P0C2D3 (OXLA_ERIMA) Reviewed, UniProtKB/Swiss-Prot
Last modified October 3, 2012. Version 29. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Eristicophis macmahoni (Leaf-nosed viper)|
|Taxonomic identifier||110227 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Eristicophis|
|Sequence length||27 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 hemolysis, edema, apoptosis, 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. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also have antibacterial and antiparasitic activities. Ref.1
An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
FAD By similarity.
Homodimer; non-covalently linked. Ref.1
Expressed by the venom gland.
Contains 2 disulfide bonds By similarity.
N-glycosylated By similarity.
Hemostasis impairing toxin
Platelet aggregation activating toxin
|Technical term||Direct protein sequencing|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWcytolysis
Inferred from electronic annotation. Source: UniProtKB-KWdefense response to bacterium
Inferred from electronic annotation. Source: UniProtKB-KWhemolysis in other organism
Inferred from electronic annotation. Source: UniProtKB-KWinflammatory response
Inferred from electronic annotation. Source: UniProtKB-KW
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)
|||"Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom."|
Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M., Neumeister B., Voelter W.
Arch. Biochem. Biophys. 384:216-226(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY.
|Accession||Primary (citable) accession number: P0C2D3|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Animal Toxin Annotation Program|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families