ID OXLA_CROAT Reviewed; 516 AA. AC P56742; Q9PWC9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 03-MAY-2023, entry version 83. DE RecName: Full=L-amino-acid oxidase apoxin-1 {ECO:0000305}; DE Short=LAAO; DE Short=LAO {ECO:0000303|PubMed:10727211, ECO:0000303|PubMed:9083096}; DE EC=1.4.3.2 {ECO:0000269|PubMed:10727211, ECO:0000269|PubMed:9083096}; DE AltName: Full=Apoxin I {ECO:0000303|PubMed:10727211, ECO:0000303|PubMed:9083096}; DE Flags: Precursor; OS Crotalus atrox (Western diamondback rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=8730; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38; 97-109; 126-138; RP 240-247 AND 491-505, CATALYTIC ACTIVITY, AND GLYCOSYLATION. RC TISSUE=Venom, and Venom gland; RX PubMed=10727211; DOI=10.1021/bi992416z; RA Torii S., Yamane K., Mashima T., Haga N., Yamamoto K., Fox J.W., Naito M., RA Tsuruo T.; RT "Molecular cloning and functional analysis of apoxin I, a snake venom- RT derived apoptosis-inducing factor with L-amino acid oxidase activity."; RL Biochemistry 39:3197-3205(2000). RN [2] RP PROTEIN SEQUENCE OF 19-38, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Venom; RX PubMed=9083096; DOI=10.1074/jbc.272.14.9539; RA Torii S., Naito M., Tsuruo T.; RT "Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase RT activity purified from Western diamondback rattlesnake venom."; RL J. Biol. Chem. 272:9539-9542(1997). RN [3] RP PROTEIN SEQUENCE OF 19-33, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=19371136; DOI=10.1021/pr900249q; RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.; RT "Exploring the venom proteome of the western diamondback rattlesnake, RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library RT approaches."; RL J. Proteome Res. 8:3055-3067(2009). 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:10727211, PubMed:9083096). Shows activity on L-Leu CC (PubMed:10727211, PubMed:9083096). Exhibits diverse biological CC activities, such as hemolysis, 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). In addition, this protein induces hemorrhage and CC apoptosis. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:10727211, CC ECO:0000269|PubMed:9083096}. 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:10727211, CC ECO:0000269|PubMed:9083096}; 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:10727211, CC ECO:0000269|PubMed:9083096}; 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:9083096}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:9083096}. CC -!- PTM: N-glycosylated. Glycosylation is needed for activity. CC {ECO:0000269|PubMed:10727211}. 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 EMBL; AF093248; AAD45200.1; -; mRNA. DR AlphaFoldDB; P56742; -. DR SMR; P56742; -. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB. 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. DR Gene3D; 3.90.660.10; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR Pfam; PF01593; Amino_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing; KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis; KW Hemorrhagic toxin; Hemostasis impairing toxin; Oxidoreductase; Secreted; KW Signal; Toxin. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:10727211, FT ECO:0000269|PubMed:19371136, ECO:0000269|PubMed:9083096" FT CHAIN 19..516 FT /note="L-amino-acid oxidase apoxin-1" FT /id="PRO_0000099870" FT BINDING 61..62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 81..82 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 103..106 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 390 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 475 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 482..487 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 482..483 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..189 FT /evidence="ECO:0000250|UniProtKB:P81382" FT DISULFID 349..430 FT /evidence="ECO:0000250|UniProtKB:P81382" SQ SEQUENCE 516 AA; 58767 MW; 6CB90A49A0C015E5 CRC64; MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VKELKRTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCK KKFWEDDGIR GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ LPKEDIQTFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF //