NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-44 AND 106-130.
TISSUE=Venom, and Venom gland;
DOI=10.1006/bbrc.1998.9024; PubMed=9703950 [NCBI, ExPASy, EBI, Israel, Japan]
Raibekas A.A., Massey V.;
"Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein.";
Biochem. Biophys. Res. Commun. 248:476-478(1998).

Comments

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Has an antibacterial effect and an ability to induce apoptosis. The H(2)O(2) produced by L-amino acid oxidation is involved apoptosis and hemorrhage caused by the venom (By similarity).
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated (By similarity).
SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF071564; AAC32267.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JE0266; JE0266.

3D structure databases

HSSP

P81382; 1F8R. [HSSP ENTRY / PDB]

SMR

O93364; 22-504.

ModBase

O93364.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0001716;	Molecular function: L-amino-acid oxidase activity (inferred from electronic annotation from EC).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR002937; Amino_oxidase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Graphical view of domain structure.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Phylogenomic databases

HOVERGEN

O93364; -.

Other

ProtoNet

O93364.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 516`	`498`	`L-amino-acid oxidase.`	`PRO_0000001706`
`NP_BIND`	`105 106`	`2`	`FAD (By similarity).`
`NP_BIND`	`484 487`	`4`	`FAD (By similarity).`
`BINDING`	`81 81`		`FAD (By similarity).`
`BINDING`	`89 89`		`FAD (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`239 239`		`Substrate (By similarity).`
`BINDING`	`279 279`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`390 390`		`Substrate (By similarity).`
`BINDING`	`475 475`		`FAD (By similarity).`
`CARBOHYD`	`379 379`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`28 189`		`By similarity.`
`DISULFID`	`349 430`		`By similarity.`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 58662 Da [This is the MW of the unprocessed precursor]

CRC64: FDFAA77A49FDA05A [This is a checksum on the sequence]

        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 
VEELRSTNCK 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 SGTKIFLTCT KKFWEDDGIH 

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

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

       490        500        510 
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF

O93364 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools