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Q9M2W2 (GSTL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase L2, chloroplastic
Short name=AtGSTL2
EC=2.5.1.18
Alternative name(s):
GST class-lambda member 2
Gene names
Name:GSTL2
Ordered Locus Names:At3g55040
ORF Names:T15C9.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. In vitro, possesses glutathione-dependent thiol transferase activity toward 2-hydroxyethyl disulfide (HED). Ref.5 Ref.7

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subcellular location

Plastid › chloroplast Ref.6.

Sequence similarities

Belongs to the GST superfamily. Lambda family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence BAC42803.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDetoxification
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein glutathionylation

Inferred from direct assay Ref.5. Source: TAIR

response to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 292236Glutathione S-transferase L2, chloroplastic
PRO_0000413578

Regions

Domain79 – 16082GST N-terminal
Domain130 – 286157GST C-terminal
Region89 – 902Glutathione binding By similarity
Region117 – 1182Glutathione binding By similarity
Region131 – 1322Glutathione binding By similarity
Region144 – 1452Glutathione binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M2W2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0EAFE884E843D39F

FASTA29233,058
        10         20         30         40         50         60 
MSVGLKVSAF LHPTLALSSR DVSLSSSSSS LYLDRKILRP GSGRRWCKSR RTEPILAVVE 

        70         80         90        100        110        120 
SSRVPELDSS SEPVQVFDGS TRLYISYTCP FAQRAWIARN YKGLQNKIEL VPIDLKNRPA 

       130        140        150        160        170        180 
WYKEKVYSAN KVPALEHNNR VLGESLDLIK YIDTNFEGPS LTPDGLEKQV VADELLSYTD 

       190        200        210        220        230        240 
SFSKAVRSTL NGTDTNAADV AFDYIEQALS KFNEGPFFLG QFSLVDVAYA PFIERFRLIL 

       250        260        270        280        290 
SDVMNVDITS GRPNLALWIQ EMNKIEAYTE TRQDPQELVE RYKRRVQAEA RL

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(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]"Arabidopsis ORF clones."
Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-292.
Strain: cv. Columbia.
[5]"Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana."
Dixon D.P., Davis B.G., Edwards R.
J. Biol. Chem. 277:30859-30869(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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		AL132970 Genomic DNA. Translation: CAB82699.1.
CP002686 Genomic DNA. Translation: AEE79331.1.
BT030006 mRNA. Translation: ABN04744.1.
AK118180 mRNA. Translation: BAC42803.1. Different initiation.
IPIIPI00536395.
PIRT47643.
RefSeqNP_191064.1. NM_115362.2.
UniGeneAt.20918.
At.48769.

3D structure databases

ProteinModelPortalQ9M2W2.
SMRQ9M2W2. Positions 50-288.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT3G55040.1-P.

Proteomic databases

PRIDEQ9M2W2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55040.1; AT3G55040.1; AT3G55040.
GeneID824670.
KEGGath:AT3G55040.

Organism-specific databases

TAIRAt3g55040.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000239968.
InParanoidQ9M2W2.
KOK00799.
OMAWITRNCK.
PhylomeDBQ9M2W2.
ProtClustDBCLSN2915762.

Gene expression databases

ArrayExpressQ9M2W2.
GenevestigatorQ9M2W2.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTL2_ARATH
AccessionPrimary (citable) accession number: Q9M2W2
Secondary accession number(s): Q8GXL1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 1, 2000
Last modified: May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents