P0C2D2 (OXLA_CRODC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=Casca LAO Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Crotalus durissus cascavella (Northeastern Brazilian rattlesnake)
Taxonomic identifier	184540 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus › Crotalus durissus

Protein attributes

Sequence length	61 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as apoptosis, antibacterial activities against both Gram-negative and Gram-positive bacteria and antiparasitic activities, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and edema. Ref.1
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD. Ref.1
Subunit structure	Homodimer; non-covalently linked. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	N-glycosylated By similarity.
Miscellaneous	Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.1).
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=46.7 µM for L-Leu Ref.1 pH dependence: Optimum pH is 6.5.

Ontologies

Keywords
Biological process	Apoptosis Cytolysis Hemolysis
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Hemostasis impairing toxin Oxidoreductase Platelet aggregation activating toxin Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›61	›61	L-amino-acid oxidase		PRO_0000273567
Regions
	Nucleotide binding	43 – 44	2	FAD By similarity
Amino acid modifications
	Disulfide bond	10 ↔ ?		By similarity
Experimental info
	Non-terminal residue	61	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D2 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 9D7F04E64267A122	FASTA	61	6,561
	10 20 30 40 50 60 ADDRNPLEQC FRETDYEEFL EIARNNLKAT SNPKHVVIVG AGMAGLSAAY VLSGGGHQVT V

References

[1]

"Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom." Toyama M.H., Toyama Dde O., Passero L.F., Laurenti M.D., Corbett C.E., Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O., Martins M.A., Monteiro H.S., Fonteles M.C. Toxicon 47:47-57(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Tissue: Venom.

Cross-references

3D structure databases
ProteinModelPortal	P0C2D2.
SMR	P0C2D2. Positions 3-61.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_CRODC

Accession

Primary (citable) accession number: P0C2D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	October 3, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program