GSTUD_ARATH
ID GSTUD_ARATH Reviewed; 227 AA.
AC Q9FUS6; Q8LBX2; Q9LFX4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutathione S-transferase U13;
DE Short=AtGSTU13;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 13;
DE AltName: Full=Glutathione S-transferase 12;
GN Name=GSTU13; Synonyms=GST12; OrderedLocusNames=At1g27130;
GN ORFNames=T7N9.190;
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], FUNCTION, INDUCTION, GENE FAMILY, AND
RP 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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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.
CC -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC).
CC May be involved in the conjugation of reduced glutathione to a wide
CC number of exogenous and endogenous hydrophobic electrophiles and have a
CC detoxification role against certain herbicides.
CC {ECO:0000269|PubMed:12090627}.
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 Hyaloperonospora parasitica. Down-regulated by salicylic
CC acid, ethylene and methyl jasmonate. {ECO:0000269|PubMed:12090627}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79859.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g27130 has been split into 2 genes: At1g27130 and At1g27140.; Evidence={ECO:0000305};
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DR EMBL; AF288193; AAG30142.1; -; mRNA.
DR EMBL; AC000348; AAF79859.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30784.1; -; Genomic_DNA.
DR EMBL; AY044324; AAK73265.1; -; mRNA.
DR EMBL; AY050343; AAK91360.1; -; mRNA.
DR EMBL; AY094051; AAM16207.1; -; mRNA.
DR EMBL; AY086946; AAM64510.1; -; mRNA.
DR PIR; H86397; H86397.
DR RefSeq; NP_174033.1; NM_102475.3.
DR AlphaFoldDB; Q9FUS6; -.
DR SMR; Q9FUS6; -.
DR STRING; 3702.AT1G27130.1; -.
DR iPTMnet; Q9FUS6; -.
DR PaxDb; Q9FUS6; -.
DR PRIDE; Q9FUS6; -.
DR ProteomicsDB; 230166; -.
DR EnsemblPlants; AT1G27130.1; AT1G27130.1; AT1G27130.
DR GeneID; 839602; -.
DR Gramene; AT1G27130.1; AT1G27130.1; AT1G27130.
DR KEGG; ath:AT1G27130; -.
DR Araport; AT1G27130; -.
DR TAIR; locus:2205784; AT1G27130.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q9FUS6; -.
DR OMA; MECLAIL; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9FUS6; -.
DR BioCyc; ARA:AT1G27130-MON; -.
DR BioCyc; MetaCyc:AT1G27130-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9FUS6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FUS6; baseline and differential.
DR Genevisible; Q9FUS6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
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; 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; PF13417; GST_N_3; 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..227
FT /note="Glutathione S-transferase U13"
FT /id="PRO_0000413559"
FT DOMAIN 5..86
FT /note="GST N-terminal"
FT DOMAIN 92..224
FT /note="GST C-terminal"
FT BINDING 15..16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 57..58
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 70..71
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 4
FT /note="N -> K (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="S -> C (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> A (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="E -> D (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> T (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="Q -> L (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="R -> S (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="T -> S (in Ref. 5; AAM64510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25131 MW; 2D0EB66EF50A690E CRC64;
MAQNDTVKLI GSWSSPYSLR ARVALHLKSV KYEYLDEPDV LKEKSELLLK SNPIHKKVPV
LLHGDLSISE SLNVVQYVDE AWPSVPSILP SDAYDRASAR FWAQYIDDKC FAAVDAVVGA
KDDEGKMAAV GKLMECLAIL EETFQKSSKG LGFFGGETIG YLDIACSALL GPISVIEAFS
GVKFLRQETT PGLIKWAERF RAHEAVKPYM PTVEEVVAFA KQKFNVQ
