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B0VXW0

- OXLA_SISCA

UniProt

B0VXW0 - OXLA_SISCA

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, 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.By similarity

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    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-EC

    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, 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
    OrganismiSistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
    Taxonomic identifieri8762 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeSistrurus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000412605Add
    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.By similarity

    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

    ProteinModelPortaliB0VXW0.
    SMRiB0VXW0. 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.

    B0VXW0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLTATSN    50
    PKRVVIVGAG MSGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKEDWYA 100
    NLGPMRLPTK HRIVREYIKK FGLELNEFFQ ENDNAWYFIK NIRKRVQEVK 150
    NNPGLLKYPV KPSETGKSAG QLYEESLRKV VEELRSTNCK YILDKYDTYS 200
    TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD 250
    EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM 300
    SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT 350
    KKFWEDEGIH GGKSTTDLPS RSIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
    ALDFKDCADI VINDLSLIHQ LPKEDIQTFC HPSKIQRWSL DRYAMGGITT 450
    FTPYQFQHFS EALTAPFNRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR 500
    ASENPSGIHL SNDNEF 516
    Length:516
    Mass (Da):58,569
    Last modified:April 8, 2008 - v1
    Checksum:iBABA9844650EB381
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ464267 mRNA. Translation: ABG26996.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ464267 mRNA. Translation: ABG26996.1 .

    3D structure databases

    ProteinModelPortali B0VXW0.
    SMRi B0VXW0. 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. "The venom gland transcriptome of the Desert Massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea)."
      Pahari S., Mackessy S.P., Kini R.M.
      BMC Mol. Biol. 8:115-115(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom gland.

    Entry informationi

    Entry nameiOXLA_SISCA
    AccessioniPrimary (citable) accession number: B0VXW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 19 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3