Skip Header

Contribute Send feedback
Read comments (?) or add your own

B5U6Y8 (OXLA_ECHOC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. 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
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=LAAO
Short name=LAO
EC=1.4.3.2
OrganismEchis ocellatus (Ocellated saw-scaled viper)
Taxonomic identifier99586 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Echis

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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, 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.

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.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

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

Signal peptide1 – 1818 By similarity
Chain19 – 504486L-amino-acid oxidase
PRO_0000412602

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding105 – 1084FAD By similarity
Nucleotide binding482 – 4876FAD By similarity
Nucleotide binding482 – 4832Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1081Substrate By similarity
Binding site2411Substrate By similarity
Binding site2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Binding site4751FAD By similarity

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 191 By similarity
Disulfide bond349 ↔ 430 By similarity

Sequences

Sequence LengthMass (Da)Tools
B5U6Y8 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 602E5B4A9FCEE797

FASTA50456,523
        10         20         30         40         50         60 
MNIFFMFSLL FLATLGSCAD DKNPLEECFR EADYEEFLEI AKNGLKKTSN PKDIVVVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL AGAGHKVTVL EASQLVGGRV RTHRNAKEGW YANLGPMRIP EKHRIVREYI 

       130        140        150        160        170        180 
RKFGLELNEF VQETDNGWYF VKNIRKRVGE VKKDPGLLKY PVKPSEAGKS AGQLYQEALG 

       190        200        210        220        230        240 
KAVEELKRTN CSYMLNKYDT YSTKEYLIKE GNLSTGAVDM IGDLMNEDSG YYVSFVESMK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE KSVLFKARVT KIQQNAEKVR VTYQTAAKTL 

       310        320        330        340        350        360 
SDVTADYVIV CTTSRAARRI NFKPPLPPKK AHALRSVHYR SATKIFLTCT KKFWEDDGIQ 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDSNFFL SLTLNECADI VFSDLSSIHQ 

       430        440        450        460        470        480 
LPKNDIQKFC NPSVIQKWSL DRYAMGAITT FTPYQFQDYS KALTAPAGRV YFAGEYTANA 

       490        500 
HGWIDSTIKS GLTAARDVNQ ASEL

« Hide

References

[1]"Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus."
Wagstaff S.C., Sanz L., Juarez P., Harrison R.A., Calvete J.J.
J. Proteomics 71:609-623(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom and Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM177950 mRNA. Translation: CAQ72894.1.

3D structure databases

ProteinModelPortalB5U6Y8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOXLA_ECHOC
AccessionPrimary (citable) accession number: B5U6Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 4, 2008
Last modified: October 3, 2012
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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents