GSTF6_ARATH
ID GSTF6_ARATH Reviewed; 208 AA.
AC P42760;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutathione S-transferase F6;
DE Short=AtGSTF6;
DE EC=2.5.1.18;
DE AltName: Full=AtGSTF3;
DE AltName: Full=GST class-phi member 6;
DE AltName: Full=Glutathione S-transferase 1;
DE Short=AtGST1;
DE AltName: Full=Protein EARLY RESPONSE TO DEHYDRATION 11;
GN Name=GSTF6; Synonyms=ERD11, GST1, GSTF3; OrderedLocusNames=At1g02930;
GN ORFNames=F22D16.7;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8253194; DOI=10.1016/0014-5793(93)80727-c;
RA Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible
RT genes that encode putative glutathione S-transferases in Arabidopsis
RT thaliana L.";
RL FEBS Lett. 335:189-192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Yang K.Y., Kim E.Y., Kim K.S., Choi S.N., Guh J.O., Kim K.C., Cho B.-H.;
RT "Characterization of a glutathione S-transferase gene ATGST1 in Arabidopsis
RT thaliana.";
RL Plant Cell Rep. 17:700-704(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Yu G.-L., Ausubel F.M.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP INDUCTION, GENE FAMILY, AND NOMENCLATURE.
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 [8]
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 [9]
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).
RN [10]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21239642; DOI=10.1105/tpc.110.079145;
RA Su T., Xu J., Li Y., Lei L., Zhao L., Yang H., Feng J., Liu G., Ren D.;
RT "Glutathione-indole-3-acetonitrile is required for camalexin biosynthesis
RT in Arabidopsis thaliana.";
RL Plant Cell 23:364-380(2011).
CC -!- FUNCTION: Involved in camalexin biosynthesis by probably catalyzing the
CC conjugation of GSH with indole-3-acetonitrile (IAN). May be involved in
CC the conjugation of reduced glutathione to a wide number of exogenous
CC and endogenous hydrophobic electrophiles and have a detoxification role
CC against certain herbicides. {ECO:0000269|PubMed:21239642}.
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: Cytoplasm, cytosol {ECO:0000305}.
CC -!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
CC jasmonate, auxin, H(2)O(2), copper, metolachlor, and the pathogens
CC P.syringae and Hyaloperonospora parasitica. Induced by cadmium
CC (PubMed:16502469). {ECO:0000269|PubMed:12090627,
CC ECO:0000269|PubMed:12881503, ECO:0000269|PubMed:15069083,
CC ECO:0000269|PubMed:16502469}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but reduced levels of camalexin production during infection
CC by B.cinerea. {ECO:0000269|PubMed:21239642}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; D17672; BAA04553.1; -; mRNA.
DR EMBL; Y11727; CAA72413.1; -; Genomic_DNA.
DR EMBL; L12057; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AC009525; AAF02873.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27497.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27498.1; -; Genomic_DNA.
DR EMBL; AY050332; AAK91349.1; -; mRNA.
DR EMBL; AY097392; AAM19908.1; -; mRNA.
DR PIR; G86159; G86159.
DR PIR; S39541; S39541.
DR RefSeq; NP_001184893.1; NM_001197964.1.
DR RefSeq; NP_171792.1; NM_100174.3.
DR AlphaFoldDB; P42760; -.
DR SMR; P42760; -.
DR BioGRID; 24750; 2.
DR IntAct; P42760; 3.
DR STRING; 3702.AT1G02930.1; -.
DR SWISS-2DPAGE; P42760; -.
DR PaxDb; P42760; -.
DR PRIDE; P42760; -.
DR ProteomicsDB; 247299; -.
DR EnsemblPlants; AT1G02930.1; AT1G02930.1; AT1G02930.
DR EnsemblPlants; AT1G02930.2; AT1G02930.2; AT1G02930.
DR GeneID; 839515; -.
DR Gramene; AT1G02930.1; AT1G02930.1; AT1G02930.
DR Gramene; AT1G02930.2; AT1G02930.2; AT1G02930.
DR KEGG; ath:AT1G02930; -.
DR Araport; AT1G02930; -.
DR TAIR; locus:2024690; AT1G02930.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; P42760; -.
DR OMA; YIAHEFS; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P42760; -.
DR BioCyc; ARA:AT1G02930-MON; -.
DR BioCyc; MetaCyc:AT1G02930-MON; -.
DR PRO; PR:P42760; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42760; baseline and differential.
DR Genevisible; P42760; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:2001147; F:camalexin binding; IDA: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:2001227; F:quercitrin binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Plant defense; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..208
FT /note="Glutathione S-transferase F6"
FT /id="PRO_0000185846"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 89..208
FT /note="GST C-terminal"
FT BINDING 12..13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="S -> F (in Ref. 1; BAA04553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 23486 MW; 113CED008A11902F CRC64;
MAGIKVFGHP ASTATRRVLI ALHEKNVDFE FVHVELKDGE HKKEPFILRN PFGKVPAFED
GDFKIFESRA ITQYIAHEFS DKGNNLLSTG KDMAIIAMGI EIESHEFDPV GSKLVWEQVL
KPLYGMTTDK TVVEEEEAKL AKVLDVYEHR LGESKYLASD HFTLVDLHTI PVIQYLLGTP
TKKLFDERPH VSAWVADITS RPSAQKVL
