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Glutathione S-transferase U19 (AtGSTU19) (EC 2.5.1.18) (GST class-tau member 19) (Glutathione S-transferase 8)

 GSTUJ_ARATH             Reviewed;         219 AA.
Q9ZRW8; Q8LBS1;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
30-AUG-2017, entry version 127.
RecName: Full=Glutathione S-transferase U19;
Short=AtGSTU19;
EC=2.5.1.18;
AltName: Full=GST class-tau member 19;
AltName: Full=Glutathione S-transferase 8;
Name=GSTU19; Synonyms=GST8; OrderedLocusNames=At1g78380;
ORFNames=F3F9.11;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=12207667; DOI=10.1034/j.1399-3054.2002.1160112.x;
Bianchi M.W., Roux C., Vartanian N.;
"Drought regulation of GST8, encoding the Arabidopsis homologue of
ParC/Nt107 glutathione transferase/peroxidase.";
Physiol. Plantarum 116:96-105(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12090627; DOI=10.1023/A:1015557300450;
Wagner U., Edwards R., Dixon D.P., Mauch F.;
"Probing the diversity of the Arabidopsis glutathione S-transferase
gene family.";
Plant Mol. Biol. 49:515-532(2002).
[7]
INDUCTION.
PubMed=12428014; DOI=10.1104/pp.010066;
DeRidder B.P., Dixon D.P., Beussman D.J., Edwards R.,
Goldsbrough P.B.;
"Induction of glutathione S-transferases in Arabidopsis by herbicide
safeners.";
Plant Physiol. 130:1497-1505(2002).
[8]
INDUCTION.
PubMed=15069083; DOI=10.1074/jbc.M402807200;
Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E.,
Goldsbrough P.B.;
"Proteomic analysis of Arabidopsis glutathione S-transferases from
benoxacor- and copper-treated seedlings.";
J. Biol. Chem. 279:26098-26104(2004).
[9]
FUNCTION, AND INDUCTION.
PubMed=16361527; DOI=10.1104/pp.105.067199;
DeRidder B.P., Goldsbrough P.B.;
"Organ-specific expression of glutathione S-transferases and the
efficacy of herbicide safeners in Arabidopsis.";
Plant Physiol. 140:167-175(2006).
[10]
FUNCTION.
PubMed=19520850; DOI=10.1074/jbc.M109.020107;
Dixon D.P., Edwards R.;
"Selective binding of glutathione conjugates of fatty acid derivatives
by plant glutathione transferases.";
J. Biol. Chem. 284:21249-21256(2009).
[11]
SUBCELLULAR LOCATION.
PubMed=19174456; DOI=10.1093/jxb/ern365;
Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
"Enzyme activities and subcellular localization of members of the
Arabidopsis glutathione transferase superfamily.";
J. Exp. Bot. 60:1207-1218(2009).
[12]
INDUCTION.
PubMed=20031254; DOI=10.1016/j.jplph.2009.11.006;
Hara M., Yatsuzuka Y., Tabata K., Kuboi T.;
"Exogenously applied isothiocyanates enhance glutathione S-transferase
expression in Arabidopsis but act as herbicides at higher
concentrations.";
J. Plant Physiol. 167:643-649(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
-!- FUNCTION: Catalyzes the glutathionylation of 12-oxophytodienoate
(OPDA). In vitro, possesses glutathione S-transferase activity
toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl
isothiocyanate (BITC), and glutathione peroxidase activity toward
cumene hydroperoxide. {ECO:0000269|PubMed:12090627,
ECO:0000269|PubMed:16361527, ECO:0000269|PubMed:19520850}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19174456}.
-!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
jasmonate, auxin, H(2)O(2), copper, benoxacor, isothiocyanates and
the pathogen Hyaloperonospora parasitica.
{ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:12207667,
ECO:0000269|PubMed:12428014, ECO:0000269|PubMed:15069083,
ECO:0000269|PubMed:16361527, ECO:0000269|PubMed:20031254}.
-!- SIMILARITY: Belongs to the GST superfamily. Tau family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ012571; CAA10060.1; -; mRNA.
EMBL; AC013430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002684; AEE36099.1; -; Genomic_DNA.
EMBL; AF385691; AAK60284.1; -; mRNA.
EMBL; AY078012; AAL77713.1; -; mRNA.
EMBL; AY087032; AAM64593.1; -; mRNA.
PIR; T51607; T51607.
RefSeq; NP_565178.1; NM_106485.4.
UniGene; At.25493; -.
UniGene; At.67704; -.
ProteinModelPortal; Q9ZRW8; -.
SMR; Q9ZRW8; -.
BioGrid; 29393; 25.
IntAct; Q9ZRW8; 5.
STRING; 3702.AT1G78380.1; -.
iPTMnet; Q9ZRW8; -.
SwissPalm; Q9ZRW8; -.
PaxDb; Q9ZRW8; -.
PRIDE; Q9ZRW8; -.
EnsemblPlants; AT1G78380.1; AT1G78380.1; AT1G78380.
GeneID; 844174; -.
Gramene; AT1G78380.1; AT1G78380.1; AT1G78380.
KEGG; ath:AT1G78380; -.
Araport; AT1G78380; -.
TAIR; locus:2032100; AT1G78380.
eggNOG; KOG0406; Eukaryota.
eggNOG; ENOG410XSIX; LUCA.
HOGENOM; HOG000125749; -.
InParanoid; Q9ZRW8; -.
KO; K00799; -.
OMA; FHAYEKY; -.
OrthoDB; EOG09360PCQ; -.
PhylomeDB; Q9ZRW8; -.
BioCyc; ARA:AT1G78380-MONOMER; -.
BioCyc; MetaCyc:AT1G78380-MONOMER; -.
BRENDA; 2.5.1.18; 399.
PRO; PR:Q9ZRW8; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9ZRW8; baseline and differential.
Genevisible; Q9ZRW8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; NAS:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0043295; F:glutathione binding; IDA:TAIR.
GO; GO:0004364; F:glutathione transferase activity; ISS:TAIR.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF02798; GST_N; 1.
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; Cytoplasm; Detoxification; Oxidoreductase;
Peroxidase; Phosphoprotein; Reference proteome; Stress response;
Transferase.
CHAIN 1 219 Glutathione S-transferase U19.
/FTId=PRO_0000413565.
DOMAIN 3 82 GST N-terminal.
DOMAIN 88 208 GST C-terminal.
REGION 13 14 Glutathione binding. {ECO:0000250}.
REGION 39 40 Glutathione binding. {ECO:0000250}.
REGION 53 54 Glutathione binding. {ECO:0000250}.
REGION 66 67 Glutathione binding. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
CONFLICT 16 16 G -> R (in Ref. 5; AAM64593).
{ECO:0000305}.
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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