ID A0A091IBB8_CALAN Unreviewed; 673 AA.
AC A0A091IBB8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=N300_13057 {ECO:0000313|EMBL:KFP04680.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP04680.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP04680.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP04680.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362052}.
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DR EMBL; KL218372; KFP04680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IBB8; -.
DR STRING; 9244.A0A091IBB8; -.
DR Proteomes; UP000054308; 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:UP000054308};
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 182..202
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..673
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP04680.1"
FT NON_TER 673
FT /evidence="ECO:0000313|EMBL:KFP04680.1"
SQ SEQUENCE 673 AA; 74057 MW; 42CAEB8E91F96587 CRC64;
HHTMFLEPQE KKSSLKALVV KQAKKTCSCT PDKVKDHVLG FFPVLQWLPK YKLREYLLGD
IMSGVIVGVL LVPQSIAYSI LAGVEPIYGL YTSFFASIIY FIFGTSLHIS VGIFGVICLM
VGQVVDREIQ RAGYDLEPAA LSVLSAAAAP GNSTISPLNQ TSPELLCDKS CYAIRVGATM
TFIAGVYQVA MGFFQVGFLS VYLSDSLLSG FVTGASFTIL TSQVKYLLGL DIPRSSGIGS
LITTWINIFR NIHKTNICDL ITSFLCFLVL IPTKELNEHF KSRLKAPIPV ELVVVVAATL
ASHYGKLRET YGSSIAEHIP TGFLPPHPPD WNLIPNVALD AIPIAIIGFA ITVSLSEMFA
KKHGYSVKAN QEMYAIGFCN IIPSFFHCFT TSAALAKTLV KESTGCRTQV SGVVTSLVIL
LVLLVIAPLF YSLQKCVLAV ITIVNLRGAL RKFKDLPKMW HLSRVDTVIW LVTMAASALI
STEIGLLVGV CFSMLCVIFR TQRPEAPLLG WVAESETYES LSAYKNLQTK PGIVVFRFEA
PLYYINKECF KSTLYKQTGV NPVWVKAVKK KAAKTMLKEK KSGGNQTDIS MDFASEPLGF
HTIVIDCCAV QFLDTAGIRT LKEVCKDYRE IDIQVLLAQC NPSVRSSLIR GEFFKEGEDP
LLFHSVHQAV DFA
//