Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-ascorbate peroxidase 3, peroxisomal

Gene

APX3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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
Sitei36 – 361Transition state stabilizerPROSITE-ProRule annotation
Active sitei40 – 401Proton acceptorPROSITE-ProRule annotation
Metal bindingi160 – 1601Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi161 – 1611Potassium or calciumBy similarity
Metal bindingi177 – 1771Potassium or calciumBy similarity
Metal bindingi184 – 1841Potassium 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 cytokinin Source: TAIR
  • 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:AT4G35000-MONOMER.

Protein family/group databases

PeroxiBasei1891. AtAPx03.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ascorbate peroxidase 3, peroxisomal (EC:1.11.1.11)
Short name:
AtAPx03
Gene namesi
Name:APX3
Synonyms:APX, APXIII
Ordered Locus Names:At4g35000
ORF Names:M4E13.60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35000.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei259 – 27921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • glyoxysomal membrane Source: UniProtKB-SubCell
  • glyoxysome Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrion Source: TAIR
  • peroxisomal membrane Source: TAIR
  • peroxisome Source: UniProtKB
  • plasmodesma Source: TAIR
  • plastid Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 287L-ascorbate peroxidase 3, peroxisomalPRO_0000261323
Initiator methionineiRemovedCombined sources
Transit peptidei2 – ?PeroxisomeSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ42564.
PRIDEiQ42564.

Expressioni

Gene expression databases

GenevisibleiQ42564. AT.

Interactioni

Subunit structurei

Interacts via its C-terminal region with AKR2A and AKR2B.2 Publications

Protein-protein interaction databases

BioGridi14934. 3 interactions.
STRINGi3702.AT4G35000.1.

Structurei

3D structure databases

ProteinModelPortaliQ42564.
SMRiQ42564. Positions 4-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi281 – 2877AKR2A-binding sequence (ABS) required for peroxisome membrane targeting1 Publication

Domaini

The transmembrane plays critical roles in migration to the peroxisome and/or subsequent insertion into the membrane.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF5T. Eukaryota.
COG0376. LUCA.
HOGENOMiHOG000189824.
InParanoidiQ42564.
KOiK00434.
OMAiKNPKITY.
PhylomeDBiQ42564.

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.

Q42564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPIVDAEY LKEITKARRE LRSLIANKNC APIMLRLAWH DAGTYDAQSK
60 70 80 90 100
TGGPNGSIRN EEEHTHGANS GLKIALDLCE GVKAKHPKIT YADLYQLAGV
110 120 130 140 150
VAVEVTGGPD IVFVPGRKDS NVCPKEGRLP DAKQGFQHLR DVFYRMGLSD
160 170 180 190 200
KDIVALSGGH TLGRAHPERS GFDGPWTQEP LKFDNSYFVE LLKGESEGLL
210 220 230 240 250
KLPTDKTLLE DPEFRRLVEL YAKDEDAFFR DYAESHKKLS ELGFNPNSSA
260 270 280
GKAVADSTIL AQSAFGVAVA AAVVAFGYFY EIRKRMK
Length:287
Mass (Da):31,572
Last modified:November 1, 1996 - v1
Checksum:iB348E74BA34115DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821K → N in CAA06823 (Ref. 4) Curated
Sequence conflicti189 – 1891V → VR in CAA06823 (Ref. 4) Curated
Sequence conflicti223 – 2231Missing in CAA06823 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98003 mRNA. Translation: CAA66640.1.
X98276 mRNA. Translation: CAA66926.1.
U69138 mRNA. Translation: AAB71493.1.
AJ006030 Genomic DNA. Translation: CAA06823.1.
AL022023 Genomic DNA. Translation: CAA17765.1.
AL161586 Genomic DNA. Translation: CAB80217.1.
CP002687 Genomic DNA. Translation: AEE86445.1.
AY065143 mRNA. Translation: AAL38319.1.
AY081646 mRNA. Translation: AAM10208.1.
AY086162 mRNA. Translation: AAM63367.1.
PIRiS71279.
RefSeqiNP_195226.1. NM_119666.3.
UniGeneiAt.47586.

Genome annotation databases

EnsemblPlantsiAT4G35000.1; AT4G35000.1; AT4G35000.
GeneIDi829652.
GrameneiAT4G35000.1; AT4G35000.1; AT4G35000.
KEGGiath:AT4G35000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98003 mRNA. Translation: CAA66640.1.
X98276 mRNA. Translation: CAA66926.1.
U69138 mRNA. Translation: AAB71493.1.
AJ006030 Genomic DNA. Translation: CAA06823.1.
AL022023 Genomic DNA. Translation: CAA17765.1.
AL161586 Genomic DNA. Translation: CAB80217.1.
CP002687 Genomic DNA. Translation: AEE86445.1.
AY065143 mRNA. Translation: AAL38319.1.
AY081646 mRNA. Translation: AAM10208.1.
AY086162 mRNA. Translation: AAM63367.1.
PIRiS71279.
RefSeqiNP_195226.1. NM_119666.3.
UniGeneiAt.47586.

3D structure databases

ProteinModelPortaliQ42564.
SMRiQ42564. Positions 4-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14934. 3 interactions.
STRINGi3702.AT4G35000.1.

Protein family/group databases

PeroxiBasei1891. AtAPx03.

Proteomic databases

PaxDbiQ42564.
PRIDEiQ42564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35000.1; AT4G35000.1; AT4G35000.
GeneIDi829652.
GrameneiAT4G35000.1; AT4G35000.1; AT4G35000.
KEGGiath:AT4G35000.

Organism-specific databases

TAIRiAT4G35000.

Phylogenomic databases

eggNOGiENOG410IF5T. Eukaryota.
COG0376. LUCA.
HOGENOMiHOG000189824.
InParanoidiQ42564.
KOiK00434.
OMAiKNPKITY.
PhylomeDBiQ42564.

Enzyme and pathway databases

BioCyciARA:AT4G35000-MONOMER.

Miscellaneous databases

PROiQ42564.

Gene expression databases

GenevisibleiQ42564. 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. "From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase."
    Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G.
    Biochem. J. 326:305-310(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  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].
    Strain: cv. Columbia.
  3. "Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase."
    Zhang H., Wang J., Nickel U., Allen R.D., Goodman H.M.
    Plant Mol. Biol. 34:967-971(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Ascorbate peroxidase III gene from Arabidopsis thaliana is regulated by light and development."
    Escobar C., Bradley D.J., Puente P., Harberd N., Creissen G.P., Mullineaux P.M.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  5. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "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.
  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. "The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development."
    Narendra S., Venkataramani S., Shen G., Wang J., Pasapula V., Lin Y., Kornyeyev D., Holaday A.S., Zhang H.
    J. Exp. Bot. 57:3033-3042(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis."
    Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.
    Plant Cell 22:811-831(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKR2A AND AKR2B, AKR2A-BINDING SEQUENCE, DOMAIN.
    Strain: cv. C24 and cv. Columbia.
  11. "Is AKR2A an essential molecular chaperone for a class of membrane-bound proteins in plants?"
    Zhang H., Li X., Zhang Y., Kuppu S., Shen G.
    Plant Signal. Behav. 5:1520-1522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: AKR2A-BINDING SEQUENCE, INTERACTION WITH AKR2A, REVIEW.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAPX3_ARATH
AccessioniPrimary (citable) accession number: Q42564
Secondary accession number(s): O81810
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 115 of the entry and version 1 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.