A0A3G9F1D7 · A0A3G9F1D7_9ADEN

  • Protein
    Shutoff protein
  • Gene
    L4
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

GO annotations

AspectTerm
Cellular Componenthost cell
Cellular Componenthost cell cytoplasm
Molecular FunctionRNA binding
Biological Processintracellular transport of viral protein in host cell
Biological Processsymbiont-mediated suppression of host translation initiation
Biological Processviral translational shunt

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Shutoff protein
  • Alternative names
    • 100 kDa protein
      (p100K
      )
    • 100K-chaperone protein
    • L4-100K
    • Shutoff protein 100K

Gene names

    • Name
      L4

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Vs9
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus

Accessions

  • Primary accession
    A0A3G9F1D7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue313Phosphotyrosine; by host
Modified residue630Phosphotyrosine; by host

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

Expression

Induction

Expressed in the late phase of the viral replicative cycle.

Keywords

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.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-34Disordered
Compositional bias17-34Polar residues
Region632-694Disordered
Compositional bias647-661Basic and acidic residues

Sequence similarities

Belongs to the adenoviridae shutoff protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    694
  • Mass (Da)
    78,161
  • Last updated
    2019-02-13 v1
  • Checksum
    3C92C6E733608E3C
MSEESIKGEVEEIQDDTLTAPPNSPVLTSEPLDSETAVVSDLDSTEPLGYLNDDLLHKHLQRQSTIVLEALQDRLQIPTSVAELSCAYERSLFSPIIPPRKQENGTCEANPRLNFYPTFVVPETLATYHIFFTNQKIPLSCRANRPRADRAFTLQEGDCLPDYETMDTVSRVFEGLGSEDVAEGALENTESMLVELKNDNPRLAVAKRSLTVTHFAYPALHLPPKVLTTMMDTLLVRRAQPKADVSEINPEDGKEVVSDSELSKWLKTDDQQEMEQQRKTVMGAVLVTVVMECMQRFFTSEGMIKKIGESLHYMFSHGYVALASKISNVQLTNVVTYMGILHENRLGQNVLHTTLKDETQRDYIRDCIFLFLVHSWQTAMGIWQQCLESENLKELVKLLQRKTKLLYTQPSQRLMAKELADIIFPPKLLETFHNGLPDIASQSMMQNFRSFILERSGIVPCVTSLFPTDFIPLFFKECPPTLWPYTYLLKLANYFMYHNDLCYDMQGEGLLEHYCRCNLCTPHRCLATNPAMLNETQLIGTFDMRGPGENGAEAATGLKLTAGVWTSAFLRKFERADYHAHKIHFYENQSKPPAVEPSPCVITQTSILAQLHDIKKAREEFLLKKGQGVYLDPQTGEPLNAADPSVERSDKNGRQGDFKHGRNLQQRGGGGPRKPPRVPGALQRGGGRASGARS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3G9E9U3A0A3G9E9U3_9ADENL4226

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias17-34Polar residues
Compositional bias647-661Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC385827
EMBL· GenBank· DDBJ
BBE29316.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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