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Q05431

- APX1_ARATH

UniProt

Q05431 - APX1_ARATH

Protein

L-ascorbate peroxidase 1, cytosolic

Gene

APX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Plays a key role in hydrogen peroxide removal. Constitutes a central component of the reactive oxygen gene network.1 Publication

    Catalytic activityi

    2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O.

    Cofactori

    Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei38 – 381Transition state stabilizerPROSITE-ProRule annotation
    Active sitei42 – 421Proton acceptorPROSITE-ProRule annotation
    Metal bindingi163 – 1631Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi164 – 1641Potassium or calciumBy similarity
    Metal bindingi180 – 1801Potassium or calciumBy similarity
    Metal bindingi182 – 1821Potassium or calciumBy similarity
    Metal bindingi185 – 1851Potassium or calcium; via carbonyl oxygenBy similarity
    Metal bindingi187 – 1871Potassium or calciumBy similarity

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. L-ascorbate peroxidase activity Source: TAIR
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. embryo development ending in seed dormancy Source: TAIR
    2. hydrogen peroxide catabolic process Source: TAIR
    3. response to cadmium ion Source: TAIR
    4. response to heat Source: TAIR
    5. response to reactive oxygen species Source: TAIR
    6. response to salt stress Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding, Potassium

    Enzyme and pathway databases

    BioCyciARA:GQT-1075-MONOMER.
    ARA:GQT-1077-MONOMER.
    ARA:GQT-2090-MONOMER.
    ARA:GQT-2091-MONOMER.
    ARA:GQT-2092-MONOMER.
    ARA:GQT-2093-MONOMER.
    ARA:GQT-2094-MONOMER.

    Protein family/group databases

    PeroxiBasei1890. AtAPx01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-ascorbate peroxidase 1, cytosolic (EC:1.11.1.11)
    Short name:
    AP
    Short name:
    AtAPx01
    Gene namesi
    Name:APX1
    Ordered Locus Names:At1g07890
    ORF Names:F24B9.2
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G07890.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. cytosol Source: TAIR
    5. Golgi apparatus Source: TAIR
    6. plasma membrane Source: TAIR
    7. plasmodesma Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 250249L-ascorbate peroxidase 1, cytosolicPRO_0000055592Add
    BLAST

    Proteomic databases

    PaxDbiQ05431.
    PRIDEiQ05431.

    2D gel databases

    SWISS-2DPAGEQ05431.

    Expressioni

    Tissue specificityi

    Predominantly expressed in flowers.1 Publication

    Inductioni

    By ethylene, ozone, sulfur dioxide, Fe exposure, oxidative and heat-shock stresses, and by excess light treatment.4 Publications

    Gene expression databases

    ArrayExpressiQ05431.
    GenevestigatoriQ05431.

    Interactioni

    Protein-protein interaction databases

    BioGridi22545. 3 interactions.
    IntActiQ05431. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05431.
    SMRiQ05431. Positions 3-250.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0376.
    HOGENOMiHOG000189824.
    InParanoidiQ05431.
    KOiK00434.
    OMAiPTVSEDY.
    PhylomeDBiQ05431.

    Family and domain databases

    InterProiIPR002207. Asc_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00459. ASPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q05431-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ    50
    SRTGGPFGTM RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA 100
    GVVAVEVTGG PDIPFHPGRE DKPQPPPEGR LPDATKGCDH LRDVFAKQMG 150
    LSDKDIVALS GAHTLGRCHK DRSGFEGAWT SNPLIFDNSY FKELLSGEKE 200
    GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM KLSELGFADA 250
    Length:250
    Mass (Da):27,561
    Last modified:January 23, 2007 - v2
    Checksum:i33A536D85B2CAA6C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59600 mRNA. Translation: CAA42168.1.
    D14442 Genomic DNA. Translation: BAA03334.1.
    U63815 Genomic DNA. Translation: AAB07880.1.
    AC007583 Genomic DNA. Translation: AAF75066.1.
    CP002684 Genomic DNA. Translation: AEE28200.1.
    CP002684 Genomic DNA. Translation: AEE28201.1.
    CP002684 Genomic DNA. Translation: AEE28202.1.
    CP002684 Genomic DNA. Translation: AEE28203.1.
    CP002684 Genomic DNA. Translation: AEE28204.1.
    CP002684 Genomic DNA. Translation: AEE28206.1.
    CP002684 Genomic DNA. Translation: AEE28207.1.
    AY039879 mRNA. Translation: AAK63983.1.
    AY056395 mRNA. Translation: AAL08251.1.
    AY094002 mRNA. Translation: AAM16263.1.
    AK230096 mRNA. Translation: BAF01915.1.
    AY086425 mRNA. Translation: AAM63427.1.
    PIRiD86214.
    S20866.
    RefSeqiNP_001030991.2. NM_001035914.2. [Q05431-1]
    NP_001030992.2. NM_001035915.2. [Q05431-1]
    NP_001077482.1. NM_001084013.1. [Q05431-1]
    NP_001117244.1. NM_001123772.1. [Q05431-1]
    NP_172267.1. NM_100663.3. [Q05431-1]
    NP_849607.1. NM_179276.2. [Q05431-1]
    NP_973786.1. NM_202057.2. [Q05431-1]
    UniGeneiAt.47584.
    At.67008.

