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Protein

D-amino-acid oxidase

Gene

DAO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.1 Publication

Catalytic activityi

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

Kineticsi

  1. KM=3.6 mM for D-serine2 Publications
  2. KM=1.7 mM for D-proline2 Publications
  3. KM=1.1 mM for D-tyrosine2 Publications
  4. KM=1.5 mM for D-DOPA2 Publications
  5. KM=1.2 mM for D-phenylalanine2 Publications
  6. KM=0.9 mM for D-alanine2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei53Substrate1
    Binding sitei164FAD; via amide nitrogen and carbonyl oxygen2 Publications1
    Binding sitei182FAD2 Publications1
    Binding sitei217Substrate1
    Binding sitei228Substrate1
    Binding sitei283Substrate1
    Binding sitei313Substrate; via carbonyl oxygen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi3 – 17FAD2 PublicationsAdd BLAST15
    Nucleotide bindingi37 – 38FAD2 Publications2
    Nucleotide bindingi44 – 45FAD2 Publications2
    Nucleotide bindingi49 – 51FAD2 Publications3
    Nucleotide bindingi312 – 317FAD2 Publications6

    GO - Molecular functioni

    • cofactor binding Source: UniProtKB
    • D-amino-acid oxidase activity Source: UniProtKB
    • FAD binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • signaling receptor binding Source: UniProtKB

    GO - Biological processi

    • cellular nitrogen compound metabolic process Source: Reactome
    • D-alanine catabolic process Source: UniProtKB
    • dopamine biosynthetic process Source: UniProtKB
    • D-serine catabolic process Source: UniProtKB
    • D-serine metabolic process Source: UniProtKB
    • proline catabolic process Source: UniProtKB
    • protein targeting to peroxisome Source: Reactome

    Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03351-MONOMER
    BRENDAi1.4.3.3 2681
    ReactomeiR-HSA-389661 Glyoxylate metabolism and glycine degradation
    R-HSA-9033241 Peroxisomal protein import

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-amino-acid oxidase (EC:1.4.3.3)
    Short name:
    DAAO
    Short name:
    DAMOX
    Short name:
    DAO
    Gene namesi
    Name:DAO
    Synonyms:DAMOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000110887.7
    HGNCiHGNC:2671 DAO
    MIMi124050 gene
    neXtProtiNX_P14920

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Schizophrenia (SCZD)1 Publication
    Disease susceptibility may be associated with variations affecting the gene represented in this entry.
    Disease descriptionA 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.
    See also OMIM:181500

    Keywords - Diseasei

    Schizophrenia

    Organism-specific databases

    DisGeNETi1610
    MalaCardsiDAO
    MIMi181500 phenotype
    OpenTargetsiENSG00000110887
    Orphaneti803 Amyotrophic lateral sclerosis
    PharmGKBiPA27139

    Chemistry databases

    ChEMBLiCHEMBL5485
    DrugBankiDB04166 2-Aminobenzoic Acid
    DB03793 Benzoic Acid
    DB03225 D-Tryptophan
    DB03147 Flavin adenine dinucleotide
    DB03531 Flavin-Adenine Dinucleotide-N5-Isobutyl Ketone
    DB02988 Imino-Tryptophan

    Polymorphism and mutation databases

    BioMutaiDAO
    DMDMi25453448

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001627611 – 347D-amino-acid oxidaseAdd BLAST347

    Proteomic databases

    PaxDbiP14920
    PeptideAtlasiP14920
    PRIDEiP14920
    ProteomicsDBi53094
    TopDownProteomicsiP14920

    PTM databases

    iPTMnetiP14920
    PhosphoSitePlusiP14920

    Expressioni

    Gene expression databases

    BgeeiENSG00000110887
    CleanExiHS_DAO
    ExpressionAtlasiP14920 baseline and differential
    GenevisibleiP14920 HS

    Organism-specific databases

    HPAiHPA038653
    HPA038654

    Interactioni

    Subunit structurei

    Homodimer (PubMed:17088322, PubMed:18455394). Interacts with DAOA (PubMed:12364586).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKAB2O437414EBI-3908043,EBI-1053424

    GO - Molecular functioni

    • protein dimerization activity Source: UniProtKB
    • signaling receptor binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi107980, 7 interactors
    IntActiP14920, 2 interactors
    STRINGi9606.ENSP00000228476

