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Protein

Peroxidase 3

Gene

PER3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 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
Sitei62 – 621Transition state stabilizerPROSITE-ProRule annotation
Active sitei66 – 661Proton acceptorPROSITE-ProRule annotation
Metal bindingi67 – 671Calcium 1PROSITE-ProRule annotation
Metal bindingi70 – 701Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi72 – 721Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi74 – 741Calcium 1PROSITE-ProRule annotation
Metal bindingi76 – 761Calcium 1PROSITE-ProRule annotation
Binding sitei161 – 1611Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi191 – 1911Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi192 – 1921Calcium 2PROSITE-ProRule annotation
Metal bindingi244 – 2441Calcium 2PROSITE-ProRule annotation
Metal bindingi247 – 2471Calcium 2PROSITE-ProRule annotation
Metal bindingi252 – 2521Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: TAIR

GO - Biological processi

  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • hyperosmotic salinity response Source: TAIR
  • plant-type cell wall organization Source: GO_Central
  • response to cold Source: TAIR
  • response to desiccation Source: TAIR
  • response to oxidative stress Source: InterPro
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:AT1G05260-MONOMER.

Protein family/group databases

PeroxiBasei79. AtPrx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 3 (EC:1.11.1.7)
Short name:
Atperox P3
Alternative name(s):
ATPRC
RCI3A
Rare cold-inducible protein
Gene namesi
Name:PER3
Synonyms:P3, RCI3
Ordered Locus Names:At1g05260
ORF Names:YUP8H12.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G05260.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • extracellular region Source: UniProtKB-SubCell
  • plant-type cell wall Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 326302Peroxidase 3PRO_0000023669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 113PROSITE-ProRule annotation
Disulfide bondi68 ↔ 73PROSITE-ProRule annotation
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence analysis
Disulfide bondi119 ↔ 321PROSITE-ProRule annotation
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi198 ↔ 231PROSITE-ProRule annotation
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO23044.
PRIDEiO23044.

PTM databases

iPTMnetiO23044.

Expressioni

Tissue specificityi

Expressed in root cells.

Inductioni

Up-regulated by cold temperatures and down-regulated by light. In response to low temperatures, transcripts accumulate in the whole etiolated seedlings but only in roots of light-grown seedlings.

Gene expression databases

ExpressionAtlasiO23044. baseline and differential.
GenevisibleiO23044. AT.

Interactioni

Protein-protein interaction databases

IntActiO23044. 1 interaction.
STRINGi3702.AT1G05260.1.

Structurei

3D structure databases

ProteinModelPortaliO23044.
SMRiO23044. Positions 26-325.
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

eggNOGiENOG410IFQR. Eukaryota.
ENOG410Y9ME. LUCA.
HOGENOMiHOG000237556.
InParanoidiO23044.
KOiK00430.
OMAiDLSYYRG.
PhylomeDBiO23044.

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.

O23044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCLIAIALS VSFFLVGIVG PIQAQLQMNF YANSCPNAEK IVQDFVSNHV
60 70 80 90 100
SNAPSLAAAL IRMHFHDCFV RGCDGSVLIN STSGNAERDA TPNLTVRGFG
110 120 130 140 150
FIDAIKSVLE AQCPGIVSCA DIIALASRDA VVFTGGPNWS VPTGRRDGRI
160 170 180 190 200
SNAAEALANI PPPTSNITNL QTLFANQGLD LKDLVLLSGA HTIGVSHCSS
210 220 230 240 250
FTNRLYNFTG RGGQDPALDS EYAANLKSRK CPSLNDNKTI VEMDPGSRKT
260 270 280 290 300
FDLSYYQLVL KRRGLFQSDS ALTTNPTTLS NINRILTGSV GSFFSEFAKS
310 320
MEKMGRINVK TGSAGVVRRQ CSVANS
Length:326
Mass (Da):34,906
Last modified:January 1, 1998 - v1
Checksum:i45D45362E5DD1B83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181I → M in AAM61240 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97684 mRNA. Translation: AAB94661.1.
AC000098 Genomic DNA. Translation: AAB71452.1.
CP002684 Genomic DNA. Translation: AEE27815.1.
BT004817 mRNA. Translation: AAO44083.1.
AY084678 mRNA. Translation: AAM61240.1.
PIRiB86187.
RefSeqiNP_172018.1. NM_100405.3.
UniGeneiAt.23986.

Genome annotation databases

EnsemblPlantsiAT1G05260.1; AT1G05260.1; AT1G05260.
GeneIDi837028.
GrameneiAT1G05260.1; AT1G05260.1; AT1G05260.
KEGGiath:AT1G05260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97684 mRNA. Translation: AAB94661.1.
AC000098 Genomic DNA. Translation: AAB71452.1.
CP002684 Genomic DNA. Translation: AEE27815.1.
BT004817 mRNA. Translation: AAO44083.1.
AY084678 mRNA. Translation: AAM61240.1.
PIRiB86187.
RefSeqiNP_172018.1. NM_100405.3.
UniGeneiAt.23986.

3D structure databases

ProteinModelPortaliO23044.
SMRiO23044. Positions 26-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO23044. 1 interaction.
STRINGi3702.AT1G05260.1.

Protein family/group databases

PeroxiBasei79. AtPrx03.

PTM databases

iPTMnetiO23044.

Proteomic databases

PaxDbiO23044.
PRIDEiO23044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G05260.1; AT1G05260.1; AT1G05260.
GeneIDi837028.
GrameneiAT1G05260.1; AT1G05260.1; AT1G05260.
KEGGiath:AT1G05260.

Organism-specific databases

TAIRiAT1G05260.

Phylogenomic databases

eggNOGiENOG410IFQR. Eukaryota.
ENOG410Y9ME. LUCA.
HOGENOMiHOG000237556.
InParanoidiO23044.
KOiK00430.
OMAiDLSYYRG.
PhylomeDBiO23044.

Enzyme and pathway databases

BioCyciARA:AT1G05260-MONOMER.

Miscellaneous databases

PROiO23044.

Gene expression databases

ExpressionAtlasiO23044. baseline and differential.
GenevisibleiO23044. 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. "A novel cold-inducible gene from Arabidopsis, RCI3, encodes a peroxidase that constitutes a component for stress tolerance."
    Llorente F., Lopez-Cobollo R.M., Catala R., Martinez-Zapater J.M., Salinas J.
    Plant J. 32:13-24(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Etiolated seedling.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [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. "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.
  5. "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].
  6. "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 nameiPER3_ARATH
AccessioniPrimary (citable) accession number: O23044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 129 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.