ID   PRO_ADE04               Reviewed;         201 AA.
AC   P07885;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Human adenovirus E serotype 4 (HAdV-4) (Human adenovirus 4).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus E.
OX   NCBI_TaxID=28280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3301540; DOI=10.1016/0378-1119(87)90346-5;
RA   Houde A., Weber J.M.;
RT   "Sequence of the protease of human subgroup E adenovirus type 4.";
RL   Gene 54:51-56(1987).
CC   -!- FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII,
CC       pVIII, and pX) inside newly assembled particles giving rise to mature
CC       virions. Protease complexed to its cofactor slides along the viral DNA
CC       to specifically locate and cleave the viral precursors. Mature virions
CC       have a weakened organization compared to the unmature virions, thereby
CC       facilitating subsequent uncoating. Without maturation, the particle
CC       lacks infectivity and is unable to uncoat. Late in adenovirus
CC       infection, in the cytoplasm, may participate in the cytoskeleton
CC       destruction. 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 two
CC         consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-
CC         Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).;
CC         EC=3.4.22.39; Evidence={ECO:0000255|HAMAP-Rule:MF_04059};
CC   -!- ACTIVITY REGULATION: Requires DNA and protease cofactor for maximal
CC       activation. Inside nascent virions, becomes partially activated by
CC       binding to the viral DNA, allowing it to cleave the cofactor that binds
CC       to the protease and fully activates it. Actin, like the viral protease
CC       cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18
CC       and of actin itself. {ECO:0000255|HAMAP-Rule:MF_04059}.
CC   -!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction is
CC       necessary for protease activation. {ECO:0000255|HAMAP-Rule:MF_04059}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04059}. Note=Present in about 10
CC       copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_04059}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC       are produced by alternative splicing and alternative polyadenylation of
CC       the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC       present in the N-terminus of all these mRNAs and is recognized by the
CC       viral shutoff protein to provide expression although conventional
CC       translation via ribosome scanning from the cap has been shut off in the
CC       host cell. {ECO:0000255|HAMAP-Rule:MF_04059}.
CC   -!- SIMILARITY: Belongs to the peptidase C5 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04059}.
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DR   EMBL; M16692; AAA42466.1; -; Genomic_DNA.
DR   PIR; A27473; W2AD04.
DR   SMR; P07885; -.
DR   MEROPS; C05.001; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Disulfide bond; DNA-binding; Host nucleus;
KW   Hydrolase; Late protein; Protease; Thiol protease; Virion.
FT   CHAIN           1..201
FT                   /note="Protease"
FT                   /id="PRO_0000218025"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT   SITE            53..54
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT   DISULFID        105
FT                   /note="Interchain (with C-10 in cleaved protease cofactor
FT                   pVI-C)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
SQ   SEQUENCE   201 AA;  22787 MW;  071B83A6CC7E4E1E CRC64;
     MAAGSGEQEL RAIIRDLGCG PYFLGTFDKR FPGFMAPHKV ACAIVNTAGR ETGGEHWLAF
     AWNPRSNTCY LFDPFGFSDQ RLKQIYQFEY EGLLRRSALA TKDRCVTWKS HQTCRVRVGR
     CGFSAACSTA CAWPTPMDKN PTMNLLTGVP NGMLQSPQVE PTLRRNQEAL YRFLNSHSAY
     FRSHRARIEK ATAFDRMNQD M