Ddo
entrez
70503
canonical
uniprot
Q922Z0
canonical
ensembl
ENSMUSG00000063428
resolver
ensp
ENSMUSP00000019977
resolver
ensp
ENSMUSP00000149767
resolver
ensp
ENSMUSP00000149768
resolver
ensp
ENSMUSP00000150979
resolver
ensp
ENSMUSP00000151066
resolver
ensp
ENSMUSP00000273045
resolver
ensp
ENSMUSP00000273053
resolver
ensp
ENSMUSP00000273055
resolver
enst
ENSMUST00000213442
resolver
enst
ENSMUST00000213503
resolver
enst
ENSMUST00000214102
resolver
genesymbol
Ddo
resolver
uniprot
A0A1L1SS55
resolver
uniprot
A0A1L1SS65
resolver
uniprot
A0A1L1SV87
resolver
uniprot
Q0E9Q7
resolver
uniprot
Q2UVA9
resolver
uniprot
Q3TT69
resolver
uniprot
Q8R2R2
resolver
uniprot
Q9CYP3
resolver
uniprot
Q9D2B4
resolver
uniprot_entry
A0A1L1SS55_MOUSE
resolver
uniprot_entry
A0A1L1SS65_MOUSE
resolver
uniprot_entry
A0A1L1SV87_MOUSE
resolver
uniprot_entry
OXDD_MOUSE
resolver
uniprot_entry
Q9CYP3_MOUSE
resolver
uniprot_entry
Q9D2B4_MOUSE
resolver
uniprot_sec
Q0E9Q7
resolver
uniprot_sec
Q2UVA9
resolver
uniprot_sec
Q3TT69
resolver
uniprot_sec
Q8R2R2
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the benzodiazepine olanzapine; chronic systemic administration of the benzodiazepine increases levels of D-aspartate and L-glutamate in the prefrontal cortex (PubMed:28393897). Efficiently inhibited by 5-aminonicotinic acid (5-AN) and 1,4-Dihydropyrido[2,3-b]pyrazine-2,3-dione (DPPD) (PubMed:32553892). Inhibited by aminooxyacetic acid, thiolactomycin, anthranilic acid, malonate, meso-tartrate and L-tartrate (PubMed:17469229, PubMed:20567862, PubMed:20603179, PubMed:25747990). Benzoate has no effect on activity (PubMed:17469229, PubMed:20567862). {ECO:0000269|PubMed:17469229, ECO:0000269|PubMed:20567862, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:28393897, ECO:0000269|PubMed:32553892}.
uniprot
proteins
amino_acid_sequence
MDTVCIAVVGAGVIGLSTAACISQLVPGCTVTVISDRFTPDTTSNVAAGMLIPHTCADTPVPTQKRWFRETFEHLSEIAKSAEAADAGVHLVSGWQIFRSVPAEEVPFWADVVLGFRKMTEAELKRFPQYVFGQAFTTLKCETSAYLPWLERRIKGSGGLLLTRRIEDLWELQPSFDIVVNCSGLGSRRLVGDPMISPVRGQVLQARAPWVKHFIRDGGGLTYVYPGMSYVTLGGTRQKGDWNRSPDAELSREIFSRCCTLEPSLHRAYDIKEKVGLRPSRPGVRLQKEILVRGQQTLPVVHNYGHGSGGISVHWGSALEATRLVMECIHTLRTPASLSKL
uniprot
proteins
ec_number
1.4.3.1
uniprot
proteins
function
FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:17469229, PubMed:18235994, PubMed:20567862, PubMed:20603179, PubMed:25747990, PubMed:26058797, PubMed:26961959, PubMed:28393897, PubMed:29292239, PubMed:32185508, PubMed:32553892, PubMed:37189369). Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (PubMed:26961959, PubMed:32185508, PubMed:35915065). Protects the organism from the toxicity of D-amino acids (By similarity). May also function in the intestine (PubMed:35915065). {ECO:0000250|UniProtKB:D3ZDM7, ECO:0000269|PubMed:17469229, ECO:0000269|PubMed:18235994, ECO:0000269|PubMed:20567862, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:26058797, ECO:0000269|PubMed:26961959, ECO:0000269|PubMed:28393897, ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32185508, ECO:0000269|PubMed:32553892, ECO:0000269|PubMed:35915065, ECO:0000269|PubMed:37189369}.; FUNCTION: [Isoform 1]: Selectively catalyzes the oxidative deamination of acidic amino acids. {ECO:0000269|PubMed:16516413}.; FUNCTION: [Isoform 2]: Does not exhibit D-aspartate oxidase activity. {ECO:0000269|PubMed:16516413}.
uniprot
proteins
mass_dalton
37546
uniprot
proteins
mutagenesis
MUTAGEN 216; /note="R->A,E,M: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:17469229"; MUTAGEN 216; /note="R->L: Decreases catalytic activity. Alters substrate specificity; when associated with Y-237."; /evidence="ECO:0000269|PubMed:17469229, ECO:0000269|PubMed:20567862"; MUTAGEN 237; /note="R->A: Resistance to thiolactomycin."; /evidence="ECO:0000269|PubMed:20603179"; MUTAGEN 237; /note="R->E,A,Y: Decreases catalytic activity."; /evidence="ECO:0000269|PubMed:17469229, ECO:0000269|PubMed:20567862, ECO:0000269|PubMed:20603179"; MUTAGEN 237; /note="R->Y: Alters substrate specificity; when associated with L-216."; /evidence="ECO:0000269|PubMed:20567862"; MUTAGEN 308; /note="S->G,A: Increases catalytic activity and FAD binding."; /evidence="ECO:0000269|PubMed:18235994"; MUTAGEN 308; /note="S->Y: Decreases catalytic activity and FAD binding."; /evidence="ECO:0000269|PubMed:18235994
uniprot
proteins
protein_family
DAMOX/DASOX family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16516413
uniprot
proteins
pubmed
16525061
uniprot
proteins
pubmed
16725213
uniprot
proteins
pubmed
17469229
uniprot
proteins
pubmed
18235994
uniprot
proteins
pubmed
18314103
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20031274
uniprot
proteins
pubmed
20567862
uniprot
proteins
pubmed
20603179
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25689573
uniprot
proteins
pubmed
25747990
uniprot
proteins
pubmed
25771393
uniprot
proteins
pubmed
25979765
uniprot
proteins
pubmed
26058797
uniprot
proteins
pubmed
26658710
uniprot
proteins
pubmed
26707656
uniprot
proteins
pubmed
26961959
uniprot
proteins
pubmed
28393897
uniprot
proteins
pubmed
29292239
uniprot
proteins
pubmed
30822420
uniprot
proteins
pubmed
32185508
uniprot
proteins
pubmed
32553892
uniprot
proteins
pubmed
35915065
uniprot
proteins
pubmed
37189369
uniprot
proteins
pubmed
7903300
uniprot
proteins
sequence_length
341
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q99489}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99489}. Note=Active in the peroxisomal matrix. {ECO:0000250|UniProtKB:Q99489}.
uniprot
proteins