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P0DI87 (OXLA_BOTIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=BiLAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops insularis (Golden lancehead) (Lachesis insularis)
Taxonomic identifier8723 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length49 AA.
Sequence statusFragment.
Protein existenceEvidence 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, 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. In addition, this protein induces apoptosis and necrosis and has inhibitory effects on rat kidney function (decrease of blood flow and glomerular filtration). 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 By similarity.

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›49›49L-amino-acid oxidase
PRO_0000412594

Regions

Nucleotide binding43 – 442FAD By similarity

Amino acid modifications

Disulfide bond10 ↔ ?

Experimental info

Non-terminal residue491

Sequences

Sequence LengthMass (Da)Tools
P0DI87 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 29BAD2AFDCBE9D1F

FASTA495,293
        10         20         30         40 
ADDKNPLEEC FREDDYEGFL EIAKNGLSTT SNPKRVVIVG AGMSGLAAY 

« Hide

References

[1]"Purification and biological effects of L-amino acid oxidase isolated from Bothrops insularis venom."
Braga M.D., Martins A.M., Amora D.N., de Menezes D.B., Toyama M.H., Toyama D.O., Marangoni S., Alves C.D., Barbosa P.S., de Sousa Alves R., Fonteles M.C., Monteiro H.S.A.
Toxicon 51:199-207(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTIN
AccessionPrimary (citable) accession number: P0DI87
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families