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Database: UniProt
Entry: A0A2U3YAJ0_LEPWE
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ID   A0A2U3YAJ0_LEPWE        Unreviewed;       741 AA.
AC   A0A2U3YAJ0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
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|RefSeq:XP_006740744.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006740744.1};
RN   [1] {ECO:0000313|RefSeq:XP_006740744.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006740744.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_006740744.1; XM_006740681.2.
DR   AlphaFoldDB; A0A2U3YAJ0; -.
DR   STRING; 9713.A0A2U3YAJ0; -.
DR   GeneID; 102727835; -.
DR   KEGG; lww:102727835; -.
DR   CTD; 1836; -.
DR   OrthoDB; 1067648at2759; -.
DR   Proteomes; UP000245341; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
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   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:UP000245341};
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        110..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        140..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        219..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        254..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        421..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        456..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        516..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          571..722
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  81702 MW;  2E17C1254C58DC4A CRC64;
     MSLESKEQYD LSPKNSVEGN HQHSPLSDMH PELEKESSTN LKQFEASDQC TPYRRIHMEP
     QEKPSTNFKQ FVTKKLQKSC QCSPAKAKNM ILGFLPVLQW LPKYDLKKNI LGDVMSGLIV
     GILLVPQSIA YSLLAGQEPI YGLYTSFFAS IIYFLSGTSR HISVGIFGIL CLMIGEVVDR
     ELHKAGYDTA ENAPSTLGMV SNGSTLLNQT SDWVCDRSCY AITVGSTVTF MAGVYQVAMG
     FFQVGFVSVY LSDALLSGFV TGASFTILTS QAKYLLGLSL PRSNGVGSLI TTWIQIFRNI
     HKTNLCDLIT SLLCLLVLLP TKELNEHFKS KLKAPIPTEL IVIVAATLAS HFGKLNEKYN
     TSIAGPIPTG FMPPKAPDWN LIPSLAVDAI AISIIGFAIT VSLSEMFAKK HGYTVKANQE
     MYAIGFCNII PSFFHCFTTS AALAKTLVKE STGCQTQLSG VVTALVLLLV LLVIAPLFYS
     LQKSVLGVIT IVNLRGALRK FKDLPNMWKV SRMDTVIWFV TMLSSALIST EIGLLIGVCF
     SMFCVILRTQ KPKTSLLGLV EESEIFESVS AYKNLQTKPG IKIFRFVAPL YYINKECFKS
     ALYKKTLNPI LVKAAQKKAA KRKITKETVI LSGIQDEVSV QLSCDPLELH TIVIDCSTIQ
     FLDTAGIHTL KEVRRDYEAI GIQVLLAQCN PSVRDSLASG EYFKEEEENL LFYSVYEAVA
     FAEYQNQKGV CIPNGLSLSS D
//
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