DAO
entrez
1610
canonical
uniprot
P14920
canonical
ensembl
ENSG00000110887
resolver
ensp
ENSP00000228476
resolver
ensp
ENSP00000573611
resolver
ensp
ENSP00000573623
resolver
ensp
ENSP00000643670
resolver
enst
ENST00000228476
resolver
genesymbol
DAO
resolver
genesymbol_syn
DAMOX
resolver
hgnc
HGNC:2671
resolver
uniprot
A0A024RBI1
resolver
uniprot
A0A0S2Z3J4
resolver
uniprot
B2R7I5
resolver
uniprot
Q16758
resolver
uniprot
Q8N6R2
resolver
uniprot_entry
A0A024RBI1_HUMAN
resolver
uniprot_entry
A0A0S2Z3J4_HUMAN
resolver
uniprot_entry
OXDA_HUMAN
resolver
uniprot_sec
B2R7I5
resolver
uniprot_sec
Q16758
resolver
uniprot_sec
Q8N6R2
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by benzoate, crotonate, thiolactomycin, chlorpromazine (CPZ), risperidone, haloperidol, sulpiride, aripiprazole, blonanserin, quetiapine, 4H-furo[3,2-b]pyrrole-5-carboxylic acid, and the substrate analog CF3-D-ala (3,3,3-trifluoro-D-alanine) (PubMed:18544534, PubMed:20521334, PubMed:20567862, PubMed:20603179, PubMed:23391306, PubMed:23631755, PubMed:25030849, PubMed:32730563). Inhibited by luvadaxistat, and 6-chloro-1,2-benzisoxazol-3(2H)-one (CBIO) (PubMed:33484270, PubMed:37289348). Also inhibited by 3-methylpyrazole-5-carboxylic acid (MPC), 3-hydroxyquinolin-2(1h)-one, 3-hydroxy-5-(2-phenylethyl)pyridin-2(1h)-one, 3-hydroxy-6-(2-phenylethyl)pyridazin-4(1h)-one, 4h-thieno[3,2-B]pyrole-5-carboxylic acid, 4-(4-chlorophenethyl)-1h-pyrrole-2-carboxylic acid, 3-phenethyl-4h-furo[3,2-B]pyrrole-5-carboxylic acid, 3-hydroxy-2h-chromen-2-one, 4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2h-chromen-6-Yl)ethyl]pyridazin-3(2h)-one, 3-(7-hydroxy-2-oxo-4-phenyl-2h-chromen-6-Yl)propanoic acid, 5-chloro thiophene-3-carboxylic acid, 5-chloro thiophene-2-carboxylic acid, (3r)-3-(5,6-Dioxo-1,4,5,6-Tetrahydropyrazin-2-Yl)-2,3-dihydro-1,4-benzoxathiine-7-carbonitrile and 5-{2-[4-(trifluoromethyl)phenyl]ethyl}-1,4-dihydropyrazine-2,3-dione (PubMed:19438227, PubMed:23566269, PubMed:23631755, PubMed:25001371, PubMed:25030849, PubMed:30265959, PubMed:35482677). Meso-tartrate, valproate, duloxetine, eschitalopram, sertraline, biperiden, trihexyphenidyl and olanzapine have no effect on activity (PubMed:20567862, PubMed:25030849). {ECO:0000269|PubMed:18544534, ECO:0000269|PubMed:19438227, ECO:0000269|PubMed:20521334, ECO:0000269|PubMed:20567862, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:23391306, ECO:0000269|PubMed:23566269, ECO:0000269|PubMed:23631755, ECO:0000269|PubMed:25001371, ECO:0000269|PubMed:25030849, ECO:0000269|PubMed:30265959, ECO:0000269|PubMed:32730563, ECO:0000269|PubMed:33484270, ECO:0000269|PubMed:35482677, ECO:0000269|PubMed:37289348}.
uniprot
proteins
amino_acid_sequence
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
uniprot
proteins
disease_involvement
DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:12364586}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:20368421, ECO:0000269|PubMed:20538972, ECO:0000269|PubMed:22203986, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:24138986, ECO:0000269|PubMed:25701391, ECO:0000269|PubMed:37558109, ECO:0000269|PubMed:38035964, ECO:0000269|PubMed:38134563}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.4.3.3
uniprot
proteins
function
FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:16616139, PubMed:17088322, PubMed:17303072, PubMed:18544534, PubMed:20368421, PubMed:20567862, PubMed:20603179, PubMed:22203986, PubMed:23219954, PubMed:23391306, PubMed:25030849, PubMed:25701391, PubMed:29274788, PubMed:29326945, PubMed:30938755, PubMed:31799256, PubMed:32730563, PubMed:33484270, PubMed:34041270, PubMed:37558109, PubMed:38035964). Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients (By similarity). Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission (PubMed:17303072). Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway (PubMed:17303072). Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor (By similarity). The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine (By similarity). Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage (PubMed:30659069). Could act as a detoxifying agent which removes D-amino acids accumulated during aging (PubMed:17303072). {ECO:0000250|UniProtKB:P18894, ECO:0000269|PubMed:16616139, ECO:0000269|PubMed:17088322, ECO:0000269|PubMed:17303072, ECO:0000269|PubMed:18544534, ECO:0000269|PubMed:20368421, ECO:0000269|PubMed:20567862, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:22203986, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:23391306, ECO:0000269|PubMed:25030849, ECO:0000269|PubMed:25701391, ECO:0000269|PubMed:29274788, ECO:0000269|PubMed:29326945, ECO:0000269|PubMed:30659069, ECO:0000269|PubMed:30938755, ECO:0000269|PubMed:31799256, ECO:0000269|PubMed:32730563, ECO:0000269|PubMed:33484270, ECO:0000269|PubMed:34041270, ECO:0000269|PubMed:37558109, ECO:0000269|PubMed:38035964}.
