A0A2Z4QJG8 · A0A2Z4QJG8_9ADEN
- ProteinShutoff protein
- GeneL4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids696 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and recruits host eIF4G, PABPC1/poly-A binding protein and 40S ribosomes subunits on viral mRNAs, allowing ribosome shunting and efficient translation of late viral mRNAs even though conventional translation via ribosome scanning from the cap has been shut off in the host cell. During assembly, acts as a chaperone protein that helps hexon proteins assembly into trimers.
Miscellaneous
All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell | |
Cellular Component | host cell cytoplasm | |
Molecular Function | RNA binding | |
Biological Process | intracellular transport of viral protein in host cell | |
Biological Process | symbiont-mediated suppression of host translation initiation | |
Biological Process | viral translational shunt |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameShutoff protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Polar bear mastadenovirus A
Accessions
- Primary accessionA0A2Z4QJG8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 308 | Phosphotyrosine; by host | ||||
Sequence: Y | ||||||
Modified residue | 625 | Phosphotyrosine; by host | ||||
Sequence: Y |
Post-translational modification
Methylated. Asymmetric dimethylation by host PRMT1 of the Arg/Gly-rich region may regulate shutoff protein binding to hexon and promote the capsid assembly in the nucleus.
Might be cleaved by the viral protease.
Phosphorylated. Tyrosine phosphorylation enhances preferential binding to tripartite leader mRNAs and allows ribosome shunting.
Keywords
- PTM
Expression
Induction
Expressed in the late phase of the viral replicative cycle.
Keywords
- Developmental stage
Interaction
Subunit
Monomer. Interacts with hexon protein; this interaction allows chaperoning and trimerization of hexon proteins. Interacts (via N-terminus) with host initiation factor EIF4G (via C-terminus). Interacts (via RRM domain) with viral mRNAs that contain the tripartite leader; this interaction allows ribosome shunting and expression of viral late mRNAs.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 665-696 | Disordered | ||||
Sequence: HGRGQQRQSRNGIANTKHSTKTRAVKGTDGSP | ||||||
Compositional bias | 669-696 | Polar residues | ||||
Sequence: QQRQSRNGIANTKHSTKTRAVKGTDGSP |
Sequence similarities
Belongs to the adenoviridae shutoff protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length696
- Mass (Da)79,200
- Last updated2018-10-10 v1
- Checksum08E9DF87C898B6B1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 669-696 | Polar residues | ||||
Sequence: QQRQSRNGIANTKHSTKTRAVKGTDGSP |
Keywords
- Technical term