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P03252 (PRO_ADE02) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protease

EC=3.4.22.39
Alternative name(s):
Adenain
Adenovirus protease
Short name=AVP
Adenovirus proteinase
Endoprotease
Gene names
ORF Names:L3
OrganismHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) [Reference proteome]
Taxonomic identifier10515 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 cells cytoskeletal keratins K7 and K18. Ref.9

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).

Enzyme 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. Ref.5 Ref.6 Ref.12

Subunit structure

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation. Ref.5

Subcellular location

Virion. Host nucleus Probable. Note: Present in about 10 copies per virion. Ref.3

Induction

Expressed in the late phase of the viral replicative cycle. Ref.5 Ref.6 Ref.12

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.

Sequence similarities

Belongs to the peptidase C5 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Protease
PRO_0000218023

Sites

Active site541 Ref.12
Active site711 Ref.12
Active site1221 Ref.12
Site46 – 472Cleavage; by autolysis Potential

Amino acid modifications

Disulfide bond104Interchain (with C-10 in cleaved protease cofactor pVI-C) Ref.6 Ref.12

Experimental info

Mutagenesis1371P → L: Loss of activity; gives rise to unprocessed capsids defective in endosomal escape. Ref.8

Secondary structure

..................................... 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03252 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E43C7DDF14A589A2

FASTA20423,087
        10         20         30         40         50         60 
MGSSEQELKA IVKDLGCGPY FLGTYDKRFP GFVSPHKLAC AIVNTAGRET GGVHWMAFAW 

        70         80         90        100        110        120 
NPRSKTCYLF EPFGFSDQRL KQVYQFEYES LLRRSAIASS PDRCITLEKS TQSVQGPNSA 

       130        140        150        160        170        180 
ACGLFCCMFL HAFANWPQTP MDHNPTMNLI TGVPNSMLNS PQVQPTLRRN QEQLYSFLER 

       190        200 
HSPYFRSHSA QIRSATSFCH LKNM 

« Hide

References

[1]"The sequence of the 3' non-coding region of the hexon mRNA discloses a novel adenovirus gene."
Akusjaervi G., Zabielski J., Perricaudet M., Pettersson U.
Nucleic Acids Res. 9:1-17(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Localization of the 3'-terminal end of the EcoRI B fragment-specific early mRNA of adenovirus type 2."
Buttner W., Veres-Molnar Z.
FEBS Lett. 122:317-321(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-204.
[3]"Analysis of the adenovirus type 5 proteome by liquid chromatography and tandem mass spectrometry methods."
Chelius D., Huhmer A.F., Shieh C.H., Lehmberg E., Traina J.A., Slattery T.K., Pungor E. Jr.
J. Proteome Res. 1:501-513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: Human adenovirus C serotype 5.
[4]"Human adenovirus proteinase: DNA binding and stimulation of proteinase activity by DNA."
McGrath W.J., Baniecki M.L., Li C., McWhirter S.M., Brown M.T., Toledo D.L., Mangel W.F.
Biochemistry 40:13237-13245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[5]"Interaction of the human adenovirus proteinase with its 11-amino acid cofactor pVIc."
Baniecki M.L., McGrath W.J., McWhirter S.M., Li C., Toledo D.L., Pellicena P., Barnard D.L., Thorn K.S., Mangel W.F.
Biochemistry 40:12349-12356(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PROTEASE COFACTOR, ENZYME REGULATION.
[6]"In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase."
McGrath W.J., Aherne K.S., Mangel W.F.
Virology 296:234-240(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND WITH PROTEASE COFACTOR, ENZYME REGULATION.
[7]"Substrate specificity of adenovirus protease."
Ruzindana-Umunyana A., Imbeault L., Weber J.M.
Virus Res. 89:41-52(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Genetic reconstitution of the human adenovirus type 2 temperature-sensitive 1 mutant defective in endosomal escape."
Imelli N., Ruzsics Z., Puntener D., Gastaldelli M., Greber U.F.
Virol. J. 6:174-174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-137.
Strain: Mutant ts-1.
[9]"The role of capsid maturation on adenovirus priming for sequential uncoating."
Perez-Berna A.J., Ortega-Esteban A., Menendez-Conejero R., Winkler D.C., Menendez M., Steven A.C., Flint S.J., de Pablo P.J., San Martin C.
J. Biol. Chem. 287:31582-31595(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. IV. viral proteinase slides along DNA to locate and process its substrates."
Blainey P.C., Graziano V., Perez-Berna A.J., McGrath W.J., Flint S.J., San Martin C., Xie X.S., Mangel W.F.
J. Biol. Chem. 288:2092-2102(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"Latest insights on adenovirus structure and assembly."
San Martin C.
Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor."
Ding J., McGrath W.J., Sweet R.M., Mangel W.F.
EMBO J. 15:1778-1783(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PROTEASE COFACTOR, DISULFIDE BOND, ACTIVE SITE, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01917 Genomic DNA. Translation: AAA92216.1.
PIRW2AD35. A03823.
RefSeqAP_000176.1. AC_000007.1.
NP_040526.1. NC_001405.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVPX-ray2.60A1-204[»]
1NLNX-ray1.60A1-204[»]
4EKFX-ray0.98A1-204[»]
ProteinModelPortalP03252.
SMRP03252. Positions 1-204.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2652998.

Family and domain databases

Gene3D3.40.395.10. 1 hit.
InterProIPR000855. Peptidase_C5.
[Graphical view]
PfamPF00770. Peptidase_C5. 1 hit.
[Graphical view]
PIRSFPIRSF001218. Protease_ADV. 1 hit.
PRINTSPR00703. ADVENDOPTASE.
ProDomPD003705. Peptidase_C5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP03252.

Entry information

Entry namePRO_ADE02
AccessionPrimary (citable) accession number: P03252
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references