OXDD_MOUSE
ID OXDD_MOUSE Reviewed; 341 AA.
AC Q922Z0; Q3TT69; Q8R2R2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=D-aspartate oxidase;
DE Short=DASOX;
DE Short=DDO;
DE EC=1.4.3.1;
GN Name=Ddo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D-
CC aspartate and its N-methylated derivative, N-methyl D-aspartate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29990; EC=1.4.3.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; AK033375; BAC28253.1; -; mRNA.
DR EMBL; AK085947; BAC39577.1; -; mRNA.
DR EMBL; AK161548; BAE36456.1; -; mRNA.
DR EMBL; BC006690; AAH06690.1; -; mRNA.
DR EMBL; BC027312; AAH27312.1; -; mRNA.
DR CCDS; CCDS23798.1; -.
DR RefSeq; NP_001303645.1; NM_001316716.1.
DR RefSeq; NP_001303646.1; NM_001316717.1.
DR RefSeq; NP_001303647.1; NM_001316718.1.
DR RefSeq; NP_001303648.1; NM_001316719.1.
DR RefSeq; NP_081718.2; NM_027442.5.
DR AlphaFoldDB; Q922Z0; -.
DR SMR; Q922Z0; -.
DR STRING; 10090.ENSMUSP00000019977; -.
DR BindingDB; Q922Z0; -.
DR ChEMBL; CHEMBL3616357; -.
DR iPTMnet; Q922Z0; -.
DR PhosphoSitePlus; Q922Z0; -.
DR MaxQB; Q922Z0; -.
DR PaxDb; Q922Z0; -.
DR PRIDE; Q922Z0; -.
DR ProteomicsDB; 294084; -.
DR Antibodypedia; 32325; 226 antibodies from 24 providers.
DR Ensembl; ENSMUST00000019977; ENSMUSP00000019977; ENSMUSG00000063428.
DR GeneID; 70503; -.
DR KEGG; mmu:70503; -.
DR UCSC; uc007exa.2; mouse.
DR CTD; 8528; -.
DR MGI; MGI:1925528; Ddo.
DR VEuPathDB; HostDB:ENSMUSG00000063428; -.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; Q922Z0; -.
DR OMA; MAIRERC; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; Q922Z0; -.
DR TreeFam; TF313887; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 70503; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ddo; mouse.
DR PRO; PR:Q922Z0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q922Z0; protein.
DR Bgee; ENSMUSG00000063428; Expressed in brain ependyma and 173 other tissues.
DR ExpressionAtlas; Q922Z0; baseline and differential.
DR Genevisible; Q922Z0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0008445; F:D-aspartate oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0006533; P:aspartate catabolic process; ISO:MGI.
DR GO; GO:0006531; P:aspartate metabolic process; IMP:MGI.
DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0007320; P:insemination; IMP:MGI.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; PTHR11530; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR PROSITE; PS00677; DAO; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..341
FT /note="D-aspartate oxidase"
FT /id="PRO_0000162771"
FT MOTIF 339..341
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 6..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307..311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 56
FT /note="C -> Y (in Ref. 2; AAH27312)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="W -> C (in Ref. 2; AAH27312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37546 MW; A80BC74CC44A601D CRC64;
MDTVCIAVVG AGVIGLSTAA CISQLVPGCT VTVISDRFTP DTTSNVAAGM LIPHTCADTP
VPTQKRWFRE TFEHLSEIAK SAEAADAGVH LVSGWQIFRS VPAEEVPFWA DVVLGFRKMT
EAELKRFPQY VFGQAFTTLK CETSAYLPWL ERRIKGSGGL LLTRRIEDLW ELQPSFDIVV
NCSGLGSRRL VGDPMISPVR GQVLQARAPW VKHFIRDGGG LTYVYPGMSY VTLGGTRQKG
DWNRSPDAEL SREIFSRCCT LEPSLHRAYD IKEKVGLRPS RPGVRLQKEI LVRGQQTLPV
VHNYGHGSGG ISVHWGSALE ATRLVMECIH TLRTPASLSK L
