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Protease (EC 3.4.22.39) (Adenain) (Adenovirus protease) (AVP) (Adenovirus proteinase) (Endoprotease)

 PRO_ADE02               Reviewed;         204 AA.
P03252;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
16-JAN-2019, entry version 108.
RecName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04059};
EC=3.4.22.39 {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenain {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenovirus protease {ECO:0000255|HAMAP-Rule:MF_04059};
Short=AVP {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenovirus proteinase {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Endoprotease {ECO:0000255|HAMAP-Rule:MF_04059};
Name=L3 {ECO:0000255|HAMAP-Rule:MF_04059};
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
NCBI_TaxID=10515;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6259616; DOI=10.1093/nar/9.1.1;
Akusjaervi G., Zabielski J., Perricaudet M., Pettersson U.;
"The sequence of the 3' non-coding region of the hexon mRNA discloses
a novel adenovirus gene.";
Nucleic Acids Res. 9:1-17(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-204.
PubMed=6258984; DOI=10.1016/0014-5793(80)80464-9;
Buttner W., Veres-Molnar Z.;
"Localization of the 3'-terminal end of the EcoRI B fragment-specific
early mRNA of adenovirus type 2.";
FEBS Lett. 122:317-321(1980).
[3]
SUBCELLULAR LOCATION.
STRAIN=Human adenovirus C serotype 5;
PubMed=12645618; DOI=10.1021/pr025528c;
Chelius D., Huhmer A.F., Shieh C.H., Lehmberg E., Traina J.A.,
Slattery T.K., Pungor E. Jr.;
"Analysis of the adenovirus type 5 proteome by liquid chromatography
and tandem mass spectrometry methods.";
J. Proteome Res. 1:501-513(2002).
[4]
DNA-BINDING.
PubMed=11683632; DOI=10.1021/bi0111653;
McGrath W.J., Baniecki M.L., Li C., McWhirter S.M., Brown M.T.,
Toledo D.L., Mangel W.F.;
"Human adenovirus proteinase: DNA binding and stimulation of
proteinase activity by DNA.";
Biochemistry 40:13237-13245(2001).
[5]
INTERACTION WITH PROTEASE COFACTOR, AND ACTIVITY REGULATION.
PubMed=11591154; DOI=10.1021/bi0109008;
Baniecki M.L., McGrath W.J., McWhirter S.M., Li C., Toledo D.L.,
Pellicena P., Barnard D.L., Thorn K.S., Mangel W.F.;
"Interaction of the human adenovirus proteinase with its 11-amino acid
cofactor pVIc.";
Biochemistry 40:12349-12356(2001).
[6]
INTERCHAIN DISULFIDE BOND WITH PROTEASE COFACTOR, AND ACTIVITY
REGULATION.
PubMed=12069522; DOI=10.1006/viro.2002.1394;
McGrath W.J., Aherne K.S., Mangel W.F.;
"In the virion, the 11-amino-acid peptide cofactor pVIc is covalently
linked to the adenovirus proteinase.";
Virology 296:234-240(2002).
[7]
CHARACTERIZATION.
PubMed=12367749; DOI=10.1016/S0168-1702(02)00111-9;
Ruzindana-Umunyana A., Imbeault L., Weber J.M.;
"Substrate specificity of adenovirus protease.";
Virus Res. 89:41-52(2002).
[8]
MUTAGENESIS OF PRO-137.
STRAIN=Mutant ts-1;
PubMed=19860872; DOI=10.1186/1743-422X-6-174;
Imelli N., Ruzsics Z., Puntener D., Gastaldelli M., Greber U.F.;
"Genetic reconstitution of the human adenovirus type 2 temperature-
sensitive 1 mutant defective in endosomal escape.";
Virol. J. 6:174-174(2009).
[9]
FUNCTION.
PubMed=22791715; DOI=10.1074/jbc.M112.389957;
Perez-Berna A.J., Ortega-Esteban A., Menendez-Conejero R.,
Winkler D.C., Menendez M., Steven A.C., Flint S.J., de Pablo P.J.,
San Martin C.;
"The role of capsid maturation on adenovirus priming for sequential
uncoating.";
J. Biol. Chem. 287:31582-31595(2012).
[10]
CHARACTERIZATION.
PubMed=23043138; DOI=10.1074/jbc.M112.407460;
Blainey P.C., Graziano V., Perez-Berna A.J., McGrath W.J., Flint S.J.,
San Martin C., Xie X.S., Mangel W.F.;
"Regulation of a viral proteinase by a peptide and DNA in one-
dimensional space. IV. viral proteinase slides along DNA to locate and
process its substrates.";
J. Biol. Chem. 288:2092-2102(2013).
[11]
REVIEW.
PubMed=22754652; DOI=10.3390/v4050847;
San Martin C.;
"Latest insights on adenovirus structure and assembly.";
Viruses 4:847-877(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PROTEASE
COFACTOR, DISULFIDE BOND, ACTIVE SITE, AND ACTIVITY REGULATION.
