Q9LZ06 (GSTL3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase L3
Short name=AtGSTL3
EC=2.5.1.18

Alternative name(s):
GST class-lambda member 3

Gene names

Name:	GSTL3
Ordered Locus Names:	At5g02790
ORF Names:	F9G14.100

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. Ref.5
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm › cytosol Probable.
Sequence similarities	Belongs to the GST superfamily. Lambda family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Detoxification
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to cadmium ion Inferred from expression pattern PubMed 16502469. Source: TAIR response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 235	235	Glutathione S-transferase L3		PRO_0000413579
Regions
	Domain	27 – 108	82	GST N-terminal
	Domain	86 – 230	145	GST C-terminal
	Region	37 – 38	2	Glutathione binding By similarity
	Region	65 – 66	2	Glutathione binding By similarity
	Region	79 – 80	2	Glutathione binding By similarity
	Region	92 – 93	2	Glutathione binding By similarity
Experimental info
	Sequence conflict	189	1	N → D in AAM61679. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9LZ06 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 52713E37176B2EB6	FASTA	235	27,090
	10 20 30 40 50 60 MAPSFIFVED RPAPLDATSD PPSLFDGTTR LYTSYVCPFA QRVWITRNFK GLQEKIKLVP 70 80 90 100 110 120 LDLGNRPAWY KEKVYPENKV PALEHNGKII GESLDLIKYL DNTFEGPSLY PEDHAKREFG 130 140 150 160 170 180 DELLKYTDTF VKTMYVSLKG DPSKETAPVL DYLENALYKF DDGPFFLGQL SLVDIAYIPF 190 200 210 220 230 IERFQTVLNE LFKCDITAER PKLSAWIEEI NKSDGYAQTK MDPKEIVEVF KKKFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Roles for stress-inducible lambda glutathione transferases in flavonoid metabolism in plants as identified by ligand fishing." Dixon D.P., Edwards R. J. Biol. Chem. 285:36322-36329(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL162973 Genomic DNA. Translation: CAB86033.1. CP002688 Genomic DNA. Translation: AED90518.1. AY140069 mRNA. Translation: AAM98210.1. BT002166 mRNA. Translation: AAN72177.1. AK227162 mRNA. Translation: BAE99204.1. AY085126 mRNA. Translation: AAM61679.1.
IPI	IPI00535440.
PIR	T48300.
RefSeq	NP_195899.1. NM_120357.5.
UniGene	At.33363.
3D structure databases
HSSP	HSSP built from PDB template 1OYJ based on UniProtKB O65032.
ProteinModelPortal	Q9LZ06.
SMR	Q9LZ06. Positions 38-228.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G02790.1-P.
Proteomic databases
PRIDE	Q9LZ06.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G02790.1; AT5G02790.1; AT5G02790.
GeneID	831798.
KEGG	ath:AT5G02790.
Organism-specific databases
TAIR	At5g02790.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000239968.
InParanoid	Q9LZ06.
KO	K00799.
OMA	IDITAPR.
PhylomeDB	Q9LZ06.
ProtClustDB	CLSN2687366.
Gene expression databases
ArrayExpress	Q9LZ06.
Genevestigator	Q9LZ06.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTL3_ARATH

Accession

Primary (citable) accession number: Q9LZ06
Secondary accession number(s): Q8LF01

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program