ID H2QRS4_PANTR Unreviewed; 739 AA.
AC H2QRS4; A0A2J8NJG4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Sulfate transporter {ECO:0000256|ARBA:ARBA00017873, ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Solute carrier family 26 member 2 {ECO:0000256|ARBA:ARBA00030135, ECO:0000256|RuleBase:RU362052};
GN Name=SLC26A2 {ECO:0000313|EMBL:JAA10498.1,
GN ECO:0000313|Ensembl:ENSPTRP00000078088.1,
GN ECO:0000313|VGNC:VGNC:13588};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000078088.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000078088.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA10498.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA10498.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA40687.1}, Skin {ECO:0000313|EMBL:JAA24856.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA14676.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000078088.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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. Mediates electroneutral
CC anion exchange of sulfate ions for oxalate ions, sulfate and oxalate
CC ions for chloride and/or hydroxyl ions and chloride ions for bromide,
CC iodide and nitrate ions. The coupling of sulfate transport to both
CC hydroxyl and chloride ions likely serves to ensure transport at both
CC acidic pH when most sulfate uptake is mediated by sulfate-hydroxide
CC exchange and alkaline pH when most sulfate uptake is mediated by
CC sulfate-chloride exchange. Essential for chondrocyte proliferation,
CC differentiation and cell size expansion.
CC {ECO:0000256|RuleBase:RU362052}.
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:0000256|ARBA:ARBA00036947};
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:0000256|ARBA:ARBA00036707};
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:0000256|ARBA:ARBA00036469};
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:0000256|ARBA:ARBA00036577};
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:0000256|ARBA:ARBA00036182};
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:0000256|ARBA:ARBA00036514};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|ARBA:ARBA00008692, ECO:0000256|RuleBase:RU362052}.
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DR EMBL; AACZ04059120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01000840; JAA10498.1; -; mRNA.
DR EMBL; GABF01007469; JAA14676.1; -; mRNA.
DR EMBL; GABD01008244; JAA24856.1; -; mRNA.
DR EMBL; GABE01004052; JAA40687.1; -; mRNA.
DR RefSeq; XP_016809513.1; XM_016954024.1.
DR STRING; 9598.ENSPTRP00000078088; -.
DR PaxDb; 9598-ENSPTRP00000029741; -.
DR Ensembl; ENSPTRT00000095738.1; ENSPTRP00000078088.1; ENSPTRG00000043485.1.
DR GeneID; 742297; -.
DR CTD; 1836; -.
DR VGNC; VGNC:13588; SLC26A2.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01100000263544; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR OMA; LGTCPQM; -.
DR OrthoDB; 1067648at2759; -.
DR TreeFam; TF313784; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000043485; Expressed in lung and 20 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR CDD; cd06844; STAS; 1.
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.
PE 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 418..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 453..476
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 513..544
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 568..719
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 1..27
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"
SQ SEQUENCE 739 AA; 81666 MW; BDFAD4F8FC1AB887 CRC64;
MSSESKEQHD VSPRDSAEGN DSYPSGIHLE LQRESSTDFK QFETNDQCRP YHRILIERQE
KSDTNFKEFV IKKLQKNCQC SPAKAKNMIL GFLPVLQWLP KYDLKKNILG DVMSGLIVGI
LLVPQSIAYS LLAGQEPVYG LYTSFFASII YFLLGTSRHI SVGIFGVLCL MIGETVDREL
QKAGYDNAHS APSLGMVSNG STLLNHTSDR ICDKSCYAIM VGSTVTFIAG VYQVAMGFFQ
VGFVSVYLSD ALLSGFVTGA SFTILTSQAK YLLGLNLPRT NGVGSLITTW IHVFRNIHKT
NLCDLITSLL CLLVLLPTKE LNEHFKSKLK APIPIELVVV VAATLASHFG KLHENYNSSI
AGHIPTGFMP PKVPEWNLIP SVAVDAIAIS IIGFAITVSL SEMFAKKHGY TVKANQEMYA
IGFCNIIPSF FHCFTTSAAL AKTLVKESTG CHTQLSGVVT ALVLLLVLLV IAPLFYSLQK
SVLGVITIVN LRGALRKFRD LPKMWSISRM DTVIWFVTML SSALLSTEIG LLVGVCFSMF
CVILRTQKPK SSLLGLVEES EVFESVSAYK NLQTKPGIKI FRFVAPLYYI NKECFKSALY
KQTVNPILIK VAWKKAAKRK IKEKVVTLGG IQDEMSVQLS HDPLELHTIV IDCSAIQFLD
TAGIHTLKEV RRDYEAIGIQ VLLAQCNPSV RDSLINGEYC KKEEENLLFY SVYEAMAFAE
VSKNQKGVCV PNGLSLSSD
//