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Database: UniProt/SWISS-PROT
Entry: GSTUJ_ARATH
LinkDB: GSTUJ_ARATH
Original site: 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   16-JAN-2019, entry version 134.
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;
GN   ORFNames=F3F9.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   gene 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.,
RA   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
RT   efficacy 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
RT   by 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
RT   concentrations.";
RL   J. Plant Physiol. 167:643-649(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
RP   BY 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
RT   using polyethylene glycol fractionation, immobilized metal-ion
RT   affinity 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
CC       toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl
CC       isothiocyanate (BITC), and glutathione peroxidase activity toward
CC       cumene hydroperoxide. {ECO:0000269|PubMed:12090627,
CC       ECO:0000269|PubMed:16361527, 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
CC       {ECO:0000269|PubMed:19174456}.
CC   -!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
CC       jasmonate, auxin, H(2)O(2), copper, benoxacor, isothiocyanates and
CC       the pathogen Hyaloperonospora parasitica.
CC       {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:12207667,
CC       ECO:0000269|PubMed:12428014, ECO:0000269|PubMed:15069083,
CC       ECO:0000269|PubMed:16361527, ECO:0000269|PubMed:20031254}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family.
CC       {ECO:0000305}.
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   UniGene; At.25493; -.
DR   UniGene; At.67704; -.
DR   ProteinModelPortal; Q9ZRW8; -.
DR   SMR; Q9ZRW8; -.
DR   BioGrid; 29393; 25.
DR   IntAct; Q9ZRW8; 23.
DR   STRING; 3702.AT1G78380.1; -.
DR   iPTMnet; Q9ZRW8; -.
DR   SwissPalm; Q9ZRW8; -.
DR   PaxDb; Q9ZRW8; -.
DR   PRIDE; Q9ZRW8; -.
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   eggNOG; ENOG410XSIX; LUCA.
DR   HOGENOM; HOG000125749; -.
DR   InParanoid; Q9ZRW8; -.
DR   KO; K00799; -.
DR   OMA; FHAYEKY; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9ZRW8; -.
DR   BioCyc; ARA:AT1G78380-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G78380-MONOMER; -.
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; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA: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:0046686; P:response to cadmium ion; IEP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
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; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF02798; GST_N; 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   Complete proteome; Cytoplasm; Detoxification; Oxidoreductase;
KW   Peroxidase; Phosphoprotein; Reference proteome; Stress response;
KW   Transferase.
FT   CHAIN         1    219       Glutathione S-transferase U19.
FT                                /FTId=PRO_0000413565.
FT   DOMAIN        3     82       GST N-terminal.
FT   DOMAIN       88    208       GST C-terminal.
FT   REGION       13     14       Glutathione binding. {ECO:0000250}.
FT   REGION       39     40       Glutathione binding. {ECO:0000250}.
FT   REGION       53     54       Glutathione binding. {ECO:0000250}.
FT   REGION       66     67       Glutathione binding. {ECO:0000250}.
FT   MOD_RES     198    198       Phosphoserine.
FT                                {ECO:0000244|PubMed:22092075}.
FT   CONFLICT     16     16       G -> R (in Ref. 5; AAM64593).
FT                                {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
//
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