ID   GST82_DICLA             Reviewed;          32 AA.
AC   P82608;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Glutathione S-transferase 8.2;
DE            Short=GST-8.2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha;
DE   Flags: Fragments;
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=10620369; DOI=10.1006/abbi.1999.1569;
RA   Angelucci S., Sacchetta P., Moio P., Melino S., Petruzzelli R., Gervasi P.,
RA   Di Ilio C.;
RT   "Purification and characterization of glutathione transferases from the sea
RT   bass (Dicentrarchus labrax) liver.";
RL   Arch. Biochem. Biophys. 373:435-441(2000).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   Proteomes; UP000694389; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT   CHAIN           <1..>32
FT                   /note="Glutathione S-transferase 8.2"
FT                   /id="PRO_0000185804"
FT   BINDING         21..22
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   NON_CONS        16..17
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3743 MW;  806C6F142ED3C3EA CRC64;
     MESIRWLLTV AQFDFDMKLV QSXAIVNYVA NK
//