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P56742

- OXLA_CROAT

UniProt

P56742 - OXLA_CROAT

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Crotalus atrox (Western diamondback rattlesnake)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. In addition, this protein induces hemorrhage and apoptosis.By similarity1 Publication

    Catalytic activityi

    An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.2 Publications

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FADBy similarity
    Binding sitei106 – 1061SubstrateBy similarity
    Binding sitei239 – 2391SubstrateBy similarity
    Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Binding sitei475 – 4751FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FADBy similarity
    Nucleotide bindingi81 – 822FADBy similarity
    Nucleotide bindingi103 – 1064FADBy similarity
    Nucleotide bindingi482 – 4876FADBy similarity
    Nucleotide bindingi482 – 4832SubstrateBy similarity

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW
    3. hemolysis in other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemorrhagic toxin, Hemostasis impairing toxin, Oxidoreductase, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    Alternative name(s):
    Apoxin I
    Apoxin-1
    OrganismiCrotalus atrox (Western diamondback rattlesnake)
    Taxonomic identifieri8730 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18183 PublicationsAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000099870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 189By similarity
    Disulfide bondi349 ↔ 430By similarity
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Glycosylation is needed for activity.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP56742.
    SMRiP56742. Positions 21-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P56742-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN    50
    PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA 100
    NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK 150
    NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VKELKRTNCK YILDKYDTYS 200
    TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD 250
    EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 300
    SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCK 350
    KKFWEDDGIR GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
    ALDFKDCADI VINDLSLIHQ LPKEDIQTFC RPSMIQRWSL DKYAMGGITT 450
    FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR 500
    ASENPSGIHL SNDNEF 516
    Length:516
    Mass (Da):58,767
    Last modified:January 23, 2007 - v2
    Checksum:i6CB90A49A0C015E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093248 mRNA. Translation: AAD45200.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093248 mRNA. Translation: AAD45200.1 .

    3D structure databases

    ProteinModelPortali P56742.
    SMRi P56742. Positions 21-503.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional analysis of apoxin I, a snake venom-derived apoptosis-inducing factor with L-amino acid oxidase activity."
      Torii S., Yamane K., Mashima T., Haga N., Yamamoto K., Fox J.W., Naito M., Tsuruo T.
      Biochemistry 39:3197-3205(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38; 97-109; 126-138; 240-247 AND 491-505, CATALYTIC ACTIVITY, GLYCOSYLATION.
      Tissue: Venom and Venom gland.
    2. "Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from Western diamondback rattlesnake venom."
      Torii S., Naito M., Tsuruo T.
      J. Biol. Chem. 272:9539-9542(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-38, FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Venom.
    3. "Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches."
      Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.
      J. Proteome Res. 8:3055-3067(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-33, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_CROAT
    AccessioniPrimary (citable) accession number: P56742
    Secondary accession number(s): Q9PWC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3