P0C2D5 (OXLA_PROFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 24.
History...
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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: L-amino-acid oxidase Short name=LAAO Short name=LAO EC=1.4.3.2 Alternative name(s): Apoxin I-like protein Okinawa Habu apoxin protein-1 Short name=OHAP-1 |
| Organism | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
| Taxonomic identifier | 88087 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus |
Protein attributes
| Sequence length | 30 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 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 |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.1 |
| Cofactor | FAD By similarity. |
| Subunit structure | Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.2 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | N-glycosylated By similarity. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
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 cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organismInferred 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 – ›30 | ›30 | L-amino-acid oxidase | PRO_0000273570 | |||||
Amino acid modifications | |||||||||
| Disulfide bond | 10 ↔ ? | By similarity | |||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | D → H AA sequence Ref.2 | ||||||
| Sequence conflict | 10 | 1 | C → Y AA sequence Ref.2 | ||||||
| Non-terminal residue | 30 | 1 | |||||||
Sequences
References
| [1] | "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. Tissue: Venom. |
| [2] | "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. Tissue: Venom. |
Cross-references
Entry information
| Entry name | OXLA_PROFL | ||||||||
| Accession | Primary (citable) accession number: P0C2D5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal Toxin Annotation Program | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |