Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protease

Gene

L3

Organism
Canine adenovirus serotype 2 (strain Toronto A 26-61) (CAdV-2) (Canine adenovirus 2 (strain Toronto A 26-61))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 annotation

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 annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei57UniRule annotation1
Active sitei74UniRule annotation1
Active sitei125UniRule annotation1

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
OrganismiCanine adenovirus serotype 2 (strain Toronto A 26-61) (CAdV-2) (Canine adenovirus 2 (strain Toronto A 26-61))
Taxonomic identifieri69152 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirusCanine mastadenovirus A
Virus hostiCanis lupus familiaris (Dog) (Canis familiaris) [TaxID: 9615]

Subcellular locationi

  • Virion UniRule annotation
  • Host nucleus UniRule annotation

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

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002180371 – 206ProteaseAdd BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi107Interchain (with C-10 in cleaved protease cofactor pVI-C)UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei54 – 55Cleavage; 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 annotation

Structurei

3D structure databases

ProteinModelPortaliP87563.
SMRiP87563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C5 family.UniRule annotation

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.

P87563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEGGSSEEE LRAIVHNLGV SPFFLGTFDK RFPGFISSQR MACAIVNTAG
60 70 80 90 100
RETGGVHWLA MAWNPRSKTF YMFDPFGFSD SKLKQVYSFE YEGLLRRSAI
110 120 130 140 150
ASSPDRCVTL AKSNETIQGP NSAACGLFCC MFLHAFVNWP DDPFDHNPTM
160 170 180 190 200
GPLKSVPNYK LNDPTVQYVL WGNQEKLYKF LEKHSAYFRA HAAAIKARTA

FNKLKQ
Length:206
Mass (Da):23,166
Last modified:May 1, 1997 - v1
Checksum:i92939659F0102132
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77082 Genomic DNA. Translation: AAB38726.1.
RefSeqiAP_000623.1. AC_000020.1.

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.

Entry informationi

Entry nameiPRO_ADECT
AccessioniPrimary (citable) accession number: P87563
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1997
Last modified: May 10, 2017
This is version 63 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families