GSTF7_ARATH
ID GSTF7_ARATH Reviewed; 209 AA.
AC Q9SRY5; O23720; Q541C6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glutathione S-transferase F7 {ECO:0000303|PubMed:12090627};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE AltName: Full=AtGSTF8 {ECO:0000303|PubMed:12090627};
DE AltName: Full=GST class-phi member 7 {ECO:0000303|PubMed:12090627};
DE AltName: Full=Glutathione S-transferase 11 {ECO:0000303|PubMed:12090627};
GN Name=GSTF7 {ECO:0000303|PubMed:12090627};
GN Synonyms=GST11 {ECO:0000303|PubMed:12090627},
GN GSTF8 {ECO:0000303|PubMed:12090627};
GN OrderedLocusNames=At1g02920 {ECO:0000312|Araport:AT1G02920};
GN ORFNames=F22D16.8 {ECO:0000312|EMBL:AAF02874.1};
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].
RC STRAIN=cv. Landsberg erecta;
RA Yang K.Y., Kim C.S., Kim K.C., Cho B.-H.;
RT "Characterization of a novel glutathione S-transferase gene in Arabidopsis
RT thaliana.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP INDUCTION.
RX PubMed=12881503; DOI=10.1093/pcp/pcg093;
RA Lieberherr D., Wagner U., Dubuis P.H., Metraux J.P., Mauch F.;
RT "The rapid induction of glutathione S-transferases AtGSTF2 and AtGSTF6 by
RT avirulent Pseudomonas syringae is the result of combined salicylic acid and
RT ethylene signaling.";
RL Plant Cell Physiol. 44:750-757(2003).
RN [7]
RP INDUCTION BY COPPER.
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).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides.
CC {ECO:0000250|UniProtKB:O80852}.
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 Evidence={ECO:0000250|UniProtKB:O80852};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- INDUCTION: By ethylene, salicylic acid, copper and the bacterial
CC pathogen P.syringae. {ECO:0000269|PubMed:12090627,
CC ECO:0000269|PubMed:12881503, ECO:0000269|PubMed:15069083}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; Y14251; CAA74639.1; -; Genomic_DNA.
DR EMBL; AF288177; AAG30126.1; -; mRNA.
DR EMBL; AC009525; AAF02874.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27496.1; -; Genomic_DNA.
DR EMBL; AY062642; AAL32720.1; -; mRNA.
DR EMBL; AY093281; AAM13280.1; -; mRNA.
DR PIR; F86159; F86159.
DR RefSeq; NP_171791.1; NM_100173.4.
DR AlphaFoldDB; Q9SRY5; -.
DR SMR; Q9SRY5; -.
DR BioGRID; 24530; 1.
DR IntAct; Q9SRY5; 2.
DR STRING; 3702.AT1G02920.1; -.
DR MetOSite; Q9SRY5; -.
DR SWISS-2DPAGE; Q9SRY5; -.
DR PaxDb; Q9SRY5; -.
DR PRIDE; Q9SRY5; -.
DR ProteomicsDB; 230162; -.
DR EnsemblPlants; AT1G02920.1; AT1G02920.1; AT1G02920.
DR GeneID; 839295; -.
DR Gramene; AT1G02920.1; AT1G02920.1; AT1G02920.
DR KEGG; ath:AT1G02920; -.
DR Araport; AT1G02920; -.
DR TAIR; locus:2024700; AT1G02920.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; Q9SRY5; -.
DR OMA; KEPFIFR; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9SRY5; -.
DR BioCyc; ARA:AT1G02920-MON; -.
DR PRO; PR:Q9SRY5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRY5; baseline and differential.
DR Genevisible; Q9SRY5; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0046686; P:response to cadmium ion; 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; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase F7"
FT /id="PRO_0000185852"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 90..209
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 12..13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT CONFLICT 187
FT /note="D -> A (in Ref. 1; CAA74639 and 2; AAG30126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23598 MW; FD2CC0FD28A31ACC CRC64;
MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED
GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV
LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT
PTKKLFDERP HVSAWVADIT SRPSAKKVL
