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P14920

- OXDA_HUMAN

UniProt

P14920 - OXDA_HUMAN

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Protein

D-amino-acid oxidase

Gene

DAO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.1 Publication

Catalytic activityi

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

Kineticsi

  1. KM=3.6 mM for D-serine2 Publications
  2. KM=1.7 mM for D-proline2 Publications
  3. KM=1.1 mM for D-tyrosine2 Publications
  4. KM=1.5 mM for D-DOPA2 Publications
  5. KM=1.2 mM for D-phenylalanine2 Publications
  6. KM=0.9 mM for D-alanine2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Substrate
Binding sitei164 – 1641FAD; via amide nitrogen and carbonyl oxygen2 Publications
Binding sitei182 – 1821FAD2 Publications
Binding sitei217 – 2171Substrate
Binding sitei228 – 2281Substrate
Binding sitei283 – 2831Substrate
Binding sitei313 – 3131Substrate; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi3 – 1715FAD2 PublicationsAdd
BLAST
Nucleotide bindingi37 – 382FAD2 Publications
Nucleotide bindingi44 – 452FAD2 Publications
Nucleotide bindingi49 – 513FAD2 Publications
Nucleotide bindingi312 – 3176FAD2 Publications

GO - Molecular functioni

  1. cofactor binding Source: UniProtKB
  2. D-amino-acid oxidase activity Source: UniProtKB
  3. FAD binding Source: UniProtKB
  4. protein dimerization activity Source: UniProtKB
  5. receptor binding Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. D-alanine catabolic process Source: UniProtKB
  3. dopamine biosynthetic process Source: UniProtKB
  4. D-serine catabolic process Source: UniProtKB
  5. D-serine metabolic process Source: UniProtKB
  6. glyoxylate metabolic process Source: Reactome
  7. leucine metabolic process Source: Ensembl
  8. proline catabolic process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS03351-MONOMER.
ReactomeiREACT_16925. Glyoxylate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
D-amino-acid oxidase (EC:1.4.3.3)
Short name:
DAAO
Short name:
DAMOX
Short name:
DAO
Gene namesi
Name:DAO
Synonyms:DAMOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2671. DAO.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. peroxisomal matrix Source: Reactome
  3. peroxisomal membrane Source: UniProtKB
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA27139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347D-amino-acid oxidasePRO_0000162761Add
BLAST

Proteomic databases

PaxDbiP14920.
PRIDEiP14920.

Expressioni

Gene expression databases

BgeeiP14920.
CleanExiHS_DAO.
ExpressionAtlasiP14920. baseline and differential.
GenevestigatoriP14920.

Organism-specific databases

HPAiHPA038653.
HPA038654.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi107980. 3 interactions.
IntActiP14920. 2 interactions.
STRINGi9606.ENSP00000228476.

