ID PRO_ADEF1 Reviewed; 204 AA. AC Q9IIH4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 05-JUN-2019, entry version 61. DE RecName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04059}; DE EC=3.4.22.39 {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenain {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus protease {ECO:0000255|HAMAP-Rule:MF_04059}; DE Short=AVP {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus proteinase {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Endoprotease {ECO:0000255|HAMAP-Rule:MF_04059}; GN Name=L3 {ECO:0000255|HAMAP-Rule:MF_04059}; OS Frog adenovirus 1 (strain ATCC VR-896) (FrAdV-1). OC Viruses; Adenoviridae; Siadenovirus. OX NCBI_TaxID=114102; OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate ATCC VR-896; RA Davison A.J., Wright K.M., Harrach B.; RT "Phylogenetic position of an amphibian adenovirus."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, CC pVIII, and pX) inside newly assembled particles giving rise to CC mature virions. Protease complexed to its cofactor slides along CC the viral DNA to specifically locate and cleave the viral CC precursors. Mature virions have a weakened organization compared CC to the unmature virions, thereby facilitating subsequent CC uncoating. Without maturation, the particle lacks infectivity and CC is unable to uncoat. Late in adenovirus infection, in the CC cytoplasm, may participate in the cytoskeleton destruction. CC Cleaves host cell cytoskeletal keratins K7 and K18. CC {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleaves proteins of the adenovirus and its host cell at CC two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly- CC Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any CC amino acid).; EC=3.4.22.39; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04059}; CC -!- ACTIVITY REGULATION: Requires DNA and protease cofactor for CC maximal activation. Inside nascent virions, becomes partially CC activated by binding to the viral DNA, allowing it to cleave the CC cofactor that binds to the protease and fully activates it. Actin, CC like the viral protease cofactor, seems to act as a cofactor in CC the cleavage of cytokeratin 18 and of actin itself. CC {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction CC is necessary for protease activation. {ECO:0000255|HAMAP- CC Rule:MF_04059}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059}. CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04059}. Note=Present in CC about 10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative CC cycle. {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- MISCELLANEOUS: All late proteins expressed from the major late CC promoter are produced by alternative splicing and alternative CC polyadenylation of the same gene giving rise to non-overlapping CC ORFs. A leader sequence is present in the N-terminus of all these CC mRNAs and is recognized by the viral shutoff protein to provide CC expression although conventional translation via ribosome scanning CC from the cap has been shut off in the host cell. CC {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- SIMILARITY: Belongs to the peptidase C5 family. CC {ECO:0000255|HAMAP-Rule:MF_04059}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF224336; AAF86933.1; -; Genomic_DNA. DR RefSeq; NP_062444.1; NC_002501.1. DR SMR; Q9IIH4; -. DR MEROPS; C05.001; -. DR GeneID; 1732705; -. DR KEGG; vg:1732705; -. DR OrthoDB; 6836at10239; -. DR Proteomes; UP000009247; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR HAMAP; MF_04059; ADV_PRO; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR000855; Peptidase_C5. DR Pfam; PF00770; Peptidase_C5; 1. DR PIRSF; PIRSF001218; Protease_ADV; 1. DR PRINTS; PR00703; ADVENDOPTASE. DR ProDom; PD003705; Peptidase_C5; 1. DR SUPFAM; SSF54001; SSF54001; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; Disulfide bond; KW DNA-binding; Host nucleus; Hydrolase; Late protein; Protease; KW Reference proteome; Thiol protease; Virion. FT CHAIN 1 204 Protease. FT /FTId=PRO_0000218042. FT ACT_SITE 54 54 {ECO:0000255|HAMAP-Rule:MF_04059}. FT ACT_SITE 71 71 {ECO:0000255|HAMAP-Rule:MF_04059}. FT ACT_SITE 121 121 {ECO:0000255|HAMAP-Rule:MF_04059}. FT SITE 51 52 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_04059}. FT DISULFID 103 103 Interchain (with C-10 in cleaved protease FT cofactor pVI-C). {ECO:0000255|HAMAP- FT Rule:MF_04059}. SQ SEQUENCE 204 AA; 23222 MW; 91DC0B01544577A5 CRC64; MGTSGADLEN IVLSLGLHSG FLGIFDKHFP GFLNVNKPSF AIVNTGDIIQ GGLHWIAFAF DNVTSTFFMF DPFGWSDMEL YRKYEFQYHR ILKSTALTKP SRCIKLVKSK EAVQCTCSAA CGLFCCLFLA SFYHYPTFPM RGNPIIDLVD GIPPTKLHSS YGIYLTHCNQ KKLIAWLLSN SAYFRKNAML MIHNTRLYYL YTHL //