ID Q9DDU5_DANRE Unreviewed; 208 AA.
AC Q9DDU5; A0A0R4IS32; B3DGD4;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU368105};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU368105};
DE AltName: Full=GST class-pi {ECO:0000256|RuleBase:RU368105};
GN Name=gstp1.2 {ECO:0000313|ZFIN:ZDB-GENE-020806-4};
GN Synonyms=cb356 {ECO:0000313|RefSeq:NP_571809.1}, fa02f07
GN {ECO:0000313|RefSeq:NP_571809.1}, gstp1
GN {ECO:0000313|RefSeq:NP_571809.1}, wu:fa02f07
GN {ECO:0000313|RefSeq:NP_571809.1}, wu:fj23a02
GN {ECO:0000313|RefSeq:NP_571809.1}, zgc:103706
GN {ECO:0000313|RefSeq:NP_571809.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI62358.1};
RN [1] {ECO:0000313|EMBL:AAG35785.1}
RP NUCLEOTIDE SEQUENCE.
RA Lee J.-S., Gye M.C.;
RT "Nucleotide sequence of glutathione S-transferase (GST) Pi gene from
RT zebrafish (Danio rerio).";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15070763;
RA Rawls J.F., Samuel B.S., Gordon J.I.;
RT "Gnotobiotic zebrafish reveal evolutionarily conserved responses to the gut
RT microbiota.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4596-4601(2004).
RN [3] {ECO:0000313|EMBL:BAD98444.1, ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15654768; DOI=10.1042/BJ20041860;
RA Suzuki T., Takagi Y., Osanai H., Li L., Takeuchi M., Katoh Y.,
RA Kobayashi M., Yamamoto M.;
RT "Pi class glutathione S-transferase genes are regulated by Nrf 2 through an
RT evolutionarily conserved regulatory element in zebrafish.";
RL Biochem. J. 388:65-73(2005).
RN [4] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16109975;
RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL Genome Res. 15:1307-1314(2005).
RN [5] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16631158;
RA Cheng W., Guo L., Zhang Z., Soo H.M., Wen C., Wu W., Peng J.;
RT "HNF factors form a network to regulate liver-enriched genes in
RT zebrafish.";
RL Dev. Biol. 294:482-496(2006).
RN [6] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17251491;
RA Leung Y.F., Ma P., Dowling J.E.;
RT "Gene expression profiling of zebrafish embryonic retinal pigment
RT epithelium in vivo.";
RL Invest. Ophthalmol. Vis. Sci. 48:881-890(2007).
RN [7] {ECO:0000313|EMBL:AAI62358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|Ensembl:ENSDARP00000138645, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000138645};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [9] {ECO:0000313|Ensembl:ENSDARP00000138645}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000138645};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [10] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30758177;
RA Wei X., Li L., Liu J., Yu L., Li H., Cheng F., Yi X., He J., Li B.;
RT "Green Synthesis of Fluorescent Carbon Dots from Gynostemma for Bioimaging
RT and Antioxidant in Zebrafish.";
RL ACS Appl. Mater. Interfaces 11:9832-9840(2019).
RN [11] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30384064;
RA Tian J., Hu J., Liu G., Yin H., Chen M., Miao P., Bai P., Yin J.;
RT "Altered Gene expression of ABC transporters, nuclear receptors and
RT oxidative stress signaling in zebrafish embryos exposed to CdTe quantum
RT dots.";
RL Environ. Pollut. 244:588-599(2019).
RN [12] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30453236;
RA Komoike Y., Matsuoka M.;
RT "In vitro and in vivo studies of oxidative stress responses against
RT acrylamide toxicity in zebrafish.";
RL J. Hazard. Mater. 365:430-439(2019).
RN [13] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30594530; DOI=10.1016/j.vascn.2018.12.006;
RA Yamashita A., Deguchi J., Honda Y., Yamada T., Miyawaki I., Nishimura Y.,
RA Tanaka T.;
RT "Increased susceptibility to oxidative stress-induced toxicological
RT evaluation by genetically modified nrf2a-deficient zebrafish.";
RL J. Pharmacol. Toxicol. Methods 96:34-45(2019).
RN [14] {ECO:0000313|RefSeq:NP_571809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30718751;
RA Park K.H., Ye Z.W., Zhang J., Hammad S.M., Townsend D.M., Rockey D.C.,
RA Kim S.H.;
RT "3-ketodihydrosphingosine reductase mutation induces steatosis and hepatic
RT injury in zebrafish.";
RL Sci. Rep. 9:1138-1138(2019).
RN [15] {ECO:0000313|RefSeq:NP_571809.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU368105}.
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:0000256|RuleBase:RU368105};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368105}.
CC Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus
CC {ECO:0000256|RuleBase:RU368105}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC {ECO:0000256|ARBA:ARBA00007297, ECO:0000256|RuleBase:RU368105}.
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DR EMBL; FP102983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF285098; AAG35785.1; -; mRNA.
DR EMBL; BC162358; AAI62358.1; -; mRNA.
DR EMBL; BC162376; AAI62376.1; -; mRNA.
DR EMBL; AB194127; BAD98444.1; -; mRNA.
DR RefSeq; NP_571809.1; NM_131734.3.
DR STRING; 7955.ENSDARP00000138645; -.
DR PaxDb; 7955-ENSDARP00000004830; -.
DR Ensembl; ENSDART00000159326; ENSDARP00000138645; ENSDARG00000104068.
DR Ensembl; ENSDART00000159326.2; ENSDARP00000138645.1; ENSDARG00000104068.2.
DR GeneID; 79381; -.
DR KEGG; dre:79381; -.
DR AGR; ZFIN:ZDB-GENE-020806-4; -.
DR CTD; 79381; -.
DR ZFIN; ZDB-GENE-020806-4; gstp1.2.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_2_1_1; -.
DR OMA; IKPKMIF; -.
DR OrthoDB; 5302341at2759; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 928.
DR Reactome; R-DRE-156590; Glutathione conjugation.
DR Reactome; R-DRE-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-9753281; Paracetamol ADME.
DR Proteomes; UP000000437; Chromosome 14.
DR Bgee; ENSDARG00000104068; Expressed in intestine and 37 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:ZFIN.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:ZFIN.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
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 Cytoplasm {ECO:0000256|RuleBase:RU368105};
KW Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW Nucleus {ECO:0000256|RuleBase:RU368105};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9DDU5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000256|RuleBase:RU368105, ECO:0000313|EMBL:AAG35785.1}.
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 83..202
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 208 AA; 23526 MW; CC8C8960C098270D CRC64;
MAPYTLTYFA VKGRCGALKI MLADKDQQLK ENLVTFEEWM KGDLKATCVF GQLPKFEDGD
LVLFQSNAML RHLGRKHAAY GKNDSEASLI DVMNDGVEDL RLKYIKLIYQ EYETGKEAFI
KDLPNHLKCF ENVLAKNKTG FLVGDQISFA DYNLFDLLLN LKVLSPSCLD SFPSLKSFVD
KISARPKVKA LLECENFKKL PINGNGKQ
//
