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Glutathione S-transferase F8, chloroplastic (AtGSTF8) (EC 2.5.1.18) (AtGSTF5) (GST class-phi member 8) (Glutathione S-transferase 6)

 GSTF8_ARATH             Reviewed;         263 AA.
Q96266; O82242; Q4PL91; Q9FUT2;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 3.
30-AUG-2017, entry version 143.
RecName: Full=Glutathione S-transferase F8, chloroplastic;
Short=AtGSTF8;
EC=2.5.1.18;
AltName: Full=AtGSTF5;
AltName: Full=GST class-phi member 8;
AltName: Full=Glutathione S-transferase 6;
Flags: Precursor;
Name=GSTF8; Synonyms=GST6, GSTF5; OrderedLocusNames=At2g47730;
ORFNames=F17A22.12;
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 [GENOMIC DNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9011080; DOI=10.1046/j.1365-313X.1996.10060955.x;
Chen W., Chao G., Singh K.B.;
"The promoter of a H2O2-inducible, Arabidopsis glutathione S-
transferase gene contains closely linked OBF- and OBP1-binding
sites.";
Plant J. 10:955-966(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=16244158; DOI=10.1104/pp.105.063479;
Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N.,
Monaghan E.L., Ayele M., Haas B.J., Wu H.C., Town C.D.;
"Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome
2 reveals numerous transcript variants.";
Plant Physiol. 139:1323-1337(2005).
[6]
INDUCTION.
PubMed=16829588; DOI=10.1104/pp.106.079509;
Foley R.C., Sappl P.G., Perl-Treves R., Millar A.H., Singh K.B.;
"Desensitization of GSTF8 induction by a prior chemical treatment is
long lasting and operates in a tissue-dependent manner.";
Plant Physiol. 142:245-253(2006).
[7]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17670748; DOI=10.1074/jbc.M702207200;
Thatcher L.F., Carrie C., Andersson C.R., Sivasithamparam K.,
Whelan J., Singh K.B.;
"Differential gene expression and subcellular targeting of Arabidopsis
glutathione S-transferase F8 is achieved through alternative
transcription start sites.";
J. Biol. Chem. 282:28915-28928(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, 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: In vitro, possesses glutathione S-transferase activity
toward 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione
peroxidase activity toward cumene hydroperoxide and linoleic acid-
13-hydroperoxide. May be involved in the conjugation of reduced
glutathione to a wide number of exogenous and endogenous
hydrophobic electrophiles and have a detoxification role against
certain herbicides. {ECO:0000269|PubMed:12090627}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:17670748}. Cytoplasm, cytosol
{ECO:0000269|PubMed:17670748}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=GSTF8-L;
IsoId=Q96266-1; Sequence=Displayed;
Name=2; Synonyms=GSTF8-S;
IsoId=Q96266-2; Sequence=VSP_041935;
-!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in leaves
and isoform 2 in roots. {ECO:0000269|PubMed:17670748}.
-!- INDUCTION: By salicylic acid, ethylene, methyl jasmonate, auxin,
H(2)O(2), metolachlor, and the pathogen Hyaloperonospora
parasitica. {ECO:0000269|PubMed:12090627,
ECO:0000269|PubMed:16829588, ECO:0000269|PubMed:9011080}.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA64613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X95295; CAA64613.1; ALT_SEQ; Genomic_DNA.
EMBL; AF288176; AAG30125.2; -; mRNA.
EMBL; AC005309; AAC63629.2; -; Genomic_DNA.
EMBL; CP002685; AEC10880.1; -; Genomic_DNA.
EMBL; CP002685; ANM61251.1; -; Genomic_DNA.
EMBL; DQ069797; AAY82256.1; -; mRNA.
PIR; H84918; H84918.
RefSeq; NP_001323480.1; NM_001337273.1. [Q96266-1]
RefSeq; NP_850479.1; NM_180148.5. [Q96266-1]
UniGene; At.25017; -.
ProteinModelPortal; Q96266; -.
SMR; Q96266; -.
BioGrid; 4721; 1.
IntAct; Q96266; 2.
STRING; 3702.AT2G47730.1; -.
iPTMnet; Q96266; -.
PaxDb; Q96266; -.
PRIDE; Q96266; -.
EnsemblPlants; AT2G47730.1; AT2G47730.1; AT2G47730. [Q96266-1]
EnsemblPlants; AT2G47730.2; AT2G47730.2; AT2G47730. [Q96266-1]
GeneID; 819386; -.
Gramene; AT2G47730.1; AT2G47730.1; AT2G47730.
Gramene; AT2G47730.2; AT2G47730.2; AT2G47730.
KEGG; ath:AT2G47730; -.
Araport; AT2G47730; -.
TAIR; locus:2043298; AT2G47730.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125746; -.
InParanoid; Q96266; -.
KO; K00799; -.
OMA; LLCQGCK; -.
OrthoDB; EOG09360M18; -.
PhylomeDB; Q96266; -.
BioCyc; ARA:AT2G47730-MONOMER; -.
BioCyc; MetaCyc:AT2G47730-MONOMER; -.
PRO; PR:Q96266; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; Q96266; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0010319; C:stromule; IDA:TAIR.
GO; GO:0009579; C:thylakoid; 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; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
CDD; cd03187; GST_C_Phi; 1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR034347; GST_Phi_C.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF00043; GST_C; 1.
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;
Alternative splicing; Chloroplast; Complete proteome; Cytoplasm;
Detoxification; Oxidoreductase; Peroxidase; Phosphoprotein; Plastid;
Reference proteome; Stress response; Transferase; Transit peptide.
TRANSIT 1 49 Chloroplast. {ECO:0000255}.
CHAIN 50 263 Glutathione S-transferase F8,
chloroplastic.
/FTId=PRO_0000185850.
DOMAIN 50 131 GST N-terminal.
DOMAIN 139 263 GST C-terminal.
REGION 60 61 Glutathione binding. {ECO:0000250}.
REGION 89 90 Glutathione binding. {ECO:0000250}.
REGION 102 103 Glutathione binding. {ECO:0000250}.
REGION 115 116 Glutathione binding. {ECO:0000250}.
MOD_RES 177 177 Phosphothreonine.
{ECO:0000244|PubMed:22092075}.
VAR_SEQ 1 48 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_041935.
SEQUENCE 263 AA; 29232 MW; 0A2927A7C4CA3047 CRC64;
MGAIQARLPL FLSPPSIKHH TFLHSSSSNS NFKIRSNKSS SSSSSSIIMA SIKVHGVPMS
TATMRVLATL YEKDLQFELI PVDMRAGAHK QEAHLALNPF GQIPALEDGD LTLFESRAIT
QYLAEEYSEK GEKLISQDCK KVKATTNVWL QVEGQQFDPN ASKLAFERVF KGMFGMTTDP
AAVQELEGKL QKVLDVYEAR LAKSEFLAGD SFTLADLHHL PAIHYLLGTD SKVLFDSRPK
VSEWIKKISA RPAWAKVIDL QKQ


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