ID F1S7C9_PIG Unreviewed; 298 AA.
AC F1S7C9; F1S7D2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
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|Ensembl:ENSSSCP00000002835.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000002835.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000002835.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000002835.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:RU003494};
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000256|ARBA:ARBA00011055, ECO:0000256|RuleBase:RU003494}.
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DR AlphaFoldDB; F1S7C9; -.
DR SMR; F1S7C9; -.
DR PeptideAtlas; F1S7C9; -.
DR Ensembl; ENSSSCT00000002914.4; ENSSSCP00000002835.4; ENSSSCG00000052947.1.
DR GeneTree; ENSGT00940000154526; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; F1S7C9; -.
DR TreeFam; TF105321; -.
DR Reactome; R-SSC-156590; Glutathione conjugation.
DR Reactome; R-SSC-189483; Heme degradation.
DR Reactome; R-SSC-9748787; Azathioprine ADME.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000002623; Expressed in ovary and 36 other cell types or tissues.
DR ExpressionAtlas; F1S7C9; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR CDD; cd03208; GST_C_Alpha; 1.
DR CDD; cd03077; GST_N_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; PF00043; GST_C; 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 Proteomics identification {ECO:0007829|PeptideAtlas:F1S7C9};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|RuleBase:RU003494}.
FT DOMAIN 78..158
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 160..283
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 298 AA; 33983 MW; 8218483411358EAB CRC64;
MVWCNFLQLT FEDENVGQGR HPRGTSTSAM KEADTPPTSF WCCSVINHKA LWLLQLYPLS
IHSFTQVERD QQTAIMAGKP ILHYFNGRGR MECIRWLLAA AGVEFEEKFI KTPEDLDKLT
NDGSLLFQQV PMVEIDGMKL VQTRAILNYI ATKYNLYGKD AKERALIDMY TEGVADLGEM
ILLLPLCPPN EKDAKVASIK EKSTNRYLPA FEKVLKSHGQ DYLVGNKLSR ADIQLVELLY
YVEELDPSLL ANFPLLKALK TRVSNLPTVK KFLQPGSQRK PPMDEKKLEE AKNIFRIK
//