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.

P56742

- OXLA_CROAT

UniProt

P56742 - OXLA_CROAT

(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
Crotalus atrox (Western diamondback rattlesnake)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 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 – 891FAD By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei239 – 2391Substrate By similarity
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei390 – 3901Substrate By similarity
Binding sitei475 – 4751FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD By similarity
Nucleotide bindingi81 – 822FAD By similarity
Nucleotide bindingi103 – 1064FAD By similarity
Nucleotide bindingi482 – 4876FAD By similarity
Nucleotide bindingi482 – 4832Substrate By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18183 Publications
Add
BLAST
Chaini19 – 516498L-amino-acid oxidase
PRO_0000099870Add
BLAST

Amino acid modifications

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

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.

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: February 19, 2014
This is version 58 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