P46422 (GSTF2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase F2
Short name=AtGSTF2
EC=2.5.1.18

Alternative name(s):
24 kDa auxin-binding protein
Short name=AtPM24
GST class-phi member 2

Gene names

Name:	GSTF2
Synonyms:	PM24.1
Ordered Locus Names:	At4g02520
ORF Names:	T10P11.18

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	212 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA. Ref.6 Ref.12
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm › cytosol. Microsome. Endoplasmic reticulum. Note: Plasma membrane vesicles. Ref.11
Tissue specificity	Expressed in the root-shoot transition zone and root tips. Ref.8
Induction	By ethylene, auxin, glutathione, salicylic acid, copper, paraquat, acetochlor, metolachlor and the pathogens P.syringae and Hyaloperonospora parasitica. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
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	Auxin signaling pathway Detoxification Plant defense Stress response
Cellular component	Cytoplasm Endoplasmic reticulum Microsome
Molecular function	Oxidoreductase Peroxidase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	auxin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from expression pattern PubMed 17028151. Source: TAIR defense response to fungus Inferred from expression pattern PubMed 21711359. Source: TAIR response to cadmium ion Inferred from expression pattern PubMed 16502469PubMed 17075075. Source: TAIR response to cold Inferred from expression pattern PubMed 14535880. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR response to toxin Inferred from electronic annotation. Source: UniProtKB-KW response to zinc ion Inferred from expression pattern PubMed 19880396. Source: TAIR toxin catabolic process Traceable author statement Ref.6. Source: TAIR
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast stroma Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR cytosol Inferred from direct assay PubMed 21166475. Source: TAIR endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 17317660Ref.1. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	camalexin binding Inferred from direct assay Ref.12. Source: TAIR glutathione binding Inferred from direct assay PubMed 15159623. Source: TAIR glutathione transferase activity Inferred from direct assay Ref.1. Source: TAIR peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW quercitrin binding Inferred from direct assay Ref.12. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 212

211

Glutathione S-transferase F2

PRO_0000185848

Regions

Domain

2 – 83

82

GST N-terminal

Domain

93 – 212

120

GST C-terminal

Region

12 – 13

2

Glutathione binding

Region

41 – 42

2

Glutathione binding

Region

54 – 55

2

Glutathione binding

Region

67 – 68

2

Glutathione binding

Secondary structure

1

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212

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

13 – 24

12

Beta strand

30 – 33

4

Helix

36 – 38

3

Helix

40 – 42

3

Helix

46 – 48

3

Beta strand

57 – 60

4

Beta strand

63 – 66

4

Helix

68 – 78

11

Turn

79 – 81

3

Beta strand

82 – 84

3

Helix

94 – 109

16

Helix

112 – 122

11

Helix

124 – 127

4

Helix

134 – 155

22

Beta strand

159 – 165

7

Helix

168 – 171

4

Helix

174 – 180

7

Helix

184 – 186

3

Helix

187 – 190

4

Helix

193 – 203

11

Helix

206 – 209

4

Sequences

	Sequence		Length	Mass (Da)
	P46422 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 90A1CBEEEBAC815B	FASTA	212	24,129
	10 20 30 40 50 60 MAGIKVFGHP ASIATRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN PFGQVPAFED 70 80 90 100 110 120 GDLKLFESRA ITQYIAHRYE NQGTNLLQTD SKNISQYAIM AIGMQVEDHQ FDPVASKLAF 130 140 150 160 170 180 EQIFKSIYGL TTDEAVVAEE EAKLAKVLDV YEARLKEFKY LAGETFTLTD LHHIPAIQYL 190 200 210 LGTPTKKLFT ERPRVNEWVA EITKRPASEK VQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase." Zettl R., Schell J., Palme K. Proc. Natl. Acad. Sci. U.S.A. 91:689-693(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"An Arabidopsis gene with homology to glutathione S-transferases is regulated by ethylene." Zhou J., Goldsbrough P.B. Plant Mol. Biol. 22:517-523(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY ETHYLENE. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [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]	"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: FUNCTION, INDUCTION, GENE FAMILY, NOMENCLATURE.
[7]	"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.
[8]	"Arabidopsis AtGSTF2 is regulated by ethylene and auxin, and encodes a glutathione S-transferase that interacts with flavonoids." Smith A.P., Nourizadeh S.D., Peer W.A., Xu J., Bandyopadhyay A., Murphy A.S., Goldsbrough P.B. Plant J. 36:433-442(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]	"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.
[10]	"Gene expression and microscopic analysis of Arabidopsis exposed to chloroacetanilide herbicides and explosive compounds. A phytoremediation approach." Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L., Schnoor J.L. Plant Physiol. 138:858-869(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[11]	"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily." Dixon D.P., Hawkins T., Hussey P.J., Edwards R. J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"The Arabidopsis phi class glutathione transferase AtGSTF2: binding and regulation by biologically active heterocyclic ligands." Dixon D.P., Sellars J.D., Edwards R. Biochem. J. 438:63-70(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2-A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture." Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Palme K., Schell J., Koelln I., Bartunik H.D., Bieseler B. J. Mol. Biol. 255:289-309(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEXYLGLUTATHIONE.
[14]	"Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase -- explanations for the selectivity of the enzyme in plants." Prade L., Huber R., Bieseler B. Structure 6:1445-1452(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X75303 mRNA. Translation: CAA53051.1.
L07589 mRNA. Translation: AAA32800.1.
L11601 mRNA. Translation: AAA32801.1.
AC002330 Genomic DNA. Translation: AAC78264.1.
AL161494 Genomic DNA. Translation: CAB80745.1.
CP002687 Genomic DNA. Translation: AEE82183.1.
AF324681 mRNA. Translation: AAG40032.1.
AF326903 mRNA. Translation: AAG41485.1.
AF349527 mRNA. Translation: AAK15574.1.
AY039580 mRNA. Translation: AAK62635.1.
AY056082 mRNA. Translation: AAL06970.1.

IPI

IPI00535149.

PIR

S35268.

RefSeq

NP_192161.1. NM_116486.2.

UniGene

At.22195.
At.24972.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BX9	X-ray	2.60	A	2-212	[»]
1GNW	X-ray	2.20	A/B	2-212	[»]

ProteinModelPortal

P46422.

SMR

P46422. Positions 3-212.

ModBase

Search...

2D gel databases

SWISS-2DPAGE

P46422.

Proteomic databases

PRIDE

P46422.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G02520.1; AT4G02520.1; AT4G02520.

GeneID

827931.

KEGG

ath:AT4G02520.

Organism-specific databases

TAIR

At4g02520.

Phylogenomic databases

HOGENOM

HOG000125746.

InParanoid

P46422.

KO

K00799.

OMA

NISQYAI.

PhylomeDB

P46422.

ProtClustDB

CLSN2679613.

Gene expression databases

Genevestigator

P46422.

GermOnline

AT4G02520. 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...

Other

EvolutionaryTrace

P46422.

Entry information

Entry name

GSTF2_ARATH

Accession

Primary (citable) accession number: P46422

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program