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Glutathione S-transferase F6 (AtGSTF6) (EC 2.5.1.18) (AtGSTF3) (GST class-phi member 6) (Glutathione S-transferase 1) (AtGST1) (Protein EARLY RESPONSE TO DEHYDRATION 11)

 GSTF6_ARATH             Reviewed;         208 AA.
P42760;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 137.
RecName: Full=Glutathione S-transferase F6;
Short=AtGSTF6;
EC=2.5.1.18;
AltName: Full=AtGSTF3;
AltName: Full=GST class-phi member 6;
AltName: Full=Glutathione S-transferase 1;
Short=AtGST1;
AltName: Full=Protein EARLY RESPONSE TO DEHYDRATION 11;
Name=GSTF6; Synonyms=ERD11, GST1, GSTF3; OrderedLocusNames=At1g02930;
ORFNames=F22D16.7;
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 [MRNA].
STRAIN=cv. Columbia;
PubMed=8253194; DOI=10.1016/0014-5793(93)80727-C;
Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
"Characterization of two cDNAs (ERD11 and ERD13) for dehydration-
inducible genes that encode putative glutathione S-transferases in
Arabidopsis thaliana L.";
FEBS Lett. 335:189-192(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Yang K.Y., Kim E.Y., Kim K.S., Choi S.N., Guh J.O., Kim K.C.,
Cho B.-H.;
"Characterization of a glutathione S-transferase gene ATGST1 in
Arabidopsis thaliana.";
Plant Cell Rep. 17:700-704(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Yu G.-L., Ausubel F.M.;
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
INDUCTION, GENE FAMILY, AND NOMENCLATURE.
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).
[8]
INDUCTION.
PubMed=12881503; DOI=10.1093/pcp/pcg093;
Lieberherr D., Wagner U., Dubuis P.H., Metraux J.P., Mauch F.;
"The rapid induction of glutathione S-transferases AtGSTF2 and AtGSTF6
by avirulent Pseudomonas syringae is the result of combined salicylic
acid and ethylene signaling.";
Plant Cell Physiol. 44:750-757(2003).
[9]
INDUCTION BY COPPER.
PubMed=15069083; DOI=10.1074/jbc.M402807200;
Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E.,
Goldsbrough P.B.;
"Proteomic analysis of Arabidopsis glutathione S-transferases from
benoxacor- and copper-treated seedlings.";
J. Biol. Chem. 279:26098-26104(2004).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21239642; DOI=10.1105/tpc.110.079145;
Su T., Xu J., Li Y., Lei L., Zhao L., Yang H., Feng J., Liu G.,
Ren D.;
"Glutathione-indole-3-acetonitrile is required for camalexin
biosynthesis in Arabidopsis thaliana.";
Plant Cell 23:364-380(2011).
-!- FUNCTION: Involved in camalexin biosynthesis by probably
catalyzing the conjugation of GSH with indole-3-acetonitrile
(IAN). 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:21239642}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
-!- INDUCTION: By dehydration stress, salicylic acid, ethylene, methyl
jasmonate, auxin, H(2)O(2), copper, metolachlor, and the pathogens
P.syringae and Hyaloperonospora parasitica.
{ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:12881503,
ECO:0000269|PubMed:15069083}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but reduced levels of camalexin production during
infection by B.cinerea. {ECO:0000269|PubMed:21239642}.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D17672; BAA04553.1; -; mRNA.
EMBL; Y11727; CAA72413.1; -; Genomic_DNA.
EMBL; L12057; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AC009525; AAF02873.1; -; Genomic_DNA.
EMBL; CP002684; AEE27497.1; -; Genomic_DNA.
EMBL; CP002684; AEE27498.1; -; Genomic_DNA.
EMBL; AY050332; AAK91349.1; -; mRNA.
EMBL; AY097392; AAM19908.1; -; mRNA.
PIR; G86159; G86159.
PIR; S39541; S39541.
RefSeq; NP_001184893.1; NM_001197964.1.
RefSeq; NP_171792.1; NM_100174.3.
UniGene; At.20350; -.
UniGene; At.23846; -.
ProteinModelPortal; P42760; -.
SMR; P42760; -.
BioGrid; 24750; 2.
IntAct; P42760; 3.
STRING; 3702.AT1G02930.1; -.
SWISS-2DPAGE; P42760; -.
PaxDb; P42760; -.
PRIDE; P42760; -.
EnsemblPlants; AT1G02930.1; AT1G02930.1; AT1G02930.
EnsemblPlants; AT1G02930.2; AT1G02930.2; AT1G02930.
GeneID; 839515; -.
Gramene; AT1G02930.1; AT1G02930.1; AT1G02930.
Gramene; AT1G02930.2; AT1G02930.2; AT1G02930.
KEGG; ath:AT1G02930; -.
Araport; AT1G02930; -.
TAIR; locus:2024690; AT1G02930.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125746; -.
InParanoid; P42760; -.
KO; K00799; -.
OMA; YIAHEFS; -.
OrthoDB; EOG09360M18; -.
PhylomeDB; P42760; -.
BioCyc; ARA:AT1G02930-MONOMER; -.
PRO; PR:P42760; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P42760; baseline and differential.
Genevisible; P42760; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; NAS:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:2001147; F:camalexin binding; IDA:TAIR.
GO; GO:0050897; F:cobalt ion binding; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0043295; F:glutathione binding; IDA:TAIR.
GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
GO; GO:2001227; F:quercitrin binding; IDA:TAIR.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009414; P:response to water deprivation; 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; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR034347; GST_Phi_C.
InterPro; IPR036249; Thioredoxin-like_sf.
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.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Detoxification; Plant defense;
Reference proteome; Stress response; Transferase.
CHAIN 1 208 Glutathione S-transferase F6.
/FTId=PRO_0000185846.
DOMAIN 2 83 GST N-terminal.
DOMAIN 89 208 GST C-terminal.
REGION 12 13 Glutathione binding. {ECO:0000250}.
REGION 41 42 Glutathione binding. {ECO:0000250}.
REGION 54 55 Glutathione binding. {ECO:0000250}.
REGION 67 68 Glutathione binding. {ECO:0000250}.
CONFLICT 12 12 S -> F (in Ref. 1; BAA04553).
{ECO:0000305}.
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


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