ID   OXLA_CROAD              Reviewed;         516 AA.
AC   O93364;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   AltName: Full=Apoxin-1;
DE   AltName: Full=Apoxin I;
DE   Flags: Precursor;
OS   Crotalus adamanteus (Eastern diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-44 AND 106-130.
RC   TISSUE=Venom, and Venom gland;
RX   MEDLINE=98369573; PubMed=9703950; DOI=10.1006/bbrc.1998.9024;
RA   Raibekas A.A., Massey V.;
RT   "Primary structure of the snake venom L-amino acid oxidase shows high
RT   homology with the mouse B cell interleukin 4-induced Fig1 protein.";
RL   Biochem. Biophys. Res. Commun. 248:476-478(1998).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Has an antibacterial
CC       effect and an ability to induce apoptosis. The H(2)O(2) produced
CC       by L-amino acid oxidation is involved apoptosis and hemorrhage
CC       caused by the venom (By similarity).
CC   -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid
CC       + NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF071564; AAC32267.1; -; mRNA.
DR   PIR; JE0266; JE0266.
DR   HSSP; P81382; 1F8R.
DR   SMR; O93364; 22-504.
DR   HOVERGEN; O93364; -.
DR   BRENDA; 1.4.3.2; 18620.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Glycoprotein; Oxidoreductase; Secreted; Signal; Toxin.
FT   SIGNAL        1     18
FT   CHAIN        19    516       L-amino-acid oxidase.
FT                                /FTId=PRO_0000001706.
FT   NP_BIND     105    106       FAD (By similarity).
FT   NP_BIND     484    487       FAD (By similarity).
FT   BINDING      81     81       FAD (By similarity).
FT   BINDING      89     89       FAD (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     239    239       Substrate (By similarity).
FT   BINDING     279    279       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     390    390       Substrate (By similarity).
FT   BINDING     475    475       FAD (By similarity).
FT   CARBOHYD    379    379       N-linked (GlcNAc...) (Potential).
FT   DISULFID     28    189       By similarity.
FT   DISULFID    349    430       By similarity.
SQ   SEQUENCE   516 AA;  58662 MW;  FDFAA77A49FDA05A CRC64;
     MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG
     MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK
     FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV
     VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD
     DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM
     SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH
     GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHE
     LPKEDIQTFC HPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF
     HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF
//