GSTL2_ARATH
ID GSTL2_ARATH Reviewed; 292 AA.
AC Q9M2W2; Q8GXL1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glutathione S-transferase L2, chloroplastic;
DE Short=AtGSTL2;
DE EC=2.5.1.18;
DE AltName: Full=GST class-lambda member 2;
DE Flags: Precursor;
GN Name=GSTL2; OrderedLocusNames=At3g55040; ORFNames=T15C9.60;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-292.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION.
RX PubMed=12077129; DOI=10.1074/jbc.m202919200;
RA Dixon D.P., Davis B.G., Edwards R.;
RT "Functional divergence in the glutathione transferase superfamily in
RT plants. Identification of two classes with putative functions in redox
RT homeostasis in Arabidopsis thaliana.";
RL J. Biol. Chem. 277:30859-30869(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).
RN [7]
RP FUNCTION.
RX PubMed=20841361; DOI=10.1074/jbc.m110.164806;
RA Dixon D.P., Edwards R.;
RT "Roles for stress-inducible lambda glutathione transferases in flavonoid
RT metabolism in plants as identified by ligand fishing.";
RL J. Biol. Chem. 285:36322-36329(2010).
CC -!- FUNCTION: Catalyzes the glutathione-dependent reduction of S-
CC glutathionylquercetin to quercetin. In vitro, possesses glutathione-
CC dependent thiol transferase activity toward 2-hydroxyethyl disulfide
CC (HED). {ECO:0000269|PubMed:12077129, ECO:0000269|PubMed:20841361}.
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:19174456}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Lambda family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42803.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL132970; CAB82699.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79331.1; -; Genomic_DNA.
DR EMBL; BT030006; ABN04744.1; -; mRNA.
DR EMBL; AK118180; BAC42803.1; ALT_INIT; mRNA.
DR PIR; T47643; T47643.
DR RefSeq; NP_191064.1; NM_115362.2.
DR AlphaFoldDB; Q9M2W2; -.
DR SMR; Q9M2W2; -.
DR STRING; 3702.AT3G55040.1; -.
DR PaxDb; Q9M2W2; -.
DR PRIDE; Q9M2W2; -.
DR ProteomicsDB; 247335; -.
DR EnsemblPlants; AT3G55040.1; AT3G55040.1; AT3G55040.
DR GeneID; 824670; -.
DR Gramene; AT3G55040.1; AT3G55040.1; AT3G55040.
DR KEGG; ath:AT3G55040; -.
DR Araport; AT3G55040; -.
DR TAIR; locus:2097233; AT3G55040.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_072699_0_0_1; -.
DR InParanoid; Q9M2W2; -.
DR OMA; EAYTETR; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9M2W2; -.
DR PRO; PR:Q9M2W2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2W2; baseline and differential.
DR Genevisible; Q9M2W2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0010731; P:protein glutathionylation; IDA:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR044629; GSTL1/2/3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44328; PTHR44328; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Chloroplast; Detoxification; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..292
FT /note="Glutathione S-transferase L2, chloroplastic"
FT /id="PRO_0000413578"
FT DOMAIN 79..160
FT /note="GST N-terminal"
FT DOMAIN 130..286
FT /note="GST C-terminal"
FT BINDING 89..90
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 117..118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 131..132
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 144..145
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33058 MW; 0EAFE884E843D39F CRC64;
MSVGLKVSAF LHPTLALSSR DVSLSSSSSS LYLDRKILRP GSGRRWCKSR RTEPILAVVE
SSRVPELDSS SEPVQVFDGS TRLYISYTCP FAQRAWIARN YKGLQNKIEL VPIDLKNRPA
WYKEKVYSAN KVPALEHNNR VLGESLDLIK YIDTNFEGPS LTPDGLEKQV VADELLSYTD
SFSKAVRSTL NGTDTNAADV AFDYIEQALS KFNEGPFFLG QFSLVDVAYA PFIERFRLIL
SDVMNVDITS GRPNLALWIQ EMNKIEAYTE TRQDPQELVE RYKRRVQAEA RL
