A0A7G5FAS9 · A0A7G5FAS9_9ADEN
- ProteinShutoff protein
- GeneL4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids812 (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
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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
- Strains
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Human mastadenovirus B
Accessions
- Primary accessionA0A7G5FAS9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 389 | Phosphotyrosine; by host | ||||
Sequence: Y | ||||||
Modified residue | 708 | 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 compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: METQPLLSTSPQVPSH | ||||||
Region | 1-70 | Disordered | ||||
Sequence: METQPLLSTSPQVPSHLVVSDEEKEQSLTIPPPSPATTSTLEDKEVDASHDMQNKKAKESETDIEQDPGY | ||||||
Compositional bias | 43-70 | Basic and acidic residues | ||||
Sequence: DKEVDASHDMQNKKAKESETDIEQDPGY | ||||||
Region | 85-106 | Disordered | ||||
Sequence: EREDENCPKQQADNYRQDAGNR | ||||||
Region | 304-369 | Binding to host EIF4G | ||||
Sequence: VMDQLLIKRARPLSEDMHDPDACDEGKPVVSDEQLTRWLGTDSPRDLEERRKLMMAVVLVTVELEC | ||||||
Region | 711-812 | Disordered | ||||
Sequence: PQTGEELNTRFPQDVPTTRKQEVEGAAAAPRRYGGRLGQSGRGSGGGQSGGQSGGRQFGGGKRGGRGGGRSNRRQTVIPGCGDKQQRYHLRSESRNAAASQQ |
Sequence similarities
Belongs to the adenoviridae shutoff protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length812
- Mass (Da)91,077
- Last updated2021-02-10 v1
- ChecksumCFC3510A945D2F90
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: METQPLLSTSPQVPSH | ||||||
Compositional bias | 43-70 | Basic and acidic residues | ||||
Sequence: DKEVDASHDMQNKKAKESETDIEQDPGY |