    Chemistry databases

    BindingDBiP14920

    Structurei

    Secondary structure

    1347
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi10 – 23Combined sources14
    Beta strandi25 – 28Combined sources4
    Beta strandi31 – 37Combined sources7
    Helixi40 – 42Combined sources3
    Helixi44 – 47Combined sources4
    Helixi63 – 77Combined sources15
    Turni78 – 80Combined sources3
    Helixi84 – 87Combined sources4
    Beta strandi89 – 100Combined sources12
    Turni106 – 110Combined sources5
    Beta strandi111 – 116Combined sources6
    Helixi119 – 122Combined sources4
    Beta strandi129 – 139Combined sources11
    Helixi141 – 154Combined sources14
    Beta strandi158 – 161Combined sources4
    Helixi167 – 172Combined sources6
    Beta strandi176 – 180Combined sources5
    Helixi183 – 188Combined sources6
    Beta strandi196 – 206Combined sources11
    Beta strandi212 – 216Combined sources5
    Turni219 – 221Combined sources3
    Beta strandi228 – 231Combined sources4
    Beta strandi233 – 239Combined sources7
    Helixi253 – 266Combined sources14
    Helixi268 – 272Combined sources5
    Beta strandi274 – 285Combined sources12
    Beta strandi290 – 296Combined sources7
    Beta strandi298 – 301Combined sources4
    Beta strandi303 – 309Combined sources7
    Helixi312 – 314Combined sources3
    Helixi315 – 336Combined sources22

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DU8X-ray2.50A/B/G/J1-347[»]
    2E48X-ray2.90A/B/C/D1-347[»]
    2E49X-ray3.20A/B/C/D1-347[»]
    2E4AX-ray2.60A/B/C/D1-347[»]
    2E82X-ray2.70A/B/C/D1-347[»]
    2GNZmodel-A1-339[»]
    3CUKX-ray2.49A/B/C/D1-347[»]
    3G3EX-ray2.20A/B/C/D1-347[»]
    3W4IX-ray2.50A/B/C/D1-347[»]
    3W4JX-ray2.74A/B/C/D1-347[»]
    3W4KX-ray2.86A/B/C/D1-347[»]
    3ZNNX-ray1.90A/B1-347[»]
    3ZNOX-ray2.30A/B1-347[»]
    3ZNPX-ray2.40A/B1-347[»]
    3ZNQX-ray2.75A/B1-347[»]
    4QFCX-ray2.40A/B1-347[»]
    4QFDX-ray2.85A/B1-347[»]
    ProteinModelPortaliP14920
    SMRiP14920
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14920

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi345 – 347Microbody targeting signal3

    Sequence similaritiesi

    Belongs to the DAMOX/DASOX family.Curated

    Phylogenomic databases

    eggNOGiKOG3923 Eukaryota
    COG0665 LUCA
    GeneTreeiENSGT00390000018635
    HOGENOMiHOG000046303
    HOVERGENiHBG003493
    InParanoidiP14920
    KOiK00273
    OMAiTEVIHNY
    OrthoDBiEOG091G0G0Y
    PhylomeDBiP14920
    TreeFamiTF313887

    Family and domain databases

    InterProiView protein in InterPro
    IPR006181 D-amino_acid_oxidase_CS
    IPR023209 DAO
    IPR006076 FAD-dep_OxRdtase
    PANTHERiPTHR11530 PTHR11530, 1 hit
    PfamiView protein in Pfam
    PF01266 DAO, 1 hit
    PIRSFiPIRSF000189 D-aa_oxidase, 1 hit
    PROSITEiView protein in PROSITE
    PS00677 DAO, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P14920-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG
    60 70 80 90 100
    LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE
    110 120 130 140 150
    AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE
    160 170 180 190 200
    RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG
    210 220 230 240 250
    QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL
    260 270 280 290 300
    NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP
    310 320 330 340
    SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL
    Length:347
    Mass (Da):39,474
    Last modified:November 25, 2002 - v3
    Checksum:iA508E603872F3072
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti31D → H in CAA31614 (PubMed:2901986).Curated1
    Sequence conflicti279R → A in CAA31614 (PubMed:2901986).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13227 mRNA Translation: CAA31614.1
    AK312995 mRNA Translation: BAG35832.1
    CH471054 Genomic DNA Translation: EAW97837.1
    BC029057 mRNA Translation: AAH29057.1
    BC074770 mRNA Translation: AAH74770.1
    D11370 Genomic DNA Translation: BAA20974.1
    CCDSiCCDS9122.1
    PIRiS01340
    RefSeqiNP_001908.3, NM_001917.4
    XP_011536306.1, XM_011538004.2
    XP_011536307.1, XM_011538005.2
    UniGeneiHs.113227

    Genome annotation databases

    EnsembliENST00000228476; ENSP00000228476; ENSG00000110887
    GeneIDi1610
    KEGGihsa:1610
    UCSCiuc001tnr.5 human

    Similar proteinsi

    Entry informationi

    Entry nameiOXDA_HUMAN
    AccessioniPrimary (citable) accession number: P14920
    Secondary accession number(s): B2R7I5, Q16758, Q8N6R2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 25, 2002
    Last modified: June 20, 2018
    This is version 177 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

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