GSTPA_CAEEL
ID GSTPA_CAEEL Reviewed; 210 AA.
AC Q9N4X8;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutathione S-transferase P 10;
DE EC=2.5.1.18;
DE AltName: Full=GST 5.4;
DE AltName: Full=GST class-pi;
DE AltName: Full=GSTP2-2;
GN Name=gst-10 {ECO:0000312|WormBase:Y45G12C.2}; ORFNames=Y45G12C.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, AND FUNCTION.
RX DOI=10.1016/S0009-2797(00)00216-7;
RA Engle M.R., Singh S.P., Nanduri B., Ji X., Zimniak P.;
RT "Invertebrate glutathione transferases conjugating 4-hydroxynonenal: CeGST
RT 5.4 from Caenorhabditis elegans.";
RL Chem. Biol. Interact. 133:244-248(2001).
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] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=16164425; DOI=10.1111/j.1474-9726.2005.00168.x;
RA Ayyadevara S., Engle M.R., Singh S.P., Dandapat A., Lichti C.F., Benes H.,
RA Shmookler Reis R.J., Liebau E., Zimniak P.;
RT "Lifespan and stress resistance of Caenorhabditis elegans are increased by
RT expression of glutathione transferases capable of metabolizing the lipid
RT peroxidation product 4-hydroxynonenal.";
RL Aging Cell 4:257-271(2005).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16300482; DOI=10.1111/j.1474-9726.2005.00172.x;
RA Ayyadevara S., Dandapat A., Singh S.P., Benes H., Zimniak L., Reis R.J.S.,
RA Zimniak P.;
RT "Lifespan extension in hypomorphic daf-2 mutants of Caenorhabditis elegans
RT is partially mediated by glutathione transferase CeGSTP2-2.";
RL Aging Cell 4:299-307(2005).
RN [5]
RP FUNCTION.
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).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Responsible for
CC approximately one-third of 4-hydroxy-2-nonenal conjugation (Ref.1,
CC PubMed:16164425, PubMed:16300482). May play a role in the
CC detoxification of reactive oxygen species produced during pathogenic
CC bacterial infection (PubMed:22216003). {ECO:0000269|PubMed:16164425,
CC ECO:0000269|PubMed:16300482, ECO:0000269|PubMed:22216003,
CC ECO:0000269|Ref.1}.
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:P10299};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 4-HNE {ECO:0000269|PubMed:16164425};
CC Vmax=10.3 umol/min/mg enzyme {ECO:0000269|PubMed:16164425};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P10299, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cells at the mouth and adjacent to the
CC pharyngeal bulbs of the head and also in the tail.
CC {ECO:0000269|PubMed:16164425}.
CC -!- DISRUPTION PHENOTYPE: Increase in susceptibility to 4-hydroxy-2-
CC nonenal, paraquat and heat shock and a reduced lifespan.
CC {ECO:0000269|PubMed:16300482}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC {ECO:0000250|UniProtKB:P10299}.
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DR EMBL; FO080245; CCD62297.1; -; Genomic_DNA.
DR RefSeq; NP_503701.1; NM_071300.7.
DR AlphaFoldDB; Q9N4X8; -.
DR SMR; Q9N4X8; -.
DR BioGRID; 43783; 12.
DR IntAct; Q9N4X8; 1.
DR STRING; 6239.Y45G12C.2; -.
DR EPD; Q9N4X8; -.
DR PaxDb; Q9N4X8; -.
DR PeptideAtlas; Q9N4X8; -.
DR EnsemblMetazoa; Y45G12C.2a.1; Y45G12C.2a.1; WBGene00001758.
DR GeneID; 178725; -.
DR KEGG; cel:CELE_Y45G12C.2; -.
DR UCSC; Y45G12C.2.1; c. elegans.
DR CTD; 178725; -.
DR WormBase; Y45G12C.2; CE21937; WBGene00001758; gst-10.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000195984; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; Q9N4X8; -.
DR OMA; VRDVRMK; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q9N4X8; -.
DR SABIO-RK; Q9N4X8; -.
DR PRO; PR:Q9N4X8; -.
DR Proteomes; UP000001940; Chromosome V.
DR ExpressionAtlas; Q9N4X8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:WormBase.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
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; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..210
FT /note="Glutathione S-transferase P 10"
FT /id="PRO_0000185912"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT DOMAIN 83..200
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 41
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
SQ SEQUENCE 210 AA; 24796 MW; 31AF3BC1ED43594B CRC64;
MAVPQLYYFT IRGFGEYIRL LFLDNGIKFE DIRFDYEGNE WQEFKKGMLL GQLPCLKVDG
QEIVQTGAIM RHLGRVHGLN GSNEQEATFL DMFFEGVRDV RMKYVRYIYY DEGTREDCVN
KTIPEALVKL EELFKAHSGD FIIGNKISYA DYILFEELDV YHVLDANILD KFPTLKSFWE
RMWKRPNLNA YLEKRKADKV WINAIEKGMN
