ID GSTP1_CAEEL Reviewed; 208 AA.
AC P10299;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Glutathione S-transferase P;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE AltName: Full=GST class-pi;
GN Name=gst-1; ORFNames=R107.7;
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=2928124; DOI=10.1093/nar/17.5.2138;
RA Weston K., Yochem J., Greenwald I.;
RT "A Caenorhabditis elegans cDNA that encodes a product resembling the rat
RT glutathione S-transferase P subunit.";
RL Nucleic Acids Res. 17:2138-2138(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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 [4]
RP FUNCTION, INDUCTION BY MANGANESE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23721876; DOI=10.1016/j.neuro.2013.05.014;
RA Settivari R., VanDuyn N., LeVora J., Nass R.;
RT "The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1
RT inhibits dopamine neuron degeneration in a Caenorhabditis elegans model of
RT manganism.";
RL NeuroToxicology 38:51-60(2013).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (By similarity).
CC Prevents dopaminergic CEP neuron degeneration in response to Mn(2+)
CC (PubMed:23721876). {ECO:0000250|UniProtKB:P09211,
CC ECO:0000269|PubMed:23721876}.
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:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P10299; P91505: gst-23; NbExp=5; IntAct=EBI-326030, EBI-326040;
CC -!- TISSUE SPECIFICITY: Expressed in dopaminergic (DA) neuron (at protein
CC levels). {ECO:0000269|PubMed:23721876}.
CC -!- INDUCTION: By manganese. {ECO:0000269|PubMed:23721876}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase in
CC Mn(2+)-mediated dopaminergic CEP neuron degeneration.
CC {ECO:0000269|PubMed:23721876}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR EMBL; X13689; CAA31979.1; -; mRNA.
DR EMBL; Z14092; CAA78471.1; -; Genomic_DNA.
DR PIR; S03615; S03615.
DR RefSeq; NP_499006.1; NM_066605.5.
DR AlphaFoldDB; P10299; -.
DR SMR; P10299; -.
DR BioGRID; 41480; 37.
DR DIP; DIP-24298N; -.
DR IntAct; P10299; 1.
DR STRING; 6239.R107.7.2; -.
DR EPD; P10299; -.
DR PaxDb; 6239-R107-7-2; -.
DR PeptideAtlas; P10299; -.
DR EnsemblMetazoa; R107.7.1; R107.7.1; WBGene00001749.
DR GeneID; 176281; -.
DR KEGG; cel:CELE_R107.7; -.
DR UCSC; R107.7.1; c. elegans.
DR AGR; WB:WBGene00001749; -.
DR WormBase; R107.7; CE00302; WBGene00001749; gst-1.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000166750; -.
DR HOGENOM; CLU_039475_2_1_1; -.
DR InParanoid; P10299; -.
DR OMA; IKPKMIF; -.
DR OrthoDB; 5302341at2759; -.
DR PhylomeDB; P10299; -.
DR Reactome; R-CEL-156590; Glutathione conjugation.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9753281; Paracetamol ADME.
DR PRO; PR:P10299; -.
DR Proteomes; UP000001940; Chromosome III.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:WormBase.
DR GO; GO:1990748; P:cellular detoxification; IGI:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:1905803; P:negative regulation of cellular response to manganese ion; IGI:UniProtKB.
DR GO; GO:1905804; P:positive regulation of cellular response to manganese ion; IMP:UniProtKB.
DR CDD; cd03210; GST_C_Pi; 1.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
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 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Glutathione S-transferase P"
FT /id="PRO_0000185911"
FT DOMAIN 1..78
FT /note="GST N-terminal"
FT DOMAIN 80..202
FT /note="GST C-terminal"
FT BINDING 7
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 49..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 62..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
SQ SEQUENCE 208 AA; 23901 MW; 3A0DC439FF8FFFBB CRC64;
MTLKLTYFDI HGLAEPIRLL LADKQVAYED HRVTYEQWAD IKPKMIFGQV PCLLSGDEEI
VQSGAIIRHL ARLNGLNGSN ETETTFIDMF YEGLRDLHTK YTTMIYRNYE DGKAPYIKDV
LPGELARLEK LFHTYKNGEH YVIGDKESYA DYVLFEELDI HLILTPNALD GVPALKKFHE
RFAERPNIKA YLNKRAAINP PVNGNGKQ
//
