ID I3MGG1_ICTTR Unreviewed; 758 AA.
AC I3MGG1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 61.
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|Ensembl:ENSSTOP00000009847.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000009847.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000009847.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGTP01013600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005319498.1; XM_005319441.1.
DR AlphaFoldDB; I3MGG1; -.
DR STRING; 43179.ENSSTOP00000009847; -.
DR Ensembl; ENSSTOT00000010976.3; ENSSTOP00000009847.3; ENSSTOG00000010967.3.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01070000253775; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; I3MGG1; -.
DR OrthoDB; 1067648at2759; -.
DR TreeFam; TF313784; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IEA:Ensembl.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0051454; P:intracellular pH elevation; IEA:Ensembl.
DR GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
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:UP000005215};
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 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 197..217
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..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 369..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 464..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 519..714
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 758 AA; 84398 MW; BE0ECC62282DBCBA CRC64;
MIEPIGNQYV VARPVYSANT FGEEHKKKHR HHKTFLDHLK LCCSCSTQKA KRIALSFFPI
ASWLPSYRIK EWLLSDIVSG ISTGLVAVLQ GLAFALLVTI PPRYGLYAAF FPVIVYFFLG
TSKHISVGPF PVLSMMVGAV VTNVVSDAST TMESSNSTEN NESILEQKKL LVATTVTVLS
GIIQLVLGVL RIGFVVIYLS ESLISAFTTA AAVHVLVSQL KFMLQLSVPA HTDPFSIFKV
LESVFTQIEK TNIADLVTSL IILFIVFVFK EINQRYKSKL PVPIPIELIV TVIATGVSYG
FDFEHRFNVS VVGQMDTGFE PPITPDVQIF QDTIGDSFGI AIVGFAVAFS VASVYSLKYD
YPIDGNQELI ALGLSNIFTG SFRGFAGSTA LSRSGVQEST GGKTQVAGLL SAIIVLIVIV
AIAFLLAPLQ KSVLAALALG NLKGMLMQFA EIGRLWRKDK YDCLVWIMTF IFAIVLGLGL
GLAASVAFQL LTIVFRTQFP KCSTLANIGR SNIYKDKKDY SDMYEPEGVK IFRCPSPIYF
ANIGFFKQKL IDAVGFTPLR ILRKRNKALK KIRKLQKRGL LQVTPKGFIC TADGFKDSDE
ELDNNQMEEL DQPINTTDLP FQIDWNADLP LNIMVPKISL HSLILDFSAV SFLDVSSMRG
LKTILQDFIR INVDVYIVGT DDDFIEKLAR CEFFDDEVKD SIFFLTIHDA VLHILMKKDY
STSKFNFNQK KEMKSDFTIN TNGGLRYREY QVPLETKF
//
