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Q9LYB4

- GPX5_ARATH

UniProt

Q9LYB4 - GPX5_ARATH

Protein

Probable glutathione peroxidase 5

Gene

GPX5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May constitute a glutathione peroxidase-like protective system against oxidative stresses.By similarity

    Catalytic activityi

    2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461By similarity

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. embryo development ending in seed dormancy Source: TAIR
    2. response to oxidative stress Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciARA:AT3G63080-MONOMER.

    Protein family/group databases

    PeroxiBasei2475. AtGPx05.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glutathione peroxidase 5 (EC:1.11.1.9)
    Gene namesi
    Name:GPX5
    Ordered Locus Names:At3g63080
    ORF Names:T20O10_180
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G63080.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: TAIR
    2. plasma membrane Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 173172Probable glutathione peroxidase 5PRO_0000066639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    PaxDbiQ9LYB4.
    PRIDEiQ9LYB4.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    By salt stress, osmotic stress and metals. Down-regulated by abscisic acid (ABA).1 Publication

    Gene expression databases

    GenevestigatoriQ9LYB4.

    Interactioni

    Protein-protein interaction databases

    BioGridi10797. 1 interaction.
    IntActiQ9LYB4. 1 interaction.
    STRINGi3702.AT3G63080.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LYB4.
    SMRiQ9LYB4. Positions 12-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG0386.
    HOGENOMiHOG000277054.
    InParanoidiQ9LYB4.
    KOiK00432.
    OMAiCGFTESN.
    PhylomeDBiQ9LYB4.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR11592. PTHR11592. 1 hit.
    PfamiPF00255. GSHPx. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
    PRINTSiPR01011. GLUTPROXDASE.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9LYB4-1 [UniParc]FASTAAdd to Basket

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    MGASSSSSVS EKSIHQFTVK DSSGKEVDLS VYQGKVLLVV NVASKCGFTE    50
    SNYTQLTELY RKYKDQGFVV LAFPCNQFLS QEPGTSEEAH QFACTRFKAE 100
    YPVFQKVRVN GQNAAPVYKF LKSKKPSFLG SRIKWNFTKF LVGKDGQVID 150
    RYGTTVSPLS IQKDIEKALA QEL 173
    Length:173
    Mass (Da):19,327
    Last modified:October 1, 2000 - v1
    Checksum:iCE3F15979C150C65
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL163816 Genomic DNA. Translation: CAB87753.1.
    CP002686 Genomic DNA. Translation: AEE80432.1.
    BT003821 mRNA. Translation: AAO41874.1.
    BT005137 mRNA. Translation: AAO50670.1.
    AY085116 mRNA. Translation: AAM61670.1.
    PIRiT48097.
    RefSeqiNP_191867.1. NM_116173.3.
    UniGeneiAt.34000.
    At.43439.

    Genome annotation databases

    EnsemblPlantsiAT3G63080.1; AT3G63080.1; AT3G63080.
    GeneIDi825483.
    KEGGiath:AT3G63080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL163816 Genomic DNA. Translation: CAB87753.1 .
    CP002686 Genomic DNA. Translation: AEE80432.1 .
    BT003821 mRNA. Translation: AAO41874.1 .
    BT005137 mRNA. Translation: AAO50670.1 .
    AY085116 mRNA. Translation: AAM61670.1 .
    PIRi T48097.
    RefSeqi NP_191867.1. NM_116173.3.
    UniGenei At.34000.
    At.43439.

    3D structure databases

    ProteinModelPortali Q9LYB4.
    SMRi Q9LYB4. Positions 12-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10797. 1 interaction.
    IntActi Q9LYB4. 1 interaction.
    STRINGi 3702.AT3G63080.1-P.

    Protein family/group databases

    PeroxiBasei 2475. AtGPx05.

    Proteomic databases

    PaxDbi Q9LYB4.
    PRIDEi Q9LYB4.

    Protocols and materials databases

    DNASUi 825483.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G63080.1 ; AT3G63080.1 ; AT3G63080 .
    GeneIDi 825483.
    KEGGi ath:AT3G63080.

    Organism-specific databases

    GeneFarmi 2054. 163.
    TAIRi AT3G63080.

    Phylogenomic databases

    eggNOGi COG0386.
    HOGENOMi HOG000277054.
    InParanoidi Q9LYB4.
    KOi K00432.
    OMAi CGFTESN.
    PhylomeDBi Q9LYB4.

    Enzyme and pathway databases

    BioCyci ARA:AT3G63080-MONOMER.

    Miscellaneous databases

    PROi Q9LYB4.

    Gene expression databases

    Genevestigatori Q9LYB4.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    PANTHERi PTHR11592. PTHR11592. 1 hit.
    Pfami PF00255. GSHPx. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
    PRINTSi PR01011. GLUTPROXDASE.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      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. "Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways."
      Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.
      Plant J. 36:602-615(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, INDUCTION.
    6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGPX5_ARATH
    AccessioniPrimary (citable) accession number: Q9LYB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 97 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