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P03252

- PRO_ADE02

UniProt

P03252 - PRO_ADE02

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Protein
Protease
Gene
L3
Organism
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 K18.1 Publication

Catalytic activityi

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 regulationi

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Cleavage; by autolysis Reviewed prediction
Active sitei54 – 5411 Publication
Active sitei71 – 7111 Publication
Active sitei122 – 12211 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. cysteine-type peptidase activity Source: CACAO
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    DNA-binding

    Protein family/group databases

    MEROPSiC05.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protease (EC:3.4.22.39)
    Alternative name(s):
    Adenain
    Adenovirus protease
    Short name:
    AVP
    Adenovirus proteinase
    Endoprotease
    Gene namesi
    ORF Names:L3
    OrganismiHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
    Taxonomic identifieri10515 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008167: Genome

    Subcellular locationi

    Virion. Host nucleus Inferred
    Note: Present in about 10 copies per virion.1 Publication

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell
    2. virion Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Host nucleus, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371P → L: Loss of activity; gives rise to unprocessed capsids defective in endosomal escape. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 204204Protease
    PRO_0000218023Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi104 – 104Interchain (with C-10 in cleaved protease cofactor pVI-C)2 Publications

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond

    Expressioni

    Inductioni

    Expressed in the late phase of the viral replicative cycle.3 Publications

    Keywords - Developmental stagei

    Late protein

    Interactioni

    Subunit structurei

    Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.1 Publication

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1410
    Helixi18 – 203
    Beta strandi21 – 288
    Beta strandi35 – 373
    Beta strandi39 – 457
    Turni48 – 503
    Beta strandi55 – 617
    Turni62 – 654
    Beta strandi66 – 705
    Helixi78 – 9518
    Beta strandi106 – 1094
    Helixi122 – 13514
    Beta strandi141 – 1444
    Helixi147 – 1493
    Helixi155 – 1573
    Helixi161 – 1633
    Helixi164 – 18118
    Helixi183 – 1875
    Helixi189 – 1957
    Turni198 – 2014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AVPX-ray2.60A1-204[»]
    1NLNX-ray1.60A1-204[»]
    4EKFX-ray0.98A1-204[»]
    ProteinModelPortaliP03252.
    SMRiP03252. Positions 1-204.

    Miscellaneous databases

    EvolutionaryTraceiP03252.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C5 family.

    Family and domain databases

    Gene3Di3.40.395.10. 1 hit.
    InterProiIPR000855. Peptidase_C5.
    [Graphical view]
    PfamiPF00770. Peptidase_C5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001218. Protease_ADV. 1 hit.
    PRINTSiPR00703. ADVENDOPTASE.
    ProDomiPD003705. Peptidase_C5. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    P03252-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSSEQELKA IVKDLGCGPY FLGTYDKRFP GFVSPHKLAC AIVNTAGRET    50
    GGVHWMAFAW NPRSKTCYLF EPFGFSDQRL KQVYQFEYES LLRRSAIASS 100
    PDRCITLEKS TQSVQGPNSA ACGLFCCMFL HAFANWPQTP MDHNPTMNLI 150
    TGVPNSMLNS PQVQPTLRRN QEQLYSFLER HSPYFRSHSA QIRSATSFCH 200
    LKNM 204
    Length:204
    Mass (Da):23,087
    Last modified:July 21, 1986 - v1
    Checksum:iE43C7DDF14A589A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01917 Genomic DNA. Translation: AAA92216.1.
    PIRiA03823. W2AD35.
    RefSeqiAP_000176.1. AC_000007.1.
    NP_040526.1. NC_001405.1.

    Genome annotation databases

    GeneIDi2652998.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01917 Genomic DNA. Translation: AAA92216.1 .
    PIRi A03823. W2AD35.
    RefSeqi AP_000176.1. AC_000007.1.
    NP_040526.1. NC_001405.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AVP X-ray 2.60 A 1-204 [» ]
    1NLN X-ray 1.60 A 1-204 [» ]
    4EKF X-ray 0.98 A 1-204 [» ]
    ProteinModelPortali P03252.
    SMRi P03252. Positions 1-204.
    ModBasei Search...

    Protein family/group databases

    MEROPSi C05.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2652998.

    Miscellaneous databases

    EvolutionaryTracei P03252.

    Family and domain databases

    Gene3Di 3.40.395.10. 1 hit.
    InterProi IPR000855. Peptidase_C5.
    [Graphical view ]
    Pfami PF00770. Peptidase_C5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001218. Protease_ADV. 1 hit.
    PRINTSi PR00703. ADVENDOPTASE.
    ProDomi PD003705. Peptidase_C5. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiPRO_ADE02
    AccessioniPrimary (citable) accession number: P03252
    Entry historyi
    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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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