PRO_ADE12
ID PRO_ADE12 Reviewed; 206 AA.
AC P09569;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 99.
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 A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pereira 1131;
RX PubMed=3043380; DOI=10.1093/nar/16.14.7195;
RA Weber J.M., Houde A.;
RT "The primary structure of human adenovirus type 12 protease.";
RL Nucleic Acids Res. 16:7195-7195(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
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; X07655; CAA30501.1; -; Genomic_DNA.
DR EMBL; X73487; CAA51892.1; -; Genomic_DNA.
DR PIR; S01731; W2AD12.
DR RefSeq; NP_040925.1; NC_001460.1.
DR SMR; P09569; -.
DR MEROPS; C05.001; -.
DR PRIDE; P09569; -.
DR GeneID; 1460858; -.
DR Proteomes; UP000004993; Genome.
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..206
FT /note="Protease"
FT /id="PRO_0000218028"
FT ACT_SITE 54
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT ACT_SITE 71
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT SITE 51..52
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT DISULFID 104
FT /note="Interchain (with C-10 in cleaved protease cofactor
FT pVI-C)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT CONFLICT 180
FT /note="N -> S (in Ref. 1; CAA30501)"
SQ SEQUENCE 206 AA; 23482 MW; 6876ED52765E7357 CRC64;
MGSSEQELTA IVRDLGCGPY FLGTFDKRFP GFVSRDRLSC AIVNTAGRET GGVHWLAFGW
NPKSHTCYLF DPFGFSDQRL KQIYQFEYES LLRRSALAAT KDRCVTLEKS TQTVQGPFSA
ACGLFCCMFL HAFTHWPDHP MDKNPTMDLL TGVPNCMLQS PQVVGTLQRN QNELYKFLNN
LSPYFRHNRE RIEKATSFTK MQNGLK
