Q96520 · PER12_ARATH

Function

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.
Exhibits a Ca2+-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site80Transition state stabilizer
Active site84Proton acceptor
Binding site85Ca2+ 1 (UniProtKB | ChEBI)
Binding site88Ca2+ 1 (UniProtKB | ChEBI)
Binding site90Ca2+ 1 (UniProtKB | ChEBI)
Binding site92Ca2+ 1 (UniProtKB | ChEBI)
Binding site94Ca2+ 1 (UniProtKB | ChEBI)
Binding site183substrate
Binding site213Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site214Ca2+ 2 (UniProtKB | ChEBI)
Binding site259Ca2+ 2 (UniProtKB | ChEBI)
Binding site262Ca2+ 2 (UniProtKB | ChEBI)
Binding site267Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentmitochondrion
Cellular Componentplant-type cell wall
Cellular Componentplant-type vacuole
Cellular Componentplasmodesma
Molecular Functionheme binding
Molecular Functionlactoperoxidase activity
Molecular Functionmetal ion binding
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxidase 12
  • EC number
  • Short names
    Atperox P12
  • Alternative names
    • ATP4a
    • PRXR6

Gene names

    • Name
      PER12
    • Synonyms
      P12
    • ORF names
      F14O23.6, F26A9.5
    • Ordered locus names
      At1g71695

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q96520
  • Secondary accessions
    • Q43734

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Secreted
Vacuole
Note: Carboxy-terminal extension appears to target the protein to vacuoles.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-31
ChainPRO_000002367832-358Peroxidase 12
Disulfide bond53↔134
Disulfide bond86↔91
Disulfide bond140↔335
Glycosylation188N-linked (GlcNAc...) asparagine
Glycosylation202N-linked (GlcNAc...) asparagine
Disulfide bond220↔247
Glycosylation251N-linked (GlcNAc...) asparagine
Glycosylation334N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in roots and leaves.

Induction

Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule.

Developmental stage

Expressed in the first stage of developing seeds.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    358
  • Mass (Da)
    39,559
  • Last updated
    1997-02-01 v1
  • Checksum
    B8F18C56CFCB4CB2
MTKAYSTRVLTFLILISLMAVTLNLFPTVEAKKRSRDAPIVKGLSWNFYQKACPKVENIIRKELKKVFKRDIGLAAAILRIHFHDCFVQGCEASVLLAGSASGPGEQSSIPNLTLRQQAFVVINNLRALVQKKCGQVVSCSDILALAARDSVVLSGGPDYAVPLGRRDSLAFASQETTLNNLPPPFFNASQLIADFANRNLNITDLVALSGGHTIGIAHCPSFTDRLYPNQDPTMNQFFANSLKRTCPTANSSNTQVNDIRSPDVFDNKYYVDLMNRQGLFTSDQDLFVDKRTRGIVESFAIDQQLFFDYFTVAMIKMGQMSVLTGTQGEIRSNCSARNTQSFMSVLEEGIEEAISMI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict257in Ref. 1; CAA66962

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X98318
EMBL· GenBank· DDBJ
CAA66962.1
EMBL· GenBank· DDBJ
mRNA
X98773
EMBL· GenBank· DDBJ
CAA67309.1
EMBL· GenBank· DDBJ
mRNA
AC012654
EMBL· GenBank· DDBJ
AAF43221.1
EMBL· GenBank· DDBJ
Genomic DNA
AC016163
EMBL· GenBank· DDBJ
AAG51834.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE35217.1
EMBL· GenBank· DDBJ
Genomic DNA
AF334732
EMBL· GenBank· DDBJ
AAG50110.1
EMBL· GenBank· DDBJ
mRNA
BT000715
EMBL· GenBank· DDBJ
AAN31858.1
EMBL· GenBank· DDBJ
mRNA
AY087964
EMBL· GenBank· DDBJ
AAM65511.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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