ID   GSTL1_ARATH             Reviewed;         237 AA.
AC   Q6NLB0; B3H6S5; Q9LZ07;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Glutathione S-transferase L1;
DE            Short=AtGSTL1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-lambda member 1;
GN   Name=GSTL1; OrderedLocusNames=At5g02780; ORFNames=F9G14.90;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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 [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND INDUCTION.
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   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: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NLB0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NLB0-2; Sequence=VSP_041941;
CC   -!- INDUCTION: By glutathione, ascorbate and auxin.
CC       {ECO:0000269|PubMed:12077129}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Lambda family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB86032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL162973; CAB86032.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90516.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90517.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70174.1; -; Genomic_DNA.
DR   EMBL; BT010718; AAR20775.1; -; mRNA.
DR   EMBL; BT012424; AAS92340.1; -; mRNA.
DR   PIR; T48299; T48299.
DR   RefSeq; NP_001119157.1; NM_001125685.1. [Q6NLB0-2]
DR   RefSeq; NP_001318461.1; NM_001342670.1. [Q6NLB0-1]
DR   RefSeq; NP_195898.2; NM_120356.4. [Q6NLB0-1]
DR   AlphaFoldDB; Q6NLB0; -.
DR   SMR; Q6NLB0; -.
DR   BioGRID; 17076; 1.
DR   IntAct; Q6NLB0; 1.
DR   STRING; 3702.Q6NLB0; -.
DR   PaxDb; 3702-AT5G02780-1; -.
DR   ProteomicsDB; 247225; -. [Q6NLB0-1]
DR   EnsemblPlants; AT5G02780.1; AT5G02780.1; AT5G02780. [Q6NLB0-1]
DR   EnsemblPlants; AT5G02780.2; AT5G02780.2; AT5G02780. [Q6NLB0-2]
DR   EnsemblPlants; AT5G02780.3; AT5G02780.3; AT5G02780. [Q6NLB0-1]
DR   GeneID; 831800; -.
DR   Gramene; AT5G02780.1; AT5G02780.1; AT5G02780. [Q6NLB0-1]
DR   Gramene; AT5G02780.2; AT5G02780.2; AT5G02780. [Q6NLB0-2]
DR   Gramene; AT5G02780.3; AT5G02780.3; AT5G02780. [Q6NLB0-1]
DR   KEGG; ath:AT5G02780; -.
DR   Araport; AT5G02780; -.
DR   TAIR; AT5G02780; GSTL1.
DR   eggNOG; KOG0406; Eukaryota.
DR   InParanoid; Q6NLB0; -.
DR   OMA; DDKPTWY; -.
DR   OrthoDB; 5491187at2759; -.
DR   PRO; PR:Q6NLB0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6NLB0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:0010731; P:protein glutathionylation; IDA:TAIR.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd03203; GST_C_Lambda; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; GLUTATHIONE S-TRANSFERASE L1; 1.
DR   PANTHER; PTHR44328:SF6; GLUTATHIONE S-TRANSFERASE L1-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; Q6NLB0; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Detoxification; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..237
FT                   /note="Glutathione S-transferase L1"
FT                   /id="PRO_0000413577"
FT   DOMAIN          29..110
FT                   /note="GST N-terminal"
FT   DOMAIN          112..232
FT                   /note="GST C-terminal"
FT   BINDING         39..40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..82
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..95
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         150..151
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041941"
SQ   SEQUENCE   237 AA;  27167 MW;  ECF926492EB1F30A CRC64;
     MALSPPKIFV EDRQVPLDAT SDPPALFDGT TRLYISYTCP FAQRVWITRN LKGLQDEIKL
     VPIDLPNRPA WLKEKVNPAN KVPALEHNGK ITGESLDLIK YVDSNFDGPS LYPEDSAKRE
     FGEELLKYVD ETFVKTVFGS FKGDPVKETA SAFDHVENAL KKFDDGPFFL GELSLVDIAY
     IPFIERFQVF LDEVFKYEII IGRPNLAAWI EQMNKMVAYT QTKTDSEYVV NYFKRFM
//