ID   GSTF8_ARATH             Reviewed;         263 AA.
AC   Q96266; O82242; Q4PL91; Q9FUT2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Glutathione S-transferase F8, chloroplastic;
DE            Short=AtGSTF8;
DE            EC=2.5.1.18;
DE   AltName: Full=AtGSTF5;
DE   AltName: Full=GST class-phi member 8;
DE   AltName: Full=Glutathione S-transferase 6;
DE   Flags: Precursor;
GN   Name=GSTF8; Synonyms=GST6, GSTF5; OrderedLocusNames=At2g47730;
GN   ORFNames=F17A22.12;
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 [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9011080; DOI=10.1046/j.1365-313x.1996.10060955.x;
RA   Chen W., Chao G., Singh K.B.;
RT   "The promoter of a H2O2-inducible, Arabidopsis glutathione S-transferase
RT   gene contains closely linked OBF- and OBP1-binding sites.";
RL   Plant J. 10:955-966(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, GENE FAMILY,
RP   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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=16244158; DOI=10.1104/pp.105.063479;
RA   Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA   Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT   "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT   reveals numerous transcript variants.";
RL   Plant Physiol. 139:1323-1337(2005).
RN   [6]
RP   INDUCTION.
RX   PubMed=16829588; DOI=10.1104/pp.106.079509;
RA   Foley R.C., Sappl P.G., Perl-Treves R., Millar A.H., Singh K.B.;
RT   "Desensitization of GSTF8 induction by a prior chemical treatment is long
RT   lasting and operates in a tissue-dependent manner.";
RL   Plant Physiol. 142:245-253(2006).
RN   [7]
RP   ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17670748; DOI=10.1074/jbc.m702207200;
RA   Thatcher L.F., Carrie C., Andersson C.R., Sivasithamparam K., Whelan J.,
RA   Singh K.B.;
RT   "Differential gene expression and subcellular targeting of Arabidopsis
RT   glutathione S-transferase F8 is achieved through alternative transcription
RT   start sites.";
RL   J. Biol. Chem. 282:28915-28928(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, 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: In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB) and glutathione peroxidase activity
CC       toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be
CC       involved in the conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles and have a
CC       detoxification role against certain herbicides.
CC       {ECO:0000269|PubMed:12090627}.
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: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17670748}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:17670748}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=GSTF8-L;
CC         IsoId=Q96266-1; Sequence=Displayed;
CC       Name=2; Synonyms=GSTF8-S;
CC         IsoId=Q96266-2; Sequence=VSP_041935;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in leaves and
CC       isoform 2 in roots. {ECO:0000269|PubMed:17670748}.
CC   -!- INDUCTION: By salicylic acid, ethylene, methyl jasmonate, auxin,
CC       H(2)O(2), metolachlor, and the pathogen Hyaloperonospora parasitica.
CC       {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16829588,
CC       ECO:0000269|PubMed:9011080}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA64613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X95295; CAA64613.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF288176; AAG30125.2; -; mRNA.
DR   EMBL; AC005309; AAC63629.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10880.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61251.1; -; Genomic_DNA.
DR   EMBL; DQ069797; AAY82256.1; -; mRNA.
DR   PIR; H84918; H84918.
DR   RefSeq; NP_001323480.1; NM_001337273.1. [Q96266-1]
DR   RefSeq; NP_850479.1; NM_180148.5. [Q96266-1]
DR   AlphaFoldDB; Q96266; -.
DR   SMR; Q96266; -.
DR   BioGRID; 4721; 1.
DR   IntAct; Q96266; 2.
DR   STRING; 3702.Q96266; -.
DR   iPTMnet; Q96266; -.
DR   MetOSite; Q96266; -.
DR   PaxDb; 3702-AT2G47730-1; -.
DR   ProteomicsDB; 247186; -. [Q96266-1]
DR   EnsemblPlants; AT2G47730.1; AT2G47730.1; AT2G47730. [Q96266-1]
DR   EnsemblPlants; AT2G47730.2; AT2G47730.2; AT2G47730. [Q96266-1]
DR   GeneID; 819386; -.
DR   Gramene; AT2G47730.1; AT2G47730.1; AT2G47730. [Q96266-1]
DR   Gramene; AT2G47730.2; AT2G47730.2; AT2G47730. [Q96266-1]
DR   KEGG; ath:AT2G47730; -.
DR   Araport; AT2G47730; -.
DR   TAIR; AT2G47730; GSTF8.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   InParanoid; Q96266; -.
DR   OMA; DYLAGNN; -.
DR   OrthoDB; 639740at2759; -.
DR   PhylomeDB; Q96266; -.
DR   BioCyc; ARA:AT2G47730-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G47730-MONOMER; -.
DR   PRO; PR:Q96266; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q96266; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0006952; P:defense response; IEP:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03187; GST_C_Phi; 1.
DR   CDD; cd03053; GST_N_Phi; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR034347; GST_Phi_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43900:SF44; GLUTATHIONE S-TRANSFERASE F8, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01154; Main.5:_Phi-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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.
DR   Genevisible; Q96266; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Cytoplasm; Detoxification;
KW   Oxidoreductase; Peroxidase; Phosphoprotein; Plastid; Reference proteome;
KW   Stress response; Transferase; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..263
FT                   /note="Glutathione S-transferase F8, chloroplastic"
FT                   /id="PRO_0000185850"
FT   DOMAIN          50..131
FT                   /note="GST N-terminal"
FT   DOMAIN          139..263
FT                   /note="GST C-terminal"
FT   BINDING         60..61
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..90
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..116
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         177
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   VAR_SEQ         1..48
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041935"
SQ   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
//