ID   OXLA_PROFL              Reviewed;          30 AA.
AC   P0C2D5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO {ECO:0000303|PubMed:12650671};
DE            Short=LAO {ECO:0000303|PubMed:9781840};
DE            EC=1.4.3.2 {ECO:0000269|PubMed:12650671};
DE   AltName: Full=Apoxin I-like protein {ECO:0000303|PubMed:9781840};
DE   AltName: Full=Okinawa Habu apoxin protein-1 {ECO:0000303|PubMed:12650671};
DE            Short=OHAP-1 {ECO:0000303|PubMed:12650671};
DE   Flags: Fragment;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Venom;
RX   PubMed=12650671; DOI=10.1016/s0887-2333(03)00010-9;
RA   Sun L.-K., Yoshii Y., Hyodo A., Tsurushima H., Saito A., Harakuni T.,
RA   Li Y.-P., Kariya K., Nozaki M., Morine N.;
RT   "Apoptotic effect in the glioma cells induced by specific protein extracted
RT   from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to
RT   oxidative stress.";
RL   Toxicol. in Vitro 17:169-177(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=9781840; DOI=10.1248/bpb.21.924;
RA   Abe Y., Shimoyama Y., Munakata H., Ito J., Nagata N., Ohtsuki K.;
RT   "Characterization of an apoptosis-inducing factor in Habu snake venom as a
RT   glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro.";
RL   Biol. Pharm. Bull. 21:924-927(1998).
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 (PubMed:12650671, PubMed:9781840). Shows activity on L-Leu
CC       (PubMed:12650671, PubMed:9781840). Exhibits diverse biological
CC       activities, such as hemorrhage, edema, antibacterial and antiparasitic
CC       activities, as well as regulation of platelet aggregation. Effects of
CC       snake L-amino oxidases on platelets are controversial, since they
CC       either induce aggregation or inhibit agonist-induced aggregation. These
CC       different effects are probably due to different experimental conditions
CC       (By similarity). This protein has an ability to induce hemolysis and
CC       apoptosis. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:12650671,
CC       ECO:0000269|PubMed:9781840}.
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; Evidence={ECO:0000269|PubMed:12650671,
CC         ECO:0000269|PubMed:9781840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:12650671,
CC         ECO:0000269|PubMed:9781840};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC       are non-covalently linked homodimers. {ECO:0000269|PubMed:9781840}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9781840}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9781840}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0C2D5; -.
DR   SMR; P0C2D5; -.
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:0044179; P:hemolysis in 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..>30
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000273570"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   CONFLICT        2
FT                   /note="D -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="C -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         30
FT                   /evidence="ECO:0000303|PubMed:12650671"
SQ   SEQUENCE   30 AA;  3603 MW;  37AE5DC946D491D0 CRC64;
     ADDRNPLEEC FRETDYEEFL EIARNGLKKT