ID   F1SL35_PIG              Unreviewed;       256 AA.
AC   F1SL35;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 4.
DT   27-MAR-2024, entry version 74.
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:ENSSSCP00000012726.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000012726.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012726.4,
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:ENSSSCP00000012726.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC       {ECO:0000256|ARBA:ARBA00005861, ECO:0000256|RuleBase:RU003494}.
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DR   RefSeq; XP_005670305.1; XM_005670248.2.
DR   AlphaFoldDB; F1SL35; -.
DR   SMR; F1SL35; -.
DR   STRING; 9823.ENSSSCP00000012726; -.
DR   PaxDb; 9823-ENSSSCP00000012726; -.
DR   PeptideAtlas; F1SL35; -.
DR   Ensembl; ENSSSCT00000013070.5; ENSSSCP00000012726.4; ENSSSCG00000011944.5.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000154679; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; F1SL35; -.
DR   TreeFam; TF353040; -.
DR   Reactome; R-SSC-156590; Glutathione conjugation.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Bgee; ENSSSCG00000011944; Expressed in testis.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03209; GST_C_Mu; 1.
DR   CDD; cd03075; GST_N_Mu; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003081; GST_mu.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF137; GLUTATHIONE S-TRANSFERASE MU 4; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDG01205; AMPS.1; 1.
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   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transferase {ECO:0000256|RuleBase:RU003494}.
FT   DOMAIN          39..126
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          128..246
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   256 AA;  29669 MW;  8E16DE8F5D698554 CRC64;
     MALPIKPSSA LNTFISRFLG KLARRKARDA GKSTEPSTTA ITLGYWDIRG LAHAIRLLLE
     YTGSNYEERK YMMGDPPDYD RSQWLNERSK LGLDFPNLPY LIDGPHKLTQ SNAILRYIAR
     KHNMCGETEK EKIQVDILES QVMDVRLHMA RVCYSSDFEK LKPGYVDEIP EKMRLFSAFL
     GKGPWFAGHT LTYVDFLAYD ILDLHRIFEP KCLDEFPNLK DFITRFEGLK KISAYMKSSR
     FLPRPLFLKI AMWGNK
//