ID GSTUK_ARATH Reviewed; 217 AA.
AC Q8L7C9; Q8LBS3; Q9M9F4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Glutathione S-transferase U20 {ECO:0000303|PubMed:12090627};
DE Short=AtGSTU20 {ECO:0000303|PubMed:12090627};
DE EC=2.5.1.18 {ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489};
DE AltName: Full=FIN219-interacting protein 1 {ECO:0000303|PubMed:17220357};
DE AltName: Full=GST class-tau member 20 {ECO:0000303|PubMed:12090627};
GN Name=GSTU20 {ECO:0000303|PubMed:12090627};
GN Synonyms=FIP1 {ECO:0000303|PubMed:17220357};
GN OrderedLocusNames=At1g78370 {ECO:0000312|Araport:AT1G78370};
GN ORFNames=F3F9.11 {ECO:0000312|EMBL:AAF71798.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16829588; DOI=10.1104/pp.106.079509;
RA Foley R.C., Sappl P.G., Perl-Treves R., Millar A.H., Singh K.B.;
RT "Desensitization of GSTF8 induction by a prior chemical treatment is long
RT lasting and operates in a tissue-dependent manner.";
RL Plant Physiol. 142:245-253(2006).
RN [7]
RP FUNCTION, INTERACTION WITH JAR1/FIN219, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=17220357; DOI=10.1104/pp.106.094185;
RA Chen I.-C., Huang I.-C., Liu M.-J., Wang Z.-G., Chung S.-S., Hsieh H.-L.;
RT "Glutathione S-transferase interacting with far-red insensitive 219 is
RT involved in phytochrome A-mediated signaling in Arabidopsis.";
RL Plant Physiol. 143:1189-1202(2007).
RN [8]
RP FUNCTION, AND INDUCTION BY GRAVITY.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=23281391; DOI=10.3732/ajb.1200339;
RA Schenck C.A., Nadella V., Clay S.L., Lindner J., Abrams Z., Wyatt S.E.;
RT "A proteomics approach identifies novel proteins involved in gravitropic
RT signal transduction.";
RL Am. J. Bot. 100:194-202(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH JAR1/FIN219 AND
RP GLUTATHIONE, FUNCTION, HOMODIMER, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=28223489; DOI=10.1073/pnas.1609980114;
RA Chen C.-Y., Ho S.-S., Kuo T.-Y., Hsieh H.-L., Cheng Y.-S.;
RT "Structural basis of jasmonate-amido synthetase FIN219 in complex with
RT glutathione S-transferase FIP1 during the JA signal regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1815-E1824(2017).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activities.
CC Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as
CC substrates. Involved in the regulation of far-red light influence on
CC development (PubMed:17220357). Regulator of the interplay between light
CC and JA signaling by increasing JAR1/FIN219 efficiency
CC (PubMed:28223489). Maybe involved in gravitropic signal transduction
CC (Probable). {ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489,
CC ECO:0000305|PubMed:23281391}.
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:17220357, ECO:0000269|PubMed:28223489};
CC -!- ACTIVITY REGULATION: Activated by JAR1/FIN219.
CC {ECO:0000269|PubMed:28223489}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.467 mM for glutathione {ECO:0000269|PubMed:17220357};
CC KM=1.794 mM for 1-chloro-2,4- dinitrobenzene
CC {ECO:0000269|PubMed:17220357};
CC -!- SUBUNIT: Homodimerization. Interacts with JAR1/FIN219 under continuous
CC far red (cFR) light to stimulate JAR1/FIN219 activity and substrate
CC selectivity. {ECO:0000269|PubMed:17220357,
CC ECO:0000269|PubMed:28223489}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17220357}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:17220357}.
CC -!- TISSUE SPECIFICITY: Mostly associated with vascular tissues, especially
CC near hydathodes. {ECO:0000269|PubMed:17220357}.
CC -!- DEVELOPMENTAL STAGE: Light-dependent expression. Developmentally
CC regulated. First observed in cotyledon vascular tissues of young
CC seedlings. Appears at the shoot apex, in the upper part of hypocotyls
CC and in roots in one week old seedlings. Later highly expressed in the
CC basal portion of trichomes, veins, shoot apex, and hypocotyls. Becomes
CC restricted to the margins of leaves and in roots. In drakness and blue
CC light (B) grown plants, localized in cotyledons vascular tissues. In
CC far-red (FR) and red (R) light conditions, mostly confined to regions
CC of vascular tissues near the hydathode of cotyledons. In adult plants,
CC expressed in vascular tissues of flower organs.
CC {ECO:0000269|PubMed:17220357}.
CC -!- INDUCTION: Induced by a gravistimulation.
CC {ECO:0000269|PubMed:23281391}.
