PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND GLYCOSYLATION.
TISSUE=Venom;
DOI=10.1016/j.bmc.2006.06.025; PubMed=16809041 [NCBI, ExPASy, EBI, Israel, Japan]
Izidoro L.F.M., Ribeiro M.C., Souza G.R.L., Sant'Ana C.D., Hamaguchi A., Homsi-Brandeburgo M.I., Goulart L.R., Beleboni R.O., Nomizo A., Sampaio S.V., Soares A.M., Rodrigues V.M.;
"Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom.";
Bioorg. Med. Chem. 14:7034-7043(2006).

Comments

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Induces platelet aggregation. Induces mouse paw edema. Has an antibacterial activity against E.coli, and P.aeruginosa. Has cytotoxic activity against Leishmania spp and tumor cells. May have an ability to induce apoptosis and hemorrhage.
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated.
SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

SMR

P0C2D1; 3-49.

ModBase

P0C2D1.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0001716;	Molecular function: L-amino-acid oxidase activity (inferred from electronic annotation from EC).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
GO:0045786;	Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

Phylogenomic databases

HOVERGEN

P0C2D1; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Anti-oncogene; Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Cell cycle; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >49`	`>49`	`L-amino-acid oxidase.`	`PRO_0000273566`
`NON_TER`	`49 49`

Sequence information

Length: 49 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 5299 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 5D190816B54BACCA [This is a checksum on the sequence]

        10         20         30         40 
ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY

P0C2D1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools