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Glutathione S-transferase F7 (EC 2.5.1.18) (AtGSTF8) (GST class-phi member 7) (Glutathione S-transferase 11)

 GSTF7_ARATH             Reviewed;         209 AA.
Q9SRY5; O23720; Q541C6;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 3.
25-APR-2018, entry version 128.
RecName: Full=Glutathione S-transferase F7;
EC=2.5.1.18;
AltName: Full=AtGSTF8;
AltName: Full=GST class-phi member 7;
AltName: Full=Glutathione S-transferase 11;
Name=GSTF7; Synonyms=GST11, GSTF8; OrderedLocusNames=At1g02920;
ORFNames=F22D16.8;
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 [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Yang K.Y., Kim C.S., Kim K.C., Cho B.-H.;
"Characterization of a novel glutathione S-transferase gene in
Arabidopsis thaliana.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
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).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
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).
[6]
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).
[7]
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).
-!- FUNCTION: 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:0000250}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
-!- INDUCTION: By ethylene, salicylic acid, copper and the bacterial
pathogen P.syringae. {ECO:0000269|PubMed:12090627,
ECO:0000269|PubMed:12881503, ECO:0000269|PubMed:15069083}.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y14251; CAA74639.1; -; Genomic_DNA.
EMBL; AF288177; AAG30126.1; -; mRNA.
EMBL; AC009525; AAF02874.1; -; Genomic_DNA.
EMBL; CP002684; AEE27496.1; -; Genomic_DNA.
EMBL; AY062642; AAL32720.1; -; mRNA.
EMBL; AY093281; AAM13280.1; -; mRNA.
PIR; F86159; F86159.
RefSeq; NP_171791.1; NM_100173.4.
UniGene; At.20350; -.
UniGene; At.23846; -.
UniGene; At.71571; -.
ProteinModelPortal; Q9SRY5; -.
SMR; Q9SRY5; -.
BioGrid; 24530; 1.
IntAct; Q9SRY5; 2.
STRING; 3702.AT1G02920.1; -.
SWISS-2DPAGE; Q9SRY5; -.
PaxDb; Q9SRY5; -.
PRIDE; Q9SRY5; -.
EnsemblPlants; AT1G02920.1; AT1G02920.1; AT1G02920.
GeneID; 839295; -.
Gramene; AT1G02920.1; AT1G02920.1; AT1G02920.
KEGG; ath:AT1G02920; -.
Araport; AT1G02920; -.
TAIR; locus:2024700; AT1G02920.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125746; -.
InParanoid; Q9SRY5; -.
KO; K00799; -.
OMA; KEPFIFR; -.
OrthoDB; EOG093616HH; -.
PhylomeDB; Q9SRY5; -.
BioCyc; ARA:AT1G02920-MONOMER; -.
PRO; PR:Q9SRY5; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SRY5; baseline and differential.
Genevisible; Q9SRY5; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005773; C:vacuole; 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:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IDA:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; 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; Reference proteome;
Stress response; Transferase.
CHAIN 1 209 Glutathione S-transferase F7.
/FTId=PRO_0000185852.
DOMAIN 2 83 GST N-terminal.
DOMAIN 90 209 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}.
COMPBIAS 135 138 Poly-Glu.
CONFLICT 187 187 D -> A (in Ref. 1; CAA74639 and 2;
AAG30126). {ECO:0000305}.
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


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