GSTL3_ARATH
ID GSTL3_ARATH Reviewed; 235 AA.
AC Q9LZ06; Q8LF01;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutathione S-transferase L3;
DE Short=AtGSTL3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-lambda member 3;
GN Name=GSTL3; OrderedLocusNames=At5g02790; ORFNames=F9G14.100;
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [5]
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. {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 -!- SIMILARITY: Belongs to the GST superfamily. Lambda family.
CC {ECO:0000305}.
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DR EMBL; AL162973; CAB86033.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90518.1; -; Genomic_DNA.
DR EMBL; AY140069; AAM98210.1; -; mRNA.
DR EMBL; BT002166; AAN72177.1; -; mRNA.
DR EMBL; AK227162; BAE99204.1; -; mRNA.
DR EMBL; AY085126; AAM61679.1; -; mRNA.
DR PIR; T48300; T48300.
DR RefSeq; NP_195899.1; NM_120357.6.
DR AlphaFoldDB; Q9LZ06; -.
DR SMR; Q9LZ06; -.
DR STRING; 3702.AT5G02790.1; -.
DR PaxDb; Q9LZ06; -.
DR PRIDE; Q9LZ06; -.
DR ProteomicsDB; 247192; -.
DR EnsemblPlants; AT5G02790.1; AT5G02790.1; AT5G02790.
DR GeneID; 831798; -.
DR Gramene; AT5G02790.1; AT5G02790.1; AT5G02790.
DR KEGG; ath:AT5G02790; -.
DR Araport; AT5G02790; -.
DR TAIR; locus:2151326; AT5G02790.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_072699_0_1_1; -.
DR InParanoid; Q9LZ06; -.
DR OMA; MQRQPEI; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9LZ06; -.
DR PRO; PR:Q9LZ06; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZ06; baseline and differential.
DR Genevisible; Q9LZ06; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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 Cytoplasm; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..235
FT /note="Glutathione S-transferase L3"
FT /id="PRO_0000413579"
FT DOMAIN 27..108
FT /note="GST N-terminal"
FT DOMAIN 86..230
FT /note="GST C-terminal"
FT BINDING 37..38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 79..80
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 189
FT /note="N -> D (in Ref. 4; AAM61679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 27090 MW; 52713E37176B2EB6 CRC64;
MAPSFIFVED RPAPLDATSD PPSLFDGTTR LYTSYVCPFA QRVWITRNFK GLQEKIKLVP
LDLGNRPAWY KEKVYPENKV PALEHNGKII GESLDLIKYL DNTFEGPSLY PEDHAKREFG
DELLKYTDTF VKTMYVSLKG DPSKETAPVL DYLENALYKF DDGPFFLGQL SLVDIAYIPF
IERFQTVLNE LFKCDITAER PKLSAWIEEI NKSDGYAQTK MDPKEIVEVF KKKFM
