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P0CC16 (OXLA_AGKCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 19. 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=ACL-LAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismAgkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Taxonomic identifier37195 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Protein attributes

Sequence length19 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Ile followed by L-Phe, L-Met, L-Val, L-Arg, L-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage (minimum hemorrhagic dose of 10 µg), and apoptosis. May also induce hemolysis, edema, antibacterial and antiparasitic activities. May also regulate 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. Ref.1

Cofactor

FMN. Ref.1

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

Contains 2 disulfide bonds By similarity.

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›19›19L-amino-acid oxidase
PRO_0000390926

Experimental info

Non-terminal residue191

Sequences

Sequence LengthMass (Da)Tools
P0CC16 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: C1D709886B68E7B5

FASTA192,375
        10 
ADSRNPLEEE FRETNYEEF 

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References

[1]"Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data."
Souza D.H.F., Eugenio L.M., Fletcher J.E., Jiang M.-S., Garratt R.C., Oliva G., Selistre-de-Araujo H.S.
Arch. Biochem. Biophys. 368:285-290(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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_AGKCL
AccessionPrimary (citable) accession number: P0CC16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 19, 2010
Last modified: April 16, 2014
This is version 19 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