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O23609 (PER41_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidase 41
Short name=Atperox P41
EC=1.11.1.7
Gene names
Name:PER41
Synonyms:P41
Ordered Locus Names:At4g17690
ORF Names:dl4880w, FCAALL.96
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.

Catalytic activity

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactor

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

Binds 2 calcium ions per subunit By similarity.

Subcellular location

Secreted By similarity.

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 326306Peroxidase 41
PRO_0000023707

Sites

Active site661Proton acceptor By similarity
Metal binding671Calcium 1 By similarity
Metal binding721Calcium 1; via carbonyl oxygen By similarity
Metal binding741Calcium 1 By similarity
Metal binding761Calcium 1 By similarity
Metal binding1941Iron (heme axial ligand) By similarity
Metal binding1951Calcium 2 By similarity
Metal binding2421Calcium 2 By similarity
Metal binding2451Calcium 2 By similarity
Metal binding2501Calcium 2 By similarity
Binding site1641Substrate; via carbonyl oxygen By similarity
Site621Transition state stabilizer By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 116 By similarity
Disulfide bond68 ↔ 73 By similarity
Disulfide bond122 ↔ 318 By similarity
Disulfide bond201 ↔ 228 By similarity

Sequences

Sequence LengthMass (Da)Tools
O23609 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 78B169B31BA85CE6

FASTA32636,198
        10         20         30         40         50         60 
MSSVINVLFV VLVFVPSIYS APPPNLTKDY YQKTCPDFNK IVRETVTPKQ GQQPTTAAGT 

        70         80         90        100        110        120 
LRLFFHDCFM EGCDASVLIA TNSFNKAERD DDLNESLPGD AFDIVTRIKT ALELSCPGVV 

       130        140        150        160        170        180 
SCADILAQAT RDLVTMVGGP FYEVKLGRKD GFESKAHKVK GNLPLANQSV PDMLSIFKKN 

       190        200        210        220        230        240 
GFTLKELVAL SGGHTIGFSH CKEFSNRIFP KVDPELNAKF AGVLKDLCKN FETNKTMAAF 

       250        260        270        280        290        300 
LDPVTPGKFD NMYFKNLKRG LGLLASDHIL FKDPSTRPFV ELYANNQTAF FEDFARAMEK 

       310        320 
LGRVGVKGEK DGEVRRRCDH FNKLNV

« Hide

References

« Hide 'large scale' references
[1]"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. expand/collapse author list , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
Nature 391:485-488(1998) [PubMed: 9461215] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana."
Tognolli M., Penel C., Greppin H., Simon P.
Gene 288:129-138(2002) [PubMed: 12034502] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z97344 Genomic DNA. Translation: CAB10549.1.
AL161547 Genomic DNA. Translation: CAB78772.1.
CP002687 Genomic DNA. Translation: AEE83934.1.
IPIIPI00538852.
PIRH71446.
RefSeqNP_193504.1. NM_117877.1.
UniGeneAt.54379.

3D structure databases

ProteinModelPortalO23609.
SMRO23609. Positions 25-323.
ModBaseSearch...

Protein-protein interaction databases

STRINGO23609.

Protein family/group databases

PeroxiBase207. AtPrx41.

Proteomic databases

PRIDEO23609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G17690.1; AT4G17690.1; AT4G17690.
GeneID827489.
GenomeReviewsGene locus AT4G17690 in contig CT486007_GR.
KEGGath:AT4G17690.
NMPDRfig|3702.1.peg.19559.

Organism-specific databases

GeneFarm1870. 61.
TAIRAt4g17690.

Phylogenomic databases

eggNOGCOG0376.
GeneTreeEPGT00050000003677.
HOGENOMHBG597790.
InParanoidO23609.
OMAVELYANN.
PhylomeDBO23609.
ProtClustDBCLSN2686001.

Gene expression databases

ArrayExpressO23609.
GenevestigatorO23609.
GermOnlineAT4G17690. Arabidopsis thaliana.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
KOK00430.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER41_ARATH
AccessionPrimary (citable) accession number: O23609
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents