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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 autolysisSequence Analysis
Active sitei54 – 5411 Publication
Active sitei71 – 7111 Publication
Active sitei122 – 12211 Publication

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
  2. cysteine-type peptidase activity Source: CACAO
  3. DNA binding Source: UniProtKB-KW
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 1 Publication. Host nucleus 1 Publication
Note: Present in about 10 copies per virion.

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-KW
  2. virion Source: UniProtKB-KW
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 – 204204ProteasePRO_0000218023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 – 104Interchain (with C-10 in cleaved protease cofactor pVI-C)1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.2 Publications

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Helixi18 – 203Combined sources
Beta strandi21 – 288Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 457Combined sources
Helixi48 – 503Combined sources
Beta strandi55 – 617Combined sources
Turni62 – 654Combined sources
Beta strandi66 – 705Combined sources
Helixi78 – 9518Combined sources
Beta strandi106 – 1094Combined sources
Helixi122 – 13514Combined sources
Beta strandi141 – 1444Combined sources
Helixi147 – 1493Combined sources
Helixi155 – 1573Combined sources
Helixi161 – 1633Combined sources
Helixi164 – 18118Combined sources
Helixi183 – 1875Combined sources
Helixi189 – 1957Combined sources
Turni198 – 2014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVPX-ray2.60A1-204[»]
1NLNX-ray1.60A1-204[»]
4EKFX-ray0.98A1-204[»]
4PIDX-ray1.59A1-204[»]
4PIEX-ray1.94A1-204[»]
ProteinModelPortaliP03252.
SMRiP03252. Positions 1-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03252.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C5 family.Curated

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

        10         20         30         40         50
MGSSEQELKA IVKDLGCGPY FLGTYDKRFP GFVSPHKLAC AIVNTAGRET
60 70 80 90 100
GGVHWMAFAW NPRSKTCYLF EPFGFSDQRL KQVYQFEYES LLRRSAIASS
110 120 130 140 150
PDRCITLEKS TQSVQGPNSA ACGLFCCMFL HAFANWPQTP MDHNPTMNLI
160 170 180 190 200
TGVPNSMLNS PQVQPTLRRN QEQLYSFLER HSPYFRSHSA QIRSATSFCH

LKNM
Length:204
Mass (Da):23,087
Last modified:July 21, 1986 - v1
Checksum:iE43C7DDF14A589A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4PID X-ray 1.59 A 1-204 [» ]
4PIE X-ray 1.94 A 1-204 [» ]
ProteinModelPortali P03252.
SMRi P03252. Positions 1-204.
ModBasei Search...
MobiDBi 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: November 26, 2014
This is version 87 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