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ProRule PRU00275


General rule information [?]

Accession PRU00275
Dates 12-DEC-2003 (Created)
18-JUL-2024 (Last updated, Version 21)
Data class Domain;
Predictors PROSITE; PS50175; ASP_PROT_RETROV
Name Eukaryotic and viral aspartyl proteases
Function Belongs to peptidase family A2
Scope(s) Eukaryota
Viruses
Example(s) P51518 (PRO_SRV2);

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OS:Human immunodeficiency virus type 1> and <FTTag:act_site>
Protein name + RecName: EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
Protein name + RecName: EC=3.4.23.47;
else case <FTTag:act_site>
Protein name + RecName: EC=3.4.23.-;
end case

Comments [?]

case <OS:Human immunodeficiency virus type 1>
FUNCTION[Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding.
else case <OC:Retroviridae>
FUNCTIONThe aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.
end case
case <OS:Human immunodeficiency virus type 1> and <FTTag:act_site>
CATALYTIC ACTIVITY Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
CATALYTIC ACTIVITY Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47;
end case

Keywords [?]

Aspartyl protease
Hydrolase
Protease
end case

Gene Ontology [?]

case <FTTag:act_site>
GO:0004190; Molecular function:aspartic-type endopeptidase activity
GO:0016787; Molecular function:hydrolase activity
GO:0008233; Molecular function:peptidase activity

Cross-references [?]

PROSITE PS00141; ASP_PROTEASE; 1;

Features [?]

From: PS50175
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase A2 #"
case <OC:Retroviridae>
ACT_SITE 6 6 /note="Protease; shared with dimeric partner" act_site D
else
ACT_SITE 6 6 /note="@TARGET_ACTIVITY_VISIBILITY|For protease activity@" act_site D
end case

Additional information [?]

Size range 40-82 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.



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UniProtKB rule member sequences [?]