Q99489 (OXDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-aspartate oxidase
Short name=DASOX
Short name=DDO
EC=1.4.3.1

Gene names

Name:

DDO

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
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.
Catalytic activity	D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.
Cofactor	FAD or 6-hydroxyflavin adenine dinucleotide.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aspartate catabolic process Traceable author statement. Source: UniProtKB
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activity Traceable author statement. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform DDO-1 (identifier: Q99489-1) Also known as: A; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform DDO-2 (identifier: Q99489-2) The sequence of this isoform differs from the canonical sequence as follows:      95-153: Missing.
Isoform 3 (identifier: Q99489-3) The sequence of this isoform differs from the canonical sequence as follows:      1-1: M → MRPARHWETRFGARDFGGFQDCFFRDRLM
Isoform 4 (identifier: Q99489-4) The sequence of this isoform differs from the canonical sequence as follows:      1-1: M → MRPARHWETRFGARDFGGFQDCFFRDRLM      95-153: Missing.
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	9	1	T → N in DN990727. Ref.6

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	D-aspartate oxidase		PRO_0000162770
Regions
	Nucleotide binding	6 – 20	15	FAD By similarity
	Nucleotide binding	36 – 37	2	FAD By similarity
	Nucleotide binding	43 – 44	2	FAD By similarity
	Nucleotide binding	48 – 50	3	FAD By similarity
	Nucleotide binding	307 – 311	5	FAD By similarity
	Motif	339 – 341	3	Microbody targeting signal Potential
Sites
	Binding site	166	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	183	1	FAD By similarity
	Binding site	223	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
	Binding site	312	1	FAD By similarity
Natural variations
	Alternative sequence	1	1	M → MRPARHWETRFGARDFGGFQ DCFFRDRLM in isoform 3 and isoform 4.		VSP_037664
	Alternative sequence	95 – 153	59	Missing in isoform DDO-2 and isoform 4.		VSP_001269
	Natural variant	136	1	F → L in a breast cancer sample; somatic mutation. Ref.7		VAR_036244
	Natural variant	189	1	Q → E. Corresponds to variant rs17622 [ dbSNP | Ensembl ].		VAR_014939
	Natural variant	230	1	H → Y. Corresponds to variant rs17621 [ dbSNP | Ensembl ].		VAR_014940
	Natural variant	255	1	L → R. Corresponds to variant rs17623 [ dbSNP | Ensembl ].		VAR_014941
Experimental info
	Sequence conflict	278	1	R → S in BAF85718. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform DDO-1 (A) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 8CAE7501FB7F215C	FASTA	341	37,535
	10 20 30 40 50 60 MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP 70 80 90 100 110 120 IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT 130 140 150 160 170 180 EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV 190 200 210 220 230 240 NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG 250 260 270 280 290 300 DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV 310 320 330 340 VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L
	Isoform DDO-2 [UniParc]. Checksum: DBD01D57E5B72F7A	FASTA	282	30,522
	10 20 30 40 50 60 MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP 70 80 90 100 110 120 IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGIKGSGG WTLTRRIEDL WELHPSFDIV 130 140 150 160 170 180 VNCSGLGSRQ LAGDSKIFPV RGQVLQVQAP WVEHFIRDGS GLTYIYPGTS HVTLGGTRQK 190 200 210 220 230 240 GDWNLSPDAE NSREILSRCC ALEPSLHGAC NIREKVGLRP YRPGVRLQTE LLARDGQRLP 250 260 270 280 VVHHYGHGSG GISVHWGTAL EAARLVSECV HALRTPIPKS NL
	Isoform 3 [UniParc]. Checksum: 4E4C372EE90DD7C5	FASTA	369	40,993
