P19119 · PRO_ADEB3

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 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
    P19119

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00002180331-204Protease
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

3D structure databases

Family & Domains

Sequence similarities

Belongs to the peptidase C5 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    204
  • Mass (Da)
    23,274
  • Last updated
    1990-11-01 v1
  • Checksum
    25E9F058FC385AC5
MGSREEELRFILHDLGVGPYFLGTFDKHFPGFISKDRMSCAIVNTAGRETGGVHWLAMAWHPASQTFYMFDPFGFSDQKLKQIYNFEYQGLLKRSALTSTADRCLTLIQSTQSVQGPNSAACGLFCCMFLHAFVRWPLRAMDNNPTMNLIHGVPNNMLESPSSQNVFLRNQQNLYRFLRRHSPHFVKHAAQIEADTAFDKMLTN

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A9W3HR49A0A9W3HR49_ADEB3L3902

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X53990
EMBL· GenBank· DDBJ
CAA37937.1
EMBL· GenBank· DDBJ
Genomic DNA
AF030154
EMBL· GenBank· DDBJ
AAD09729.1
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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