uniprot
proteins
mass_dalton
39474
uniprot
proteins
mutagenesis
MUTAGEN 31; /note="D->H: Increases affinity for the FAD cofactor and D-serine. Decreases the cellular ratio of D-serine to L-serine."; /evidence="ECO:0000269|PubMed:23219954"; MUTAGEN 120; /note="R->E,L: Increases activity and FAD-binding. Decreases protein localization to peroxisomes with protein mislocalized to the nucleus and cytosol."; /evidence="ECO:0000269|PubMed:31799256"; MUTAGEN 183; /note="G->R: Abolishes activity. Impairs the ability to bind the FAD cofactor. Impairs targeting to peroxisomes and results in abnormal peroxisomal morphology. Leads to the formation of ubiquitinated protein aggregates and the induction of apoptosis."; /evidence="ECO:0000269|PubMed:24138986, ECO:0000269|PubMed:29274788"; MUTAGEN 219; /note="P->L: Increases catalytic efficiency and inhibition by benzoate."; /evidence="ECO:0000269|PubMed:32730563"; MUTAGEN 224; /note="Y->F: Decreases activity."; /evidence="ECO:0000269|PubMed:23391306"; MUTAGEN 279; /note="R->A: Increases affinity for the FAD cofactor and D-serine. Decreases the cellular ratio of D-serine to L-serine."; /evidence="ECO:0000269|PubMed:23219954
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in the cerebellum; probably not by PRKACA, PRKCA or PRKCE. {ECO:0000269|PubMed:34041270}.; PTM: May be S-nitrosylated, which partially inactivates the enzyme. {ECO:0000269|PubMed:34041270}.
uniprot
proteins
protein_family
DAMOX/DASOX family
uniprot
proteins
pubmed
12364586
uniprot
proteins
pubmed
1356107
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16616139
uniprot
proteins
pubmed
17088322
uniprot
proteins
pubmed
17303072
uniprot
proteins
pubmed
17684499
uniprot
proteins
pubmed
17880399
uniprot
proteins
pubmed
18455394
uniprot
proteins
pubmed
18544534
uniprot
proteins
pubmed
18560437
uniprot
proteins
pubmed
19438227
uniprot
proteins
pubmed
20368421
uniprot
proteins
pubmed
20521334
uniprot
proteins
pubmed
20538972
uniprot
proteins
pubmed
20567862
uniprot
proteins
pubmed
20603179
uniprot
proteins
pubmed
21679769
uniprot
proteins
pubmed
22203986
uniprot
proteins
pubmed
23219954
uniprot
proteins
pubmed
23391306
uniprot
proteins
pubmed
23566269
uniprot
proteins
pubmed
23631755
uniprot
proteins
pubmed
24138986
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24362575
uniprot
proteins
pubmed
25001371
uniprot
proteins
pubmed
25030849
uniprot
proteins
pubmed
25701391
uniprot
proteins
pubmed
27670111
uniprot
proteins
pubmed
28629864
uniprot
proteins
pubmed
2901986
uniprot
proteins
pubmed
29274788
uniprot
proteins
pubmed
29326945
uniprot
proteins
pubmed
30265959
uniprot
proteins
pubmed
30659069
uniprot
proteins
pubmed
30938755
uniprot
proteins
pubmed
31799256
uniprot
proteins
pubmed
32730563
uniprot
proteins
pubmed
33484270
uniprot
proteins
pubmed
34041270
uniprot
proteins
pubmed
35482677
uniprot
proteins
pubmed
37289348
uniprot
proteins
pubmed
37440119
uniprot
proteins
pubmed
37558109
uniprot
proteins
pubmed
38035964
uniprot
proteins
pubmed
38134563
uniprot
proteins
sequence_length
347
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:18544534, ECO:0000269|PubMed:20368421, ECO:0000269|PubMed:21679769, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:31799256, ECO:0000305|PubMed:17880399, ECO:0000305|PubMed:29274788}. Cytoplasm, cytosol {ECO:0000269|PubMed:18544534, ECO:0000269|PubMed:21679769, ECO:0000269|PubMed:31799256}. Presynaptic active zone {ECO:0000250|UniProtKB:O35078}. Secreted {ECO:0000269|PubMed:27670111}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (PubMed:21679769, PubMed:31799256). In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (By similarity). Secreted into the lumen of the small intestine (PubMed:27670111). {ECO:0000250|UniProtKB:O35078, ECO:0000269|PubMed:21679769, ECO:0000269|PubMed:27670111, ECO:0000269|PubMed:31799256}.
uniprot
proteins