OXDA_MOUSE
ID OXDA_MOUSE Reviewed; 345 AA.
AC P18894; Q64465; Q8VCW7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
GN Name=Dao; Synonyms=Dao1;
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 [MRNA].
RC TISSUE=Kidney;
RX PubMed=1976103; DOI=10.1016/0378-1119(90)90193-u;
RA Tada M., Fukui K., Momoi K., Miyake Y.;
RT "Cloning and expression of a cDNA encoding mouse kidney D-amino acid
RT oxidase.";
RL Gene 90:293-297(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION OF VARIANT ARG-181.
RC TISSUE=Kidney;
RX PubMed=1355365; DOI=10.1016/0925-4439(92)90107-x;
RA Sasaki M., Konno R., Nishio M., Niwa A., Yasumura Y., Enami J.;
RT "A single-base-pair substitution abolishes D-amino-acid oxidase activity in
RT the mouse.";
RL Biochim. Biophys. Acta 1139:315-318(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Regulates the level of the neuromodulator D-serine in the
CC brain. Has high activity towards D-DOPA and contributes to dopamine
CC synthesis. Could act as a detoxifying agent which removes D-amino acids
CC accumulated during aging. Acts on a variety of D-amino acids with a
CC preference for those having small hydrophobic side chains followed by
CC those bearing polar, aromatic, and basic groups. Does not act on acidic
CC amino acids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; EC=1.4.3.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; M32299; AAA39367.1; -; mRNA.
DR EMBL; D10210; BAA01062.1; -; mRNA.
DR EMBL; D10211; BAA01063.1; -; mRNA.
DR EMBL; AK134813; BAE22296.1; -; mRNA.
DR EMBL; BC018377; AAH18377.1; -; mRNA.
DR CCDS; CCDS19557.1; -.
DR PIR; JH0185; JH0185.
DR RefSeq; NP_001273325.1; NM_001286396.1.
DR RefSeq; NP_034148.2; NM_010018.3.
DR RefSeq; XP_006530224.1; XM_006530161.2.
DR RefSeq; XP_006530225.1; XM_006530162.3.
DR AlphaFoldDB; P18894; -.
DR SMR; P18894; -.
DR STRING; 10090.ENSMUSP00000107911; -.
DR BindingDB; P18894; -.
DR ChEMBL; CHEMBL2331068; -.
DR iPTMnet; P18894; -.
DR PhosphoSitePlus; P18894; -.
DR SwissPalm; P18894; -.
DR jPOST; P18894; -.
DR MaxQB; P18894; -.
DR PaxDb; P18894; -.
DR PeptideAtlas; P18894; -.
DR PRIDE; P18894; -.
DR ProteomicsDB; 294229; -.
DR DNASU; 13142; -.
DR GeneID; 13142; -.
DR KEGG; mmu:13142; -.
DR UCSC; uc008yza.2; mouse.
DR CTD; 1610; -.
DR MGI; MGI:94859; Dao.
DR eggNOG; KOG3923; Eukaryota.
DR InParanoid; P18894; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; P18894; -.
DR TreeFam; TF313887; -.
DR BRENDA; 1.4.3.3; 3474.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 13142; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Aoc1; mouse.
DR PRO; PR:P18894; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P18894; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0055130; P:D-alanine catabolic process; IDA:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR GO; GO:0036088; P:D-serine catabolic process; ISO:MGI.
DR GO; GO:0070178; P:D-serine metabolic process; ISO:MGI.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:MGI.
DR GO; GO:0006551; P:leucine metabolic process; IMP:MGI.
DR GO; GO:0006562; P:proline catabolic process; ISO: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..345
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162762"
FT MOTIF 343..345
FT /note="Microbody targeting signal"
FT BINDING 3..17
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 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310..314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VARIANT 181
FT /note="G -> R (abolishes activity)"
FT /evidence="ECO:0000269|PubMed:1355365"
FT CONFLICT 64
FT /note="A -> V (in Ref. 1; AAA39367 and 2; BAA01063)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="K -> N (in Ref. 2; BAA01062)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="R -> RG (in Ref. 2; BAA01062)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="H -> F (in Ref. 1; AAA39367 and 2; BAA01062/
FT BAA01063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38661 MW; 29A5D9B55D64700F CRC64;
MRVAVIGAGV IGLSTALCIH ERYHPTQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN
PQEAEWSQQT FDYLLSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKNAV LGFRKLTPSE
MDLFPDYGYG WFNTSLLLEG KSYLPWLTER LTERGVKLIH RKVESLEEVA RGVDVIINCT
GVWAGALQAD ASLQPGRGQI IQVEAPWIKH FILTHDPSLG IYNSPYIIPG SKTVTLGGIF
QLGNWSGLNS VRDHNTIWKS CCKLEPTLKN ARIVGELTGF RPVRPQVRLE REWLRHGSSS
AEVIHNYGHG GYGLTIHWGC AMEAANLFGK ILEEKKLSRL PPSHL
