Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0C2D5

- OXLA_PROFL

UniProt

P0C2D5 - OXLA_PROFL

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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, 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. This protein has an ability to induce hemolysis and apoptosis.By similarity2 Publications

    Catalytic activityi

    An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

    Cofactori

    FAD.By 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
    Alternative name(s):
    Apoxin I-like protein
    Okinawa Habu apoxin protein-1
    Short name:
    OHAP-1
    OrganismiProtobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
    Taxonomic identifieri88087 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

    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
    Chaini1 – ›30›30L-amino-acid oxidasePRO_0000273570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi10 ↔ ?By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Sequencei

    Sequence statusi: Fragment.

    P0C2D5-1 [UniParc]FASTAAdd to Basket

    « Hide

    ADDRNPLEEC FRETDYEEFL EIARNGLKKT                         30
    Length:30
    Mass (Da):3,603
    Last modified:September 21, 2011 - v2
    Checksum:i37AE5DC946D491D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21D → H AA sequence (PubMed:9781840)Curated
    Sequence conflicti10 – 101C → Y AA sequence (PubMed:9781840)Curated
    Non-terminal residuei30 – 301

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Apoptotic effect in the glioma cells induced by specific protein extracted from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to oxidative stress."
      Sun L.-K., Yoshii Y., Hyodo A., Tsurushima H., Saito A., Harakuni T., Li Y.-P., Kariya K., Nozaki M., Morine N.
      Toxicol. in Vitro 17:169-177(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Venom.
    2. "Characterization of an apoptosis-inducing factor in Habu snake venom as a glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro."
      Abe Y., Shimoyama Y., Munakata H., Ito J., Nagata N., Ohtsuki K.
      Biol. Pharm. Bull. 21:924-927(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBUNIT.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_PROFL
    AccessioniPrimary (citable) accession number: P0C2D5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 28 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3