GSTL1_ARATH
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 03-AUG-2022, entry version 137.
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.AT5G02780.1; -.
DR PaxDb; Q6NLB0; -.
DR PRIDE; Q6NLB0; -.
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; locus:2151286; AT5G02780.
DR eggNOG; KOG0406; Eukaryota.
DR InParanoid; Q6NLB0; -.
DR OMA; MVACTET; -.
DR OrthoDB; 1225872at2759; -.
DR PRO; PR:Q6NLB0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NLB0; baseline and differential.
DR Genevisible; Q6NLB0; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 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
