AC   PRU00275;
DC   Domain;
TR   PROSITE; PS50175; ASP_PROT_RETROV; 1; level=0
XX
Names: Eukaryotic and viral aspartyl proteases
Function: Belongs to peptidase family A2
XX
case <OS:Human immunodeficiency virus type 1> and <FTTag:act_site>
DE   + RecName: EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
DE   + RecName: EC=3.4.23.47;
else case <FTTag:act_site>
DE   + RecName: EC=3.4.23.-;
end case
XX
case <OS:Human immunodeficiency virus type 1>
CC   -!- FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic
CC       cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC       release of the virion from the plasma membrane. Cleavages take place as
CC       an ordered, step-wise cascade to yield mature proteins. This process is
CC       called maturation. Displays maximal activity during the budding process
CC       just prior to particle release from the cell. Also cleaves Nef and Vif,
CC       probably concomitantly with viral structural proteins on maturation of
CC       virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off
CC       the capped cellular mRNA translation. The resulting inhibition of
CC       cellular protein synthesis serves to ensure maximal viral gene
CC       expression and to evade host immune response. Also mediates cleavage of
CC       host YTHDF3. Mediates cleavage of host CARD8, thereby activating the
CC       CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient
CC       CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade
CC       CARD8-sensing when its protease remains inactive in infected cells
CC       prior to viral budding.
else case <OC:Retroviridae>
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
CC       and Gag-Pol polyproteins during or shortly after the release of the
CC       virion from the plasma membrane. Cleavages take place as an ordered,
CC       step-wise cascade to yield mature proteins. This process is called
CC       maturation. Displays maximal activity during the budding process just
CC       prior to particle release from the cell.
end case
case <OS:Human immunodeficiency virus type 1> and <FTTag:act_site>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific for a P1 residue that is hydrophobic, and P1'
CC         variable, but often Pro.; EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase for which the P1 residue is preferably
CC         hydrophobic.; EC=3.4.23.47;
end case
XX
DR   PROSITE; PS00141; ASP_PROTEASE; 1; trigger=no
XX
case <FTTag:act_site>
GO   GO:0004190; F:aspartic-type endopeptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
XX
KW   Aspartyl protease
KW   Hydrolase
KW   Protease
end case
XX
FT   From: PS50175
FT   DOMAIN          from..to
FT                   /note="Peptidase A2 #"
case <OC:Retroviridae>
FT   ACT_SITE        6
FT                   /note="Protease; shared with dimeric partner"
FT   Tag: act_site; Condition: D
else
FT   ACT_SITE        6
FT                   /note="@TARGET_ACTIVITY_VISIBILITY|For protease activity@"
FT   Tag: act_site; Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 40-82;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P51518;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Version: 22
# Last updated date: 2024-07-18
# Created date: 2003-12-12
//