ID I3L7B9_PIG Unreviewed; 193 AA.
AC I3L7B9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU368105};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU368105};
DE AltName: Full=GST class-pi {ECO:0000256|RuleBase:RU368105};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:HDC01514.1};
RN [1] {ECO:0000313|EMBL:HDC01514.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU368105}.
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 Evidence={ECO:0000256|RuleBase:RU368105};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368105}.
CC Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus
CC {ECO:0000256|RuleBase:RU368105}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC {ECO:0000256|ARBA:ARBA00007297, ECO:0000256|RuleBase:RU368105}.
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DR EMBL; DQIR01246036; HDC01514.1; -; Transcribed_RNA.
DR AlphaFoldDB; I3L7B9; -.
DR PeptideAtlas; I3L7B9; -.
DR HOGENOM; CLU_039475_2_1_1; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF248; GLUTATHIONE S-TRANSFERASE; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU368105};
KW Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW Nucleus {ECO:0000256|RuleBase:RU368105};
KW Transferase {ECO:0000256|RuleBase:RU368105, ECO:0000313|EMBL:HDC01514.1}.
FT DOMAIN 1..64
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 66..187
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 193 AA; 21761 MW; 87B0A9ED1B8E6FB5 CRC64;
MRMLLADQGQ SWKEEVVTKE TWLQGPLKAT CLYGQLPKFQ DGDLTLYQSN AILRHLGRSL
GLYGKDLQEA ALLDMVNDGV EDLRRLCGHL IRHNYEEDKA RYVEELPGHL RPFETLLSQN
QGGQAFIVGS QISFADYNLL DLLLSHQVLV PSCLDAFPLL SAYVARLSAR PKLKAFLASP
EHVNRPIFGS RKI
//
