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S26A9_XENTR
ID   S26A9_XENTR             Reviewed;         794 AA.
AC   A4IIF2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Solute carrier family 26 member 9;
DE   AltName: Full=Anion transporter/exchanger protein 9;
GN   Name=slc26a9;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DIDS- and thiosulfate- sensitive anion exchanger mediating
CC       chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate
CC       exchange or chloride-independent bicarbonate extrusion thus assuring
CC       bicarbonate secretion. May prefer chloride anions and mediate uncoupled
CC       chloride anion transport in an alternate-access mechanism where a
CC       saturable binding site is alternately exposed to either one or the
CC       other side of the membrane. {ECO:0000250|UniProtKB:Q8BU91}.
CC   -!- ACTIVITY REGULATION: Inhibited by ammonium and thiosulfate.
CC       {ECO:0000250|UniProtKB:Q8BU91}.
CC   -!- SUBUNIT: May form homodimers (in vitro).
CC       {ECO:0000250|UniProtKB:Q8BU91}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BU91};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000305}.
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DR   EMBL; BC135993; AAI35994.1; -; mRNA.
DR   RefSeq; NP_001096210.1; NM_001102740.1.
DR   AlphaFoldDB; A4IIF2; -.
DR   SMR; A4IIF2; -.
DR   STRING; 8364.ENSXETP00000013074; -.
DR   PaxDb; A4IIF2; -.
DR   DNASU; 100124761; -.
DR   GeneID; 100124761; -.
DR   KEGG; xtr:100124761; -.
DR   CTD; 115019; -.
DR   Xenbase; XB-GENE-996559; slc26a9.
DR   eggNOG; KOG0236; Eukaryota.
DR   InParanoid; A4IIF2; -.
DR   OrthoDB; 690428at2759; -.
DR   Reactome; R-XTR-427601; Multifunctional anion exchangers.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:InterPro.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   InterPro; IPR030306; SLC26A9.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR11814; PTHR11814; 1.
DR   PANTHER; PTHR11814:SF17; PTHR11814:SF17; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   TIGRFAMs; TIGR00815; sulP; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..794
FT                   /note="Solute carrier family 26 member 9"
FT                   /id="PRO_0000324494"
FT   TOPO_DOM        1..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        71..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        97..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        101..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        110..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        130..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        143..160
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        161..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        190..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        223..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   INTRAMEM        236..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        245..252
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        274..284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        285..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        298..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        333..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        357..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        364..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        378..388
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        389..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        399..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        404..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        418..429
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        430..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        456..459
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        460..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        475..477
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TRANSMEM        478..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   TOPO_DOM        497..794
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT   DOMAIN          517..739
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
SQ   SEQUENCE   794 AA;  87172 MW;  A37479DE42B1DD95 CRC64;
     MNKVRPRYII DRPAYSVELF NEEYEKKIRS YPIGGKARKL FSCSTSKIKN FIFRLFPILS
     WLPKYNIKGN LLNDALGGIS AGTIQIPQGM AFALLANLPP VNGLYSSFFP LVVYFFMGGI
     PQMVPGTFAV ISIIVGNVCL KLAPESHFQN VTSNGTITNI EAMNTARMHI SATLACLTAI
     IQIALSFVQF GFVAIYLSES FIRGFMTAAG LQILISVLKY IFGVSIPPYS GVLAIIYTFI
     DICKELPKTN VASLIFALIS TVLLIIVKEL NMKFMHKIRF PIPMEIIIVI VATAVSGSFK
     LPERYHMNVV GHIPLGFPSP TVPNVTQWDE MVGTAFSLAI VGYVINLAMG RTLGAKHGFD
     VDANQEMLAL GSGNFFGSFF FIHVICCALS VTLAVDGAGG KSQIASFFVM MSVMVTILAL
     GTYLNPLPKS VLGALIAVNL KNSLKQLSDP FYLWKKSKLD CLVWLVSFFS TFILGLPYGL
     AVGVAFSILV VIFNTQFRNG SSLNQVTATD IYVNPKVYSK VQPIDGIKIV TYCSPLYFAN
     SEIFRQKVIK KTGLDPGKVY LSKKKYLKQQ EQELKKKEQK KKRGSLFMKN KTLSLQELQE
     DFDGVSPTDS NNNSTVNGTA SAISYISSNT LTSGSQTTEN VQNGFSTPAQ TQDPIIAAPP
     IVNFHTVIID MSGVCFVDLM GIKALGKLCT SFQRIGVNVY LADVQAQVYD DIENGGMFAE
     GSLDRKHLFI TVHDAVLYAE ANNTGIVNTD SKKKGAGDTE IYITDTQDEI SEDYPNLEEA
     MFGSMFQTEI QTAL
 
 
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