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Q6WP39

- OXLA_TRIST

UniProt

Q6WP39 - OXLA_TRIST

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
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, 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.
Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication.

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 – 891FAD By similarity
Binding sitei108 – 1081Substrate By similarity
Binding sitei241 – 2411Substrate 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 bindingi105 – 1084FAD By similarity
Nucleotide bindingi482 – 4876FAD By similarity
Nucleotide bindingi482 – 4832Substrate 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
Short name:
TSV-LAO
OrganismiTrimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Taxonomic identifieri39682 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeTrimeresurus

Subcellular locationi

Secreted By similarity

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
Signal peptidei1 – 1818 By similarityAdd
BLAST
Chaini19 – 516498L-amino-acid oxidasePRO_0000273572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 191 By similarity
Glycosylationi190 – 1901N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi349 ↔ 430 By similarity
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6WP39.
SMRiQ6WP39. 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.

Q6WP39-1 [UniParc]FASTAAdd to Basket

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MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN    50
PKHVVIVGAG MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW 100
YANLGPMRLP EKHRIVREYI RKFNLQLNEF SQENDNAWHF VKNIRKTVGE 150
VKKDPGVLKY PVKPSEEGKS AEQLYEESLR KVEKELKRTN CSYILNKYDT 200
YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK HDDIFAYEKR 250
FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT 300
SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT 350
KKFREDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ 400
ALDLKDCGDI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT 450
FTPYQFQHFS EALTSHVDRI YFAGEYTAHA HGWIDSSIKS GLTAARDVNR 500
ASENPSGIHL SNDDEL 516
Length:516
Mass (Da):58,601
Last modified:July 5, 2004 - v1
Checksum:iFB5AC0BC171B9288
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161G → E in AAQ16182. 1 Publication
Sequence conflicti53 – 531H → R in AAQ16182. 1 Publication
Sequence conflicti73 – 731A → T in AAQ16182. 1 Publication
Sequence conflicti181 – 1811K → E in AAQ16182. 1 Publication
Sequence conflicti294 – 2941H → Q in AAQ16182. 1 Publication
Sequence conflicti315 – 3151R → G in AAQ16182. 1 Publication
Sequence conflicti354 – 3541R → W in AAQ16182. 1 Publication
Sequence conflicti514 – 5141D → N in AAQ16182. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277739 mRNA. Translation: AAQ56232.1.
AY338966 mRNA. Translation: AAQ16182.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277739 mRNA. Translation: AAQ56232.1 .
AY338966 mRNA. Translation: AAQ16182.1 .

3D structure databases

ProteinModelPortali Q6WP39.
SMRi Q6WP39. 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 characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity."
    Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.
    Biochem. Biophys. Res. Commun. 309:598-604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom and Venom gland.
  2. "Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri."
    Wang J., Huang Q., Teng M., Niu L.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.

Entry informationi

Entry nameiOXLA_TRIST
AccessioniPrimary (citable) accession number: Q6WP39
Secondary accession number(s): Q7T062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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