AC   MF_04060;
DC   Protein; auto
TR   HAMAP; MF_04060; -; 1; level=0
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Names: ADV_SHUT
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ID   SHUT
DE   RecName: Full=Shutoff protein;
DE   AltName: Full=100 kDa protein;
DE            Short=p100K;
DE   AltName: Full=100K-chaperone protein;
DE   AltName: Full=L4-100K;
DE   AltName: Full=Shutoff protein 100K;
GN   Name=L4;
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CC   -!- FUNCTION: Protein that inhibits host translation while promoting late
CC       viral translation by ribosome shunting. Blocks host cap-dependent
CC       translation by binding to eIF4G, displacing MKNK1 from cap initiation
CC       complexes and preventing EIF4E phosphorylation. Binds to the tripartite
CC       leader sequence of viral late mRNAs and recruits host eIF4G,
CC       PABPC1/poly-A binding protein and 40S ribosomes subunits on viral
CC       mRNAs, allowing ribosome shunting and efficient translation of late
CC       viral mRNAs even though conventional translation via ribosome scanning
CC       from the cap has been shut off in the host cell. During assembly, acts
CC       as a chaperone protein that helps hexon proteins assembly into trimers.
CC   -!- SUBUNIT: Monomer. Interacts with hexon protein; this interaction allows
CC       chaperoning and trimerization of hexon proteins. Interacts (via N-
CC       terminus) with host initiation factor EIF4G (via C-terminus). Interacts
CC       (via RRM domain) with viral mRNAs that contain the tripartite leader;
CC       this interaction allows ribosome shunting and expression of viral late
CC       mRNAs.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Phosphorylated. Tyrosine phosphorylation enhances preferential
CC       binding to tripartite leader mRNAs and allows ribosome shunting.
CC   -!- PTM: Methylated. Asymmetric dimethylation by host PRMT1 of the Arg/Gly-
CC       rich region may regulate shutoff protein binding to hexon and promote
CC       the capsid assembly in the nucleus.
CC   -!- PTM: Might be cleaved by the viral protease.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC       are produced by alternative splicing and alternative polyadenylation of
CC       the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC       present in the N-terminus of all these mRNAs and is recognized by the
CC       viral shutoff protein to provide expression although conventional
CC       translation via ribosome scanning from the cap has been shut off in the
CC       host cell.
CC   -!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
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DR   Pfam; PF02438; Adeno_100; 1; trigger=no
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KW   Chaperone
KW   Eukaryotic host gene expression shutoff by virus
KW   Eukaryotic host translation shutoff by virus
KW   Host cytoplasm
KW   Host gene expression shutoff by virus
KW   Host-virus interaction
KW   Inhibition of eukaryotic host translation factors by virus
KW   Late protein
KW   Methylation
KW   Phosphoprotein
KW   RNA-binding
KW   Translational shunt
KW   Transport
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GO   GO:0030430; C:host cell cytoplasm
GO   GO:0003723; F:RNA binding
GO   GO:0019060; P:intracellular transport of viral protein in host cell
GO   GO:0039657; P:suppression by virus of host gene expression
GO   GO:0039704; P:viral translational shunt
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FT   From: SHUT_ADE02 (P24932)
FT   DOMAIN          348..466
FT                   /note="RRM"
FT   REGION          280..345
FT                   /note="Binding to host EIF4G"
FT   MOD_RES         365
FT                   /note="Phosphotyrosine; by host"
FT   Condition: Y
FT   MOD_RES         682
FT                   /note="Phosphotyrosine; by host"
FT   Condition: Y
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Size: 679-984;
Related: None;
Template: P24932;
Scope:
 Viruses; Adenoviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.3 2019/11/20
//