ID A0A3B3DYT1_ORYME Unreviewed; 717 AA.
AC A0A3B3DYT1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:ENSOMEP00000034614.1};
GN ORFNames=FQA47_007889 {ECO:0000313|EMBL:KAF6728174.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000034614.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000034614.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6728174.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6728174.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
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 EMBL; WKFB01000291; KAF6728174.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000034614; -.
DR PaxDb; 30732-ENSOMEP00000034614; -.
DR Ensembl; ENSOMET00000028820.1; ENSOMEP00000034614.1; ENSOMEG00000021337.1.
DR GeneTree; ENSGT01100000263544; -.
DR OMA; LGTCPQM; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
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:UP000646548};
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 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 307..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 344..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 484..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 538..703
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 589..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 78625 MW; 297F7CD761F567C4 CRC64;
MLQEDGCCPA ELDRTEAHLQ EPLILEKAEK QPSQKWHVAV SQRLKKHCSC TPQKVKFKIL
GFVPILQWLP RYQLRNWILG DVMSGVIVGI LLVPQSIAYS LLASQDPIYG LYTSFFSSII
YTLLGSSRHI SVGIFGVLCL LVGQVVDREL ALAGYLTESS ISADNATVLL AGQGNISDGQ
ICDRSCYAIT VGATVTFTAG IYQVLMGLLQ IGFVSVYLSD SLLSGFATGA SLTILTSQIK
YLLGLKIPRP QGWFTLFKTW YGLLTNIGKT NICDLITSLV CLAVLIPAKE LNDRFKAKLK
APIPFELFAV IIATLASHFG HFNAEYGSGV AGEIPTGFLP PQMPSWSLIP NVAVDAFSIA
IVGFAITVSL SEMFAKKHGY KVDANQEMYA IGFCNILPSF FRCFTTSAAL TKTLVKESTG
CQTQISGLVT ALILLLVLLV IAPLFYSLQK CVLAVIIVVN LRGALRKFLD VPRLWRVNRV
DASIWLITMG TSALVNTELG LLVGVLASAF FVLGRTQRAQ ILELGRAETR EHYEDVSSYR
GLQTHPEVAV FRYAAPIYYA NQSLFKKCLY KRIGLNPVKE KARRIKFSKC KHQEENGGKP
NTKPEENSPE VLTLVLDQES SRKLHSLVID CSGVLFLDTA GVNALKEVRK DYGEVGIKVV
LVQCNPSVLD SLERGGYFSS KDDGDVGNNK MIFFTISDGV RYAQSLATAN GDYGNQS
//