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   24-JAN-2024, entry version 150.
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}, TT19
GN   {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.Q9FE46; -.
DR   PaxDb; 3702-AT5G17220-1; -.
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; AT5G17220; GSTF12.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   InParanoid; Q9FE46; -.
DR   OMA; YLMSITD; -.
DR   OrthoDB; 639740at2759; -.
DR   PhylomeDB; Q9FE46; -.
DR   BioCyc; ARA:AT5G17220-MONOMER; -.
DR   PRO; PR:Q9FE46; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FE46; baseline and differential.
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:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IMP:TAIR.
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   CDD; cd03053; GST_N_Phi; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   PANTHER; PTHR43900:SF54; GLUTATHIONE S-TRANSFERASE F12; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; Q9FE46; AT.
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
//