ID A0A2U4BSK8_TURTR Unreviewed; 759 AA.
AC A0A2U4BSK8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chloride anion exchanger {ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Solute carrier family 26 member 3 {ECO:0000256|RuleBase:RU362052};
GN Name=SLC26A3 {ECO:0000313|RefSeq:XP_019796193.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019796193.1};
RN [1] {ECO:0000313|RefSeq:XP_019796193.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019796193.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates chloride-bicarbonate exchange with a chloride
CC bicarbonate stoichiometry of 2:1 in the intestinal epithelia. Plays a
CC role in the chloride and bicarbonate homeostasis during sperm
CC epididymal maturation and capacitation.
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 RefSeq; XP_019796193.1; XM_019940634.2.
DR AlphaFoldDB; A0A2U4BSK8; -.
DR STRING; 9739.ENSTTRP00000006467; -.
DR GeneID; 101330210; -.
DR InParanoid; A0A2U4BSK8; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000245320; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
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 CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
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:SF19; CHLORIDE ANION EXCHANGER; 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; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|RuleBase:RU362052};
KW Chloride {ECO:0000256|RuleBase:RU362052};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
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 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 171..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 253..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 370..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 464..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 520..715
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 759 AA; 84327 MW; AFF0B65E6B1EDE95 CRC64;
MIEPIGNQYV VARPVYSTKA FDEEHKKKHR HHKTLLDHLK TWFRCSAQKA KRIALSLFPI
ASWLPAYRIK EWLLSDIVSG ISTGLVAVLQ GLAFALLVTI PPSYGLYAAF FPVIIYFFLG
TSRHISVGPF PVLSMMVGAV VVRLTPIADT ADPTVTNSSV ANDSSLDDHK VMVAATVTIL
SGIIQLLMGV LQLGFVVIYL SESLISGFTT AAAVHVLVSQ LKFILQLTVP AHADPFSIFK
VLTSIFSQIE KTNIADLVTS LVILLVVFVV KEINQRYKAK LPVPIPIELI MTVIATAVSY
GFDFKNRFNV AVVGEMESGF QAPIAPNVQT FRDTIGDCFG IAIVGFAVAF SVASVYSLKY
DYPIDGNQEL IALGVSNIFG GSFRGFAAST ALSRSGVQES TGGKTQVAGL LSAVIVLIVI
LAIGFLLEPL QKSVLAALAL GNLKGMLMQF TEIRRLWRKD KYDCLIWVMT FIFAVVLGLG
LGLAASVALQ LLTIVFRTQF PKCSTLANVG RSNIYKNRKD YSEMYEPDGV KIFRCPSPIY
FANISFFKQK LIDAVGFSPL RILRKRNKAL KKIRKLQKKG LLQVTLKGYI CTVDGFKDSD
EELDNDNIEE LDQPINTTDL PFQIDWNADL PFNIMVPKIN LHSLILDFSA VSFLDISSMR
GLKMILQEFI RIQVDVYIVG TDDDFIEKLA RCEFFDDEVK DSIFFLTIHD AVLHILMKKD
YSTSKFNPSQ EKEAKFDFTI NTNGALRNRE CQVPSETKF
//