Reviewed,
UniProtKB/Swiss-Prot P0C2D6 (OXLA_TRIMU)
Last modified
June 16, 2009.
Version 12.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names 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 | Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops 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. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Has an ability to induce apoptosis, and hemorrhage By similarity. Has an antibacterial activity against E.coli, S.aureus, and B.dysenteriae. Has cytotoxic activity and induces platelet aggregation. |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. |
| Cofactor | FAD By similarity. |
| Subunit structure | Homodimer. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated By similarity. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Apoptosis Blood coagulation |
| Cellular component | Secreted |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial Oxidoreductase Toxin |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulationInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred 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_TRIMU | ||||||||
| Accession | Primary (citable) accession number: P0C2D6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

Clusters with


