M4DUF2 · ASO_BRARP

Function

function

Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) (PubMed:27255930).
The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity).
Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA) (PubMed:27255930).

Catalytic activity

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 4 Cu cations per monomer.

Pathway

Cofactor degradation; L-ascorbate degradation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site77Cu cation 1 (UniProtKB | ChEBI); type 2 copper site
Binding site79Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site121Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site123Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site463Cu cation 4 (UniProtKB | ChEBI); type 1 copper site
Binding site466Cu cation 1 (UniProtKB | ChEBI); type 2 copper site
Binding site468Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site525Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site526Cu cation 4 (UniProtKB | ChEBI); type 1 copper site
Binding site527Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site531Cu cation 4 (UniProtKB | ChEBI); type 1 copper site
Binding site536Cu cation 4 (UniProtKB | ChEBI); type 1 copper site

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncopper ion binding
Molecular FunctionL-ascorbate oxidase activity
Molecular Functionoxidoreductase activity
Biological Processdefense response
Biological ProcessL-ascorbic acid catabolic process
Biological Processnegative regulation of defense response to virus
Biological Processresponse to hydrogen peroxide
Biological Processresponse to jasmonic acid
Biological Processresponse to virus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-ascorbate oxidase
  • EC number
  • Short names
    AAO
    ; AO
    ; ASO
    ; Ascorbase

Gene names

    • Name
      AO

Organism names

Accessions

  • Primary accession
    M4DUF2

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
ChainPRO_500405151719-570L-ascorbate oxidase
Disulfide bond36↔219
Disulfide bond98↔557
Glycosylation109N-linked (GlcNAc...) asparagine
Glycosylation196N-linked (GlcNAc...) asparagine
Disulfide bond197↔211
Glycosylation229N-linked (GlcNAc...) asparagine
Glycosylation343N-linked (GlcNAc...) asparagine
Glycosylation384N-linked (GlcNAc...) asparagine
Glycosylation407N-linked (GlcNAc...) asparagine
Glycosylation434N-linked (GlcNAc...) asparagine
Glycosylation442N-linked (GlcNAc...) asparagine
Glycosylation458N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Repressed progressively during incompatible Turnip mosaic virus (TuMV) infection (strain UK1) in resistant cultivars (e.g. cv. Aki-masari) but not in susceptible cultivars (e.g. cv. Yukihime-kabu) (PubMed:27255930).
When the plant is infected by a compatible TuMV strain (UK1 m2), the down-regulation is transient and last two days (PubMed:27255930).
Induced by jasmonic acid (JA) and hydrogen peroxide H2O2 treatments (PubMed:27255930).

Interaction

Subunit

Dimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain33-140Plastocyanin-like 1
Domain154-317Plastocyanin-like 2
Domain426-543Plastocyanin-like 3

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    570
  • Mass (Da)
    63,250
  • Last updated
    2013-05-01 v1
  • Checksum
    92CB2E18AFA1CF20
MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM001635
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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