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Protein

L-ascorbate peroxidase 2, cytosolic

Gene

APX2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in hydrogen peroxide removal.By similarity

Catalytic activityi

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

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei39 – 391Transition state stabilizerPROSITE-ProRule annotation
Active sitei43 – 431Proton 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

  • heme binding Source: InterPro
  • L-ascorbate peroxidase activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, Potassium

Enzyme and pathway databases

BioCyciARA:AT3G09640-MONOMER.
ARA:GQT-2248-MONOMER.

Protein family/group databases

PeroxiBasei1888. AtAPx02.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ascorbate peroxidase 2, cytosolic (EC:1.11.1.11)
Alternative name(s):
L-ascorbate peroxidase 1b
Short name:
APX1b
Short name:
AtAPx02
Gene namesi
Name:APX2
Synonyms:APX1B
Ordered Locus Names:At3g09640
ORF Names:F11F8_23
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G09640.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251L-ascorbate peroxidase 2, cytosolicPRO_0000261322Add
BLAST

Proteomic databases

PaxDbiQ1PER6.
PRIDEiQ1PER6.

Expressioni

Tissue specificityi

Detected in bundle sheath cells, the photosynthetic cells that surround the phloem and xylem.1 Publication

Inductioni

By excess light treatment, by wounding and by heat-shock stress.4 Publications

Gene expression databases

GenevisibleiQ1PER6. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G09640.1.

Structurei

3D structure databases

ProteinModelPortaliQ1PER6.
SMRiQ1PER6. Positions 4-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IF5T. Eukaryota.
COG0376. LUCA.
InParanoidiQ1PER6.
KOiK00434.
OMAiVFKKQMG.
PhylomeDBiQ1PER6.

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.

Q1PER6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV
60 70 80 90 100
KTKTGGPFGT IRHPQELAHD ANNGLDIAVR LLDPIKELFP ILSYADFYQL
110 120 130 140 150
AGVVAVEITG GPEIPFHPGR LDKVEPPPEG RLPQATKGVD HLRDVFGRMG
160 170 180 190 200
LNDKDIVALS GGHTLGRCHK ERSGFEGAWT PNPLIFDNSY FKEILSGEKE
210 220 230 240 250
GLLQLPTDKA LLDDPLFLPF VEKYAADEDA FFEDYTEAHL KLSELGFADK

E
Length:251
Mass (Da):28,006
Last modified:January 23, 2007 - v3
Checksum:iFFC7F6D82A4EF3E0
GO

Sequence cautioni

The sequence AAF23294.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Y → F in ABE65932 (PubMed:17147637).Curated
Sequence conflicti231 – 2311F → S in CAA66925 (PubMed:8580771).Curated
Sequence conflicti231 – 2311F → S in CAA56340 (PubMed:9144965).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80036 Genomic DNA. Translation: CAA56340.1.
X98275 mRNA. Translation: CAA66925.1.
AC016661 Genomic DNA. Translation: AAF23294.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74791.1.
CP002686 Genomic DNA. Translation: AEE74792.1.
AK176821 mRNA. Translation: BAD44584.1.
AK176908 mRNA. Translation: BAD44671.1.
DQ446651 mRNA. Translation: ABE65932.1.
RefSeqiNP_001030664.1. NM_001035587.2.
NP_187575.2. NM_111798.3.
UniGeneiAt.129.

Genome annotation databases

EnsemblPlantsiAT3G09640.1; AT3G09640.1; AT3G09640.
AT3G09640.2; AT3G09640.2; AT3G09640.
GeneIDi820121.
GrameneiAT3G09640.1; AT3G09640.1; AT3G09640.
AT3G09640.2; AT3G09640.2; AT3G09640.
KEGGiath:AT3G09640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80036 Genomic DNA. Translation: CAA56340.1.
X98275 mRNA. Translation: CAA66925.1.
AC016661 Genomic DNA. Translation: AAF23294.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74791.1.
CP002686 Genomic DNA. Translation: AEE74792.1.
AK176821 mRNA. Translation: BAD44584.1.
AK176908 mRNA. Translation: BAD44671.1.
DQ446651 mRNA. Translation: ABE65932.1.
RefSeqiNP_001030664.1. NM_001035587.2.
NP_187575.2. NM_111798.3.
UniGeneiAt.129.

3D structure databases

ProteinModelPortaliQ1PER6.
SMRiQ1PER6. Positions 4-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G09640.1.

Protein family/group databases

PeroxiBasei1888. AtAPx02.

Proteomic databases

PaxDbiQ1PER6.
PRIDEiQ1PER6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G09640.1; AT3G09640.1; AT3G09640.
AT3G09640.2; AT3G09640.2; AT3G09640.
GeneIDi820121.
GrameneiAT3G09640.1; AT3G09640.1; AT3G09640.
AT3G09640.2; AT3G09640.2; AT3G09640.
KEGGiath:AT3G09640.

Organism-specific databases

TAIRiAT3G09640.

Phylogenomic databases

eggNOGiENOG410IF5T. Eukaryota.
COG0376. LUCA.
InParanoidiQ1PER6.
KOiK00434.
OMAiVFKKQMG.
PhylomeDBiQ1PER6.

Enzyme and pathway databases

BioCyciARA:AT3G09640-MONOMER.
ARA:GQT-2248-MONOMER.

Miscellaneous databases

PROiQ1PER6.

Gene expression databases

GenevisibleiQ1PER6. AT.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family."
    Santos M., Gosseau H., Lister C., Foyer C., Creissen G.P., Mullineaux P.M.
    Planta 198:64-69(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Columbia.
    Tissue: Leaf.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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 (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis."
    Panchuk I.I., Volkov R.A., Schoffl F.
    Plant Physiol. 129:838-853(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Induction of ASCORBATE PEROXIDASE 2 expression in wounded Arabidopsis leaves does not involve known wound-signalling pathways but is associated with changes in photosynthesis."
    Chang C.C., Ball L., Fryer M.J., Baker N.R., Karpinski S., Mullineaux P.M.
    Plant J. 38:499-511(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves."
    Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R.
    Plant J. 33:691-705(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAPX2_ARATH
AccessioniPrimary (citable) accession number: Q1PER6
Secondary accession number(s): Q39006, Q67XB1, Q9SF39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 74 of the entry and version 3 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, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.