AC   MF_04088;
DC   Protein; auto
TR   HAMAP; MF_04088; -; 1; level=0
XX
Names: ROTA_NSP1
XX
ID   NSP1
DE   RecName: Full=Non-structural protein 1;
DE            Short=NSP1;
DE   AltName: Full=NCVP2;
DE   AltName: Full=Non-structural RNA-binding protein 53;
DE            Short=NS53;
XX
case <FTTag:ILD>
CC   -!- FUNCTION: Plays a role in the inhibition of host innate immunity by
CC       inducing the degradation of key host factors required to activate
CC       interferon production such as IRF3, IRF5 or IRF7. Associates with
CC       components of cullin RING ligases (CRLs) including CUL1 or CUL3, which
CC       are essential multisubunit ubiquitination complexes, to modulate their
CC       activities. Recognizes the host NF-kappa-B regulator BTRC through the
CC       presence of a DSGXS motif in the C-terminal substrate recognition
CC       domain.
CC   -!- SUBUNIT: Interacts (via C-terminus) with host IRF3; this interaction
CC       leads to IRF3 degradation. Interacts with host IRF7; this interaction
CC       leads to IRF7 degradation. Interacts with host CUL1 and CUL3. Interacts
CC       with host BTRC.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton.
CC   -!- DOMAIN: The integrity of the zinc-binding domain in NSP1 is important
CC       for degradation of host IRF3.
CC   -!- PTM: The C-terminal region is phosphorylated by host CKII/CSNK2A1.
CC       Phosphorylation of the DSGXS motif is essential for host NF-kappa-B
CC       inhibition.
else
CC   -!- FUNCTION: Plays a role in the inhibition of host innate immunity by
CC       inducing the degradation of key host factors required to activate
CC       interferon production such as IRF3, IRF5 or IRF7. Associates with
CC       components of cullin RING ligases (CRLs) including CUL1 or CUL3, which
CC       are essential multisubunit ubiquitination complexes, to modulate their
CC       activities.
CC   -!- SUBUNIT: Interacts (via C-terminus) with host IRF3; this interaction
CC       leads to IRF3 degradation. Interacts with host IRF7; this interaction
CC       leads to IRF7 degradation. Interacts with host CUL1 and CUL3.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton.
CC   -!- DOMAIN: The integrity of the zinc-binding domain in NSP1 is important
CC       for degradation of host IRF3.
end case
CC   -!- SIMILARITY: Belongs to the rotavirus NSP1 family.
XX
DR   Pfam; PF00981; Rota_NS53; 1; trigger=no
XX
KW   Host cytoplasm
KW   Host cytoskeleton
KW   Host-virus interaction
KW   Inhibition of host innate immune response by virus
KW   Inhibition of host IRF3 by virus
KW   Inhibition of host IRF7 by virus
case <FTTag:ILD>
KW   Phosphoprotein
KW   Inhibition of host NF-kappa-B by virus
end case
KW   Inhibition of host RLR pathway by virus
KW   Interferon antiviral system evasion
KW   Metal-binding
KW   RNA-binding
KW   Viral immunoevasion
XX
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0044163; C:host cytoskeleton
GO   GO:0046872; F:metal ion binding
GO   GO:0003723; F:RNA binding
GO   GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
GO   GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity
case <FTTag:ILD>
GO   GO:0039644; P:suppression by virus of host NF-kappaB cascade
end case
XX
FT   From: NSP1_ROTS4 (Q99FX5)
FT   REGION          1..81
FT                   /note="RNA-binding"
FT   REGION          82..177
FT                   /note="Important for cytoskeleton localization"
FT   From: NSP1_ROTP5 (Q84940)
FT   REGION          42..79
FT                   /note="Zinc-binding domain"
FT   REGION          317..Cter
FT                   /note="Interaction with host IRF3"
FT   MOTIF           479..483
FT                   /note="IKBKB-like degron (ILD) motif"
FT   Tag: ILD; Condition: D-S-G-x-S
XX
Size: 393-496;
Related: None;
Template: Q99FX5; Q84940;
Scope:
 Viruses; Rotavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.4 2021/10/28
//