PRO_ADE05
ID PRO_ADE05 Reviewed; 204 AA.
AC P03253;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6258160; DOI=10.1093/nar/8.24.6033;
RA Kruijer W., van Schaik F.M.A., Sussenbach J.S.;
RT "Nucleotide sequence analysis of a region of adenovirus 5 DNA encoding a
RT hitherto unidentified gene.";
RL Nucleic Acids Res. 8:6033-6042(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12645618; DOI=10.1021/pr025528c;
RA Chelius D., Huhmer A.F., Shieh C.H., Lehmberg E., Traina J.A.,
RA Slattery T.K., Pungor E. Jr.;
RT "Analysis of the adenovirus type 5 proteome by liquid chromatography and
RT tandem mass spectrometry methods.";
RL J. Proteome Res. 1:501-513(2002).
RN [5]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
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,
CC ECO:0000269|PubMed:12645618}. Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04059}. Note=Present in about 10 copies per virion.
CC {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; X02997; CAA26754.1; -; Genomic_DNA.
DR EMBL; V00031; CAA23412.1; -; Genomic_DNA.
DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C03823; W2AD55.
DR RefSeq; AP_000212.1; AC_000008.1.
DR SMR; P03253; -.
DR MEROPS; C05.001; -.
DR Proteomes; UP000004992; 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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Disulfide bond; DNA-binding; Host nucleus;
KW Hydrolase; Late protein; Protease; Thiol protease; Virion.
FT CHAIN 1..204
FT /note="Protease"
FT /id="PRO_0000218026"
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"
SQ SEQUENCE 204 AA; 23068 MW; 7E5C7DCFCEC9A1DE CRC64;
MGSSEQELKA IVKDLGCGPY FLGTYDKRFP GFVSPHKLAC AIVNTAGRET GGVHWMAFAW
NPHSKTCYLF EPFGFSDQRL KQVYQFEYES LLRRSAIASS PDRCITLEKS TQSVQGPNSA
ACGLFCCMFL HAFANWPQTP MDHNPTMNLI TGVPNSMLNS PQVQPTLRRN QEQLYSFLER
HSPYFRSHSA QIRSATSFCH LKNM
