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Protein

D-amino-acid oxidase

Gene

Dao

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521SubstrateBy similarity
Binding sitei163 – 1631FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei180 – 1801FADBy similarity
Binding sitei215 – 2151SubstrateBy similarity
Binding sitei226 – 2261SubstrateBy similarity
Binding sitei281 – 2811SubstrateBy similarity
Binding sitei311 – 3111Substrate; via carbonyl oxygenBy similarity
Binding sitei315 – 3151FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi3 – 1715FADBy similarityAdd
BLAST
Nucleotide bindingi36 – 372FADBy similarity
Nucleotide bindingi43 – 442FADBy similarity
Nucleotide bindingi48 – 503FADBy similarity
Nucleotide bindingi310 – 3145FADBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • D-alanine catabolic process Source: UniProtKB
  • dopamine biosynthetic process Source: MGI
  • D-serine catabolic process Source: MGI
  • D-serine metabolic process Source: MGI
  • leucine metabolic process Source: MGI
  • proline catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.3. 3474.

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:Dao1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:94859. Dao.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2331068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345D-amino-acid oxidasePRO_0000162762Add
BLAST

Proteomic databases

MaxQBiP18894.
PaxDbiP18894.
PRIDEiP18894.

PTM databases

iPTMnetiP18894.

Expressioni

Gene expression databases

BgeeiP18894.
CleanExiMM_DAO1.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP18894. 2 interactions.
MINTiMINT-4105961.
STRINGi10090.ENSMUSP00000107911.

Chemistry

BindingDBiP18894.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DXOmodel-@1-336[»]
ProteinModelPortaliP18894.
SMRiP18894. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi343 – 3453Microbody targeting signal

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiP18894.
KOiK00273.
OrthoDBiEOG7B31NB.
PhylomeDBiP18894.
TreeFamiTF313887.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 1 hit.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVAVIGAGV IGLSTALCIH ERYHPTQPLH MKIYADRFTP FTTSDVAAGL
60 70 80 90 100
WQPYLSDPSN PQEAEWSQQT FDYLLSCLHS PNAEKMGLAL ISGYNLFRDE
110 120 130 140 150
VPDPFWKNAV LGFRKLTPSE MDLFPDYGYG WFNTSLLLEG KSYLPWLTER
160 170 180 190 200
LTERGVKLIH RKVESLEEVA RGVDVIINCT GVWAGALQAD ASLQPGRGQI
210 220 230 240 250
IQVEAPWIKH FILTHDPSLG IYNSPYIIPG SKTVTLGGIF QLGNWSGLNS
260 270 280 290 300
VRDHNTIWKS CCKLEPTLKN ARIVGELTGF RPVRPQVRLE REWLRHGSSS
310 320 330 340
AEVIHNYGHG GYGLTIHWGC AMEAANLFGK ILEEKKLSRL PPSHL
Length:345
Mass (Da):38,661
Last modified:April 29, 2008 - v3
Checksum:i29A5D9B55D64700F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641A → V in AAA39367 (PubMed:1976103).Curated
Sequence conflicti64 – 641A → V in BAA01063 (PubMed:1355365).Curated
Sequence conflicti157 – 1571K → N in BAA01062 (PubMed:1355365).Curated
Sequence conflicti171 – 1711R → RG in BAA01062 (PubMed:1355365).Curated
Sequence conflicti296 – 2961H → F in AAA39367 (PubMed:1976103).Curated
Sequence conflicti296 – 2961H → F in BAA01062 (PubMed:1355365).Curated
Sequence conflicti296 – 2961H → F in BAA01063 (PubMed:1355365).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811G → R Abolishes activity. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32299 mRNA. Translation: AAA39367.1.
D10210 mRNA. Translation: BAA01062.1.
D10211 mRNA. Translation: BAA01063.1.
AK134813 mRNA. Translation: BAE22296.1.
BC018377 mRNA. Translation: AAH18377.1.
CCDSiCCDS19557.1.
PIRiJH0185.
RefSeqiNP_001273325.1. NM_001286396.1.
NP_034148.2. NM_010018.3.
XP_006530224.1. XM_006530161.2.
XP_006530225.1. XM_006530162.2.
UniGeneiMm.20115.

Genome annotation databases

GeneIDi13142.
KEGGimmu:13142.
UCSCiuc008yza.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32299 mRNA. Translation: AAA39367.1.
D10210 mRNA. Translation: BAA01062.1.
D10211 mRNA. Translation: BAA01063.1.
AK134813 mRNA. Translation: BAE22296.1.
BC018377 mRNA. Translation: AAH18377.1.
CCDSiCCDS19557.1.
PIRiJH0185.
RefSeqiNP_001273325.1. NM_001286396.1.
NP_034148.2. NM_010018.3.
XP_006530224.1. XM_006530161.2.
XP_006530225.1. XM_006530162.2.
UniGeneiMm.20115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DXOmodel-@1-336[»]
ProteinModelPortaliP18894.
SMRiP18894. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18894. 2 interactions.
MINTiMINT-4105961.
STRINGi10090.ENSMUSP00000107911.

Chemistry

BindingDBiP18894.
ChEMBLiCHEMBL2331068.

PTM databases

iPTMnetiP18894.

Proteomic databases

MaxQBiP18894.
PaxDbiP18894.
PRIDEiP18894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13142.
KEGGimmu:13142.
UCSCiuc008yza.2. mouse.

Organism-specific databases

CTDi1610.
MGIiMGI:94859. Dao.

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiP18894.
KOiK00273.
OrthoDBiEOG7B31NB.
PhylomeDBiP18894.
TreeFamiTF313887.

Enzyme and pathway databases

BRENDAi1.4.3.3. 3474.

Miscellaneous databases

NextBioi283222.
PROiP18894.
SOURCEiSearch...

Gene expression databases

BgeeiP18894.
CleanExiMM_DAO1.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 1 hit.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cDNA encoding mouse kidney D-amino acid oxidase."
    Tada M., Fukui K., Momoi K., Miyake Y.
    Gene 90:293-297(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "A single-base-pair substitution abolishes D-amino-acid oxidase activity in the mouse."
    Sasaki M., Konno R., Nishio M., Niwa A., Yasumura Y., Enami J.
    Biochim. Biophys. Acta 1139:315-318(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF VARIANT ARG-181.
    Tissue: Kidney.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Kidney.

Entry informationi

Entry nameiOXDA_MOUSE
AccessioniPrimary (citable) accession number: P18894
Secondary accession number(s): Q64465, Q8VCW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 29, 2008
Last modified: January 20, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.