Reviewed, UniProtKB/Swiss-Prot Q6WP39 (OXLA_TRIST)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase     EC=1.4.3.2 Alternative name(s):     TSV-LAO     LAAO       Short name=LAO
Organism	Trimeresurus stejnegeri (Chinese green tree viper)
Taxonomic identifier	39682 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Viridovipera

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Inhibits platelet aggregation. Has an ability to induce apoptosis, and hemorrhage. Has an antibacterial activity By similarity. Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.
Catalytic activity	An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
Cofactor	FAD By similarity.
Subunit structure	Homodimer.
Subcellular location	SecretedBy similarity.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation
Cellular component	Secreted
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Antiviral protein Oxidoreductase Toxin
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 516	498	L-amino-acid oxidase		PRO_0000273572
Regions
	Nucleotide binding	107 – 108	2	FAD By similarity
	Nucleotide binding	484 – 487	4	FAD By similarity
Sites
	Binding site	62	1	FAD By similarity
	Binding site	81	1	FAD By similarity
	Binding site	89	1	FAD By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	241	1	Substrate By similarity
	Binding site	279	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	390	1	Substrate By similarity
	Binding site	475	1	FAD By similarity
Amino acid modifications
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 191		By similarity
	Disulfide bond	349 ↔ 430		By similarity
Experimental info
	Sequence conflict	16	1	G → E in AAQ16182. Ref.2
	Sequence conflict	53	1	H → R in AAQ16182. Ref.2
	Sequence conflict	73	1	A → T in AAQ16182. Ref.2
	Sequence conflict	181	1	K → E in AAQ16182. Ref.2
	Sequence conflict	294	1	H → Q in AAQ16182. Ref.2
	Sequence conflict	315	1	R → G in AAQ16182. Ref.2
	Sequence conflict	354	1	R → W in AAQ16182. Ref.2
	Sequence conflict	514	1	D → N in AAQ16182. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6WP39-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FB5AC0BC171B9288	FASTA	516	58,601
	10 20 30 40 50 60 MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG 70 80 90 100 110 120 MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW YANLGPMRLP EKHRIVREYI 130 140 150 160 170 180 RKFNLQLNEF SQENDNAWHF VKNIRKTVGE VKKDPGVLKY PVKPSEEGKS AEQLYEESLR 190 200 210 220 230 240 KVEKELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK 250 260 270 280 290 300 HDDIFAYEKR FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT 310 320 330 340 350 360 SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFREDEGIH 370 380 390 400 410 420 GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDLKDCGDI VINDLSLIHQ 430 440 450 460 470 480 LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTSHVDRI YFAGEYTAHA 490 500 510 HGWIDSSIKS GLTAARDVNR ASENPSGIHL SNDDEL

References

[1]	"Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity." Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y. Biochem. Biophys. Res. Commun. 309:598-604(2003) [PubMed: 12963032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY. Tissue: Venom and Venom gland.
[2]	"Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri." Wang J., Huang Q., Teng M., Niu L. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY277739 mRNA. Translation: AAQ56232.1. AY338966 mRNA. Translation: AAQ16182.1.
3D structure databases
HSSP	HSSP built from PDB template 1F8R based on UniProtKB P81382.
SMR	Q6WP39. Positions 22-504.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q6WP39.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE. PR00757. AMINEOXDASEF. PR00368. FADPNR.
ProtoNet	Search...

Entry information

Entry name

OXLA_TRIST

Accession

Primary (citable) accession number: Q6WP39
Secondary accession number(s): Q7T062

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)