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Reviewed, UniProtKB/Swiss-Prot Q9SI16 (PER15_ARATH)

Last modified June 16, 2009. Version 75. 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

Names and origin

Protein namesRecommended name:
    Peroxidase 15
      Short name=Atperox P15
    EC=1.11.1.7
Alternative name(s):
    ATP36
Gene names
Name: PER15
Synonyms: P15
Ordered Locus Names: At2g18150
ORF Names: F8D23.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length338 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

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.

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
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 componentcell wall

Inferred from direct assay. Source: TAIR

extracellular 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 338316Peroxidase 15
PRO_0000023681

Sites

Active site761Proton acceptor By similarity
Metal binding771Calcium 1 By similarity
Metal binding801Calcium 1; via carbonyl oxygen By similarity
Metal binding821Calcium 1; via carbonyl oxygen By similarity
Metal binding841Calcium 1 By similarity
Metal binding861Calcium 1 By similarity
Metal binding2031Iron (heme axial ligand) By similarity
Metal binding2041Calcium 2 By similarity
Metal binding2551Calcium 2 By similarity
Metal binding2581Calcium 2 By similarity
Metal binding2631Calcium 2 By similarity
Binding site1731Substrate; via carbonyl oxygen By similarity
Site721Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 125 By similarity
Disulfide bond78 ↔ 83 By similarity
Disulfide bond131 ↔ 332 By similarity
Disulfide bond210 ↔ 242 By similarity

Experimental info

Sequence conflict141I → T in AAM61616. Ref.3
Sequence conflict211I → V in AAM61616. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SI16-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9496FE1962DEC27E

FASTA33837,079
        10         20         30         40         50         60 
MARIGSFLII LYLIYALTLC ICDDDESNYG GDKGNLFPGF YRSSCPRAEE IVRSVVAKAV 

        70         80         90        100        110        120 
ARETRMAASL MRLHFHDCFV QGCDGSLLLD TSGSIVTEKN SNPNSRSARG FEVVDEIKAA 

       130        140        150        160        170        180 
LENECPNTVS CADALTLAAR DSSVLTGGPS WMVPLGRRDS TSASLSGSNN NIPAPNNTFN 

       190        200        210        220        230        240 
TIVTRFNNQG LDLTDVVALS GSHTIGFSRC TSFRQRLYNQ SGNGSPDRTL EQSYAANLRQ 

       250        260        270        280        290        300 
RCPRSGGDQN LSELDINSAG RFDNSYFKNL IENMGLLNSD EVLFSSNEQS RELVKKYAED 

       310        320        330 
QEEFFEQFAE SMIKMGNISP LTGSSGEIRK NCRKINNS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"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].
[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.

Cross-references

Sequence databases

AC007212 Genomic DNA. Translation: AAD31351.1.
AY081298 mRNA. Translation: AAL91187.1.
BT002557 mRNA. Translation: AAO00917.1.
AY085060 mRNA. Translation: AAM61616.1.
IPIIPI00544435.
PIRH84560.
RefSeqNP_179407.1.
UniGeneAt.28467

3D structure databases

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

Protein family/group databases

PeroxiBase96. AtPrx15.

Proteomic databases

PRIDEQ9SI16.

Genome annotation databases

GeneID816328.
GenomeReviewsGene locus AT2G18150 in contig CT485783_GR.
KEGGath:AT2G18150.
NMPDRfig|3702.1.peg.8809.

Organism-specific databases

GeneFarm1838. 61.
TAIRAt2g18150.

Phylogenomic databases

OMAQ9SI16. AREIVNS.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ9SI16.
GermOnlineAT2G18150. 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...

Entry information

Entry namePER15_ARATH
AccessionPrimary (citable) accession number: Q9SI16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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