ID A0A091KGD0_EGRGA Unreviewed; 675 AA.
AC A0A091KGD0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=Z169_04301 {ECO:0000313|EMBL:KFP22801.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP22801.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP22801.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP22801.1};
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; KK502338; KFP22801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KGD0; -.
DR STRING; 188379.A0A091KGD0; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma 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 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:UP000053119};
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..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 98..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 284..304
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:KFP22801.1"
FT NON_TER 675
FT /evidence="ECO:0000313|EMBL:KFP22801.1"
SQ SEQUENCE 675 AA; 74758 MW; DB35B82F1E3CC1EB CRC64;
HNRMFLEPQE KKRSMKALVV KQAKKTCSCT PAKVKEYIFS FFPVLQWLPK YKLREYLLGD
IMSGVIVGVL LVPQSIAYSL LAGQEPIYGL YTSFFASIIY FIFGTSRHIS VGIFGVICLM
VGQVVDREIQ RAGYDLEPAV LSGLPDTAAY VNTTISPVNQ TLQKLLCDKS CYAITVGATM
TFIAGVYQVA MGFFQVGFVS VYLSDSLLSG FVTGASFTIL TSQAKYLLGL DIPRSSGIGS
LIATWINIFR NIHKTNICDV ITSLLCFLLL IPTKELNEHF KSKLKAPIPV ELVVIVVATV
ASHFGKLKET YGSSVAGHIP TGFLPPRPPD WNLIPNVALD AIPIAIIGFA ITVSLSEMFA
KKHGYSVRAN QEMYAIGFCN IIPSFFHCFT TSAALAKTLV KESTGCRTQM SGMVTSLVIL
LVLLVIAPLF YSLQKCVLAV ITIVNLRGAL RKFKDLPKMW HLSRVDTVIW LVTMAASALI
STEIGLLVGV CFSMLCVIFR TQRPEAPLLG WVAESETYES LSAYKNLQTK PGIVVFRFEA
PLYYINKECF KSTLYKQTGV NPVWVKAAKK KAAKRMLREK EVDSDGNQTS ISMDFVSEPL
GFHTIVIDCC AVQFLDTAGI RTLKEVCKDY REINVQVLLA QCNPSVRSSL IRGEFFREGE
DHLLFHSVHQ AVDFA
//
