P0C2D5 (OXLA_PROFL) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 26. History...
Names and origin
|Protein names||Recommended name:|
Apoxin I-like protein
Okinawa Habu apoxin protein-1
|Organism||Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)|
|Taxonomic identifier||88087 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Crotalinae › Protobothrops|
|Sequence length||30 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 hemorrhage, edema, antibacterial and antiparasitic activities, 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 has an ability to induce hemolysis and apoptosis. Ref.1 Ref.2
An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.1
FAD By similarity.
Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.2
Expressed by the venom gland.
N-glycosylated By similarity.
Hemostasis impairing 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-KW
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Molecular_function||L-amino-acid oxidase activity|
Inferred from electronic annotation. Source: UniProtKB-EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – ›30||›30||L-amino-acid oxidase||PRO_0000273570|
Amino acid modifications
|Disulfide bond||10 ↔ ?||By similarity|
|Sequence conflict||2||1||D → H AA sequence Ref.2|
|Sequence conflict||10||1||C → Y AA sequence Ref.2|
|||"Apoptotic effect in the glioma cells induced by specific protein extracted from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to oxidative stress."|
Sun L.-K., Yoshii Y., Hyodo A., Tsurushima H., Saito A., Harakuni T., Li Y.-P., Kariya K., Nozaki M., Morine N.
Toxicol. in Vitro 17:169-177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY.
|||"Characterization of an apoptosis-inducing factor in Habu snake venom as a glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro."|
Abe Y., Shimoyama Y., Munakata H., Ito J., Nagata N., Ohtsuki K.
Biol. Pharm. Bull. 21:924-927(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBUNIT.
|Accession||Primary (citable) accession number: P0C2D5|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
|Annotation program||Animal Toxin Annotation Program|
Index of protein domains and families