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Reviewed, UniProtKB/Swiss-Prot P18894 (OXDA_MOUSE)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    D-amino-acid oxidase
      Short name=DAMOX
      Short name=DAAO
      Short name=DAO
    EC=1.4.3.3
Gene names
Name: Dao
Synonyms: Dao1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

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

Cofactor

FAD.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Ontologies

Keywords
   Cellular componentPeroxisome
   Coding sequence diversityPolymorphism
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processleucine metabolic process

Inferred from mutant phenotype. Source: MGI

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345D-amino-acid oxidase
PRO_0000162762

Regions

Nucleotide binding3 – 1715FAD By similarity
Nucleotide binding36 – 372FAD By similarity
Nucleotide binding43 – 442FAD By similarity
Nucleotide binding48 – 503FAD By similarity
Nucleotide binding310 – 3145FAD By similarity
Motif343 – 3453Microbody targeting signal

Sites

Binding site521Substrate By similarity
Binding site1631FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1801FAD By similarity
Binding site2151Substrate By similarity
Binding site2261Substrate By similarity
Binding site2811Substrate By similarity
Binding site3111Substrate; via carbonyl oxygen By similarity
Binding site3151FAD By similarity

Natural variations

Natural variant1811G → R Abolishes activity. Ref.2

Experimental info

Sequence conflict641A → V in AAA39367. Ref.1
Sequence conflict641A → V in BAA01063. Ref.2
Sequence conflict1571K → N in BAA01062. Ref.2
Sequence conflict1711R → RG in BAA01062. Ref.2
Sequence conflict2961H → F in AAA39367. Ref.1
Sequence conflict2961H → F in BAA01062. Ref.2
Sequence conflict2961H → F in BAA01063. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P18894-1 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: 29A5D9B55D64700F

FASTA34538,661
        10         20         30         40         50         60 
MRVAVIGAGV IGLSTALCIH ERYHPTQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN 

        70         80         90        100        110        120 
PQEAEWSQQT FDYLLSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKNAV LGFRKLTPSE 

       130        140        150        160        170        180 
MDLFPDYGYG WFNTSLLLEG KSYLPWLTER LTERGVKLIH RKVESLEEVA RGVDVIINCT 

       190        200        210        220        230        240 
GVWAGALQAD ASLQPGRGQI IQVEAPWIKH FILTHDPSLG IYNSPYIIPG SKTVTLGGIF 

       250        260        270        280        290        300 
QLGNWSGLNS VRDHNTIWKS CCKLEPTLKN ARIVGELTGF RPVRPQVRLE REWLRHGSSS 

       310        320        330        340 
AEVIHNYGHG GYGLTIHWGC AMEAANLFGK ILEEKKLSRL PPSHL

« Hide

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References

« Hide 'large scale' references
[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: 1976103] [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: 1355365] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00115604.
PIRJH0185.
RefSeqNP_034148.2.
UniGeneMm.20115

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DXOmodel-@1-336[»]
SMRP18894. Positions 1-339.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000042096. Mus musculus. [Contig view]
GeneID13142.
KEGGmmu:13142.

Organism-specific databases

MGIMGI:94859. Dao.

Phylogenomic databases

HOGENOMP18894.
HOVERGENP18894.

Enzyme and pathway databases

BRENDA1.4.3.3. 244.

Gene expression databases

BgeeP18894.
CleanExMM_DAO1.
GermOnlineENSMUSG00000042096. Mus musculus.

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio283222.
SOURCESearch...

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Entry information

Entry nameOXDA_MOUSE
AccessionPrimary (citable) accession number: P18894
Secondary accession number(s): Q64465, Q8VCW7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 29, 2008
Last modified: June 16, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents