M4DUF2 · ASO_BRARP
- ProteinL-ascorbate oxidase
- GeneAO
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids570 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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
- 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Cofactor
Note: Binds 4 Cu cations per monomer.
Pathway
Cofactor degradation; L-ascorbate degradation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 77 | Cu cation 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 79 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 121 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 123 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 463 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 466 | Cu cation 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 468 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 525 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 526 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 527 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 531 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 536 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | copper ion binding | |
Molecular Function | L-ascorbate oxidase activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | defense response | |
Biological Process | L-ascorbic acid catabolic process | |
Biological Process | negative regulation of defense response to virus | |
Biological Process | response to hydrogen peroxide | |
Biological Process | response to jasmonic acid | |
Biological Process | response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-ascorbate oxidase
- EC number
- Short namesAAO ; AO ; ASO ; Ascorbase
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionM4DUF2
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MGMWWIVAVAILAHTASA | ||||||
Chain | PRO_5004051517 | 19-570 | L-ascorbate oxidase | |||
Sequence: AVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP | ||||||
Disulfide bond | 36↔219 | |||||
Sequence: CKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQC | ||||||
Disulfide bond | 98↔557 | |||||
Sequence: CAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGC | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 196 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 197↔211 | |||||
Sequence: CSLAAQFSSTSLPTC | ||||||
Glycosylation | 229 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 343 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 384 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 407 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 434 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 442 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 458 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
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).
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
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-140 | Plastocyanin-like 1 | ||||
Sequence: WPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDV | ||||||
Domain | 154-317 | Plastocyanin-like 2 | ||||
Sequence: FNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYV | ||||||
Domain | 426-543 | Plastocyanin-like 3 | ||||
Sequence: RNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEG |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length570
- Mass (Da)63,250
- Last updated2013-05-01 v1
- Checksum92CB2E18AFA1CF20
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM001635 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |