GSTFC_ARATH
ID GSTFC_ARATH Reviewed; 214 AA.
AC Q9FE46; Q5DWV6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glutathione S-transferase F12 {ECO:0000303|PubMed:12090627};
DE Short=AtGSTF12 {ECO:0000303|PubMed:12090627};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE AltName: Full=GST class-phi member 12 {ECO:0000303|PubMed:12090627};
DE AltName: Full=Glutathione S-transferase 26 {ECO:0000303|PubMed:12090627};
DE AltName: Full=Protein TRANSPARENT TESTA 19 {ECO:0000303|PubMed:14675436};
GN Name=GSTF12 {ECO:0000303|PubMed:12090627};
GN Synonyms=GST26 {ECO:0000303|PubMed:12090627},
GN TT19 {ECO:0000303|PubMed:14675436};
GN OrderedLocusNames=At5g17220 {ECO:0000312|Araport:AT5G17220};
GN ORFNames=MKP11.22 {ECO:0000312|EMBL:BAB10509.1};
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14675436; DOI=10.1046/j.1365-313x.2003.01943.x;
RA Kitamura S., Shikazono N., Tanaka A.;
RT "TRANSPARENT TESTA 19 is involved in the accumulation of both anthocyanins
RT and proanthocyanidins in Arabidopsis.";
RL Plant J. 37:104-114(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 INDUCTION.
RX PubMed=20447269; DOI=10.1111/j.1364-3703.2009.00592.x;
RA Pantelides I.S., Tjamos S.E., Paplomatas E.J.;
RT "Ethylene perception via ETR1 is required in Arabidopsis infection by
RT Verticillium dahliae.";
RL Mol. Plant Pathol. 11:191-202(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20180920; DOI=10.1111/j.1365-313x.2010.04174.x;
RA Kitamura S., Matsuda F., Tohge T., Yonekura-Sakakibara K., Yamazaki M.,
RA Saito K., Narumi I.;
RT "Metabolic profiling and cytological analysis of proanthocyanidins in
RT immature seeds of Arabidopsis thaliana flavonoid accumulation mutants.";
RL Plant J. 62:549-559(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-205.
RX PubMed=21054438; DOI=10.1111/j.1365-3040.2010.02249.x;
RA Li X., Gao P., Cui D., Wu L., Parkin I., Saberianfar R., Menassa R.,
RA Pan H., Westcott N., Gruber M.Y.;
RT "The Arabidopsis tt19-4 mutant differentially accumulates proanthocyanidin
RT and anthocyanin through a 3' amino acid substitution in glutathione S-
RT transferase.";
RL Plant Cell Environ. 34:374-388(2011).
RN [8]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Involved in the transport and/or accumulation of both
CC anthocyanins and proanthocyanidins (PA)s in the vacuole. Functions in
CC the cytosol to maintain the regular accumulation in the vacuole of PA
CC precursors, such as epicatechin and glycosylated epicatechin.
CC {ECO:0000269|PubMed:14675436, ECO:0000269|PubMed:21054438}.
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:0000250|UniProtKB:O80852};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20180920}.
CC -!- INDUCTION: By the fungal pathogen Verticillium dahliae.
CC {ECO:0000269|PubMed:20447269}.
CC -!- DISRUPTION PHENOTYPE: Great reduction of anthocyanin pigments in the
CC vegetative parts and brown pigments in the seed coat. Accumulation of
CC unextractable proanthocyanidins. {ECO:0000269|PubMed:14675436,
CC ECO:0000269|PubMed:21054438}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; AF288189; AAG30138.1; -; mRNA.
DR EMBL; AB117793; BAD89984.1; -; Genomic_DNA.
DR EMBL; AB005238; BAB10509.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92398.1; -; Genomic_DNA.
DR RefSeq; NP_197224.1; NM_121728.4.
DR AlphaFoldDB; Q9FE46; -.
DR SMR; Q9FE46; -.
DR STRING; 3702.AT5G17220.1; -.
DR PaxDb; Q9FE46; -.
DR PRIDE; Q9FE46; -.
DR ProteomicsDB; 247258; -.
DR EnsemblPlants; AT5G17220.1; AT5G17220.1; AT5G17220.
DR GeneID; 831586; -.
DR Gramene; AT5G17220.1; AT5G17220.1; AT5G17220.
DR KEGG; ath:AT5G17220; -.
DR Araport; AT5G17220; -.
DR TAIR; locus:2167215; AT5G17220.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; Q9FE46; -.
DR OMA; NDSYAIC; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9FE46; -.
DR BioCyc; ARA:AT5G17220-MON; -.
DR PRO; PR:Q9FE46; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE46; baseline and differential.
DR Genevisible; Q9FE46; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0043169; F:cation binding; IDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:1900384; P:regulation of flavonol biosynthetic process; IMP: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; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..214
FT /note="Glutathione S-transferase F12"
FT /id="PRO_0000413545"
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 89..214
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 40..41
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT MUTAGEN 205
FT /note="W->L: In tt19-4; accumulation of unextractable
FT proanthocyanidins."
FT /evidence="ECO:0000269|PubMed:21054438"
FT CONFLICT 70
FT /note="I -> F (in Ref. 2; BAD89984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24581 MW; ACB25BD7CF65FB39 CRC64;
MVVKLYGQVT AACPQRVLLC FLEKGIEFEI IHIDLDTFEQ KKPEHLLRQP FGQVPAIEDG
DFKLFESRAI ARYYATKFAD QGTNLLGKSL EHRAIVDQWA DVETYYFNVL AQPLVINLII
KPRLGEKCDV VLVEDLKVKL GVVLDIYNNR LSSNRFLAGE EFTMADLTHM PAMGYLMSIT
DINQMVKARG SFNRWWEEIS DRPSWKKLMV LAGH
