P0CC16 (OXLA_AGKCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=ACL-LAO Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Taxonomic identifier	37195 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Agkistrodon › Agkistrodon contortrix

Protein attributes

Sequence length	19 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 (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.

Ontologies

Keywords
Biological process	Apoptosis Cytolysis Hemolysis
Cellular component	Secreted
Ligand	FMN Flavoprotein
Molecular function	Antibiotic Antimicrobial Hemorrhagic toxin 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 cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW killing of cells of other organism Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	FMN binding Inferred from direct assay Ref.1. Source: UniProtKB L-amino-acid oxidase activity Inferred from direct assay Ref.1. Source: UniProtKB protein dimerization activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›19	›19	L-amino-acid oxidase		PRO_0000390926
Experimental info
	Non-terminal residue	19	1

Sequences

	Sequence		Length	Mass (Da)
	P0CC16 [UniParc]. Last modified January 19, 2010. Version 1. Checksum: C1D709886B68E7B5	FASTA	19	2,375
	10 ADSRNPLEEE FRETNYEEF

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
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_AGKCL

Accession

Primary (citable) accession number: P0CC16

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 19, 2010
Last sequence update:	January 19, 2010
Last modified:	January 9, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program