GSTFA_ARATH
ID GSTFA_ARATH Reviewed; 215 AA.
AC P42761;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Glutathione S-transferase F10 {ECO:0000303|PubMed:12090627};
DE Short=AtGSTF10 {ECO:0000303|PubMed:12090627};
DE EC=2.5.1.18 {ECO:0000269|PubMed:12090627};
DE AltName: Full=AtGSTF4 {ECO:0000303|PubMed:12090627};
DE AltName: Full=GST class-phi member 10 {ECO:0000303|PubMed:12090627};
DE AltName: Full=Protein EARLY RESPONSE TO DEHYDRATION 13 {ECO:0000303|PubMed:8253194};
GN Name=GSTF10 {ECO:0000303|PubMed:12090627};
GN Synonyms=ERD13 {ECO:0000303|PubMed:8253194},
GN GSTF4 {ECO:0000303|PubMed:12090627};
GN OrderedLocusNames=At2g30870 {ECO:0000312|Araport:AT2G30870};
GN ORFNames=F7F1.8 {ECO:0000312|EMBL:AAC20721.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=8253194; DOI=10.1016/0014-5793(93)80727-c;
RA Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible
RT genes that encode putative glutathione S-transferases in Arabidopsis
RT thaliana L.";
RL FEBS Lett. 335:189-192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-7.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [6]
RP INDUCTION.
RX PubMed=12207667; DOI=10.1034/j.1399-3054.2002.1160112.x;
RA Bianchi M.W., Roux C., Vartanian N.;
RT "Drought regulation of GST8, encoding the Arabidopsis homologue of
RT ParC/Nt107 glutathione transferase/peroxidase.";
RL Physiol. Plantarum 116:96-105(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [8]
RP TISSUE SPECIFICITY, INDUCTION BY GROWTH REGULATORS, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH BAK1.
RX PubMed=19118534; DOI=10.1016/j.bbrc.2008.11.156;
RA Ryu H.Y., Kim S.Y., Park H.M., You J.Y., Kim B.H., Lee J.S., Nam K.H.;
RT "Modulations of AtGSTF10 expression induce stress tolerance and BAK1-
RT mediated cell death.";
RL Biochem. Biophys. Res. Commun. 379:417-422(2009).
CC -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC).
CC May be involved in the conjugation of reduced glutathione to a wide
CC number of exogenous and endogenous hydrophobic electrophiles and have a
CC detoxification role against certain herbicides.
CC {ECO:0000269|PubMed:12090627}.
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 Evidence={ECO:0000269|PubMed:12090627};
CC -!- SUBUNIT: Interacts with BAK1. {ECO:0000269|PubMed:19118534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, floral buds, mature
CC flowers and leaves. {ECO:0000269|PubMed:19118534}.
CC -!- INDUCTION: By dehydration stress, wounding, H(2)O(2) and jasmonate, but
CC not by growth regulators. {ECO:0000269|PubMed:12207667,
CC ECO:0000269|PubMed:19118534}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, maybe due to the possible
CC redundancy with GSTF9. {ECO:0000269|PubMed:19118534}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; D17673; BAA04554.1; -; mRNA.
DR EMBL; AC004669; AAC20721.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08450.1; -; Genomic_DNA.
DR EMBL; AY128398; AAM91601.1; -; mRNA.
DR EMBL; BT000077; AAN15396.1; -; mRNA.
DR PIR; S39542; S39542.
DR RefSeq; NP_180644.1; NM_128639.4.
DR AlphaFoldDB; P42761; -.
DR SMR; P42761; -.
DR BioGRID; 2986; 1.
DR IntAct; P42761; 1.
DR STRING; 3702.AT2G30870.1; -.
DR iPTMnet; P42761; -.
DR SWISS-2DPAGE; P42761; -.
DR PaxDb; P42761; -.
DR PRIDE; P42761; -.
DR ProteomicsDB; 247136; -.
DR EnsemblPlants; AT2G30870.1; AT2G30870.1; AT2G30870.
DR GeneID; 817637; -.
DR Gramene; AT2G30870.1; AT2G30870.1; AT2G30870.
DR KEGG; ath:AT2G30870; -.
DR Araport; AT2G30870; -.
DR TAIR; locus:2052826; AT2G30870.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; P42761; -.
DR OMA; TRAVMMT; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P42761; -.
DR BioCyc; ARA:AT2G30870-MON; -.
DR PRO; PR:P42761; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P42761; baseline and differential.
DR Genevisible; P42761; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009414; P:response to water deprivation; 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; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Cytoplasm; Detoxification; Direct protein sequencing; Reference proteome;
KW Stress response; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9188482"
FT CHAIN 2..215
FT /note="Glutathione S-transferase F10"
FT /id="PRO_0000185847"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 88..215
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 11..12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 39..40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
SQ SEQUENCE 215 AA; 24230 MW; 9A53C0AD19580C79 CRC64;
MVLTIYAPLF ASSKRAVVTL VEKGVSFETV NVDLMKGEQR QPEYLAIQPF GKIPVLVDGD
YKIFESRAIM RYIAEKYRSQ GPDLLGKTIE ERGQVEQWLD VEATSYHPPL LALTLNIVFA
PLMGFPADEK VIKESEEKLA EVLDVYEAQL SKNEYLAGDF VSLADLAHLP FTEYLVGPIG
KAHLIKDRKH VSAWWDKISS RAAWKEVSAK YSLPV
