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Protein

Protease

Gene

L3

Organism
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Status
Reviewed-Annotation score: 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 cell cytoskeletal keratins K7 and K18.UniRule annotation1 Publication

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.UniRule annotation

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).
Cleaves adenovirus and host cell proteins 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).UniRule annotation

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.UniRule annotation3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei54UniRule annotation1 Publication1
Active sitei71UniRule annotation1 Publication1
Active sitei122UniRule annotation1 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionDNA-binding, Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC05.001.

Names & Taxonomyi

Protein namesi
Recommended name:
ProteaseUniRule annotation (EC:3.4.22.39UniRule annotation)
Alternative name(s):
AdenainUniRule annotation
Adenovirus proteaseUniRule annotation
Short name:
AVPUniRule annotation
Adenovirus proteinaseUniRule annotation
EndoproteaseUniRule annotation
Gene namesi
Name:L3UniRule annotation
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]
Proteomesi
  • UP000008167 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation1 Publication
  • Host nucleus UniRule annotation1 Publication

  • Note: Present in about 10 copies per virion.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137P → L: Loss of activity; gives rise to unprocessed capsids defective in endosomal escape. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002180231 – 204ProteaseAdd BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104Interchain (with C-10 in cleaved protease cofactor pVI-C)UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei51 – 52Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.UniRule annotation

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.UniRule annotation2 Publications

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Helixi18 – 20Combined sources3
Beta strandi21 – 28Combined sources8
Beta strandi35 – 37Combined sources3
Beta strandi39 – 45Combined sources7
Helixi48 – 50Combined sources3
Beta strandi55 – 61Combined sources7
Turni62 – 65Combined sources4
Beta strandi66 – 70Combined sources5
Helixi78 – 95Combined sources18
Beta strandi106 – 109Combined sources4
Helixi122 – 135Combined sources14
Beta strandi141 – 144Combined sources4
Helixi147 – 149Combined sources3
Helixi155 – 157Combined sources3
Helixi161 – 163Combined sources3
Helixi164 – 181Combined sources18
Helixi183 – 187Combined sources5
Helixi189 – 195Combined sources7
Turni198 – 201Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AVPX-ray2.60A1-204[»]
1NLNX-ray1.60A1-204[»]
4EKFX-ray0.98A1-204[»]
4PIDX-ray1.59A1-204[»]
4PIEX-ray1.94A1-204[»]
5FGYX-ray2.10A1-204[»]
ProteinModelPortaliP03252.
SMRiP03252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03252.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C5 family.UniRule annotationCurated

Phylogenomic databases

OrthoDBiVOG090000OU.

Family and domain databases

HAMAPiMF_04059. ADV_PRO. 1 hit.
InterProiView protein in InterPro
IPR000855. Peptidase_C5.
PfamiView protein in Pfam
PF00770. Peptidase_C5. 1 hit.
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003705. Peptidase_C5. 1 hit.

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.
PIRiA03823. W2AD35.
RefSeqiAP_000176.1. AC_000007.1.
NP_040526.1. NC_001405.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AVPX-ray2.60A1-204[»]
1NLNX-ray1.60A1-204[»]
4EKFX-ray0.98A1-204[»]
4PIDX-ray1.59A1-204[»]
4PIEX-ray1.94A1-204[»]
5FGYX-ray2.10A1-204[»]
ProteinModelPortaliP03252.
SMRiP03252.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC05.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652998.

Phylogenomic databases

OrthoDBiVOG090000OU.

Miscellaneous databases

EvolutionaryTraceiP03252.

Family and domain databases

HAMAPiMF_04059. ADV_PRO. 1 hit.
InterProiView protein in InterPro
IPR000855. Peptidase_C5.
PfamiView protein in Pfam
PF00770. Peptidase_C5. 1 hit.
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003705. Peptidase_C5. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRO_ADE02
AccessioniPrimary (citable) accession number: P03252
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 10, 2017
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.