCALPIAVLS FSLIGSYGFQ
     EIEMSKFRYN PSESLFEVAQ IHSLSFKAIG SAMGLGFLLS LLFFIEQNLV AALVNAPENR
     LVKGTAYHWD LLLLAIINTG LSLFGLPWIH AAYPHSPLHV RALALVEERV ENGHIYETIV
     DVKETRLTAL GASVLVGLSL LLLPFPLQWI PKPVLYGLFL YIALTSLDGN QLFSRVALLL
     KEQTSYPPTH YIRRVPQRKI HYFTGLQILQ LLLLCAFGMS SLPYMKMVFP LIMIAMIPIR
     YNLLPRIIEA KYLDVMDAEH RP
//