GSTUO_ARATH
ID GSTUO_ARATH Reviewed; 218 AA.
AC Q9SHH6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutathione S-transferase U24;
DE Short=AtGSTU24;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 24;
GN Name=GSTU24; OrderedLocusNames=At1g17170; ORFNames=F20D23.13;
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=17368510; DOI=10.1016/j.chemosphere.2007.02.003;
RA Yoon J.M., Oliver D.J., Shanks J.V.;
RT "Phytotoxicity and phytoremediation of 2,6-dinitrotoluene using a model
RT plant, Arabidopsis thaliana.";
RL Chemosphere 68:1050-1057(2007).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- INDUCTION: By acetochlor, metolachlor, 2,4,6-trinitrotoluene (TNT) and
CC 2,6-dinitrotoluene (2,6-DNT). {ECO:0000269|PubMed:15923336,
CC ECO:0000269|PubMed:17368510}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR EMBL; AC007651; AAD50016.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29554.1; -; Genomic_DNA.
DR EMBL; BT012184; AAS76278.1; -; mRNA.
DR PIR; G86307; G86307.
DR RefSeq; NP_173160.1; NM_101578.3.
DR AlphaFoldDB; Q9SHH6; -.
DR SMR; Q9SHH6; -.
DR BioGRID; 23528; 1.
DR STRING; 3702.AT1G17170.1; -.
DR PaxDb; Q9SHH6; -.
DR PRIDE; Q9SHH6; -.
DR ProteomicsDB; 247263; -.
DR EnsemblPlants; AT1G17170.1; AT1G17170.1; AT1G17170.
DR GeneID; 838288; -.
DR Gramene; AT1G17170.1; AT1G17170.1; AT1G17170.
DR KEGG; ath:AT1G17170; -.
DR Araport; AT1G17170; -.
DR TAIR; locus:2020322; AT1G17170.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_2_1; -.
DR InParanoid; Q9SHH6; -.
DR OMA; IETECPT; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9SHH6; -.
DR BioCyc; ARA:AT1G17170-MON; -.
DR BioCyc; MetaCyc:AT1G17170-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9SHH6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHH6; baseline and differential.
DR Genevisible; Q9SHH6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR GO; GO:0046256; P:2,4,6-trinitrotoluene catabolic process; IDA:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; PTHR11260; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Phosphoprotein; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase U24"
FT /id="PRO_0000413569"
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT DOMAIN 88..215
FT /note="GST C-terminal"
FT BINDING 13..14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
SQ SEQUENCE 218 AA; 25306 MW; AEC9508B1A776560 CRC64;
MADEVILLDF WASMFGMRTR IALAEKRVKY DHREEDLWNK SSLLLEMNPV HKKIPVLIHN
GKPVCESLIQ IEYIDETWPD NNPLLPSDPY KRAHAKFWAD FIDKKVNVTA RRIWAVKGEE
QEAAKELIEI LKTLESELGD KKYFGDETFG YVDIALIGFH SWFAVYEKFG NVSIESECSK
LVAWAKRCLE RESVAKALPE SEKVITFISE RRKKLGLE
