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Q05431 (APX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

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

Names and origin

Protein namesRecommended name:
L-ascorbate peroxidase 1, cytosolic

Short name=AP
Short name=AtAPx01
EC=1.11.1.11
Gene names
Name:APX1
Ordered Locus Names:At1g07890
ORF Names:F24B9.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in hydrogen peroxide removal. Constitutes a central component of the reactive oxygen gene network. Ref.13

Catalytic activity

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

Cofactor

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

Subcellular location

Cytoplasm.

Tissue specificity

Predominantly expressed in flowers. Ref.11

Induction

By ethylene, ozone, sulfur dioxide, Fe exposure, oxidative and heat-shock stresses, and by excess light treatment. Ref.9 Ref.10 Ref.11 Ref.12

Miscellaneous

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

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandCalcium
Heme
Iron
Metal-binding
Potassium
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processembryo development ending in seed dormancy

Inferred from mutant phenotype PubMed 15634699. Source: TAIR

hydrogen peroxide catabolic process

Inferred from mutant phenotype Ref.13. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to heat

Inferred from expression pattern Ref.11. Source: TAIR

response to reactive oxygen species

Inferred from mutant phenotype Ref.13. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 22430844. Source: TAIR

cell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

   Molecular_functionL-ascorbate peroxidase activity

Inferred from mutant phenotype Ref.13. Source: TAIR

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q05431-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 250249L-ascorbate peroxidase 1, cytosolic
PRO_0000055592

Sites

Active site421Proton acceptor By similarity
Metal binding1631Iron (heme axial ligand) By similarity
Metal binding1641Potassium or calcium By similarity
Metal binding1801Potassium or calcium By similarity
Metal binding1821Potassium or calcium By similarity
Metal binding1851Potassium or calcium; via carbonyl oxygen By similarity
Metal binding1871Potassium or calcium By similarity
Site381Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 33A536D85B2CAA6C

FASTA25027,561
        10         20         30         40         50         60 
MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ SRTGGPFGTM 

        70         80         90        100        110        120 
RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA GVVAVEVTGG PDIPFHPGRE 

       130        140        150        160        170        180 
DKPQPPPEGR LPDATKGCDH LRDVFAKQMG LSDKDIVALS GAHTLGRCHK DRSGFEGAWT 

       190        200        210        220        230        240 
SNPLIFDNSY FKELLSGEKE GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM 

       250 
KLSELGFADA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRD86214.
S20866.
RefSeqNP_001030991.2. NM_001035914.2.
NP_001030992.2. NM_001035915.2.
NP_001077482.1. NM_001084013.1.
NP_001117244.1. NM_001123772.1.
NP_172267.1. NM_100663.3.
NP_849607.1. NM_179276.2.
NP_973786.1. NM_202057.2.
UniGeneAt.47584.
At.67008.

3D structure databases

ProteinModelPortalQ05431.
SMRQ05431. Positions 3-250.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid22545. 3 interactions.
IntActQ05431. 4 interactions.

Protein family/group databases

PeroxiBase1890. AtAPx01.

2D gel databases

SWISS-2DPAGEQ05431.

Proteomic databases

PaxDbQ05431.
PRIDEQ05431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G07890.1; 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]
GeneID837304.
KEGGath:AT1G07890.

Organism-specific databases

GeneFarm1942. 146.
TAIRAT1G07890.

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHOG000189824.
InParanoidQ05431.
KOK00434.
OMAIAEKNCA.
PhylomeDBQ05431.
ProtClustDBPLN02364.

Enzyme and pathway databases

BioCycARA: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

ArrayExpressQ05431.
GenevestigatorQ05431.

Family and domain databases

InterProIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPX1_ARATH
AccessionPrimary (citable) accession number: Q05431
Secondary accession number(s): Q0WLU2, Q2V4P8, Q2V4P9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names