ID   GST4_CAEEL              Reviewed;         207 AA.
AC   Q21355;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Glutathione S-transferase 4;
DE            EC=2.5.1.18;
DE   AltName: Full=CeGST1;
DE   AltName: Full=GST class-sigma;
GN   Name=gst-4 {ECO:0000312|WormBase:K08F4.7};
GN   ORFNames=K08F4.7 {ECO:0000312|WormBase:K08F4.7};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9512531; DOI=10.1093/nar/26.7.1621;
RA   Tawe W.N., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.;
RT   "Identification of stress-responsive genes in Caenorhabditis elegans using
RT   RT-PCR differential display.";
RL   Nucleic Acids Res. 26:1621-1627(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND INDUCTION BY PARAQUAT.
RX   PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
RA   Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
RT   "Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1
RT   activity via p38 MAPK signaling during infection in C. elegans.";
RL   PLoS Pathog. 7:E1002453-E1002453(2011).
RN   [4]
RP   INDUCTION.
RX   PubMed=29500338; DOI=10.1038/s41467-018-02934-5;
RA   De Magalhaes Filho C.D., Henriquez B., Seah N.E., Evans R.M.,
RA   Lapierre L.R., Dillin A.;
RT   "Visible light reduces C. elegans longevity.";
RL   Nat. Commun. 9:927-927(2018).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles (By similarity). May
CC       play a role in the detoxification of reactive oxygen species produced
CC       during pathogenic bacterial infection (PubMed:22216003).
CC       {ECO:0000250|UniProtKB:P46436, ECO:0000269|PubMed:22216003}.
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:0000250|UniProtKB:P46436};
CC   -!- INDUCTION: By paraquat. Induced by white light exposure
CC       (PubMed:29500338). {ECO:0000269|PubMed:22216003,
CC       ECO:0000269|PubMed:29500338}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; AF010239; AAB65417.1; -; mRNA.
DR   EMBL; BX284604; CAA93086.1; -; Genomic_DNA.
DR   PIR; T37462; T37462.
DR   RefSeq; NP_501848.1; NM_069447.6.
DR   AlphaFoldDB; Q21355; -.
DR   SMR; Q21355; -.
DR   BioGRID; 42988; 5.
DR   DIP; DIP-24743N; -.
DR   STRING; 6239.K08F4.7.1; -.
DR   EPD; Q21355; -.
DR   PaxDb; 6239-K08F4-7; -.
DR   PeptideAtlas; Q21355; -.
DR   EnsemblMetazoa; K08F4.7.1; K08F4.7.1; WBGene00001752.
DR   GeneID; 177886; -.
DR   KEGG; cel:CELE_K08F4.7; -.
DR   UCSC; K08F4.7.1; c. elegans.
DR   AGR; WB:WBGene00001752; -.
DR   WormBase; K08F4.7; CE06155; WBGene00001752; gst-4.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00970000195858; -.
DR   HOGENOM; CLU_039475_1_1_1; -.
DR   InParanoid; Q21355; -.
DR   OMA; VHEYMDA; -.
DR   OrthoDB; 1385810at2759; -.
DR   PhylomeDB; Q21355; -.
DR   PRO; PR:Q21355; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   GO; GO:0043292; C:contractile fiber; IDA:WormBase.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:WormBase.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:WormBase.
DR   CDD; cd03192; GST_C_Sigma_like; 1.
DR   CDD; cd03039; GST_N_Sigma_like; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF155; GLUTATHIONE S-TRANSFERASE 4; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
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   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..207
FT                   /note="Glutathione S-transferase 4"
FT                   /id="PRO_0000185927"
FT   DOMAIN          2..79
FT                   /note="GST N-terminal"
FT   DOMAIN          81..207
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         43
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P46088"
FT   BINDING         49..51
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         63..64
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
SQ   SEQUENCE   207 AA;  23891 MW;  7152BC3F891B61FB CRC64;
     MPNYKLLYFD ARALAEPIRI MFAMLNVPYE DYRVSVEEWS KLKPTTPFGQ LPILQVDGEQ
     FGQSMSITRY LARKFGLAGK TAEEEAYADS IVDQYRDFIF FFRQFTSSVF YGSDADHINK
     VRFEVVEPAR DDFLAIINKF LAKSKSGFLV GDSLTWADIV IADNLTSLLK NGFLDFNKEK
     KLEEFYNKIH SIPEIKNYVA TRKDSIV
//