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Glutathione S-transferase P (EC 2.5.1.18) (GST class-pi)

 GSTP1_CAEEL             Reviewed;         208 AA.
P10299;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Glutathione S-transferase P;
EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
AltName: Full=GST class-pi;
Name=gst-1; ORFNames=R107.7;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Bristol N2;
PubMed=2928124; DOI=10.1093/nar/17.5.2138;
Weston K., Yochem J., Greenwald I.;
"A Caenorhabditis elegans cDNA that encodes a product resembling the
rat glutathione S-transferase P subunit.";
Nucleic Acids Res. 17:2138-2138(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=7906398; DOI=10.1038/368032a0;
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
Wohldman P.;
"2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
elegans.";
Nature 368:32-38(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION, INDUCTION BY MANGANESE, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=23721876; DOI=10.1016/j.neuro.2013.05.014;
Settivari R., VanDuyn N., LeVora J., Nass R.;
"The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1
inhibits dopamine neuron degeneration in a Caenorhabditis elegans
model of manganism.";
NeuroToxicology 38:51-60(2013).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles (By
similarity). Prevents dopaminergic CEP neuron degeneration in
response to Mn(2+) (PubMed:23721876).
{ECO:0000250|UniProtKB:P09211, ECO:0000269|PubMed:23721876}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000250|UniProtKB:P09211}.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P91505:gst-23; NbExp=5; IntAct=EBI-326030, EBI-326040;
-!- TISSUE SPECIFICITY: Expressed in dopaminergic (DA) neuron (at
protein levels). {ECO:0000269|PubMed:23721876}.
-!- INDUCTION: By manganese. {ECO:0000269|PubMed:23721876}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase
in Mn(2+)-mediated dopaminergic CEP neuron degeneration.
{ECO:0000269|PubMed:23721876}.
-!- SIMILARITY: Belongs to the GST superfamily. Pi family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X13689; CAA31979.1; -; mRNA.
EMBL; Z14092; CAA78471.1; -; Genomic_DNA.
PIR; S03615; S03615.
RefSeq; NP_499006.1; NM_066605.5.
UniGene; Cel.19723; -.
ProteinModelPortal; P10299; -.
SMR; P10299; -.
BioGrid; 41480; 1.
DIP; DIP-24298N; -.
IntAct; P10299; 1.
MINT; MINT-1090976; -.
STRING; 6239.R107.7.2; -.
EPD; P10299; -.
PaxDb; P10299; -.
PeptideAtlas; P10299; -.
PRIDE; P10299; -.
EnsemblMetazoa; R107.7.1; R107.7.1; WBGene00001749.
EnsemblMetazoa; R107.7.2; R107.7.2; WBGene00001749.
EnsemblMetazoa; R107.7.3; R107.7.3; WBGene00001749.
GeneID; 176281; -.
KEGG; cel:CELE_R107.7; -.
UCSC; R107.7.1; c. elegans.
CTD; 176281; -.
WormBase; R107.7; CE00302; WBGene00001749; gst-1.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115733; -.
InParanoid; P10299; -.
KO; K00799; -.
OMA; LRCKYAT; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P10299; -.
Reactome; R-CEL-156590; Glutathione conjugation.
Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-CEL-6798695; Neutrophil degranulation.
PRO; PR:P10299; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00001749; -.
GO; GO:0004364; F:glutathione transferase activity; IDA:WormBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
GO; GO:0045087; P:innate immune response; IMP:WormBase.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
GO; GO:1905803; P:negative regulation of cellular response to manganese ion; IGI:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
GO; GO:1905804; P:positive regulation of cellular response to manganese ion; IMP:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IGI:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003082; GST_pi.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01268; GSTRNSFRASEP.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
Complete proteome; Reference proteome; Transferase.
CHAIN 1 208 Glutathione S-transferase P.
/FTId=PRO_0000185911.
DOMAIN 1 78 GST N-terminal.
DOMAIN 80 202 GST C-terminal.
REGION 49 50 Glutathione binding.
{ECO:0000250|UniProtKB:P09211}.
REGION 62 63 Glutathione binding.
{ECO:0000250|UniProtKB:P09211}.
BINDING 7 7 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
BINDING 38 38 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
BINDING 42 42 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
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


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