ID   OXLA_TRIFL              Reviewed;          20 AA.
AC   P0C2D5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   AltName: Full=Apoxin I-like protein;
DE   Flags: Fragment;
OS   Trimeresurus flavoviridis (Habu) (Protobothrops flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=88087;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=9781840;
RA   Abe Y., Shimoyama Y., Munakata H., Ito J., Nagata N., Ohtsuki K.;
RT   "Characterization of an apoptosis-inducing factor in Habu snake venom
RT   as a glycyrrhizin (GL)-binding protein potently inhibited by GL in
RT   vitro.";
RL   Biol. Pharm. Bull. 21:924-927(1998).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Inhibits platelet
CC       aggregation. Has an ability to induce hemorrhage. Has an
CC       antibacterial activity (By similarity). Has an ability to induce
CC       hemolysis and apoptosis.
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 (By similarity).
CC   -!- SUBUNIT: Monomer.
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.
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DR   HOVERGEN; P0C2D5; -.
DR   BRENDA; 1.4.3.2; 18619.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Cytolysis;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >20       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273570.
FT   NON_TER      20     20
SQ   SEQUENCE   20 AA;  2574 MW;  95E97283C86588E7 CRC64;
     AHDRNPLEEY FRETDYEEFL
//