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Reviewed, UniProtKB/Swiss-Prot Q42592 (APXS_ARATH)

Last modified February 9, 2010. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    L-ascorbate peroxidase S, chloroplastic/mitochondrial
    EC=1.11.1.11
Alternative name(s):
    Stromal ascorbate peroxidase
      Short name=sAPX
      Short name=AtAPx05
Gene names
Name: APXS
Ordered Locus Names: At4g08390
ORF Names: T28D5.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays a key role in hydrogen peroxide removal By similarity.

Catalytic activity

L-ascorbate + H2O2 = dehydroascorbate + 2 H2O.

Cofactor

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

Binds 1 potassium or calcium ion per subunit By similarity.

Subcellular location

Mitochondrion. Plastid › chloroplast stroma Potential Ref.4.

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

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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: Q42592-1)

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast and mitochondrion Potential
Chain? – 372L-ascorbate peroxidase S, chloroplastic/mitochondrialPRO_0000261326

Sites

Active site1331Proton acceptor By similarity
Metal binding2621Iron (heme axial ligand) By similarity
Metal binding2631Potassium or calcium By similarity
Metal binding2951Potassium or calcium By similarity
Metal binding3021Potassium or calcium By similarity
Site1291Transition state stabilizer By similarity

Experimental info

Sequence conflict111G → V in CAA67425. Ref.1
Sequence conflict751S → P in CAA67425. Ref.1
Sequence conflict811Y → C in CAA67425. Ref.1
Sequence conflict3711V → I in CAA67425. Ref.1

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Sequences

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

Last modified November 28, 2006. Version 2.
Checksum: A5D94B9A20720B87

FASTA37240,407
        10         20         30         40         50         60 
MAERVSLTLN GTLLSPPPTT TTTTMSSSLR STTAASLLLR SSSSSSRSTL TLSASSSLSF 

        70         80         90        100        110        120 
VRSLVSSPRL SSSSSLSQKK YRIASVNRSF NSTTAATKSS SSDPDQLKNA REDIKELLST 

       130        140        150        160        170        180 
KFCHPILVRL GWHDAGTYNK NIKEWPQRGG ANGSLRFDIE LKHAANAGLV NALNLIKDIK 

       190        200        210        220        230        240 
EKYSGISYAD LFQLASATAI EEAGGPKIPM KYGRVDASGP EDCPEEGRLP DAGPPSPATH 

       250        260        270        280        290        300 
LREVFYRMGL DDKDIVALSG AHTLGRSRPE RSGWGKPETK YTKEGPGAPG GQSWTPEWLK 

       310        320        330        340        350        360 
FDNSYFKEIK EKRDEDLLVL PTDAAIFEDS SFKVYAEKYA ADQDAFFKDY AVAHAKLSNL 

       370 
GAEFNPPEGI VI

« Hide

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References

« Hide 'large scale' references
[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: 9291097] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"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. expand/collapse author list , 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: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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. 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants."
Chew O., Whelan J., Millar A.H.
J. Biol. Chem. 278:46869-46877(2003) [PubMed: 12954611] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X98925 mRNA. Translation: CAA67425.1.
AL109819 Genomic DNA. Translation: CAB52561.1.
AL161511 Genomic DNA. Translation: CAB77964.1.
AY056319 mRNA. Translation: AAL07168.1.
AY114065 mRNA. Translation: AAM45113.1.
IPIIPI00522703.
PIRT14193.
RefSeqNP_192579.1.
NP_974520.1.
UniGeneAt.22866
Rsa.3511

3D structure databases

HSSPHSSP built from PDB template 1APX based on UniProtKB P48534.
SMRQ42592. Positions 100-369.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ42592.

Proteomic databases

PRIDEQ42592.
ProMEXQ42592.

Genome annotation databases

GeneID826396.
GenomeReviewsGene locus AT4G08390 in contig CT486007_GR.
NMPDRfig|3702.1.peg.18492.

Organism-specific databases

GeneFarm1956. 146.
TAIRAt4g08390.

Phylogenomic databases

HOGENOMHBG597790.
InParanoidQ42592.
OMAKAAREDI.
PhylomeDBQ42592.

Enzyme and pathway databases

BRENDA1.11.1.11. 302.

Gene expression databases

GenevestigatorQ42592.

Family and domain databases

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

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Entry information

Entry nameAPXS_ARATH
AccessionPrimary (citable) accession number: Q42592
Secondary accession number(s): Q9STM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: February 9, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents