ID   S26A2_MOUSE             Reviewed;         739 AA.
AC   Q62273; Q543D6; Q8R2L9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Sulfate transporter;
DE   AltName: Full=Diastrophic dysplasia protein homolog;
DE   AltName: Full=ST-OB;
DE   AltName: Full=Solute carrier family 26 member 2;
GN   Name=Slc26a2; Synonyms=Dtd, Dtdst;
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].
RX   PubMed=9370300; DOI=10.1016/s0378-1119(97)00336-3;
RA   Kobayashi T., Sugimoto T., Saijoh K., Fukase M., Chihara K.;
RT   "Cloning of mouse diastrophic dysplasia sulfate transporter gene induced
RT   during osteoblast differentiation by bone morphogenetic protein-2.";
RL   Gene 198:341-349(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
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).
RN   [6]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=20219950; DOI=10.1152/ajpcell.00004.2010;
RA   Heneghan J.F., Akhavein A., Salas M.J., Shmukler B.E., Karniski L.P.,
RA   Vandorpe D.H., Alper S.L.;
RT   "Regulated transport of sulfate and oxalate by SLC26A2/DTDST.";
RL   Am. J. Physiol. 298:C1363-C1375(2010).
RN   [7]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF PHE-368 AND GLU-417.
RX   PubMed=22190686; DOI=10.1074/jbc.m111.297192;
RA   Ohana E., Shcheynikov N., Park M., Muallem S.;
RT   "Solute carrier family 26 member a2 (Slc26a2) protein functions as an
RT   electroneutral SOFormula/OH-/Cl- exchanger regulated by extracellular
RT   Cl-.";
RL   J. Biol. Chem. 287:5122-5132(2012).
RN   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=24302720; DOI=10.1074/jbc.m113.503466;
RA   Park M., Ohana E., Choi S.Y., Lee M.S., Park J.H., Muallem S.;
RT   "Multiple roles of the SO4(2-)/Cl-/OH- exchanger protein Slc26a2 in
RT   chondrocyte functions.";
RL   J. Biol. Chem. 289:1993-2001(2014).
CC   -!- FUNCTION: Sulfate transporter which mediates sulfate uptake into
CC       chondrocytes in order to maintain adequate sulfation of proteoglycans
CC       which is needed for cartilage development (PubMed:24302720). Mediates
CC       electroneutral anion exchange of sulfate ions for oxalate ions, sulfate
CC       and oxalate ions for chloride and/or hydroxyl ions and chloride ions
CC       for bromide, iodide and nitrate ions (PubMed:20219950, PubMed:22190686,
CC       PubMed:24302720). The coupling of sulfate transport to both hydroxyl
CC       and chloride ions likely serves to ensure transport at both acidic pH
CC       when most sulfate uptake is mediated by sulfate-hydroxide exchange and
CC       alkaline pH when most sulfate uptake is mediated by sulfate-chloride
CC       exchange (PubMed:22190686). Essential for chondrocyte proliferation,
CC       differentiation and cell size expansion (PubMed:24302720).
CC       {ECO:0000269|PubMed:20219950, ECO:0000269|PubMed:22190686,
CC       ECO:0000269|PubMed:24302720}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in);
CC         Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623;
CC         Evidence={ECO:0000269|PubMed:20219950};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 chloride(in) + sulfate(out) = 2 chloride(out) + sulfate(in);
CC         Xref=Rhea:RHEA:75091, ChEBI:CHEBI:16189, ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000269|PubMed:20219950, ECO:0000269|PubMed:22190686,
CC         ECO:0000269|PubMed:24302720};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 chloride(in) + oxalate(out) = 2 chloride(out) + oxalate(in);
CC         Xref=Rhea:RHEA:75095, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623;
CC         Evidence={ECO:0000269|PubMed:20219950, ECO:0000269|PubMed:22190686};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bromide(in) + chloride(out) = bromide(out) + chloride(in);
CC         Xref=Rhea:RHEA:75335, ChEBI:CHEBI:15858, ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000269|PubMed:22190686};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + nitrate(in) = chloride(in) + nitrate(out);
CC         Xref=Rhea:RHEA:75339, ChEBI:CHEBI:17632, ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000269|PubMed:22190686};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + iodide(in) = chloride(in) + iodide(out);
CC         Xref=Rhea:RHEA:72379, ChEBI:CHEBI:16382, ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000269|PubMed:22190686};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50443};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:O70531}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Distributed mainly in the thymus, testis and
CC       osteoblastic cells (PubMed:9370300). Highly expressed in the bone,
CC       cartilage, kidney and colon (PubMed:24302720).
CC       {ECO:0000269|PubMed:24302720, ECO:0000269|PubMed:9370300}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P50443}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000305}.
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DR   EMBL; D42049; BAA07650.1; -; mRNA.
DR   EMBL; AK052942; BAC35214.1; -; mRNA.
DR   EMBL; AK163974; BAE37562.1; -; mRNA.
DR   EMBL; CH466528; EDL09779.1; -; Genomic_DNA.
