P0DI88 (OXLA_BOTJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=BjarLAAO-I Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Bothrops jararaca (Jararaca)
Taxonomic identifier	8724 [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 › Bothrops

Protein attributes

Sequence length	37 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 (L-Met, L-Leu, L-Phe, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, edema, apoptosis of vascular endothelial cells or tumor cell lines, as well as regulation 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 By similarity. This protein induce hemolysis and has antibacterial and antiparasitic activities (against the Gram-positive S.aureus). Tested in vivo, this protein significantly inhibits Ehrlich ascite tumors growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of hydrogen peroxide from peritoneal macrophages. Ref.1 Ref.2 Ref.3
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer; non-covalently linked. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	N-Glycosylated. Ref.2
Miscellaneous	Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.3 and Ref.2).
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Caution	Bothrops jararaca venom seems to contain 2 isoforms with different hydrophobic properties (Ref.1). These isoforms may reflect different glycosylation of the protein or they may have been synthesized from different genes.

Ontologies

Keywords
Biological process	Apoptosis Cytolysis Hemolysis
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Hemostasis impairing toxin Oxidoreductase 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 – ›37	›37	L-amino-acid oxidase		PRO_0000412595
Amino acid modifications
	Disulfide bond	10 ↔ ?		By similarity
Experimental info
	Non-terminal residue	37	1

Sequences

	Sequence		Length	Mass (Da)
	P0DI88 [UniParc]. Last modified September 21, 2011. Version 1. Checksum: 9C3BDE3E1E664AE7	FASTA	37	4,299
	10 20 30 ADDKNPLEEC FRETDYEEFL EIARNGLKAT SNPKRVV

References

[1]	"Antitumoural effect of an L-amino acid oxidase isolated from Bothrops jararaca snake venom." de Vieira Santos M.M., Sant'Ana C.D., Giglio J.R., da Silva R.J., Sampaio S.V., Soares A.M., Fecchio D. Basic Clin. Pharmacol. Toxicol. 102:533-542(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom.
[2]	"Antigenic, microbicidal and antiparasitic properties of an L-amino acid oxidase isolated from Bothrops jararaca snake venom." Ciscotto P., Machado de Avila R.A., Coelho E.A., Oliveira J., Diniz C.G., Farias L.M., de Carvalho M.A., Maria W.S., Sanchez E.F., Borges A., Chavez-Olortegui C. Toxicon 53:330-341(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, GLYCOSYLATION. Tissue: Venom.
[3]	"L-amino acid oxidase activity present in fractions of Bothrops jararaca venom is responsible for the induction of programmed cell death in Trypanosoma cruzi." Deolindo P., Teixeira-Ferreira A.S., DaMatta R.A., Alves E.W. Toxicon 56:944-955(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_BOTJA

Accession

Primary (citable) accession number: P0DI88

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	October 31, 2012
This is version 7 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