GSTUJ_ARATH
ID GSTUJ_ARATH Reviewed; 219 AA.
AC Q9ZRW8; Q8LBS1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glutathione S-transferase U19;
DE Short=AtGSTU19;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 19;
DE AltName: Full=Glutathione S-transferase 8;
GN Name=GSTU19; Synonyms=GST8; OrderedLocusNames=At1g78380; ORFNames=F3F9.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=12207667; DOI=10.1034/j.1399-3054.2002.1160112.x;
RA Bianchi M.W., Roux C., Vartanian N.;
RT "Drought regulation of GST8, encoding the Arabidopsis homologue of
RT ParC/Nt107 glutathione transferase/peroxidase.";
RL Physiol. Plantarum 116:96-105(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
RN [7]
RP INDUCTION.
RX PubMed=12428014; DOI=10.1104/pp.010066;
RA DeRidder B.P., Dixon D.P., Beussman D.J., Edwards R., Goldsbrough P.B.;
RT "Induction of glutathione S-transferases in Arabidopsis by herbicide
RT safeners.";
RL Plant Physiol. 130:1497-1505(2002).
RN [8]
RP INDUCTION.
RX PubMed=15069083; DOI=10.1074/jbc.m402807200;
RA Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E.,
RA Goldsbrough P.B.;
RT "Proteomic analysis of Arabidopsis glutathione S-transferases from
RT benoxacor- and copper-treated seedlings.";
RL J. Biol. Chem. 279:26098-26104(2004).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=16361527; DOI=10.1104/pp.105.067199;
RA DeRidder B.P., Goldsbrough P.B.;
RT "Organ-specific expression of glutathione S-transferases and the efficacy
RT of herbicide safeners in Arabidopsis.";
RL Plant Physiol. 140:167-175(2006).
RN [10]
RP FUNCTION.
RX PubMed=19520850; DOI=10.1074/jbc.m109.020107;
RA Dixon D.P., Edwards R.;
RT "Selective binding of glutathione conjugates of fatty acid derivatives by
RT plant glutathione transferases.";
RL J. Biol. Chem. 284:21249-21256(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19174456; DOI=10.1093/jxb/ern365;
RA Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT "Enzyme activities and subcellular localization of members of the
RT Arabidopsis glutathione transferase superfamily.";
RL J. Exp. Bot. 60:1207-1218(2009).
RN [12]
RP INDUCTION.
RX PubMed=20031254; DOI=10.1016/j.jplph.2009.11.006;
RA Hara M., Yatsuzuka Y., Tabata K., Kuboi T.;
RT "Exogenously applied isothiocyanates enhance glutathione S-transferase
RT expression in Arabidopsis but act as herbicides at higher concentrations.";
RL J. Plant Physiol. 167:643-649(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Catalyzes the glutathionylation of 12-oxophytodienoate
CC (OPDA). In vitro, possesses glutathione S-transferase activity toward
CC 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC),
CC and glutathione peroxidase activity toward cumene hydroperoxide.
CC {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16361527,
CC ECO:0000269|PubMed:19520850}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19174456}.
CC -!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
CC jasmonate, auxin, H(2)O(2), copper, benoxacor, isothiocyanates and the
CC pathogen Hyaloperonospora parasitica. {ECO:0000269|PubMed:12090627,
CC ECO:0000269|PubMed:12207667, ECO:0000269|PubMed:12428014,
CC ECO:0000269|PubMed:15069083, ECO:0000269|PubMed:16361527,
CC ECO:0000269|PubMed:20031254}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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; AJ012571; CAA10060.1; -; mRNA.
DR EMBL; AC013430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE36099.1; -; Genomic_DNA.
DR EMBL; AF385691; AAK60284.1; -; mRNA.
DR EMBL; AY078012; AAL77713.1; -; mRNA.
DR EMBL; AY087032; AAM64593.1; -; mRNA.
DR PIR; T51607; T51607.
DR RefSeq; NP_565178.1; NM_106485.4.
DR AlphaFoldDB; Q9ZRW8; -.
DR SMR; Q9ZRW8; -.
DR BioGRID; 29393; 26.
DR IntAct; Q9ZRW8; 23.
DR STRING; 3702.AT1G78380.1; -.
DR iPTMnet; Q9ZRW8; -.
DR SwissPalm; Q9ZRW8; -.
DR PaxDb; Q9ZRW8; -.
DR PRIDE; Q9ZRW8; -.
DR ProteomicsDB; 247232; -.
DR EnsemblPlants; AT1G78380.1; AT1G78380.1; AT1G78380.
DR GeneID; 844174; -.
DR Gramene; AT1G78380.1; AT1G78380.1; AT1G78380.
DR KEGG; ath:AT1G78380; -.
DR Araport; AT1G78380; -.
DR TAIR; locus:2032100; AT1G78380.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_2_1; -.
DR InParanoid; Q9ZRW8; -.
DR OMA; FHAYEKY; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9ZRW8; -.
DR BioCyc; ARA:AT1G78380-MON; -.
DR BioCyc; MetaCyc:AT1G78380-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9ZRW8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZRW8; baseline and differential.
DR Genevisible; Q9ZRW8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; PTHR11260; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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 Cytoplasm; Detoxification; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Reference proteome; Stress response; Transferase.
FT CHAIN 1..219
FT /note="Glutathione S-transferase U19"
FT /id="PRO_0000413565"
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT DOMAIN 88..208
FT /note="GST C-terminal"
FT BINDING 13..14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 16
FT /note="G -> R (in Ref. 5; AAM64593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 25651 MW; E79AABD8C14C6F15 CRC64;
MANEVILLDF WPSMFGMRTR IALREKGVEF EYREEDLRNK SPLLLQMNPI HKKIPVLIHN
GKPVNESIIQ VQYIDEVWSH KNPILPSDPY LRAQARFWAD FIDKKLYDAQ RKVWATKGEE
QEAGKKDFIE ILKTLESELG DKPYFSGDDF GYVDIALIGF YTWFPAYEKF ANFSIESEVP
KLIAWVKKCL QRESVAKSLP DPEKVTEFVS ELRKKFVPE
