ID OXDD_HUMAN Reviewed; 341 AA. AC Q99489; A8KAG4; Q5JXM4; Q5JXM6; Q8N552; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 07-JUL-2009, entry version 83. DE RecName: Full=D-aspartate oxidase; DE Short=DASOX; DE EC=1.4.3.1; DE AltName: Full=DDO; GN Name=DDO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DDO-1 AND DDO-2). RC TISSUE=Brain; RX MEDLINE=97306065; PubMed=9163533; RA Setoyama C., Miura R.; RT "Structural and functional characterization of the human brain D- RT aspartate oxidase."; RL J. Biochem. 121:798-803(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ISOFORM 4). RA Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., RA Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., RA Jay G., He W.; RT "High-throughput cloning of full-length human cDNAs directly from cDNA RT libraries optimized for large and rare transcripts."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP VARIANT [LARGE SCALE ANALYSIS] LEU-136. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D- CC aspartate and its N-methylated derivative, N-methyl D-aspartate. CC -!- CATALYTIC ACTIVITY: D-aspartate + H(2)O + O(2) = oxaloacetate + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD or 6-hydroxyflavin adenine dinucleotide. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=DDO-1; Synonyms=A; CC IsoId=Q99489-1; Sequence=Displayed; CC Name=DDO-2; CC IsoId=Q99489-2; Sequence=VSP_001269; CC Name=3; CC IsoId=Q99489-3; Sequence=VSP_037664; CC Name=4; CC IsoId=Q99489-4; Sequence=VSP_037664, VSP_001269; CC Note=Ref.6 (DN990727) sequence is in conflict in position: CC 9:T->N; CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D89858; BAA14031.1; -; mRNA. DR EMBL; AK293029; BAF85718.1; -; mRNA. DR EMBL; AL050350; CAI42511.1; -; Genomic_DNA. DR EMBL; AL050350; CAI42509.1; -; Genomic_DNA. DR EMBL; CH471051; EAW48316.1; -; Genomic_DNA. DR EMBL; BC032786; AAH32786.3; -; mRNA. DR EMBL; DN990727; -; NOT_ANNOTATED_CDS; mRNA. DR IPI; IPI00015389; -. DR IPI; IPI00215860; -. DR PIR; JC5438; JC5438. DR PIR; JC5439; JC5439. DR RefSeq; NP_003640.2; -. DR RefSeq; NP_004023.2; -. DR UniGene; Hs.591348; -. DR UniGene; Hs.648053; -. DR HSSP; P00371; 1AN9. DR PRIDE; Q99489; -. DR Ensembl; ENSG00000203797; Homo sapiens. DR GeneID; 8528; -. DR KEGG; hsa:8528; -. DR UCSC; uc003puc.1; human. DR UCSC; uc003pud.1; human. DR GeneCards; GC06M110758; -. DR H-InvDB; HIX0022729; -. DR HGNC; HGNC:2727; DDO. DR MIM; 124450; gene. DR PharmGKB; PA27194; -. DR HOVERGEN; Q99489; -. DR BRENDA; 1.4.3.1; 247. DR NextBio; 31934; -. DR ArrayExpress; Q99489; -. DR Bgee; Q99489; -. DR CleanEx; HS_DDO; -. DR GermOnline; ENSG00000203797; Homo sapiens. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro. DR GO; GO:0008445; F:D-aspartate oxidase activity; TAS:UniProtKB. DR GO; GO:0006533; P:aspartate catabolic process; TAS:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; TAS:UniProtKB. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Oxidoreductase; Peroxisome; Polymorphism. FT CHAIN 1 341 D-aspartate oxidase. FT /FTId=PRO_0000162770. FT NP_BIND 6 20 FAD (By similarity). FT NP_BIND 36 37 FAD (By similarity). FT NP_BIND 43 44 FAD (By similarity). FT NP_BIND 48 50 FAD (By similarity). FT NP_BIND 307 311 FAD (By similarity). FT MOTIF 339 341 Microbody targeting signal (Potential). FT BINDING 166 166 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 183 183 FAD (By similarity). FT BINDING 223 223 Substrate (By similarity). FT BINDING 278 278 Substrate (By similarity). FT BINDING 312 312 FAD (By similarity). FT VAR_SEQ 1 1 M -> MRPARHWETRFGARDFGGFQDCFFRDRLM (in FT isoform 3 and isoform 4). FT /FTId=VSP_037664. FT VAR_SEQ 95 153 Missing (in isoform DDO-2 and isoform 4). FT /FTId=VSP_001269. FT VARIANT 136 136 F -> L (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_036244. FT VARIANT 189 189 Q -> E (in dbSNP:rs17622). FT /FTId=VAR_014939. FT VARIANT 230 230 H -> Y (in dbSNP:rs17621). FT /FTId=VAR_014940. FT VARIANT 255 255 L -> R (in dbSNP:rs17623). FT /FTId=VAR_014941. FT CONFLICT 278 278 R -> S (in Ref. 2; BAF85718). SQ SEQUENCE 341 AA; 37535 MW; 8CAE7501FB7F215C CRC64; MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L //