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Database: UniProt
Entry: I3J8X3_ORENI
LinkDB: I3J8X3_ORENI
Original site: I3J8X3_ORENI 
ID   I3J8X3_ORENI            Unreviewed;       716 AA.
AC   I3J8X3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 72.
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:ENSONIP00000005313.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005313.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000005313.2}
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|RuleBase:RU362052}.
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DR   RefSeq; XP_019211041.1; XM_019355496.1.
DR   RefSeq; XP_019211042.1; XM_019355497.1.
DR   RefSeq; XP_019211043.1; XM_019355498.1.
DR   RefSeq; XP_019211044.1; XM_019355499.1.
DR   RefSeq; XP_019211045.1; XM_019355500.1.
DR   RefSeq; XP_019211047.1; XM_019355502.1.
DR   AlphaFoldDB; I3J8X3; -.
DR   STRING; 8128.ENSONIP00000005313; -.
DR   Ensembl; ENSONIT00000005317.2; ENSONIP00000005313.2; ENSONIG00000004222.2.
DR   GeneID; 100696803; -.
DR   KEGG; onl:100696803; -.
DR   CTD; 1836; -.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01100000263544; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   InParanoid; I3J8X3; -.
DR   OMA; LGTCPQM; -.
DR   OrthoDB; 1067648at2759; -.
DR   TreeFam; TF313784; -.
DR   Proteomes; UP000005207; Linkage group LG2.
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   GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl.
DR   GO; GO:0048884; P:neuromast development; IEA:Ensembl.
DR   GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 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:UP000005207};
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        77..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        129..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        219..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        305..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        342..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        387..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        426..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        480..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          536..703
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          582..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78248 MW;  2EE99F3B0E38C803 CRC64;
     MLHGEDSCAA VEDGGEEDQH RPLILERIEK ETGRTWRTVL SQRLRKHCSC TPEKAKSRIL
     SFFPVLQWLP RYKLRDWILG DAMSGVIVGI LLVPQSIAYS LLANQDPIYG LYTSFFASII
     YALLGTSRHI SVGIFGVLCL LIGQVVDREL ALAGYLPESS LSGNDSSVPL AGNDSGVVGC
     DQSCYAIAVG ATVTFTAGIY QVLMGLLQVG FVSVYLSDSL LSGFATGASL TILTSQIKYL
     LGLKIPRPQG WFTLFKTWYG LLSNLGNTNV CDLITSLVCL AVLIPTKELN DRFKSKLKAP
     IPFELFVVII ATLASHFGHF NAKYGSGVAG VIPTGFLPPQ MPMWSLIPNV AVDAFSIAIV
     GFAITVSLSE MFAKKHGYTV DANQEMYAIG FCNILPSFFH CFTSSAALTK TLVKESTGCQ
     TQLSGLISAL LLLLVLLVIA PLFYSLQKCV LAAIIVVNLR GALRKFTDIP CMWRANHIDA
     FIWLITMATS ALVNTELGLL VGVLVSAFCV LGRTQRVQVL ELGRAMTREH YEDLASYKGL
     QTHPDVAIFR YEAPIYYANQ NLFKKSLYRC VGLDPVKEKS RRVKFQNSKR QEEAAGVPTS
     NSDEKEAEAP PAVTLMMNTA SRQLRRVVID CSAVLFLDTA GVNALKEVRK DYGELGVVVE
     LAQCNTSVLD TLERGGYYSN QKGGNAGENR TIFFTIEDAV LHVQSPSTPN GDCDKS
//
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