B9A5C3 · B9A5C3_ADE08

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

Accessions

  • Primary accession
    B9A5C3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue325Phosphotyrosine; by host
Modified residue638Phosphotyrosine; 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.

TypeIDPosition(s)Description
Region1-46Disordered
Region645-715Disordered

Sequence similarities

Belongs to the adenoviridae shutoff protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    715
  • Mass (Da)
    80,255
  • Last updated
    2009-03-24 v1
  • Checksum
    2D4EF8B4D61A2DF5
MEEQPRKQEQEEENLTTHEQPKIEQDLGLEEPARLEPPHDEQEKTNAGLEHGYLGGQEDVLLKHLQRQSFILRDALADRSKTPLSVQELCRAYELNLFSPRVPPKRQPNGTCEPNPRLNFYPVFAVPEALATYHIFFKNQKIPVSCRANRTRADALLALGPGARIPDIASLEEVPKIFEGLGRDETRAANALKETAEEKGYTSALVELEGDNARLAVLKRSVELTHFAYPAVNLPPKVMRRIMDQLITPHIEALDESQKQRPEDARPVVSDEMLARWLGNRDPQSLEQRRKLMLAVVLVTLELECMRRFFSDPETLRKVEETLHYTFRHGFVRQACKISNVELTNLVSCLGILHENRLGQTVLHSTLKGEARRDYIRDCVFLFLCHTWQSAMGVWQQCLQDENLKELDKLLAKNLKKLWTGFDERTVASDLAEIVFPERLRQTLKGGLPDFMSQSMLQNYRTFILERSGILPATCNAFPSDFVPLSYRQCPPPLWSHCYLLQLANYIAHHSDVIEDVSGEGLLECHCRCNLCSPHRSLVCNPQLLSETQVIGTFELQGPENSTTPLKLTPGLWTSAYLRKFVPQDYHAHEIKFFEDQLCPQHADLTACVITQGAILAQLHAIQKSRQEFLLKKGKGVYLDPQTGEVLNPGLPQHAEEEAGATSGGDGRRMGQPGRGGRMGGGGGGRIGRGATGAGNRAARRRTIRAGSPSGQASS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB448767
EMBL· GenBank· DDBJ
BAH18787.1
EMBL· GenBank· DDBJ
Genomic DNA
AB746853
EMBL· GenBank· DDBJ
BAM66723.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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