ID   OXLA8_DEIAC             Reviewed;          19 AA.
AC   P0DI85;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-MAY-2023, entry version 21.
DE   RecName: Full=L-amino-acid oxidase ACTX-8 {ECO:0000303|PubMed:17275856};
DE            Short=LAAO;
DE            Short=LAO {ECO:0000303|PubMed:17275856};
DE            EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE   Flags: Fragment;
OS   Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX   NCBI_TaxID=36307;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION IN INDUCTION OF APOPTOSIS, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17275856; DOI=10.1016/j.lfs.2006.12.024;
RA   Zhang L., Wei L.J.;
RT   "ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus
RT   snake venom, induces apoptosis in Hela cervical cancer cells.";
RL   Life Sci. 80:1189-1197(2007).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme. Exhibits diverse biological activities, such as hemorrhage,
CC       hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell
CC       lines, antibacterial and antiparasitic activities, as well as
CC       regulation of platelet aggregation. Its effect on platelets is
CC       controversial, since it either induces aggregation or inhibits agonist-
CC       induced aggregation. These different effects are probably due to
CC       different experimental conditions (By similarity). Induces apoptosis in
CC       HeLa cervical cancer cells. Both the caspase-dependent and the
CC       mitochondrial pathways seem to be involved in apoptosis
CC       (PubMed:17275856). {ECO:0000250, ECO:0000269|PubMed:17275856}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000250|UniProtKB:P81382}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17275856}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17275856}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DI85; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemostasis impairing toxin; Oxidoreductase; Secreted; Toxin.
FT   CHAIN           1..>19
FT                   /note="L-amino-acid oxidase ACTX-8"
FT                   /id="PRO_0000412592"
FT   NON_TER         19
FT                   /evidence="ECO:0000303|PubMed:17275856"
SQ   SEQUENCE   19 AA;  2400 MW;  DDC54698346D08FA CRC64;
     ADDRNPLEEF RENNYEEFL
//