CC -!- DISRUPTION PHENOTYPE: Hyposensitive hypocotyl phenotype under
CC continuous far red (cFR) light and a delayed flowering phenotype under
CC long-day conditions. {ECO:0000269|PubMed:17220357}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013430; AAF71798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36098.1; -; Genomic_DNA.
DR EMBL; AY136338; AAM97004.1; -; mRNA.
DR EMBL; BT000168; AAN15487.1; -; mRNA.
DR EMBL; AY087026; AAM64587.1; -; mRNA.
DR RefSeq; NP_177958.1; NM_106484.4.
DR PDB; 5ECH; X-ray; 2.14 A; B/C/E/F=1-217.
DR PDB; 5ECI; X-ray; 1.56 A; B/C/E/F=1-217.
DR PDB; 5ECK; X-ray; 1.54 A; B/C/E/F=1-217.
DR PDB; 5ECL; X-ray; 1.85 A; B/C/E/F=1-217.
DR PDB; 5ECM; X-ray; 1.60 A; B/C/E/F=1-217.
DR PDB; 5ECN; X-ray; 1.72 A; B/C/E/F=1-217.
DR PDB; 5ECO; X-ray; 1.80 A; B/C/E/F=1-217.
DR PDB; 5ECP; X-ray; 2.25 A; B/C/E/F=1-217.
DR PDB; 5ECQ; X-ray; 1.66 A; B/C/E/F=1-217.
DR PDB; 5ECR; X-ray; 1.72 A; B/C/E/F=1-217.
DR PDB; 5ECS; X-ray; 1.65 A; A/B=1-217.
DR PDBsum; 5ECH; -.
DR PDBsum; 5ECI; -.
DR PDBsum; 5ECK; -.
DR PDBsum; 5ECL; -.
DR PDBsum; 5ECM; -.
DR PDBsum; 5ECN; -.
DR PDBsum; 5ECO; -.
DR PDBsum; 5ECP; -.
DR PDBsum; 5ECQ; -.
DR PDBsum; 5ECR; -.
DR PDBsum; 5ECS; -.
DR AlphaFoldDB; Q8L7C9; -.
DR SMR; Q8L7C9; -.
DR BioGRID; 29392; 4.
DR STRING; 3702.Q8L7C9; -.
DR iPTMnet; Q8L7C9; -.
DR PaxDb; 3702-AT1G78370-1; -.
DR ProteomicsDB; 247262; -.
DR EnsemblPlants; AT1G78370.1; AT1G78370.1; AT1G78370.
DR GeneID; 844173; -.
DR Gramene; AT1G78370.1; AT1G78370.1; AT1G78370.
DR KEGG; ath:AT1G78370; -.
DR Araport; AT1G78370; -.
DR TAIR; AT1G78370; GSTU20.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_2_1; -.
DR InParanoid; Q8L7C9; -.
DR OMA; FESREED; -.
DR OrthoDB; 767442at2759; -.
DR PhylomeDB; Q8L7C9; -.
DR BioCyc; ARA:AT1G78370-MONOMER; -.
DR SABIO-RK; Q8L7C9; -.
DR PRO; PR:Q8L7C9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7C9; baseline and differential.
DR Genevisible; Q8L7C9; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:2000030; P:regulation of response to red or far red light; IMP:UniProtKB.
DR GO; GO:0009629; P:response to gravity; IEP:UniProtKB.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 1.
DR CDD; cd03058; GST_N_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260:SF601; GLUTATHIONE S-TRANSFERASE U20; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Detoxification; Growth regulation; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..217
FT /note="Glutathione S-transferase U20"
FT /id="PRO_0000403932"
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 88..208
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT BINDING 13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL,
FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP,
FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR,
FT ECO:0007744|PDB:5ECS"
FT BINDING 54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL,
FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP,
FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR,
FT ECO:0007744|PDB:5ECS"
FT BINDING 67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL,
FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP,
FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR,
FT ECO:0007744|PDB:5ECS"
FT CONFLICT 181
FT /note="K -> N (in Ref. 4; AAM64587)"
FT /evidence="ECO:0000305"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5ECS"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5ECR"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 119..139
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 193..198
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:5ECK"
SQ SEQUENCE 217 AA; 25006 MW; 5BD5DEB175079DA9 CRC64;
MANLPILLDY WPSMFGMRAR VALREKGVEF EYREEDFSNK SPLLLQSNPI HKKIPVLVHN
GKPVCESLNV VQYVDEAWPE KNPFFPSDPY GRAQARFWAD FVDKKFTDAQ FKVWGKKGEE
QEAGKKEFIE AVKILESELG DKPYFGGDSF GYVDISLITF SSWFQAYEKF GNFSIESESP
KLIAWAKRCM EKESVSKSLP DSEKIVAYAA EYRKNNL
//
