SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0C2D5

- OXLA_PROFL

UniProt

P0C2D5 - OXLA_PROFL

(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)

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.2 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
Complete GO annotation...

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
Complete GO annotation...

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → H AA sequence 1 Publication
Sequence conflicti10 – 101C → Y AA sequence 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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: February 19, 2014
This is version 27 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

Similar proteinsi