Structurei

Secondary structure

1
347
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 2314Combined sources
Beta strandi25 – 284Combined sources
Beta strandi31 – 377Combined sources
Helixi40 – 423Combined sources
Helixi44 – 474Combined sources
Helixi63 – 7715Combined sources
Turni78 – 803Combined sources
Helixi84 – 874Combined sources
Beta strandi89 – 10012Combined sources
Turni106 – 1105Combined sources
Beta strandi111 – 1166Combined sources
Helixi119 – 1224Combined sources
Beta strandi129 – 13911Combined sources
Helixi141 – 15414Combined sources
Beta strandi158 – 1614Combined sources
Helixi167 – 1726Combined sources
Beta strandi176 – 1805Combined sources
Helixi183 – 1886Combined sources
Beta strandi196 – 20611Combined sources
Beta strandi212 – 2165Combined sources
Turni219 – 2213Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi233 – 2397Combined sources
Helixi253 – 26614Combined sources
Helixi268 – 2725Combined sources
Beta strandi274 – 28512Combined sources
Beta strandi290 – 2967Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi303 – 3097Combined sources
Helixi312 – 3143Combined sources
Helixi315 – 33622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DU8X-ray2.50A/B/G/J1-347[»]
2E48X-ray2.90A/B/C/D1-347[»]
2E49X-ray3.20A/B/C/D1-347[»]
2E4AX-ray2.60A/B/C/D1-347[»]
2E82X-ray2.70A/B/C/D1-347[»]
2GNZmodel-A1-339[»]
3CUKX-ray2.49A/B/C/D1-347[»]
3G3EX-ray2.20A/B/C/D1-347[»]
3W4IX-ray2.50A/B/C/D1-347[»]
3W4JX-ray2.74A/B/C/D1-347[»]
3W4KX-ray2.86A/B/C/D1-347[»]
3ZNNX-ray1.90A/B1-347[»]
3ZNOX-ray2.30A/B1-347[»]
3ZNPX-ray2.40A/B1-347[»]
3ZNQX-ray2.75A/B1-347[»]
4QFCX-ray2.40A/B1-347[»]
4QFDX-ray2.85A/B1-347[»]
ProteinModelPortaliP14920.
SMRiP14920. Positions 1-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14920.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi345 – 3473Microbody targeting signal

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Phylogenomic databases

eggNOGiCOG0665.
GeneTreeiENSGT00390000018635.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiP14920.
KOiK00273.
OMAiPNAEKMG.
OrthoDBiEOG7B31NB.
PhylomeDBiP14920.
TreeFamiTF313887.

Family and domain databases

InterProiIPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[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.

P14920-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG
60 70 80 90 100
LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE
110 120 130 140 150
AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE
160 170 180 190 200
RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG
210 220 230 240 250
QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL
260 270 280 290 300
NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP
310 320 330 340
SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL
Length:347
Mass (Da):39,474
Last modified:November 25, 2002 - v3
Checksum:iA508E603872F3072
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311D → H in CAA31614. (PubMed:2901986)Curated
Sequence conflicti279 – 2791R → A in CAA31614. (PubMed:2901986)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13227 mRNA. Translation: CAA31614.1.
AK312995 mRNA. Translation: BAG35832.1.
CH471054 Genomic DNA. Translation: EAW97837.1.
BC029057 mRNA. Translation: AAH29057.1.
BC074770 mRNA. Translation: AAH74770.1.
D11370 Genomic DNA. Translation: BAA20974.1.
CCDSiCCDS9122.1.
PIRiS01340.
RefSeqiNP_001908.3. NM_001917.4.
XP_006719331.1. XM_006719268.1.
UniGeneiHs.113227.

Genome annotation databases

EnsembliENST00000228476; ENSP00000228476; ENSG00000110887.
GeneIDi1610.
KEGGihsa:1610.
UCSCiuc001tnq.4. human.

Polymorphism databases

DMDMi25453448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13227 mRNA. Translation: CAA31614.1 .
AK312995 mRNA. Translation: BAG35832.1 .
CH471054 Genomic DNA. Translation: EAW97837.1 .
BC029057 mRNA. Translation: AAH29057.1 .
BC074770 mRNA. Translation: AAH74770.1 .
D11370 Genomic DNA. Translation: BAA20974.1 .
CCDSi CCDS9122.1.
PIRi S01340.
RefSeqi NP_001908.3. NM_001917.4.
XP_006719331.1. XM_006719268.1.
UniGenei Hs.113227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DU8 X-ray 2.50 A/B/G/J 1-347 [» ]
2E48 X-ray 2.90 A/B/C/D 1-347 [» ]
2E49 X-ray 3.20 A/B/C/D 1-347 [» ]
2E4A X-ray 2.60 A/B/C/D 1-347 [» ]
2E82 X-ray 2.70 A/B/C/D 1-347 [» ]
2GNZ model - A 1-339 [» ]
3CUK X-ray 2.49 A/B/C/D 1-347 [» ]
3G3E X-ray 2.20 A/B/C/D 1-347 [» ]
3W4I X-ray 2.50 A/B/C/D 1-347 [» ]
3W4J X-ray 2.74 A/B/C/D 1-347 [» ]
3W4K X-ray 2.86 A/B/C/D 1-347 [» ]
3ZNN X-ray 1.90 A/B 1-347 [» ]
3ZNO X-ray 2.30 A/B 1-347 [» ]
3ZNP X-ray 2.40 A/B 1-347 [» ]
3ZNQ X-ray 2.75 A/B 1-347 [» ]
4QFC X-ray 2.40 A/B 1-347 [» ]
4QFD X-ray 2.85 A/B 1-347 [» ]
ProteinModelPortali P14920.
SMRi P14920. Positions 1-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107980. 3 interactions.
IntActi P14920. 2 interactions.
STRINGi 9606.ENSP00000228476.

