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P0C2D3 (OXLA_ERIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismEristicophis macmahoni (Leaf-nosed viper)
Taxonomic identifier110227 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEristicophis

Protein attributes

Sequence length27 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 hemolysis, edema, apoptosis, as well as induction 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. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also have antibacterial and antiparasitic activities. 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

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Contains 2 disulfide bonds By similarity.

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Mass spectrometry

Molecular mass is 58734.0 Da from positions 1 - ?. Determined by MALDI. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›27›27L-amino-acid oxidase
PRO_0000273568

Experimental info

Non-terminal residue271

Sequences

Sequence LengthMass (Da)Tools
P0C2D3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 18DBFD66E0655CE7

FASTA273,097
        10         20 
ADDKNPLEEA FREADYEVFL EIAKNGL 

« Hide

References

[1]"Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom."
Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M., Neumeister B., Voelter W.
Arch. Biochem. Biophys. 384:216-226(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_ERIMA
AccessionPrimary (citable) accession number: P0C2D3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families