A0A7G5FAS9 · A0A7G5FAS9_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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
  • Strains
    • NAMRU3 2005-908017
    • NAMRU3 2005-909685
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Human mastadenovirus B

Accessions

  • Primary accession
    A0A7G5FAS9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue389Phosphotyrosine; by host
Modified residue708Phosphotyrosine; 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 compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-16Polar residues
Region1-70Disordered
Compositional bias43-70Basic and acidic residues
Region85-106Disordered
Region304-369Binding to host EIF4G
Region711-812Disordered

Sequence similarities

Belongs to the adenoviridae shutoff protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    812
  • Mass (Da)
    91,077
  • Last updated
    2021-02-10 v1
  • Checksum
    CFC3510A945D2F90
METQPLLSTSPQVPSHLVVSDEEKEQSLTIPPPSPATTSTLEDKEVDASHDMQNKKAKESETDIEQDPGYVTPVEHEEELKRFLEREDENCPKQQADNYRQDAGNRDQNTDYLIGLDGEDALLKHLARQSLIVKDALLDRTEVPISVEELSRAYELNLFSPRTPPKRQPNGTCEPNPRLNFYPAFAVPEVLATYHIFFKNQKIPVSCRANRTRADALLNLGPGSRLPDIASLEEVPKIFEGLGNNETRAANALQKGENGMDEHHSVLVELEGDNARLAVLKRSVEVTHFAYPAVNLPPKVMTAVMDQLLIKRARPLSEDMHDPDACDEGKPVVSDEQLTRWLGTDSPRDLEERRKLMMAVVLVTVELECLRRFFTDSETLRKLEENLHYTFRHGFVRQACKISNVELTNLVSYMGILHENRLGQSVLHSTLKGEARRDYIRDCVYLYLCHTWQTGMGVWQQCLEEQNLKELNKLLQKSLKVLWTGFDERTVASDLADLIFPERLRVTLRNGLPDFMSQSMLNNFRSFILERSGILPATCCALPSDFVPLTYRECPPPLWSHCYLFRLANYLSYHSDVIEDVSGDGLLECHCRCNLCTPHRSLACNPQLMSETQIIGTFELQGPSSQGDGSSPGQSLKLTPGLWTSAYLRKFAPEDYHPYEIKFYEDQSQPPKAELSACVITQGAILAQLQAIQKSRQEFLLKKGKGVYLDPQTGEELNTRFPQDVPTTRKQEVEGAAAAPRRYGGRLGQSGRGSGGGQSGGQSGGRQFGGGKRGGRGGGRSNRRQTVIPGCGDKQQRYHLRSESRNAAASQQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-16Polar residues
Compositional bias43-70Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MN654390
EMBL· GenBank· DDBJ
QMV83720.1
EMBL· GenBank· DDBJ
Genomic DNA
MN654391
EMBL· GenBank· DDBJ
QMV83757.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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