P03252 · PRO_ADE02

Function

function

Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.

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.

Catalytic activity

  • Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).
    EC:3.4.22.39 (UniProtKB | ENZYME | Rhea)

Activity regulation

Requires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site51-52Cleavage; by autolysis
Active site54
Active site71
Active site122

GO annotations

AspectTerm
Cellular Componenthost cell nucleus
Cellular Componentvirion component
Molecular Functioncysteine-type endopeptidase activity
Molecular Functioncysteine-type peptidase activity
Molecular FunctionDNA binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Protease
  • EC number
  • Alternative names
    • Adenain
    • Adenovirus protease
      (AVP
      )
    • Adenovirus proteinase
    • Endoprotease

Gene names

    • Name
      L3

Organism names

Accessions

  • Primary accession
    P03252

Proteomes

Subcellular Location

Virion
Host nucleus
Note: Present in about 10 copies per virion.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis137Loss of activity; gives rise to unprocessed capsids defective in endosomal escape.

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00002180231-204Protease
Disulfide bond104Interchain (with C-10 in cleaved protease cofactor pVI-C)

Keywords

Expression

Induction

Expressed in the late phase of the viral replicative cycle.

Keywords

Interaction

Subunit

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase C5 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    204
  • Mass (Da)
    23,087
  • Last updated
    1986-07-21 v1
  • Checksum
    E43C7DDF14A589A2
MGSSEQELKAIVKDLGCGPYFLGTYDKRFPGFVSPHKLACAIVNTAGRETGGVHWMAFAWNPRSKTCYLFEPFGFSDQRLKQVYQFEYESLLRRSAIASSPDRCITLEKSTQSVQGPNSAACGLFCCMFLHAFANWPQTPMDHNPTMNLITGVPNSMLNSPQVQPTLRRNQEQLYSFLERHSPYFRSHSAQIRSATSFCHLKNM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J01917
EMBL· GenBank· DDBJ
AAA92216.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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