Reviewed, UniProtKB/Swiss-Prot O01739 (OXDA1_CAEEL)

Names and origin

Protein names

Recommended name:
    Putative D-amino-acid oxidase 1
      Short name=DAMOX 1
      Short name=DAAO 1
      Short name=DAO 1
    EC=1.4.3.-

Gene names

ORF Names:

F20H11.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could act as a detoxifying agent which removes D-amino acids accumulated during aging By similarity.
Cofactor	FAD By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 383	366	Putative D-amino-acid oxidase 1		PRO_0000248529
Regions
	Nucleotide binding	20 – 34	15	FAD By similarity
	Nucleotide binding	55 – 56	2	FAD By similarity
	Nucleotide binding	62 – 63	2	FAD By similarity
	Nucleotide binding	67 – 69	3	FAD By similarity
	Nucleotide binding	334 – 338	5	FAD By similarity
Sites
	Binding site	190	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	304	1	Substrate By similarity
	Binding site	335	1	Substrate; via carbonyl oxygen By similarity
	Binding site	339	1	FAD By similarity
Amino acid modifications
	Glycosylation	152	1	N-linked (GlcNAc...) Ref.4
	Glycosylation	271	1	N-linked (GlcNAc...) Ref.4 Ref.3
	Glycosylation	320	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O01739-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: CECAB15AEC1E93B5	FASTA	383	42,502
	10 20 30 40 50 60 MLYALLLLFG GVSTVSSLRV AVVGEGVIGL STATAILDLA EKRNIPAPEI HIFHHKPFEK 70 80 90 100 110 120 ILSRHIAGLF RIDSGSEIDR KYGYDTFEKL ATLWREYGGL SGVQLVSGHI LSDSKTKLDS 130 140 150 160 170 180 QRESYGSLVY NYRDLAEPEL FGPTSLFDLP RNTTTRGIHY TAYTSEGLRF CPFLKKELMT 190 200 210 220 230 240 KGVRFTQRRI GNLEELGAEF DVVVNSAGLL GGVLAGDDAG NMKPIRGVLI RVDAPWQKHF 250 260 270 280 290 300 LYRDFSTITI PVIDHVYMGT VKQEGAFGPN NVTSADIQDI TSRYVALQPS FKRVHMLSSF 310 320 330 340 350 360 VGYRPGRKQV RVEKQIRETN GSKKFTVVHN YGHSGNGFTL GYGSAVHAAH IVLDLPLDAY 370 380 HGLVPEPLPI NATISEWVKY LDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases." Katane M., Seida Y., Sekine M., Furuchi T., Homma H. FEBS J. 274:137-149(2007) [PubMed: 17140416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-271, MASS SPECTROMETRY.
[4]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-152 AND ASN-271, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB275893 mRNA. Translation: BAF34316.1. AF002197 Genomic DNA. Translation: AAB53982.1.
PIR	F88486.
RefSeq	NP_498453.1.
UniGene	Cel.10588
3D structure databases
HSSP	HSSP built from PDB template 1AN9 based on UniProtKB P00371.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:25818N.
IntAct	O01739. 1 interaction.
Genome annotation databases
Ensembl	F20H11.5. Caenorhabditis elegans. [Contig view]
GeneID	184746.
KEGG	cel:F20H11.5.
Organism-specific databases
WormBase	WBGene00017648. F20H11.5.
WormPep	F20H11.5. CE09514. [WorfDB]
Phylogenomic databases
OMA	O01739. IAGLFRI.
Gene expression databases
ArrayExpress	O01739.
Family and domain databases
InterPro	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. 1 hit.
Pfam	PF01266. DAO. 1 hit. [Graphical view]
PROSITE	PS00677. DAO. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	925848.

Entry information

Entry name

OXDA1_CAEEL

Accession

Primary (citable) accession number: O01739
Secondary accession number(s): Q08I98

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project