Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9M2W2

- GSTL2_ARATH

UniProt

Q9M2W2 - GSTL2_ARATH

Protein

Glutathione S-transferase L2, chloroplastic

Gene

GSTL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

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

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein glutathionylation Source: TAIR
    2. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Detoxification

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase L2, chloroplastic (EC:2.5.1.18)
    Short name:
    AtGSTL2
    Alternative name(s):
    GST class-lambda member 2
    Gene namesi
    Name:GSTL2
    Ordered Locus Names:At3g55040
    ORF Names:T15C9.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G55040.

    Subcellular locationi

    Plastidchloroplast 1 Publication

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5656ChloroplastSequence AnalysisAdd
    BLAST
    Chaini57 – 292236Glutathione S-transferase L2, chloroplasticPRO_0000413578Add
    BLAST

    Proteomic databases

    PRIDEiQ9M2W2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9M2W2.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G55040.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M2W2.
    SMRiQ9M2W2. Positions 50-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini79 – 16082GST N-terminalAdd
    BLAST
    Domaini130 – 286157GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni89 – 902Glutathione bindingBy similarity
    Regioni117 – 1182Glutathione bindingBy similarity
    Regioni131 – 1322Glutathione bindingBy similarity
    Regioni144 – 1452Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Lambda family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000239968.
    InParanoidiQ9M2W2.
    KOiK00799.
    OMAiIEAYTET.
    PhylomeDBiQ9M2W2.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF13409. GST_N_2. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9M2W2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVGLKVSAF LHPTLALSSR DVSLSSSSSS LYLDRKILRP GSGRRWCKSR    50
    RTEPILAVVE SSRVPELDSS SEPVQVFDGS TRLYISYTCP FAQRAWIARN 100
    YKGLQNKIEL VPIDLKNRPA WYKEKVYSAN KVPALEHNNR VLGESLDLIK 150
    YIDTNFEGPS LTPDGLEKQV VADELLSYTD SFSKAVRSTL NGTDTNAADV 200
    AFDYIEQALS KFNEGPFFLG QFSLVDVAYA PFIERFRLIL SDVMNVDITS 250
    GRPNLALWIQ EMNKIEAYTE TRQDPQELVE RYKRRVQAEA RL 292
    Length:292
    Mass (Da):33,058
    Last modified:October 1, 2000 - v1
    Checksum:i0EAFE884E843D39F
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL132970 Genomic DNA. Translation: CAB82699.1.
    CP002686 Genomic DNA. Translation: AEE79331.1.
    BT030006 mRNA. Translation: ABN04744.1.
    AK118180 mRNA. Translation: BAC42803.1. Different initiation.
    PIRiT47643.
    RefSeqiNP_191064.1. NM_115362.2.
    UniGeneiAt.20918.
    At.48769.

    Genome annotation databases

    EnsemblPlantsiAT3G55040.1; AT3G55040.1; AT3G55040.
    GeneIDi824670.
    KEGGiath:AT3G55040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL132970 Genomic DNA. Translation: CAB82699.1 .
    CP002686 Genomic DNA. Translation: AEE79331.1 .
    BT030006 mRNA. Translation: ABN04744.1 .
    AK118180 mRNA. Translation: BAC42803.1 . Different initiation.
    PIRi T47643.
    RefSeqi NP_191064.1. NM_115362.2.
    UniGenei At.20918.
    At.48769.

    3D structure databases

    ProteinModelPortali Q9M2W2.
    SMRi Q9M2W2. Positions 50-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G55040.1-P.

    Proteomic databases

    PRIDEi Q9M2W2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G55040.1 ; AT3G55040.1 ; AT3G55040 .
    GeneIDi 824670.
    KEGGi ath:AT3G55040.

    Organism-specific databases

    TAIRi AT3G55040.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000239968.
    InParanoidi Q9M2W2.
    KOi K00799.
    OMAi IEAYTET.
    PhylomeDBi Q9M2W2.

    Gene expression databases

    Genevestigatori Q9M2W2.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF13409. GST_N_2. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiGSTL2_ARATH
    AccessioniPrimary (citable) accession number: Q9M2W2
    Secondary accession number(s): Q8GXL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3