	10 20 30 40 50 60 MRPARHWETR FGARDFGGFQ DCFFRDRLMD TARIAVVGAG VVGLSTAVCI SKLVPRCSVT 70 80 90 100 110 120 IISDKFTPDT TSDVAAGMLI PHTYPDTPIH TQKQWFRETF NHLFAIANSA EAGDAGVHLV 130 140 150 160 170 180 SGWQIFQSTP TEEVPFWADV VLGFRKMTEA ELKKFPQYVF GQAFTTLKCE CPAYLPWLEK 190 200 210 220 230 240 RIKGSGGWTL TRRIEDLWEL HPSFDIVVNC SGLGSRQLAG DSKIFPVRGQ VLQVQAPWVE 250 260 270 280 290 300 HFIRDGSGLT YIYPGTSHVT LGGTRQKGDW NLSPDAENSR EILSRCCALE PSLHGACNIR 310 320 330 340 350 360 EKVGLRPYRP GVRLQTELLA RDGQRLPVVH HYGHGSGGIS VHWGTALEAA RLVSECVHAL RTPIPKSNL
	Isoform 4 [UniParc]. Checksum: E74BBF6D27BE5CB3	FASTA	310	33,980
	10 20 30 40 50 60 MRPARHWETR FGARDFGGFQ DCFFRDRLMD TARIAVVGAG VVGLSTAVCI SKLVPRCSVT 70 80 90 100 110 120 IISDKFTPDT TSDVAAGMLI PHTYPDTPIH TQKQWFRETF NHLFAIANSA EAGDAGVHLV 130 140 150 160 170 180 SGIKGSGGWT LTRRIEDLWE LHPSFDIVVN CSGLGSRQLA GDSKIFPVRG QVLQVQAPWV 190 200 210 220 230 240 EHFIRDGSGL TYIYPGTSHV TLGGTRQKGD WNLSPDAENS REILSRCCAL EPSLHGACNI 250 260 270 280 290 300 REKVGLRPYR PGVRLQTELL ARDGQRLPVV HHYGHGSGGI SVHWGTALEA ARLVSECVHA 310 LRTPIPKSNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and functional characterization of the human brain D-aspartate oxidase." Setoyama C., Miura R. J. Biochem. 121:798-803(1997) [PubMed: 9163533] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DDO-1 AND DDO-2). Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Uterus.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 3). Tissue: Brain.
[6]	"High-throughput cloning of full-length human cDNAs directly from cDNA libraries optimized for large and rare transcripts." Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G., He W. Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ISOFORM 4).
[7]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-136.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89858 mRNA. Translation: BAA14031.1. AK293029 mRNA. Translation: BAF85718.1. AL050350 Genomic DNA. Translation: CAI42511.1. AL050350 Genomic DNA. Translation: CAI42509.1. AL050350 Genomic DNA. Translation: CAI42510.1. CH471051 Genomic DNA. Translation: EAW48316.1. CH471051 Genomic DNA. Translation: EAW48317.1. BC032786 mRNA. Translation: AAH32786.3. DN990727 mRNA. No translation available.
IPI	IPI00015389. IPI00215860. IPI00641084. IPI00937691.
PIR	JC5438. JC5439.
RefSeq	NP_003640.2. NM_003649.2. NP_004023.2. NM_004032.2.
UniGene	Hs.591348.
3D structure databases
ProteinModelPortal	Q99489.
SMR	Q99489. Positions 2-332.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99489. 1 interaction.
STRING	Q99489.
Polymorphism databases
DMDM	2494037.
Proteomic databases
PRIDE	Q99489.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368924; ENSP00000357920; ENSG00000203797. ENST00000368925; ENSP00000357921; ENSG00000203797.
GeneID	8528.
KEGG	hsa:8528.
UCSC	uc003puc.1. human. uc003pud.1. human.
Organism-specific databases
CTD	8528.
GeneCards	GC06M110672.
H-InvDB	HIX0200890.
HGNC	HGNC:2727. DDO.
HPA	HPA037526.
MIM	124450. gene.
neXtProt	NX_Q99489.
PharmGKB	PA27194.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07752.
GeneTree	ENSGT00390000018635.
HOVERGEN	HBG003493.
InParanoid	Q99489.
OMA	STAVCIS.
OrthoDB	EOG4TB4BJ.
Gene expression databases
ArrayExpress	Q99489.
Bgee	Q99489.
CleanEx	HS_DDO.
Genevestigator	Q99489.
GermOnline	ENSG00000203797. Homo sapiens.
Family and domain databases
InterPro	IPR023209. D-aa_oxidase. IPR006181. D-amino_acid_oxidase_CS. IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 3 hits.
KO	K00272.
PANTHER	PTHR11530. PTHR11530. 1 hit.
Pfam	PF01266. DAO. 1 hit. [Graphical view]
PIRSF	PIRSF000189. D-aa_oxidase. 1 hit.
PROSITE	PS00677. DAO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	31934.
SOURCE	Search...

Entry information

Entry name

OXDD_HUMAN

Accession

Primary (citable) accession number: Q99489
Secondary accession number(s): A8KAG4 , Q5JXM4, Q5JXM5, Q5JXM6, Q8N552

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.