Reviewed, UniProtKB/Swiss-Prot P56742 (OXLA_CROAT)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2 Alternative name(s):     Apoxin-1     Apoxin I
Organism	Crotalus atrox (Western diamondback rattlesnake)
Taxonomic identifier	8730 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

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 By similarity. Has an antibacterial activity. Has an ability to induce hemorrhage and apoptosis.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated By similarity.
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 Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
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
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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	Ref.2
	Chain	19 – 516	498	L-amino-acid oxidase		PRO_0000099870
Regions
	Nucleotide binding	105 – 106	2	FAD By similarity
	Nucleotide binding	484 – 487	4	FAD By similarity
Sites
	Binding site	81	1	FAD By similarity
	Binding site	89	1	FAD By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	239	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	379	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 189		By similarity
	Disulfide bond	349 ↔ 430		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56742-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6CB90A49A0C015E5	FASTA	516	58,767
	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

References

[1]	"Molecular cloning and its expression of Apoxin 1, an apoptosis inducing protein having L-amino acid oxidase activity from western diamondback rattlesnake venom." Torii S., Mashima T., Naito M., Haga N., Yamane K., Yamamoto K., Fox J.W., Tsuruo T. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from Western diamondback rattlesnake venom." Torii S., Naito M., Tsuruo T. J. Biol. Chem. 272:9539-9542(1997) [PubMed: 9083096] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-38, FUNCTION. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF093248 mRNA. Translation: AAD45200.1.
3D structure databases
HSSP	HSSP built from PDB template 1F8R based on UniProtKB P81382.
SMR	P56742. Positions 22-504.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P56742.
Enzyme and pathway databases
BRENDA	1.4.3.2. 18621.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

OXLA_CROAT

Accession

Primary (citable) accession number: P56742
Secondary accession number(s): Q9PWC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)