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Reviewed, UniProtKB/Swiss-Prot Q96510 (PER35_ARATH)

Last modified June 16, 2009. Version 78. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Peroxidase 35
      Short name=Atperox P35
    EC=1.11.1.7
Alternative name(s):
    ATP21a
Gene names
Name: PER35
Synonyms: P35
Ordered Locus Names: At3g49960
ORF Names: F3A4.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length329 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

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

Donor + H2O2 = oxidized 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.

Tissue specificity

Slightly expressed in roots.

Induction

Up-regulated transiently by a cold treatment. Ref.4

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

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

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 329304Peroxidase 35
PRO_0000023701

Sites

Active site671Proton acceptor By similarity
Metal binding681Calcium 1 By similarity
Metal binding711Calcium 1; via carbonyl oxygen By similarity
Metal binding731Calcium 1; via carbonyl oxygen By similarity
Metal binding751Calcium 1 By similarity
Metal binding771Calcium 1 By similarity
Metal binding1971Iron (heme axial ligand) By similarity
Metal binding1981Calcium 2 By similarity
Metal binding2491Calcium 2 By similarity
Metal binding2521Calcium 2 By similarity
Metal binding2571Calcium 2 By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Site631Transition state stabilizer By similarity

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid By similarity
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 119 By similarity
Disulfide bond69 ↔ 74 By similarity
Disulfide bond125 ↔ 325 By similarity
Disulfide bond204 ↔ 236 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q96510-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: EDD91B0099A6A2C2

FASTA32935,756
        10         20         30         40         50         60 
MARFDIVLLI GLCLIISVFP DTTTAQLSRG FYSKTCPNVE QIVRNAVQKK IKKTFVAVPA 

        70         80         90        100        110        120 
TLRLFFHDCF VNGCDASVMI QSTPKNKAEK DHPDNISLAG DGFDVVIQAK KALDSNPSCR 

       130        140        150        160        170        180 
NKVSCADILT LATRDVVVAA GGPSYEVELG RFDGLVSTAS SVEGNLPGPS DNVDKLNALF 

       190        200        210        220        230        240 
TKNKLTQEDM IALSAAHTLG FAHCGKVFKR IHKFNGINSV DPTLNKAYAI ELQKACPKNV 

       250        260        270        280        290        300 
DPRIAINMDP VTPKTFDNTY FKNLQQGKGL FTSDQVLFTD GRSRPTVNAW ASNSTAFNRA 

       310        320 
FVIAMTKLGR VGVKNSSNGN IRRDCGAFN

« Hide

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References

« Hide 'large scale' references
[1]"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases."
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Hansen L.N., Rasmussen S.K.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"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. expand/collapse author list , 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: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Computational analyses and annotations of the Arabidopsis peroxidase gene family."
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.
FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract]
Cited for: CHARACTERIZATION.
Strain: cv. Columbia.
[4]"Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway."
Fowler S., Thomashow M.F.
Plant Cell 14:1675-1690(2002) [PubMed: 12172015] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[5]"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.

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Cross-references

Sequence databases

X98807 mRNA. Translation: CAA67339.1.
AL132978 Genomic DNA. Translation: CAB62104.1.
IPIIPI00532358.
PIRT45849.
RefSeqNP_190565.1.
UniGeneAt.19626

3D structure databases

HSSPHSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBaseSearch...

Protein family/group databases

PeroxiBase201. AtPrx35.

Proteomic databases

PRIDEQ96510.

Genome annotation databases

GeneID824158.
GenomeReviewsGene locus AT3G49960 in contig BA000014_GR.
KEGGath:AT3G49960.
NMPDRfig|3702.1.peg.16244.

Organism-specific databases

GeneFarm1862. 61.
TAIRAt3g49960.

Phylogenomic databases

OMAQ96510. NIRRDCA.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ96510.
GermOnlineAT3G49960. Arabidopsis thaliana.

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePER35_ARATH
AccessionPrimary (citable) accession number: Q96510
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 78 of the entry and version 1 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents