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Database: UniProt
Entry: A0A091IBB8_CALAN
LinkDB: A0A091IBB8_CALAN
Original site: A0A091IBB8_CALAN 
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
//
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