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Protein

D-aspartate oxidase

Gene

Ddo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.By similarity

Catalytic activityi

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.

Cofactori

FADBy similarity, 6-hydroxy-FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei166 – 1661FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei183 – 1831FADBy similarity
Binding sitei223 – 2231SubstrateBy similarity
Binding sitei278 – 2781SubstrateBy similarity
Binding sitei312 – 3121FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 2015FADBy similarityAdd
BLAST
Nucleotide bindingi36 – 372FADBy similarity
Nucleotide bindingi43 – 442FADBy similarity
Nucleotide bindingi48 – 503FADBy similarity
Nucleotide bindingi307 – 3115FADBy similarity

GO - Molecular functioni

  • cofactor binding Source: UniProtKB
  • D-aspartate oxidase activity Source: UniProtKB
  • FAD binding Source: InterPro
  • receptor binding Source: MGI

GO - Biological processi

  • aspartate catabolic process Source: MGI
  • aspartate metabolic process Source: MGI
  • D-amino acid catabolic process Source: UniProtKB
  • grooming behavior Source: MGI
  • hormone metabolic process Source: MGI
  • insemination Source: MGI
  • oxidation-reduction process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
D-aspartate oxidase (EC:1.4.3.1)
Short name:
DASOX
Short name:
DDO
Gene namesi
Name:Ddo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1925528. Ddo.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341D-aspartate oxidasePRO_0000162771Add
BLAST

Proteomic databases

MaxQBiQ922Z0.
PaxDbiQ922Z0.
PRIDEiQ922Z0.

PTM databases

PhosphoSiteiQ922Z0.

Expressioni

Gene expression databases

BgeeiQ922Z0.
CleanExiMM_DDO.
GenevisibleiQ922Z0. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019977.

Structurei

3D structure databases

ProteinModelPortaliQ922Z0.
SMRiQ922Z0. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi339 – 3413Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000018635.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiQ922Z0.
KOiK00272.
OMAiHVFGHAF.
OrthoDBiEOG7B31NB.
PhylomeDBiQ922Z0.
TreeFamiTF313887.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_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.

Q922Z0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTVCIAVVG AGVIGLSTAA CISQLVPGCT VTVISDRFTP DTTSNVAAGM
60 70 80 90 100
LIPHTCADTP VPTQKRWFRE TFEHLSEIAK SAEAADAGVH LVSGWQIFRS
110 120 130 140 150
VPAEEVPFWA DVVLGFRKMT EAELKRFPQY VFGQAFTTLK CETSAYLPWL
160 170 180 190 200
ERRIKGSGGL LLTRRIEDLW ELQPSFDIVV NCSGLGSRRL VGDPMISPVR
210 220 230 240 250
GQVLQARAPW VKHFIRDGGG LTYVYPGMSY VTLGGTRQKG DWNRSPDAEL
260 270 280 290 300
SREIFSRCCT LEPSLHRAYD IKEKVGLRPS RPGVRLQKEI LVRGQQTLPV
310 320 330 340
VHNYGHGSGG ISVHWGSALE ATRLVMECIH TLRTPASLSK L
Length:341
Mass (Da):37,546
Last modified:December 1, 2001 - v1
Checksum:iA80BC74CC44A601D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561C → Y in AAH27312 (PubMed:15489334).Curated
Sequence conflicti67 – 671W → C in AAH27312 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23798.1.
RefSeqiNP_001303645.1. NM_001316716.1.
NP_001303646.1. NM_001316717.1.
NP_001303647.1. NM_001316718.1.
NP_001303648.1. NM_001316719.1.
NP_081718.2. NM_027442.5.
UniGeneiMm.252862.

Genome annotation databases

EnsembliENSMUST00000019977; ENSMUSP00000019977; ENSMUSG00000063428.
GeneIDi70503.
KEGGimmu:70503.
UCSCiuc007exa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23798.1.
RefSeqiNP_001303645.1. NM_001316716.1.
NP_001303646.1. NM_001316717.1.
NP_001303647.1. NM_001316718.1.
NP_001303648.1. NM_001316719.1.
NP_081718.2. NM_027442.5.
UniGeneiMm.252862.

3D structure databases

ProteinModelPortaliQ922Z0.
SMRiQ922Z0. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019977.

PTM databases

PhosphoSiteiQ922Z0.

Proteomic databases

MaxQBiQ922Z0.
PaxDbiQ922Z0.
PRIDEiQ922Z0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019977; ENSMUSP00000019977; ENSMUSG00000063428.
GeneIDi70503.
KEGGimmu:70503.
UCSCiuc007exa.2. mouse.

Organism-specific databases

CTDi8528.
MGIiMGI:1925528. Ddo.

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000018635.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiQ922Z0.
KOiK00272.
OMAiHVFGHAF.
OrthoDBiEOG7B31NB.
PhylomeDBiQ922Z0.
TreeFamiTF313887.

Miscellaneous databases

NextBioi331757.
PROiQ922Z0.
SOURCEiSearch...

Gene expression databases

BgeeiQ922Z0.
CleanExiMM_DDO.
GenevisibleiQ922Z0. MM.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_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

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart and Kidney.

Entry informationi

Entry nameiOXDD_MOUSE
AccessioniPrimary (citable) accession number: Q922Z0
Secondary accession number(s): Q3TT69, Q8R2R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 1, 2001
Last modified: January 20, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.