[1]	PROTEIN SEQUENCE. TISSUE=Venom; DOI=10.1016/S0041-0101(01)00133-7; PubMed=11600144 [NCBI, ExPASy, EBI, Israel, Japan] Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M., Titani K., Fujimura Y.; "Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom."; Toxicon 39:1827-1833(2001).
[2]	FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. TISSUE=Venom; DOI=10.1016/0020-711X(92)90105-A; PubMed=1612186 [NCBI, ExPASy, EBI, Israel, Japan] Tan N.-H., Swaminathan S.; "Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom."; Int. J. Biochem. 24:967-973(1992).

Comments

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Is very active against L-Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, and L-Arg. Inhibits both agonist- and shear stress-induced platelet aggregation (SIPA) dose-dependently through the formation of hydrogen peroxide (H(2)O(2)). May induce apoptosis and hemorrhage. May have an antibacterial activity.
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is also stable in alkaline medium;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated (By similarity).
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

ModBase

P0C2D4.

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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
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Phylogenomic databases

HOVERGEN

P0C2D4; -.

Other

ProtoNet

P0C2D4.

UniRef

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

Keywords

Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >38`	`>38`	`L-amino-acid oxidase.`	`PRO_0000273569`
`NON_TER`	`38 38`

Sequence information

Length: 38 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 4514 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: D988B9FC32DDDE08 [This is a checksum on the sequence]

        10         20         30 
DDRRSPLEEC FQQNDYEEFL EIAKNGLKKT XNPKHVXV

P0C2D4 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