ID A0A091EAH8_CORBR Unreviewed; 804 AA.
AC A0A091EAH8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=Solute carrier family 26 member 9 {ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Anion transporter/exchanger protein 9 {ECO:0000256|RuleBase:RU362052};
GN ORFNames=N302_14793 {ECO:0000313|EMBL:KFO55048.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO55048.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO55048.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO55048.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ion transporter that can act both as an ion channel and anion
CC exchanger. Mainly acts as a chloride channel, which 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. Also acts as a DIDS- and
CC thiosulfate- sensitive anion exchanger the exchange of chloride for
CC bicarbonate ions across the cell membrane.
CC {ECO:0000256|RuleBase:RU362052}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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; KK718210; KFO55048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EAH8; -.
DR STRING; 85066.A0A091EAH8; -.
DR Proteomes; UP000052976; 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 CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
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 PANTHER; PTHR11814:SF17; SOLUTE CARRIER FAMILY 26 MEMBER 9; 1.
DR PANTHER; PTHR11814; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
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 108..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 172..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 253..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 284..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 466..497
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 521..748
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 804 AA; 88020 MW; 0D83A7A216BAC74B CRC64;
MSQARPRYVI ERPAYSVSLF DEEFEKKSRT YPVGEKLRNL FRCSASRFKL TLFRLFPILA
WLPKYKIKDY ILPDVLGGLS AGTIQVPQGM AFALLANLPP VNGLYSSFFP LITYLFLGGI
HQMVPGTFAV ISIIVGNICN ELAPESDFQY FNHTTNETSV NTTALEAARL EISATLACLT
AIIQLCLGFL QFGFVAIYLS ESFIRGFMTA AGLQILISVL KYVFGLTVPS YTGPLAIVYT
FIDICKGLPQ TNLASLVYAL VSAVLLIIVK ELNLKYMKKI RMPIPMEIII VIVATAISGS
FDMPDKYGMP IVGKISMGFP EPTLPLVSKW KDMVGTAFSL AIVGYVINLA MGRTLAAKHG
YDVDPNQVLL GLGQPRAAPF ALRRGGTRRG ALGSPDVCRS DFLSSLQVAS FFVALVVMVT
MLSLGIYLEP LPKSVLGALI AVNLKNSLKQ LADPFYLWKK SKLDCLVWLV SFLSAFFLSL
PYGVAVGVGF SVLVVVFHTQ FRNGSALGQV TSTDIYKNPK TYNKVHEVNG IKIVTYCSPL
YFANSEIFRE KIIAKTGVDP GKVYLARRKF VKRQGPHLLP CPDCISSLLQ TLSLQELQKD
FESASPTDTN NNQTTANGAS ISYITFRPAA HGAGPGQSPG ELGSTTTLQG STFSVLPTAD
TDPVLTAPPY ISFHTIILDM SGVCFVDLMG TKALSKLCSS YQKIGIKVFL ANVHAQVYND
ISTGGVFEEG GLDRSHIFLT IHDAVLFALA SIREVVHPPI LEERPNQTEL SIYDESVDES
SAEYKNLEEE MFGSMFHSET QTAL
//