ID   GSTA6_RAT               Reviewed;         222 AA.
AC   Q6AXY0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Glutathione S-transferase A6;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha member 6;
GN   Name=Gsta6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-33 AND 139-152, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; BC079271; AAH79271.1; -; mRNA.
DR   RefSeq; NP_001019532.1; NM_001024361.1.
DR   RefSeq; XP_006244718.1; XM_006244656.3.
DR   RefSeq; XP_006244719.1; XM_006244657.3.
DR   RefSeq; XP_006244720.1; XM_006244658.3.
DR   AlphaFoldDB; Q6AXY0; -.
DR   SMR; Q6AXY0; -.
DR   BioGRID; 272417; 1.
DR   STRING; 10116.ENSRNOP00000031201; -.
DR   iPTMnet; Q6AXY0; -.
DR   PhosphoSitePlus; Q6AXY0; -.
DR   PaxDb; 10116-ENSRNOP00000031201; -.
DR   Ensembl; ENSRNOT00000036813.3; ENSRNOP00000031201.2; ENSRNOG00000033402.3.
DR   Ensembl; ENSRNOT00055033965; ENSRNOP00055027583; ENSRNOG00055019883.
DR   Ensembl; ENSRNOT00060026532; ENSRNOP00060021213; ENSRNOG00060015492.
DR   Ensembl; ENSRNOT00065031345; ENSRNOP00065024975; ENSRNOG00065018669.
DR   GeneID; 501110; -.
DR   KEGG; rno:501110; -.
DR   UCSC; RGD:1565402; rat.
DR   AGR; RGD:1565402; -.
DR   CTD; 501110; -.
DR   RGD; 1565402; Gsta6.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000154526; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; Q6AXY0; -.
DR   OMA; HLVEMIY; -.
DR   OrthoDB; 3412208at2759; -.
DR   PhylomeDB; Q6AXY0; -.
DR   TreeFam; TF105321; -.
DR   Reactome; R-RNO-156590; Glutathione conjugation.
DR   Reactome; R-RNO-189483; Heme degradation.
DR   Reactome; R-RNO-9748787; Azathioprine ADME.
DR   PRO; PR:Q6AXY0; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000033402; Expressed in ovary and 18 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd03208; GST_C_Alpha; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF107; GLUTATHIONE S-TRANSFERASE A2; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT   CHAIN           1..222
FT                   /note="Glutathione S-transferase A6"
FT                   /id="PRO_0000288804"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
SQ   SEQUENCE   222 AA;  25808 MW;  B45C055D23578F77 CRC64;
     MAEKPLFHYD EARGRMESVR WLLAAAGVEY EEKFIHTNED LEKLRSDGVL MFQQVPMVEV
     DGMKLVQTRA IMNYFSSKYN LYGKDMKERA LIDMYSEGLA DLNEMFILYP FDPPGVKEAN
     IALMKEKATN RYFPAFEKVF ESHGQDYLVG NKLSKADVHL VEMIYNMEEL DTNILANFPL
     LQALKTRISD MPTIKKFLQP GSQRQPPVDE KSIQKTRKIF KF
//