GSTF8_ARATH
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 03-AUG-2022, entry version 168.
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.AT2G47730.1; -.
DR iPTMnet; Q96266; -.
DR MetOSite; Q96266; -.
DR PaxDb; Q96266; -.
DR PRIDE; Q96266; -.
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; locus:2043298; AT2G47730.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; Q96266; -.
DR OMA; RIPAFEH; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q96266; -.
DR BioCyc; ARA:AT2G47730-MON; -.
DR BioCyc; MetaCyc:AT2G47730-MON; -.
DR PRO; PR:Q96266; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q96266; baseline and differential.
DR Genevisible; Q96266; AT.
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:0005737; C:cytoplasm; IBA:GO_Central.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
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 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 Pfam; PF00043; GST_C; 1.
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 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
