P0C2D6 (OXLA_PROMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 21.
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 Short name=TM-LAO EC=1.4.3.2 |
| Organism | Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus) |
| Taxonomic identifier | 103944 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Protobothrops |
Protein attributes
| Sequence length | 24 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, hemolysis, edema, apoptosis, and antiparasitic activities By similarity. This protein has antibacterial activity (against E.coli, S.aureus, and B.dysenteriae), cytotoxic activity, as well as an ability to induce 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. Ref.1 |
| 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 | |
| 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 Blood coagulation Cytolysis Hemolysis |
| Cellular component | Secreted |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial 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 blood coagulationInferred 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)
Sequences
References
| [1] | "Purification, characterization and biological activity of an L-amino acid oxidase from Trimeresurus mucrosquamatus venom." Wei J.-F., Wei Q., Lu Q.-M., Tai H., Jin Y., Wang W.-Y., Xiong Y.-L. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:219-224(2003) [PubMed: 12621545] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom. |
Cross-references
Entry information
| Entry name | OXLA_PROMU | ||||||||
| Accession | Primary (citable) accession number: P0C2D6 | ||||||||
| 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 |