GSTF2_ARATH
ID GSTF2_ARATH Reviewed; 212 AA.
AC P46422;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Glutathione S-transferase F2;
DE Short=AtGSTF2;
DE EC=2.5.1.18;
DE AltName: Full=24 kDa auxin-binding protein;
DE Short=AtPM24;
DE AltName: Full=GST class-phi member 2;
GN Name=GSTF2; Synonyms=PM24.1; OrderedLocusNames=At4g02520;
GN ORFNames=T10P11.18;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8290582; DOI=10.1073/pnas.91.2.689;
RA Zettl R., Schell J., Palme K.;
RT "Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by
RT 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-
RT transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:689-693(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY ETHYLENE.
RC TISSUE=Leaf;
RX PubMed=8329687; DOI=10.1007/bf00015980;
RA Zhou J., Goldsbrough P.B.;
RT "An Arabidopsis gene with homology to glutathione S-transferases is
RT regulated by ethylene.";
RL Plant Mol. Biol. 22:517-523(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION, 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 [7]
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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14617075; DOI=10.1046/j.1365-313x.2003.01890.x;
RA Smith A.P., Nourizadeh S.D., Peer W.A., Xu J., Bandyopadhyay A.,
RA Murphy A.S., Goldsbrough P.B.;
RT "Arabidopsis AtGSTF2 is regulated by ethylene and auxin, and encodes a
RT glutathione S-transferase that interacts with flavonoids.";
RL Plant J. 36:433-442(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.
RX PubMed=15923336; DOI=10.1104/pp.104.056168;
RA Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L., Schnoor J.L.;
RT "Gene expression and microscopic analysis of Arabidopsis exposed to
RT chloroacetanilide herbicides and explosive compounds. A phytoremediation
RT approach.";
RL Plant Physiol. 138:858-869(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19174456; DOI=10.1093/jxb/ern365;
RA Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT "Enzyme activities and subcellular localization of members of the
RT Arabidopsis glutathione transferase superfamily.";
RL J. Exp. Bot. 60:1207-1218(2009).
RN [12]
RP FUNCTION.
RX PubMed=21631432; DOI=10.1042/bj20101884;
RA Dixon D.P., Sellars J.D., Edwards R.;
RT "The Arabidopsis phi class glutathione transferase AtGSTF2: binding and
RT regulation by biologically active heterocyclic ligands.";
RL Biochem. J. 438:63-70(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEXYLGLUTATHIONE.
RX PubMed=8551521; DOI=10.1006/jmbi.1996.0024;
RA Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Palme K.,
RA Schell J., Koelln I., Bartunik H.D., Bieseler B.;
RT "Three-dimensional structure of glutathione S-transferase from Arabidopsis
RT thaliana at 2.2-A resolution: structural characterization of herbicide-
RT conjugating plant glutathione S-transferases and a novel active site
RT architecture.";
RL J. Mol. Biol. 255:289-309(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
RX PubMed=9817846; DOI=10.1016/s0969-2126(98)00143-9;
RA Prade L., Huber R., Bieseler B.;
RT "Structures of herbicides in complex with their detoxifying enzyme
RT glutathione S-transferase -- explanations for the selectivity of the enzyme
RT in plants.";
RL Structure 6:1445-1452(1998).
CC -!- FUNCTION: Binds auxin, endogenous flavonoids and the phytoalexin
CC camalexin and may be involved in regulating the binding and transport
CC of small bioactive natural products and defense-related compounds
CC during plant stress. Binds a series of heterocyclic compounds,
CC including lumichrome, harmane, norharmane and indole-3-aldehyde. In
CC vitro, possesses glutathione S-transferase activity toward 1-chloro-
CC 2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as
CC glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-
CC hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or
CC IAA-CoA. {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:21631432}.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8551521,
CC ECO:0000269|PubMed:9817846}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19174456}.
CC Microsome {ECO:0000269|PubMed:19174456}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:19174456}. Note=Plasma membrane vesicles.
CC -!- TISSUE SPECIFICITY: Expressed in the root-shoot transition zone and
CC root tips. {ECO:0000269|PubMed:14617075}.
CC -!- INDUCTION: By ethylene, auxin, glutathione, salicylic acid, copper,
CC paraquat, acetochlor, metolachlor and the pathogens P.syringae and
CC Hyaloperonospora parasitica. {ECO:0000269|PubMed:12090627,
CC ECO:0000269|PubMed:12881503, ECO:0000269|PubMed:14617075,
CC ECO:0000269|PubMed:15069083, ECO:0000269|PubMed:15923336,
CC ECO:0000269|PubMed:8329687}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; X75303; CAA53051.1; -; mRNA.
DR EMBL; L07589; AAA32800.1; -; mRNA.
DR EMBL; L11601; AAA32801.1; -; mRNA.
DR EMBL; AC002330; AAC78264.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80745.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82183.1; -; Genomic_DNA.
DR EMBL; AF324681; AAG40032.1; -; mRNA.
DR EMBL; AF326903; AAG41485.1; -; mRNA.
DR EMBL; AF349527; AAK15574.1; -; mRNA.
DR EMBL; AY039580; AAK62635.1; -; mRNA.
DR EMBL; AY056082; AAL06970.1; -; mRNA.
DR PIR; S35268; S35268.
DR RefSeq; NP_192161.1; NM_116486.3.
DR PDB; 1BX9; X-ray; 2.60 A; A=2-212.
DR PDB; 1GNW; X-ray; 2.20 A; A/B=2-212.
DR PDB; 5A4U; X-ray; 2.00 A; A/B/C/D/E/F=1-212.
DR PDB; 5A4V; X-ray; 2.38 A; A/B/C/D/E/F=1-212.
DR PDB; 5A4W; X-ray; 2.25 A; A/B/C/D/E/F=1-212.
DR PDB; 5A5K; X-ray; 2.77 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-212.
DR PDBsum; 1BX9; -.
DR PDBsum; 1GNW; -.
DR PDBsum; 5A4U; -.
DR PDBsum; 5A4V; -.
DR PDBsum; 5A4W; -.
DR PDBsum; 5A5K; -.
DR AlphaFoldDB; P46422; -.
DR SMR; P46422; -.
DR BioGRID; 13222; 8.
DR IntAct; P46422; 1.
DR STRING; 3702.AT4G02520.1; -.
DR iPTMnet; P46422; -.
DR MetOSite; P46422; -.
DR SWISS-2DPAGE; P46422; -.
DR PaxDb; P46422; -.
DR PRIDE; P46422; -.
DR ProteomicsDB; 230161; -.
DR EnsemblPlants; AT4G02520.1; AT4G02520.1; AT4G02520.
DR GeneID; 827931; -.
DR Gramene; AT4G02520.1; AT4G02520.1; AT4G02520.
DR KEGG; ath:AT4G02520; -.
DR Araport; AT4G02520; -.
DR TAIR; locus:2132308; AT4G02520.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; P46422; -.
DR OMA; NARRVWV; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P46422; -.
DR BioCyc; ARA:AT4G02520-MON; -.
DR EvolutionaryTrace; P46422; -.
DR PRO; PR:P46422; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46422; baseline and differential.
DR Genevisible; P46422; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:2001147; F:camalexin binding; IDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:2001227; F:quercitrin binding; IDA:TAIR.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
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:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0002239; P:response to oomycetes; IEP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; 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 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Cytoplasm; Detoxification;
KW Direct protein sequencing; Endoplasmic reticulum; Microsome;
KW Oxidoreductase; Peroxidase; Plant defense; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..212
FT /note="Glutathione S-transferase F2"
FT /id="PRO_0000185848"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 93..212
FT /note="GST C-terminal"
FT BINDING 12..13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5A4U"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:5A4U"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:5A4U"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:5A4U"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5A4U"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 134..157
FT /evidence="ECO:0007829|PDB:5A4U"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5A4V"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:5A4U"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:5A4U"
SQ SEQUENCE 212 AA; 24129 MW; 90A1CBEEEBAC815B CRC64;
MAGIKVFGHP ASIATRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN PFGQVPAFED
GDLKLFESRA ITQYIAHRYE NQGTNLLQTD SKNISQYAIM AIGMQVEDHQ FDPVASKLAF
EQIFKSIYGL TTDEAVVAEE EAKLAKVLDV YEARLKEFKY LAGETFTLTD LHHIPAIQYL
LGTPTKKLFT ERPRVNEWVA EITKRPASEK VQ
