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Reviewed, UniProtKB/Swiss-Prot Q9SJZ2 (PER17_ARATH)

Last modified June 16, 2009. Version 72. 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 17
      Short name=Atperox P17
    EC=1.11.1.7
Alternative name(s):
    ATP25a
Gene names
Name: PER17
Synonyms: P17
Ordered Locus Names: At2g22420
ORF Names: F14M13.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length329 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 Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.

Induction

Early induced by infection with an incompatible bacterial plant pathogen. Ref.4

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
Vacuole
   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 componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuole

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 – 1919 Potential
Chain20 – 329310Peroxidase 17
PRO_0000023683

Sites

Active site631Proton acceptor By similarity
Metal binding641Calcium 1 By similarity
Metal binding671Calcium 1; via carbonyl oxygen By similarity
Metal binding691Calcium 1; via carbonyl oxygen By similarity
Metal binding711Calcium 1 By similarity
Metal binding731Calcium 1 By similarity
Metal binding1901Iron (heme axial ligand) By similarity
Metal binding1911Calcium 2 By similarity
Metal binding2421Calcium 2 By similarity
Metal binding2441Calcium 2 By similarity
Metal binding2491Calcium 2 By similarity
Binding site1601Substrate; via carbonyl oxygen By similarity
Site591Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 112 By similarity
Disulfide bond65 ↔ 70 By similarity
Disulfide bond118 ↔ 315 By similarity
Disulfide bond197 ↔ 229 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SJZ2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6BF861DE592968BA

FASTA32936,670
        10         20         30         40         50         60 
MSLLPHLILY LTLLTVVVTG ETLRPRFYSE TCPEAESIVR REMKKAMIKE ARSVASVMRF 

        70         80         90        100        110        120 
QFHDCFVNGC DASLLLDDTP NMLGEKLSLS NIDSLRSFEV VDDIKEALEK ACPATVSCAD 

       130        140        150        160        170        180 
IVIMAARDAV ALTGGPDWEV KLGRKDSLTA SQQDSDDIMP SPRANATFLI DLFERFNLSV 

       190        200        210        220        230        240 
KDMVALSGSH SIGQGRCFSI MFRLYNQSGS GKPDPALEPS YRKKLDKLCP LGGDENVTGD 

       250        260        270        280        290        300 
LDATPQVFDN QYFKDLVSGR GFLNSDQTLY TNLVTREYVK MFSEDQDEFF RAFAEGMVKL 

       310        320 
GDLQSGRPGE IRFNCRVVNR RPIDVLLVS 

« 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]"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., Jensen R.B., Hansen L.N., Rasmussen S.K.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 227-329.
Strain: cv. Columbia.
[4]"Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays."
Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D.
J. Biol. Chem. 277:10555-10561(2002) [PubMed: 11748215] [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.

Cross-references

Sequence databases

AC006592 Genomic DNA. Translation: AAD22357.1.
BT004021 mRNA. Translation: AAO42057.1.
BT005050 mRNA. Translation: AAO50583.1.
Y11790 mRNA. Translation: CAA72486.1.
IPIIPI00537519.
PIRD84612.
RefSeqNP_179828.1.
UniGeneAt.24416

3D structure databases

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

Protein family/group databases

PeroxiBase98. AtPrx17.

Proteomic databases

PRIDEQ9SJZ2.

Genome annotation databases

GeneID816773.
GenomeReviewsGene locus AT2G22420 in contig CT485783_GR.
KEGGath:AT2G22420.
NMPDRfig|3702.1.peg.9260.

Organism-specific databases

GeneFarm1841. 61.
TAIRAt2g22420.

Phylogenomic databases

OMAQ9SJZ2. TASQEDS.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ9SJZ2.
GermOnlineAT2G22420. 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. False negative.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER17_ARATH
AccessionPrimary (citable) accession number: Q9SJZ2
Secondary accession number(s): P93725
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 72 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