ID A0A087XKB4_POEFO Unreviewed; 718 AA.
AC A0A087XKB4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 52.
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:ENSPFOP00000006217.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000006217.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000006217.2}
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}.
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DR EMBL; AYCK01006045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007555094.1; XM_007555032.2.
DR AlphaFoldDB; A0A087XKB4; -.
DR STRING; 48698.ENSPFOP00000006217; -.
DR Ensembl; ENSPFOT00000006227.1; ENSPFOP00000006217.2; ENSPFOG00000006250.1.
DR GeneID; 103140084; -.
DR KEGG; pfor:103140084; -.
DR CTD; 1836; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01100000263544; -.
DR OMA; LGTCPQM; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000028760; 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:UP000028760};
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 73..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 182..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 300..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 338..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 426..456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 477..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 533..704
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 581..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 78551 MW; 5AE44717D0B89EED CRC64;
MLDGGNCCTA VEADPQQPLI LERAEKEPEK KWHTVVSHRV KKHCSCSPEK VKSKILSFVP
ILQWLPRYKL KDWILGDIMS GLIVGILLVP QSIAYSLLAS QDPIYGLYTS FFSSIIYAIL
GSSRHISVGI FGVLCLLVGQ VVDRELAVAG YLPESSFGSN NSDALLAGQG NSSNVECDRS
CYAITVGATV TFTAGIYQVL MGLLQVGFVS VYLSDSLLSG FATGASLTIL TSQIKYLLGL
NVPRAQGWFT LFKTWYSLLT NMAETNICDL ITSLVCLAVL IPAKELNDRF KSKLKAPIPF
ELFVVVIATV ASHFSHFNSK YGSGVAGVIP TGFAPPQLPA WTLIPNVAVD AFSIAIVGFA
ITVSLSEMFA KKHGYTVDAN QEMYAIGFCN ILPSFFRCFT TSAALTKTLV KESTGCQTQM
SGLVTAAILL LVLLVIAPLF YSLQKCVLAV IIVVNLRGAL RKFRDVPRMW RVNKIDASIW
LITMATSALV NTELGLLVGV LVSAFFVLGR TQQAQVLELG RAASREHYEN VSSYRGLQTH
FGVAVFRYGA PIYYANQSLF KKSLYKCANL NPVKEKAQRL KFEKNKKQKD TEEGAKGMPE
DKQNRESEAS SSVILMLDEK SSRSVCSLVI DCSGILFLDT AGVNALKEVR KDYRELAVEV
VLAQCNTSVL DSLERGGYYD SKKDGEVGKN NMIFFTIADA VSYVQNLNVP NGDCDNKS
//