DR   EMBL; BC028345; AAH28345.1; -; mRNA.
DR   CCDS; CCDS29282.1; -.
DR   RefSeq; NP_031911.1; NM_007885.2.
DR   AlphaFoldDB; Q62273; -.
DR   SMR; Q62273; -.
DR   BioGRID; 199329; 1.
DR   STRING; 10090.ENSMUSP00000119447; -.
DR   GlyCosmos; Q62273; 2 sites, No reported glycans.
DR   GlyGen; Q62273; 2 sites.
DR   iPTMnet; Q62273; -.
DR   PhosphoSitePlus; Q62273; -.
DR   SwissPalm; Q62273; -.
DR   EPD; Q62273; -.
DR   MaxQB; Q62273; -.
DR   PaxDb; 10090-ENSMUSP00000119447; -.
DR   PeptideAtlas; Q62273; -.
DR   ProteomicsDB; 260769; -.
DR   Antibodypedia; 27892; 174 antibodies from 24 providers.
DR   DNASU; 13521; -.
DR   Ensembl; ENSMUST00000146409.8; ENSMUSP00000119447.2; ENSMUSG00000034320.15.
DR   GeneID; 13521; -.
DR   KEGG; mmu:13521; -.
DR   UCSC; uc008fbu.1; mouse.
DR   AGR; MGI:892977; -.
DR   CTD; 1836; -.
DR   MGI; MGI:892977; Slc26a2.
DR   VEuPathDB; HostDB:ENSMUSG00000034320; -.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01100000263544; -.
DR   InParanoid; Q62273; -.
DR   OMA; PALYWIP; -.
DR   OrthoDB; 1067648at2759; -.
DR   PhylomeDB; Q62273; -.
DR   TreeFam; TF313784; -.
DR   Reactome; R-MMU-174362; Transport and synthesis of PAPS.
DR   Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR   BioGRID-ORCS; 13521; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Nqo1; mouse.
DR   PRO; PR:Q62273; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q62273; Protein.
DR   Bgee; ENSMUSG00000034320; Expressed in left colon and 266 other cell types or tissues.
DR   ExpressionAtlas; Q62273; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IMP:MGI.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0035988; P:chondrocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0001503; P:ossification; ISO:MGI.
DR   GO; GO:1902358; P:sulfate transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0008272; P:sulfate transport; IMP:UniProtKB.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR018045; S04_transporter_CS.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00815; sulP; 1.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   PANTHER; PTHR11814:SF16; SULFATE TRANSPORTER; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS01130; SLC26A; 1.
DR   PROSITE; PS50801; STAS; 1.
DR   Genevisible; Q62273; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..739
FT                   /note="Sulfate transporter"
FT                   /id="PRO_0000080159"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          568..719
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50443"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         368
FT                   /note="F->A: Reduced sulfate-chloride exchange activity."
FT                   /evidence="ECO:0000269|PubMed:22190686"
FT   MUTAGEN         417
FT                   /note="E->A,K: Loss of sulfate-chloride exchange activity."
FT                   /evidence="ECO:0000269|PubMed:22190686"
FT   CONFLICT        31
FT                   /note="T -> A (in Ref. 4; AAH28345)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   739 AA;  81604 MW;  EEDB1DA6278EC6BD CRC64;
     MSSENKEQHD LSPRDLPEEA FGFPSELPLE TQRRSGTDLR QSETGHGRRA FRRIHMELRE
     KPDTDIKQFV IRELQKSCQC SAAKVRDGAF DFFPVLRWLP KYDLKKNILG DVMSGLIVGI
     LLVPQSIAYS LLAGQEPIYG LYTSFFASII YFLFGTSRHI SVGIFGILCL MIGEVVDREL
     HKACPDTDAT SSSIAVFSSG CVVVNHTLDG LCDKSCYAIK IGSTVTFMAG VYQVAMGFFQ
     VGFVSVYLSD ALLSGFVTGA SFTILTSQAK YLLGLSLPRS HGVGSVITTW IHIFRNIRNT
     NICDLITSLL CLLVLVPSKE LNEHFKDKLK APIPVELIVV VAATLASHFG KLNGNYNSSI
     AGHIPTGFMP PKAPDWSLIP NVAVDAIAIS IIGFAITVSL SEMFAKKHGY TVKANQEMYA
     IGFCNIIPSF FHCITTSAAL AKTLVKESTG CQTQLSAIVT ALVLLLVLLV IAPLFYSLQK
     CVLGVITIVN LRGALLKFRD LPKMWRLSRM DTVIWFVTML SSALLSTEIG LLVGVCFSMF
     CVILRTQKPK NSLLGLEEES ETFESISTYK NLRSKSGIKV FRFIAPLYYI NKECFKSALY
     KKALNPVLVK AAWKKAAKRK LKEEMVTFRG DPDEVSMQLS HDPLEVHTIV IDCSAIQFLD
     TAGIHTLKEV RRDYEAVGIQ VLLAQCNPSV RDSLARGEYC KKEEETLLFY SLSEAVAFAE
     DSQNQKGVCV VNGLSLSGD
//