A0A5B8KHU7 · A0A5B8KHU7_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
    • CH/GDLZ/201801
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Aviadenovirus

Accessions

  • Primary accession
    A0A5B8KHU7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue885Phosphotyrosine; 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
Region83-133Disordered
Compositional bias95-118Basic and acidic residues
Region145-307Disordered
Compositional bias146-179Acidic residues
Compositional bias203-220Acidic residues
Region484-549Binding to host EIF4G
Region884-1076Disordered
Compositional bias966-986Basic and acidic residues
Compositional bias1062-1076Basic and acidic residues

Sequence similarities

Belongs to the adenoviridae shutoff protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,076
  • Mass (Da)
    119,325
  • Last updated
    2019-11-13 v1
  • Checksum
    8BA1959A04FAC020
MQAARERKAVATLGLVFATVKEKIGWRRFVEAIQRYVADAYGAFLTLNAETAPVDNAVSVLIDTLGEERAILAAYRVAEELLDDKPLPNDGENNGTENPRDDAHTLGESPESDEDVPKASAESSPGTPARDLTAEAVIVYIDSDGGCEEDSSEEDQEEEEDVEEEEEEDEEEEEDDGTPESTPSTVIEAANLSPIGTDESHGEPDGEPDDDGEEDEGRNSDEDSGYYSADGGPDRSPPPSVSEQDRPPSPVTPLELVRDRGDSDHGEPDSTAPSDGPGEAPSTADGVDEEQEQDEQEGETAVPAATAQPAFDKCLQRQAMMLTGALKDALPEQERDVPLCVDSVQYQLERYIFNPDMRAPPEYREVRFNFYPPFMRPKAIANYHIFAVTAPIPASCKANRSGSQLLEACRDMKVFKRLPRWRLNVQSDDGLGDEVVPVTELTDAKLVPLKDDVSRLQWAKMRGEHIRFFSYPSLHMPPKISRMLMECLLQPFANENDKAEQVAPCVSDEELRLIVDPEQRMRGEELYKAMLKRRAVVTMAVRYTALLELMERVFREPSSVKKAQEVLHHTLHHGFVAQVRETAKVNLSNYATYHGVTYNDPLNNCTSAKLFEGRDKEDYVLDTVYLFLVLNWQTAMGMWQQAIDDTTLDIYAKAFTRQRRAIYSLGSVTEVSKVIVDILMDGDRLTEEMRKALPNFVTQSQISDFRHFVTERSNVPSMAAPFYPSDFIPLAFRQSAPLLWDQVYLLQIAFFLTNHGGYLWEPPESEAEVPQHRTYCPCNLCSPHRMPADNVALHNEVLAIGTFEIRSAEGKSFRLTPELWANAYLDKFVPEDFHPFTVFHFPENRSSFTKNHTGCVTESPEILSLIRQIQASREEFLLTRGKGLYKDPQTGETLTTSVGAENRPGASGGAPLPPAAASTCGGARAPPKPPRALRSACSAADPDSQSDYGEAALASNYGRYGSEDAGRENQSYRRPSGTRERRSLPYGRPVRGGFARGGGPGSERIRRRNVRKPGHRGGSEYHLGGGGGPRRDGEREYPTAALLAASGRDAEPQAPLRILAREGAEETSDPKESQIR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias95-118Basic and acidic residues
Compositional bias146-179Acidic residues
Compositional bias203-220Acidic residues
Compositional bias966-986Basic and acidic residues
Compositional bias1062-1076Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK387061
EMBL· GenBank· DDBJ
QDY98264.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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