GST4_CAEEL
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 03-AUG-2022, entry version 142.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; -.
DR EPD; Q21355; -.
DR PaxDb; Q21355; -.
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 CTD; 177886; -.
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; AWRFGLS; -.
DR OrthoDB; 1162336at2759; -.
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 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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 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
