GSTUF_ARATH
ID GSTUF_ARATH Reviewed; 233 AA.
AC Q9LQ48; A0MED4; Q8LF83;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Glutathione S-transferase U15;
DE Short=AtGSTU15;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 15;
GN Name=GSTU15; OrderedLocusNames=At1g59670; ORFNames=T30E16.25;
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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).
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 -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28444.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009317; AAF79758.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33601.1; -; Genomic_DNA.
DR EMBL; DQ446376; ABE65725.1; -; mRNA.
DR EMBL; DQ652904; ABK28444.1; ALT_SEQ; mRNA.
DR EMBL; AY084992; AAM61551.1; -; mRNA.
DR PIR; D96620; D96620.
DR RefSeq; NP_176176.1; NM_104660.2.
DR AlphaFoldDB; Q9LQ48; -.
DR SMR; Q9LQ48; -.
DR BioGRID; 27482; 1.
DR STRING; 3702.AT1G59670.1; -.
DR PaxDb; Q9LQ48; -.
DR PRIDE; Q9LQ48; -.
DR ProteomicsDB; 247261; -.
DR EnsemblPlants; AT1G59670.1; AT1G59670.1; AT1G59670.
DR GeneID; 842257; -.
DR Gramene; AT1G59670.1; AT1G59670.1; AT1G59670.
DR KEGG; ath:AT1G59670; -.
DR Araport; AT1G59670; -.
DR TAIR; locus:2202897; AT1G59670.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q9LQ48; -.
DR OMA; WFKVFEK; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9LQ48; -.
DR BioCyc; ARA:AT1G59670-MON; -.
DR PRO; PR:Q9LQ48; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ48; baseline and differential.
DR Genevisible; Q9LQ48; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
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; PF00043; GST_C; 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; 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; Transferase.
FT CHAIN 1..233
FT /note="Glutathione S-transferase U15"
FT /id="PRO_0000413561"
FT DOMAIN 5..85
FT /note="GST N-terminal"
FT DOMAIN 92..219
FT /note="GST C-terminal"
FT BINDING 15..16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 56..57
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
FT CONFLICT 6
FT /note="E -> Q (in Ref. 4; AAM61551)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="A -> D (in Ref. 4; AAM61551)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="D -> N (in Ref. 4; AAM61551)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="IF -> VY (in Ref. 4; AAM61551)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> D (in Ref. 4; AAM61551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26535 MW; 8722CA2CE7AEC09D CRC64;
MGEREEVKLL GTWYSPVVIR AKIALRLKSV DYDYVEEDLF GSKSELLLKS NPIFKKVPVL
IHNTKPVCVS LNIVEYIDET WNSSGSSILP SHPYDRALAR FWSVFVDDKW LPTLMAAVVA
KSEEAKAKGM EEVEEGLLQL EAAFIALSKG KSFFGGETIG FIDICLGSFL VLLKAREKLK
NEKILDELKT PSLYRWANQF LSNEMVKNVV PDIDKVAKFI EEFEDRAQYI RCF