Chemistry

BindingDBi P14920.
ChEMBLi CHEMBL5485.
DrugBanki DB03147. Flavin adenine dinucleotide.

Polymorphism databases

DMDMi 25453448.

Proteomic databases

PaxDbi P14920.
PRIDEi P14920.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228476 ; ENSP00000228476 ; ENSG00000110887 .
GeneIDi 1610.
KEGGi hsa:1610.
UCSCi uc001tnq.4. human.

Organism-specific databases

CTDi 1610.
GeneCardsi GC12P109273.
HGNCi HGNC:2671. DAO.
HPAi HPA038653.
HPA038654.
MIMi 124050. gene.
neXtProti NX_P14920.
Orphaneti 803. Amyotrophic lateral sclerosis.
PharmGKBi PA27139.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0665.
GeneTreei ENSGT00390000018635.
HOGENOMi HOG000046303.
HOVERGENi HBG003493.
InParanoidi P14920.
KOi K00273.
OMAi PNAEKMG.
OrthoDBi EOG7B31NB.
PhylomeDBi P14920.
TreeFami TF313887.

Enzyme and pathway databases

BioCyci MetaCyc:HS03351-MONOMER.
Reactomei REACT_16925. Glyoxylate metabolism.

Miscellaneous databases

ChiTaRSi DAO. human.
EvolutionaryTracei P14920.
GenomeRNAii 1610.
NextBioi 6618.
PROi P14920.
SOURCEi Search...

Gene expression databases

Bgeei P14920.
CleanExi HS_DAO.
ExpressionAtlasi P14920. baseline and differential.
Genevestigatori P14920.

Family and domain databases

InterProi IPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view ]
PANTHERi PTHR11530. PTHR11530. 1 hit.
Pfami PF01266. DAO. 1 hit.
[Graphical view ]
PIRSFi PIRSF000189. D-aa_oxidase. 1 hit.
PROSITEi PS00677. DAO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase."
    Momoi K., Fukui K., Watanabe F., Miyake Y.
    FEBS Lett. 238:180-184(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. Momoi K.
    Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Colon and Kidney.
  6. "Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase."
    Fukui K., Miyake Y.
    J. Biol. Chem. 267:18631-18638(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
  7. "Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring."
    Kawazoe T., Tsuge H., Pilone M.S., Fukui K.
    Protein Sci. 15:2708-2717(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR BENZOATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  8. "Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis."
    Kawazoe T., Tsuge H., Imagawa T., Aki K., Kuramitsu S., Fukui K.
    Biochem. Biophys. Res. Commun. 355:385-391(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH FAD AND IMINO-SERINE; IMINO-DOPA AND O-AMINOBENZOATE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH FAD AND SYNTHETIC INHIBITOR.

Entry informationi

Entry nameiOXDA_HUMAN
AccessioniPrimary (citable) accession number: P14920
Secondary accession number(s): B2R7I5, Q16758, Q8N6R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2002
Last modified: November 26, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3