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Database: UniProt
Entry: U3IQR8_ANAPP
LinkDB: U3IQR8_ANAPP
Original site: U3IQR8_ANAPP 
ID   U3IQR8_ANAPP            Unreviewed;       719 AA.
AC   U3IQR8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   24-JAN-2024, entry version 60.
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|Ensembl:ENSAPLP00000009591.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000009591.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000009591.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000009591.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|RuleBase:RU362052}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362052}.
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DR   AlphaFoldDB; U3IQR8; -.
DR   STRING; 8840.ENSAPLP00000009591; -.
DR   Ensembl; ENSAPLT00000010286.2; ENSAPLP00000009591.2; ENSAPLG00000009889.2.
DR   GeneTree; ENSGT01100000263544; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   OMA; LGTCPQM; -.
DR   Proteomes; UP000016666; Chromosome 14.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:Ensembl.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
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; PS50801; STAS; 1.
PE   3: Inferred from homology;
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:UP000016666};
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        88..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        129..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        404..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        446..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        497..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          553..705
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
SQ   SEQUENCE   719 AA;  78940 MW;  AC5A91DAFB930BD6 CRC64;
     MAVLKMAATA EFSSVRSVAE VPEGDDAKHV FHHRMFLEPQ EEKRDLKALM VKRAKEICSC
     TPAKVKDCVF SLFPILQWLP KYKLKECLLG DVMSGVIVGV LLVPQSIAYS LLAGQEPIYG
     LYTSFFAGII YSIFGTSHHI SVGIFGALCL MVGQVVDREV QRAGYDLEAT VSAHTDTVTQ
     VNTTIVPLNQ TSQILLCDKT CYAIKVGATM TFIAGVYQVA MGFFQVGFVS VYLSDSLLSG
     FVTGASFTIL TSQAKYLLGL DIPRSSGVGS VITTWINIFR NIHKTNICDL ITSFLCFLVL
     IPTKELNERF KSRLKAPIPI ELAVVVAATL ASHLGKLRET YGSSIAGEIP TGFLPPRPPE
     WNLIPNVALD AIPIAIIGFA ITVSLSEMFA KKHGYTVRAN QEMYAIGFCN IIPSFFHCFT
     TSAALAKTLV KESTGCRTQI SGIVTSLLIL IVLLVIAPLF YSLQKCVLAV ITIVNLRGAL
     RKFKDLPKMW HLSRVDTIIW IVTMASSALI STEIGLLVGV CFSMLCVIFR TQKPEAPLLG
     WVAESETYES LSAYKNLQTK PGVMVFRFEA PLYYINKECF KSTLYKQTGV NPAQVKAAKK
     KAAKRMLRHK EMGSGGNQTG ISLELVSEPL GFHTIVIDCC AVQFLDTAGI RTLKEVCKDY
     KEIDVQVLLA QCNPSVRSSL IRGEFFKEGE DHLLFHSVHQ AVDFALGVQE HSGTSASKN
//
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