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 27-MAR-2024, entry version 146. 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}. 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; 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.2a.1; -. DR EPD; Q9N4X8; -. DR PaxDb; 6239-Y45G12C-2; -. 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 AGR; WB:WBGene00001758; -. 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; NDWRTQW; -. DR OrthoDB; 5302341at2759; -. 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 CDD; cd03076; GST_N_Pi; 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; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF120; GST N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. 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 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 //