ID   S26A2_RAT               Reviewed;         739 AA.
AC   O70531;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Sulfate transporter;
DE   AltName: Full=Diastrophic dysplasia protein homolog;
DE   AltName: Full=Solute carrier family 26 member 2;
GN   Name=Slc26a2; Synonyms=Dtdst;
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, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Osteosarcoma;
RX   PubMed=9575183; DOI=10.1074/jbc.273.20.12307;
RA   Satoh H., Susaki M., Shukunami C., Iyama K., Negoro T., Hiraki Y.;
RT   "Functional analysis of diastrophic dysplasia sulfate transporter. Its
RT   involvement in growth regulation of chondrocytes mediated by sulfated
RT   proteoglycans.";
RL   J. Biol. Chem. 273:12307-12315(1998).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20369363; DOI=10.1007/s00418-010-0694-x;
RA   Chapman J.M., Karniski L.P.;
RT   "Protein localization of SLC26A2 (DTDST) in rat kidney.";
RL   Histochem. Cell Biol. 133:541-547(2010).
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:9575183). 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 (By similarity). The coupling of
CC       sulfate transport to both hydroxyl and chloride ions likely serves to
CC       ensure transport at both acidic pH when most sulfate uptake is mediated
CC       by sulfate-hydroxide exchange and alkaline pH when most sulfate uptake
CC       is mediated by sulfate-chloride exchange (By similarity). Essential for
CC       chondrocyte proliferation, differentiation and cell size expansion (By
CC       similarity). {ECO:0000250|UniProtKB:Q62273,
CC       ECO:0000269|PubMed:9575183}.
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:0000250|UniProtKB:Q62273};
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:0000250|UniProtKB:Q62273};
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:0000250|UniProtKB:Q62273};
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:0000250|UniProtKB:Q62273};
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:0000250|UniProtKB:Q62273};
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:0000250|UniProtKB:Q62273};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9575183};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000269|PubMed:20369363}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Cartilage and intestine (PubMed:9575183). Expressed
CC       in the kidney (at protein level) (PubMed:20369363).
CC       {ECO:0000269|PubMed:20369363, ECO:0000269|PubMed:9575183}.
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; D82883; BAA25987.1; -; mRNA.
DR   RefSeq; NP_476468.1; NM_057127.1.
DR   RefSeq; XP_006254849.1; XM_006254787.2.
DR   RefSeq; XP_006254850.1; XM_006254788.2.
DR   RefSeq; XP_017456324.1; XM_017600835.1.
DR   AlphaFoldDB; O70531; -.
DR   SMR; O70531; -.
DR   STRING; 10116.ENSRNOP00000024374; -.
DR   GlyCosmos; O70531; 2 sites, No reported glycans.
DR   GlyGen; O70531; 2 sites.
DR   PhosphoSitePlus; O70531; -.
DR   PaxDb; 10116-ENSRNOP00000024374; -.
DR   Ensembl; ENSRNOT00000024374.3; ENSRNOP00000024374.1; ENSRNOG00000018082.3.
DR   Ensembl; ENSRNOT00055023419; ENSRNOP00055019031; ENSRNOG00055013647.
DR   Ensembl; ENSRNOT00060042897; ENSRNOP00060035524; ENSRNOG00060024801.
DR   Ensembl; ENSRNOT00065036443; ENSRNOP00065029364; ENSRNOG00065021437.
DR   GeneID; 117267; -.
DR   KEGG; rno:117267; -.
DR   UCSC; RGD:620622; rat.
DR   AGR; RGD:620622; -.
DR   CTD; 1836; -.
DR   RGD; 620622; Slc26a2.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01100000263544; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   InParanoid; O70531; -.
DR   OMA; PALYWIP; -.
DR   OrthoDB; 1067648at2759; -.
DR   PhylomeDB; O70531; -.
DR   TreeFam; TF313784; -.
DR   Reactome; R-RNO-174362; Transport and synthesis of PAPS.
DR   Reactome; R-RNO-427601; Multifunctional anion exchangers.
DR   PRO; PR:O70531; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000018082; Expressed in jejunum and 18 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0031528; C:microvillus membrane; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISO:RGD.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0035988; P:chondrocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0001503; P:ossification; IDA:RGD.
DR   GO; GO:1902358; P:sulfate transmembrane transport; ISO:RGD.
DR   GO; GO:0008272; P:sulfate transport; IDA:RGD.
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; O70531; RN.
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_0000080160"
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..44
FT                   /note="Disordered"
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"
SQ   SEQUENCE   739 AA;  82028 MW;  0C539F66D478C8DA CRC64;
     MSSENKEQHN LSPRDLPEEA YGFPPELPLG AQRGSSTDLR QFEPSDRRRA FRRIHMELHE
     KPDTNIRQLV MRKLQKSCQC NATKIRNRIF DFFPVLRWLP KYDLKKNILG DMMSGLIVGI
     LLVPQSIAYS LLAGQEPIYG LYTSFFASII YFLFGTSRHI SVGIFGILCL MIGEVVDREL
     HKACPDIDTT SSSIAMFSNG CVVVNHTLDG LCDKSCYAIK IGSTVTFMAG VYQVAMGFFQ
     VGFVSVYLSD ALLSGFVTGA SFTILTSQAK YLLGLSLPRS NGVGSVITTW IHIFRNIHKT
     NICDLITSLL CLLVLVPTKE LNEYFKSKLP APIPTELIVV VAATLASHFG KLNENYNSSI
     AGQIPTGFMP PQAPDWSLIP NVAVDAIAIS IIGFAITVSL SEMFAKKHGY TVKANQEMYA
     IGFCNIIPSF FHCITTSAAL AKTLVKESTG CQTQLSAIVT SLVLLLVLLL IAPLFYSLQK
     CVLGVITIVN LRGALLKFRD LPKMWRLSRM DTVIWFVTML SSALLSTEIG LLVGVCFSMF
     CVILRTQMPK ISLLGLEEES EIFESISTYK NLRSKSGIKV FRFIAPLYYI NKECFKSALY
     KKTLNPVLVK AAWKKAAKRK LKEETVTFHG DPDEVSMQLS HDPLELHTVV IDCSAIQFLD
     TAGIHTLKEV RRDYEAIGIQ VLLAQCNPSV RDSLAKGEYC KKEEENLLFY SLSEAVAFAE
     ESQKEKGVCV VNGLSLSGD
//