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Q4JHE2 (OXLA_NOTSC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 47. 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
OrganismNotechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
Taxonomic identifier70142 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Notechis ›

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. 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 By similarity.

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 – 517499L-amino-acid oxidase
PRO_5000140379

Regions

Nucleotide binding62 – 632FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding106 – 1094FAD By similarity
Nucleotide binding483 – 4886FAD By similarity
Nucleotide binding483 – 4842Substrate By similarity

Sites

Binding site901FAD By similarity
Binding site1091Substrate By similarity
Binding site2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3911Substrate By similarity
Binding site4761FAD By similarity

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 192 By similarity
Disulfide bond350 ↔ 431 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JHE2 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: E5A0DFF675FF34E1

FASTA51759,058
        10         20         30         40         50         60 
MNVFFMFSLL FLAALESCAD DRRRPLEECF QEADYEEFLE IARNGLNETS NPKHVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LAGAGHNVTL LEASERVGGR VNTYRNETEG WYVNLGPMRL PERHRIIREY 

       130        140        150        160        170        180 
IRKFGLKLNE FLQENENAWY FIRNIRKRVW EVKKDPGVFK YPVEPSEEGK SASQLYRESL 

       190        200        210        220        230        240 
EKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSRGAVD MIGKLPNEDS SYYLSFIESL 

       250        260        270        280        290        300 
KSDDLFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEEV RVAYQTPAKT 

       310        320        330        340        350        360 
LSYVTADYVI VCSTSRAARR IYFEPPLPPK KAHALRSIHY RSGTKIFLTC TRKFWEADGI 

       370        380        390        400        410        420 
HGGKSTTDLP SRFIYYPNHN FTSDVGVIVA YTLADDADFF QALDIKTSAD IVINDLSLIH 

       430        440        450        460        470        480 
QLPKEEIQAL CYPSMIKKWS LDKYAMGAIT SFTPYQFQDF IETVAAPVGR IYFAGEYTAR 

       490        500        510 
VHGWLDSTIK SGLTAARDVN RASQKPSRRQ LSNDNEL

« Hide

References

[1]"Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species."
St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.
Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ088991 mRNA. Translation: AAY89681.1.

3D structure databases

HSSPHSSP built from PDB template 2BXR based on UniProtKB P21397.
ProteinModelPortalQ4JHE2.
SMRQ4JHE2. Positions 23-505.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameOXLA_NOTSC
AccessionPrimary (citable) accession number: Q4JHE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: August 2, 2005
Last modified: March 6, 2013
This is version 47 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

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