GSTT2_ARATH
ID GSTT2_ARATH Reviewed; 591 AA.
AC Q8L727; Q9FHD9; Q9FHE0; Q9ZRR6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutathione S-transferase T2;
DE Short=AtGSTT2;
DE EC=2.5.1.18;
DE AltName: Full=GST class-theta member 2;
DE AltName: Full=Glutathione S-transferase 10B;
GN Name=GSTT2; Synonyms=GST10B; OrderedLocusNames=At5g41240/At5g41230;
GN ORFNames=K1O13.3/K1O13.2;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 [MRNA] OF 1-245.
RC STRAIN=cv. Columbia;
RA Dixon D.P., Cole D.J., Edwards R.;
RT "Identification and cloning of AtGST 10, members of a novel type of plant
RT glutathione transferases.";
RL (er) Plant Gene Register PGR99-053(1999).
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 SUBCELLULAR LOCATION.
RX PubMed=19174456; DOI=10.1093/jxb/ern365;
RA Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT "Enzyme activities and subcellular localization of members of the
RT Arabidopsis glutathione transferase superfamily.";
RL J. Exp. Bot. 60:1207-1218(2009).
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: Peroxisome {ECO:0000269|PubMed:19174456}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11099.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g41230 and At5g41240.; Evidence={ECO:0000305};
CC Sequence=BAB11100.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g41230 and At5g41240.; Evidence={ECO:0000305};
CC Sequence=CAA10662.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB019225; BAB11099.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB019225; BAB11100.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94656.1; -; Genomic_DNA.
DR EMBL; AY139996; AAM98138.1; -; mRNA.
DR EMBL; BT008361; AAP37720.1; -; mRNA.
DR EMBL; AJ132398; CAA10662.1; ALT_SEQ; mRNA.
DR PIR; T52580; T52580.
DR RefSeq; NP_198940.3; NM_123489.4.
DR AlphaFoldDB; Q8L727; -.
DR SMR; Q8L727; -.
DR STRING; 3702.AT5G41240.1; -.
DR PaxDb; Q8L727; -.
DR PRIDE; Q8L727; -.
DR ProteomicsDB; 248518; -.
DR EnsemblPlants; AT5G41240.1; AT5G41240.1; AT5G41240.
DR GeneID; 834125; -.
DR Gramene; AT5G41240.1; AT5G41240.1; AT5G41240.
DR KEGG; ath:AT5G41240; -.
DR Araport; AT5G41240; -.
DR TAIR; locus:2155105; AT5G41240.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_462617_0_0_1; -.
DR InParanoid; Q8L727; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q8L727; -.
DR BioCyc; ARA:AT5G41240-MON; -.
DR PRO; PR:Q8L727; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L727; baseline and differential.
DR Genevisible; Q8L727; AT.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03183; GST_C_Theta; 1.
DR CDD; cd03050; GST_N_Theta; 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; IPR040077; GST_C_Theta.
DR InterPro; IPR040075; GST_N_Theta.
DR InterPro; IPR043377; GSTT1/2/3.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44750; PTHR44750; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 2: Evidence at transcript level;
KW Detoxification; Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..591
FT /note="Glutathione S-transferase T2"
FT /id="PRO_0000413575"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT DOMAIN 89..226
FT /note="GST C-terminal"
FT DOMAIN 265..338
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 229..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 40..41
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 CONFLICT 1
FT /note="M -> MM (in Ref. 4; CAA10662)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="R -> K (in Ref. 4; CAA10662)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="G -> S (in Ref. 4; CAA10662)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="I -> M (in Ref. 4; CAA10662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 67689 MW; D1F401C7FDA853D9 CRC64;
MKLKVYADRM SQPSRAVLIF CKVNEIQFDE ILISLGKRQQ LSPEFKEINP MGKVPAIVDG
RLKLFESHAI LIYLSSAYAS VVDHWYPNDL SKRAKIHSVL DWHHTNLRPG ASGYVLNSVL
APALGLPLNP KAAAEAENIL TNSLSTLETF WLKGSAKFLL GGKQPSIADL SLVCELMQLQ
VLDDKDRLRL LSPHKKVEQW IESTRKATMP HSDEVHEVLF RAKDRFQKQR EMATASKPGP
QSKIIQFSSI GGTSDGPNLV QDTTDRKARR RKWSPPDDVI LISAWLNTSK DRKVVVYDEQ
QAHTFWKRIG AHVSNSASLA NLPKREWNHC RQRWRKINDY VCKFVGCYDQ ALNQRASGQS
EDDVFQVAYQ LYYNNYMSNF KLEHAWRELR HNKKWCSTYT SENSKGGGSS KRTKLNGGGV
YSSSCNPESV PIALDGEEQV MDRPLGVKSS KQKEKKVATK TMLEEREADS RSRLENLWVL
DEEEQVMDLP LGVKSSKQKE RKVATKTMIE EREAANFRSR LGNLWLLKEK EEREADSRSR
LENLWALKEK DIEEQKKLTR MEVLKSLLGR RTGETSEKEE TLKNKLIDEM L
