Reviewed, UniProtKB/Swiss-Prot Q922Z0 (OXDD_MOUSE)

Names and origin

Protein names

Recommended name:
    D-aspartate oxidase
      Short name=DASOX
    EC=1.4.3.1
Alternative name(s):
    DDO

Gene names

Name:

Ddo

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate By similarity.
Catalytic activity	D-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2).
Cofactor	FAD or 6-hydroxyflavin adenine dinucleotide By similarity.
Subcellular location	PeroxisomeBy similarity.
Sequence similarities	Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	aspartate metabolic process Inferred from mutant phenotype. Source: MGI grooming behavior Inferred from mutant phenotype. Source: MGI hormone metabolic process Inferred from mutant phenotype. Source: MGI insemination Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	D-aspartate oxidase		PRO_0000162771
Regions
	Nucleotide binding	6 – 20	15	FAD Potential
	Motif	339 – 341	3	Microbody targeting signal Potential
Sites
	Active site	223	1	By similarity
	Active site	302	1	By similarity
Experimental info
	Sequence conflict	56	1	C → Y in AAH27312. Ref.2
	Sequence conflict	67	1	W → C in AAH27312. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q922Z0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: A80BC74CC44A601D	FASTA	341	37,546
	10 20 30 40 50 60 MDTVCIAVVG AGVIGLSTAA CISQLVPGCT VTVISDRFTP DTTSNVAAGM LIPHTCADTP 70 80 90 100 110 120 VPTQKRWFRE TFEHLSEIAK SAEAADAGVH LVSGWQIFRS VPAEEVPFWA DVVLGFRKMT 130 140 150 160 170 180 EAELKRFPQY VFGQAFTTLK CETSAYLPWL ERRIKGSGGL LLTRRIEDLW ELQPSFDIVV 190 200 210 220 230 240 NCSGLGSRRL VGDPMISPVR GQVLQARAPW VKHFIRDGGG LTYVYPGMSY VTLGGTRQKG 250 260 270 280 290 300 DWNRSPDAEL SREIFSRCCT LEPSLHRAYD IKEKVGLRPS RPGVRLQKEI LVRGQQTLPV 310 320 330 340 VHNYGHGSGG ISVHWGSALE ATRLVMECIH TLRTPASLSK L

References

[1]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart, Lung and Pituitary.
[2]	"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: Czech II and FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK033375 mRNA. Translation: BAC28253.1. AK085947 mRNA. Translation: BAC39577.1. AK161548 mRNA. Translation: BAE36456.1. BC006690 mRNA. Translation: AAH06690.1. BC027312 mRNA. Translation: AAH27312.1.
RefSeq	NP_081718.2.
UniGene	Mm.252862
3D structure databases
HSSP	HSSP built from PDB template 1VE9 based on UniProtKB P00371.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000063428. Mus musculus. [Contig view]
GeneID	70503.
KEGG	mmu:70503.
Organism-specific databases
MGI	MGI:1925528. Ddo.
Phylogenomic databases
HOGENOM	Q922Z0.
HOVERGEN	Q922Z0.
Gene expression databases
ArrayExpress	Q922Z0.
CleanEx	MM_DDO.
GermOnline	ENSMUSG00000063428. Mus musculus.
Family and domain databases
InterPro	IPR006181. D-amino_acid_oxidase_CS. IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01266. DAO. 1 hit. [Graphical view]
PROSITE	PS00677. DAO. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	331757.
SOURCE	Search...

Entry information

Entry name

OXDD_MOUSE

Accession

Primary (citable) accession number: Q922Z0
Secondary accession number(s): Q3TT69, Q8R2R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	December 1, 2001
Last modified:	November 25, 2008
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)