    Genome annotation databases

    EnsemblPlantsiAT1G07890.1; AT1G07890.1; AT1G07890. [Q05431-1]
    AT1G07890.2; AT1G07890.2; AT1G07890. [Q05431-1]
    AT1G07890.3; AT1G07890.3; AT1G07890. [Q05431-1]
    AT1G07890.4; AT1G07890.4; AT1G07890. [Q05431-1]
    AT1G07890.5; AT1G07890.5; AT1G07890. [Q05431-1]
    AT1G07890.7; AT1G07890.7; AT1G07890. [Q05431-1]
    AT1G07890.8; AT1G07890.8; AT1G07890. [Q05431-1]
    GeneIDi837304.
    KEGGiath:AT1G07890.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59600 mRNA. Translation: CAA42168.1 .
    D14442 Genomic DNA. Translation: BAA03334.1 .
    U63815 Genomic DNA. Translation: AAB07880.1 .
    AC007583 Genomic DNA. Translation: AAF75066.1 .
    CP002684 Genomic DNA. Translation: AEE28200.1 .
    CP002684 Genomic DNA. Translation: AEE28201.1 .
    CP002684 Genomic DNA. Translation: AEE28202.1 .
    CP002684 Genomic DNA. Translation: AEE28203.1 .
    CP002684 Genomic DNA. Translation: AEE28204.1 .
    CP002684 Genomic DNA. Translation: AEE28206.1 .
    CP002684 Genomic DNA. Translation: AEE28207.1 .
    AY039879 mRNA. Translation: AAK63983.1 .
    AY056395 mRNA. Translation: AAL08251.1 .
    AY094002 mRNA. Translation: AAM16263.1 .
    AK230096 mRNA. Translation: BAF01915.1 .
    AY086425 mRNA. Translation: AAM63427.1 .
    PIRi D86214.
    S20866.
    RefSeqi NP_001030991.2. NM_001035914.2. [Q05431-1 ]
    NP_001030992.2. NM_001035915.2. [Q05431-1 ]
    NP_001077482.1. NM_001084013.1. [Q05431-1 ]
    NP_001117244.1. NM_001123772.1. [Q05431-1 ]
    NP_172267.1. NM_100663.3. [Q05431-1 ]
    NP_849607.1. NM_179276.2. [Q05431-1 ]
    NP_973786.1. NM_202057.2. [Q05431-1 ]
    UniGenei At.47584.
    At.67008.

    3D structure databases

    ProteinModelPortali Q05431.
    SMRi Q05431. Positions 3-250.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 22545. 3 interactions.
    IntActi Q05431. 4 interactions.

    Protein family/group databases

    PeroxiBasei 1890. AtAPx01.

    2D gel databases

    SWISS-2DPAGE Q05431.

    Proteomic databases

    PaxDbi Q05431.
    PRIDEi Q05431.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G07890.1 ; AT1G07890.1 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.2 ; AT1G07890.2 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.3 ; AT1G07890.3 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.4 ; AT1G07890.4 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.5 ; AT1G07890.5 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.7 ; AT1G07890.7 ; AT1G07890 . [Q05431-1 ]
    AT1G07890.8 ; AT1G07890.8 ; AT1G07890 . [Q05431-1 ]
    GeneIDi 837304.
    KEGGi ath:AT1G07890.

    Organism-specific databases

    GeneFarmi 1942. 146.
    TAIRi AT1G07890.

    Phylogenomic databases

    eggNOGi COG0376.
    HOGENOMi HOG000189824.
    InParanoidi Q05431.
    KOi K00434.
    OMAi PTVSEDY.
    PhylomeDBi Q05431.

    Enzyme and pathway databases

    BioCyci ARA:GQT-1075-MONOMER.
    ARA:GQT-1077-MONOMER.
    ARA:GQT-2090-MONOMER.
    ARA:GQT-2091-MONOMER.
    ARA:GQT-2092-MONOMER.
    ARA:GQT-2093-MONOMER.
    ARA:GQT-2094-MONOMER.

    Gene expression databases

    ArrayExpressi Q05431.
    Genevestigatori Q05431.

    Family and domain databases

    InterProi IPR002207. Asc_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view ]
    Pfami PF00141. peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00459. ASPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a cDNA encoding ascorbate peroxidase from Arabidopsis thaliana."
      Kubo A., Saji H., Tanaka K., Tanaka K., Kondo N.
      Plant Mol. Biol. 18:691-701(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17.
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Genomic DNA structure of a gene encoding cytosolic ascorbate peroxidase from Arabidopsis thaliana."
      Kubo A., Saji H., Tanaka K., Kondo N.
      FEBS Lett. 315:313-317(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    3. Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    4. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "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.
    7. "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.
    8. "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].
    9. "Expression of Arabidopsis cytosolic ascorbate peroxidase gene in response to ozone or sulfur dioxide."
      Kubo A., Saji H., Tanaka K., Kondo N.
      Plant Mol. Biol. 29:479-489(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress."
      Karpinski S., Escobar C., Karpinski B., Creissen G.P., Mullineaux P.M.
      Plant Cell 9:627-640(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "The heat-shock element is a functional component of the Arabidopsis APX1 gene promoter."
      Storozhenko S., De Pauw P., Van Montagu M., Inze D., Kushnir S.
      Plant Physiol. 118:1005-1014(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    12. "Iron-regulated expression of a cytosolic ascorbate peroxidase encoded by the APX1 gene in Arabidopsis seedlings."
      Fourcroy P., Vansuyt G., Kushnir S., Inze D., Briat J.-F.
      Plant Physiol. 134:605-613(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis."
      Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J., Shulaev V., Schlauch K., Mittler R.
      Plant Cell 17:268-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiAPX1_ARATH
    AccessioniPrimary (citable) accession number: Q05431
    Secondary accession number(s): Q0WLU2, Q2V4P8, Q2V4P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds one cation per subunit; probably K+, but might also be Ca2+.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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