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F8S0Z5 (OXLA2_CROAD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 13. 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
OrganismCrotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifier8729 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Protein attributes

Sequence length516 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 (L-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemolysis, edema, hemorrhage, apoptosis, antibacterial and antiparasitic activities, as well as regulation 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 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. Glycosylation is needed for activity 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 Ref.3
Chain19 – 516498L-amino-acid oxidase
PRO_5000771366

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding103 – 1064FAD By similarity
Nucleotide binding482 – 4876FAD By similarity
Nucleotide binding482 – 4832Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1061Substrate By similarity
Binding site2391Substrate By similarity
Binding site2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Binding site4751FAD By similarity

Amino acid modifications

Glycosylation3791N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 189 By similarity
Disulfide bond349 ↔ 430 By similarity

Sequences

Sequence LengthMass (Da)Tools
F8S0Z5 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 6CB90A49A0C015E5

FASTA51658,767
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG 

        70         80         90        100        110        120 
MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK 

       130        140        150        160        170        180 
FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV 

       190        200        210        220        230        240 
VKELKRTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD 

       250        260        270        280        290        300 
DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 

       310        320        330        340        350        360 
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCK KKFWEDDGIR 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ 

       430        440        450        460        470        480 
LPKEDIQTFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF 

       490        500        510 
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF 

« Hide

References

[1]"A high-throughput venom-gland transcriptome for the eastern diamondback rattlesnake (Crotalus adamanteus) and evidence for pervasive positive selection across toxin classes."
Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.
Toxicon 57:657-671(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus)."
Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.
BMC Genomics 13:312-312(2012)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[3]"Linking the transcriptome and proteome to characterize the venom of the eastern diamondback rattlesnake (Crotalus adamanteus)."
Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.
J. Proteomics 96:145-158(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-27, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HQ414099 mRNA. Translation: AEJ31977.1.
JU173667 mRNA. Translation: AFJ49193.1.

3D structure databases

ProteinModelPortalF8S0Z5.
SMRF8S0Z5. Positions 21-503.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameOXLA2_CROAD
AccessionPrimary (citable) accession number: F8S0Z5
Secondary accession number(s): J3S821
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 13 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