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

Peroxidase 15

Gene

PER15

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+PROSITE-ProRule annotationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 721Transition state stabilizerPROSITE-ProRule annotation
Active sitei76 – 761Proton acceptorPROSITE-ProRule annotation
Metal bindingi77 – 771Calcium 1PROSITE-ProRule annotation
Metal bindingi80 – 801Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi82 – 821Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi84 – 841Calcium 1PROSITE-ProRule annotation
Metal bindingi86 – 861Calcium 1PROSITE-ProRule annotation
Binding sitei173 – 1731Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi203 – 2031Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi204 – 2041Calcium 2PROSITE-ProRule annotation
Metal bindingi255 – 2551Calcium 2PROSITE-ProRule annotation
Metal bindingi258 – 2581Calcium 2PROSITE-ProRule annotation
Metal bindingi263 – 2631Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT2G18150-MONOMER.

Protein family/group databases

PeroxiBasei96. AtPrx15.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 15 (EC:1.11.1.7)
Short name:
Atperox P15
Alternative name(s):
ATP36
Gene namesi
Name:PER15
Synonyms:P15
Ordered Locus Names:At2g18150
ORF Names:F8D23.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G18150.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

  • cell wall Source: TAIR
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 338316Peroxidase 15PRO_0000023681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 125PROSITE-ProRule annotation
Disulfide bondi78 ↔ 83PROSITE-ProRule annotation
Disulfide bondi131 ↔ 332PROSITE-ProRule annotation
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi210 ↔ 242PROSITE-ProRule annotation
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9SI16.
PRIDEiQ9SI16.

Expressioni

Gene expression databases

GenevisibleiQ9SI16. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G18150.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SI16.
SMRiQ9SI16. Positions 40-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIQM. Eukaryota.
ENOG410YA1B. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9SI16.
KOiK00430.
OMAiPGFYRSS.
PhylomeDBiQ9SI16.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
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.

Q9SI16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARIGSFLII LYLIYALTLC ICDDDESNYG GDKGNLFPGF YRSSCPRAEE
60 70 80 90 100
IVRSVVAKAV ARETRMAASL MRLHFHDCFV QGCDGSLLLD TSGSIVTEKN
110 120 130 140 150
SNPNSRSARG FEVVDEIKAA LENECPNTVS CADALTLAAR DSSVLTGGPS
160 170 180 190 200
WMVPLGRRDS TSASLSGSNN NIPAPNNTFN TIVTRFNNQG LDLTDVVALS
210 220 230 240 250
GSHTIGFSRC TSFRQRLYNQ SGNGSPDRTL EQSYAANLRQ RCPRSGGDQN
260 270 280 290 300
LSELDINSAG RFDNSYFKNL IENMGLLNSD EVLFSSNEQS RELVKKYAED
310 320 330
QEEFFEQFAE SMIKMGNISP LTGSSGEIRK NCRKINNS
Length:338
Mass (Da):37,079
Last modified:May 1, 2000 - v1
Checksum:i9496FE1962DEC27E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141I → T in AAM61616 (Ref. 4) Curated
Sequence conflicti21 – 211I → V in AAM61616 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007212 Genomic DNA. Translation: AAD31351.1.
CP002685 Genomic DNA. Translation: AEC06731.1.
AY081298 mRNA. Translation: AAL91187.1.
BT002557 mRNA. Translation: AAO00917.1.
AY085060 mRNA. Translation: AAM61616.1.
PIRiH84560.
RefSeqiNP_179407.1. NM_127372.3.
UniGeneiAt.28467.

Genome annotation databases

EnsemblPlantsiAT2G18150.1; AT2G18150.1; AT2G18150.
GeneIDi816328.
GrameneiAT2G18150.1; AT2G18150.1; AT2G18150.
KEGGiath:AT2G18150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007212 Genomic DNA. Translation: AAD31351.1.
CP002685 Genomic DNA. Translation: AEC06731.1.
AY081298 mRNA. Translation: AAL91187.1.
BT002557 mRNA. Translation: AAO00917.1.
AY085060 mRNA. Translation: AAM61616.1.
PIRiH84560.
RefSeqiNP_179407.1. NM_127372.3.
UniGeneiAt.28467.

3D structure databases

ProteinModelPortaliQ9SI16.
SMRiQ9SI16. Positions 40-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G18150.1.

Protein family/group databases

PeroxiBasei96. AtPrx15.

Proteomic databases

PaxDbiQ9SI16.
PRIDEiQ9SI16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G18150.1; AT2G18150.1; AT2G18150.
GeneIDi816328.
GrameneiAT2G18150.1; AT2G18150.1; AT2G18150.
KEGGiath:AT2G18150.

Organism-specific databases

TAIRiAT2G18150.

Phylogenomic databases

eggNOGiENOG410IIQM. Eukaryota.
ENOG410YA1B. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9SI16.
KOiK00430.
OMAiPGFYRSS.
PhylomeDBiQ9SI16.

Enzyme and pathway databases

BioCyciARA:AT2G18150-MONOMER.

Miscellaneous databases

PROiQ9SI16.

Gene expression databases

GenevisibleiQ9SI16. AT.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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.
    , 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.
  4. "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].
  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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
    Strain: cv. Columbia.

Entry informationi

Entry nameiPER15_ARATH
AccessioniPrimary (citable) accession number: Q9SI16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

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.