ID A0A091W9W6_OPIHO Unreviewed; 675 AA.
AC A0A091W9W6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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};
DE Flags: Fragment;
GN ORFNames=N306_14476 {ECO:0000313|EMBL:KFR11643.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR11643.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR11643.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR11643.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK734937; KFR11643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091W9W6; -.
DR STRING; 30419.A0A091W9W6; -.
DR PhylomeDB; A0A091W9W6; -.
DR Proteomes; UP000053605; 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:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
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:UP000053605};
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 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 88..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 196..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 416..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 467..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 523..675
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR11643.1"
FT NON_TER 675
FT /evidence="ECO:0000313|EMBL:KFR11643.1"
SQ SEQUENCE 675 AA; 74339 MW; 058D7E19D42250AF CRC64;
HHRMFLEPQE KKRNMKALVV KQAKKTCSCS PAKVKDGVFS FFPILQWLPK YKLGEYLLGD
IMSGVIVGVL LVPQSIAYSL LAGQEPIYGL YTSFFASVIY CIFGTSHHIS VGVFGVICLM
VGQVVDRELQ RAGYDLEPAA LDVLTDAAAY VNTTTSPVNQ TSQELLCDKS CYAITVGATM
TFIAGVYQVA MGFFQVGFVS VYLSDSLLSG FVTGASFTIL TSQAKYLLGL DIPRSSGVGS
LIATWINIFR NIHKTNICDL ITSFLCFLVL VPTKELNDHF KSRLKAPIPV ELVVVVAATL
ASHFGKLRET YGSSVAGHIP TGFLPPRPPD WSLIPSVALD AIPIAIIGFA ITVSLSEMFA
KKHGYSVKAN QEMYAIGFCN IIPSFFHCFT TSAALAKTLV KESTGCRTQV SGMVTGLVIL
LVLLVIAPLF YSLQKCVLAV ITIVNLRGAL RKFKDLPKMW HLSRVDTVIW LVTMAASALL
STEIGLLVGV CFSMLCVIFR TQRPEAPLLG WVAESETYES LSAYKNLQTK PGIVVFRFEA
PLYYINKECF KSTLYKQTGV NPVWVKAAKK KAAKRMLREK ELDSDGNRTS ISMDFVSEPL
GFHTIVIDCC AVQFLDTAGI RTLKEVCKDY REVDVQVLLA QCNPSVRSSL IRGEFFKEGE
DHLLFHSVHQ AVDFA
//