Q9SRY5 (GSTF7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase F7
EC=2.5.1.18

Alternative name(s):
AtGSTF8
GST class-phi member 7
Glutathione S-transferase 11

Gene names

Name:	GSTF7
Synonyms:	GST11, GSTF8
Ordered Locus Names:	At1g02920
ORF Names:	F22D16.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm › cytosol Probable.
Induction	By ethylene, salicylic acid, copper and the bacterial pathogen P.syringae. Ref.2 Ref.6 Ref.7
Sequence similarities	Belongs to the GST superfamily. Phi family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Detoxification Stress response
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from expression pattern PubMed 17028151. Source: TAIR defense response to fungus, incompatible interaction Inferred from direct assay PubMed 19857612. Source: TAIR response to cadmium ion Inferred from expression pattern PubMed 16502469PubMed 17075075. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR response to toxin Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.2. Source: TAIR
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 15610358. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	cobalt ion binding Inferred from direct assay PubMed 20018591. Source: TAIR copper ion binding Inferred from direct assay PubMed 16526091. Source: TAIR glutathione binding Inferred from direct assay PubMed 15159623. Source: TAIR glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	Glutathione S-transferase F7		PRO_0000185852
Regions
	Domain	2 – 83	82	GST N-terminal
	Domain	90 – 209	120	GST C-terminal
	Region	12 – 13	2	Glutathione binding By similarity
	Region	41 – 42	2	Glutathione binding By similarity
	Region	54 – 55	2	Glutathione binding By similarity
	Region	67 – 68	2	Glutathione binding By similarity
	Compositional bias	135 – 138	4	Poly-Glu
Experimental info
	Sequence conflict	187	1	D → A in CAA74639. Ref.1
	Sequence conflict	187	1	D → A in AAG30126. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SRY5 [UniParc]. Last modified February 5, 2008. Version 3. Checksum: FD2CC0FD28A31ACC	FASTA	209	23,598
	10 20 30 40 50 60 MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED 70 80 90 100 110 120 GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV 130 140 150 160 170 180 LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT 190 200 PTKKLFDERP HVSAWVADIT SRPSAKKVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel glutathione S-transferase gene in Arabidopsis thaliana." Yang K.Y., Kim C.S., Kim K.C., Cho B.-H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"Probing the diversity of the Arabidopsis glutathione S-transferase gene family." Wagner U., Edwards R., Dixon D.P., Mauch F. Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"The rapid induction of glutathione S-transferases AtGSTF2 and AtGSTF6 by avirulent Pseudomonas syringae is the result of combined salicylic acid and ethylene signaling." Lieberherr D., Wagner U., Dubuis P.H., Metraux J.P., Mauch F. Plant Cell Physiol. 44:750-757(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"Proteomic analysis of Arabidopsis glutathione S-transferases from benoxacor- and copper-treated seedlings." Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E., Goldsbrough P.B. J. Biol. Chem. 279:26098-26104(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY COPPER.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14251 Genomic DNA. Translation: CAA74639.1. AF288177 mRNA. Translation: AAG30126.1. AC009525 Genomic DNA. Translation: AAF02874.1. CP002684 Genomic DNA. Translation: AEE27496.1. AY062642 mRNA. Translation: AAL32720.1. AY093281 mRNA. Translation: AAM13280.1.
IPI	IPI00530258.
PIR	F86159.
RefSeq	NP_171791.1. NM_100173.3.
UniGene	At.20350. At.23846. At.71571.
3D structure databases
ProteinModelPortal	Q9SRY5.
SMR	Q9SRY5. Positions 3-208.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SRY5. 2 interactions.
2D gel databases
SWISS-2DPAGE	Q9SRY5.
Proteomic databases
PaxDb	Q9SRY5.
PRIDE	Q9SRY5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G02920.1; AT1G02920.1; AT1G02920.
GeneID	839295.
KEGG	ath:AT1G02920.
Organism-specific databases
TAIR	At1g02920.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000125746.
InParanoid	Q9SRY5.
KO	K00799.
OMA	KEPFIFR.
PhylomeDB	Q9SRY5.
ProtClustDB	CLSN2679613.
Gene expression databases
Genevestigator	Q9SRY5.
GermOnline	AT1G02920. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTF7_ARATH

Accession

Primary (citable) accession number: Q9SRY5
Secondary accession number(s): O23720, Q541C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program