P86535 (OXLA1_DABRR) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 12.
History...
Clusters with 
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 L1 Short name=LAAO Short name=LAAO-L1 Short name=LAO EC=1.4.3.2 |
| Organism | Daboia russelii (Russel's viper) (Vipera russelii) |
| Taxonomic identifier | 31159 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Daboia ›  |
Protein attributes
| Sequence length | 20 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 of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. UniProtKB P81375 |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. UniProtKB P81375 |
| Cofactor | FAD. Ref.1 |
| Subunit structure | Monomer Probable. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.1 |
| Subcellular location | |
| Tissue specificity | |
| Post-translational modification | N-glycosylated Probable. Ref.1 |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=0.297 mM for L-Met Ref.1 KM=1.44 mM for L-Ile KM=0.750 mM for L-Leu KM=0.066 mM for L-Phe KM=0.210 mM for L-Trp KM=0.052 mM for L-Tyr Vmax=8.96 µmol/min/mg enzyme toward L-Phe |
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 – ›20 | ›20 | L-amino-acid oxidase L1 | PRO_0000394725 | |||||
Amino acid modifications | |||||||||
| Disulfide bond | 10 ↔ ? | By similarity UniProtKB Q90W54 | |||||||
Experimental info | |||||||||
| Sequence conflict | 4 | 1 | I → K AA sequence Ref.2 | ||||||
| Sequence conflict | 7 | 1 | K → L AA sequence Ref.2 | ||||||
| Sequence conflict | 12 | 1 | F → R AA sequence Ref.2 | ||||||
| Sequence conflict | 17 | 1 | Y → E AA sequence Ref.2 | ||||||
| Non-terminal residue | 20 | 1 | |||||||
Sequences
References
| [1] | "Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs." Mandal S., Bhattacharyya D. FEBS J. 275:2078-2095(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INHIBITION BY SUBSTRATE ANALOGS. Tissue: Venom. |
| [2] | "Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka." Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A. Biomed. Res. 31:71-81(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Venom. |
Cross-references
Entry information
| Entry name | OXLA1_DABRR | ||||||||
| Accession | Primary (citable) accession number: P86535 | ||||||||
| 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 |