PubMed=8617222;
Ding J., McGrath W.J., Sweet R.M., Mangel W.F.;
"Crystal structure of the human adenovirus proteinase with its 11
amino acid cofactor.";
EMBO J. 15:1778-1783(1996).
-!- FUNCTION: 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.
{ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:22791715}.
-!- CATALYTIC ACTIVITY:
Reaction=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).; EC=3.4.22.39; Evidence={ECO:0000255|HAMAP-
Rule:MF_04059};
-!- ACTIVITY REGULATION: 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.
{ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:11591154,
ECO:0000269|PubMed:12069522, ECO:0000269|PubMed:8617222}.
-!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction
is necessary for protease activation. {ECO:0000255|HAMAP-
Rule:MF_04059, ECO:0000269|PubMed:11591154,
ECO:0000269|PubMed:8617222}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059,
ECO:0000269|PubMed:12645618}. Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04059, ECO:0000305|PubMed:12645618}. Note=Present in about
10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04059}.
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_04059}.
-!- SIMILARITY: Belongs to the peptidase C5 family.
{ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J01917; AAA92216.1; -; Genomic_DNA.
PIR; A03823; W2AD35.
RefSeq; AP_000176.1; AC_000007.1.
RefSeq; NP_040526.1; NC_001405.1.
PDB; 1AVP; X-ray; 2.60 A; A=1-204.
PDB; 1NLN; X-ray; 1.60 A; A=1-204.
PDB; 4EKF; X-ray; 0.98 A; A=1-204.
PDB; 4PID; X-ray; 1.59 A; A=1-204.
PDB; 4PIE; X-ray; 1.94 A; A=1-204.
PDB; 5FGY; X-ray; 2.10 A; A=1-204.
PDBsum; 1AVP; -.
PDBsum; 1NLN; -.
PDBsum; 4EKF; -.
PDBsum; 4PID; -.
PDBsum; 4PIE; -.
PDBsum; 5FGY; -.
ProteinModelPortal; P03252; -.
SMR; P03252; -.
MEROPS; C05.001; -.
GeneID; 2652998; -.
EvolutionaryTrace; P03252; -.
Proteomes; UP000008167; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:CACAO.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
HAMAP; MF_04059; ADV_PRO; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR000855; Peptidase_C5.
Pfam; PF00770; Peptidase_C5; 1.
PIRSF; PIRSF001218; Protease_ADV; 1.
PRINTS; PR00703; ADVENDOPTASE.
ProDom; PD003705; Peptidase_C5; 1.
SUPFAM; SSF54001; SSF54001; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Complete proteome;
Disulfide bond; DNA-binding; Host nucleus; Hydrolase; Late protein;
Protease; Reference proteome; Thiol protease; Virion.
CHAIN 1 204 Protease.
/FTId=PRO_0000218023.
ACT_SITE 54 54 {ECO:0000255|HAMAP-Rule:MF_04059,
ECO:0000269|PubMed:8617222}.
ACT_SITE 71 71 {ECO:0000255|HAMAP-Rule:MF_04059,
ECO:0000269|PubMed:8617222}.
ACT_SITE 122 122 {ECO:0000255|HAMAP-Rule:MF_04059,
ECO:0000269|PubMed:8617222}.
SITE 51 52 Cleavage; by autolysis.
{ECO:0000255|HAMAP-Rule:MF_04059}.
DISULFID 104 104 Interchain (with C-10 in cleaved protease
cofactor pVI-C). {ECO:0000255|HAMAP-
Rule:MF_04059,
ECO:0000269|PubMed:8617222}.
MUTAGEN 137 137 P->L: Loss of activity; gives rise to
unprocessed capsids defective in
endosomal escape.
{ECO:0000269|PubMed:19860872}.
HELIX 5 14 {ECO:0000244|PDB:4EKF}.
HELIX 18 20 {ECO:0000244|PDB:4EKF}.
STRAND 21 28 {ECO:0000244|PDB:4EKF}.
STRAND 35 37 {ECO:0000244|PDB:5FGY}.
STRAND 39 45 {ECO:0000244|PDB:4EKF}.
HELIX 48 50 {ECO:0000244|PDB:4PID}.
STRAND 55 61 {ECO:0000244|PDB:4EKF}.
TURN 62 65 {ECO:0000244|PDB:4EKF}.
STRAND 66 70 {ECO:0000244|PDB:4EKF}.
HELIX 78 95 {ECO:0000244|PDB:4EKF}.
STRAND 106 109 {ECO:0000244|PDB:4EKF}.
HELIX 122 135 {ECO:0000244|PDB:4EKF}.
STRAND 141 144 {ECO:0000244|PDB:4EKF}.
HELIX 147 149 {ECO:0000244|PDB:4EKF}.
HELIX 155 157 {ECO:0000244|PDB:4EKF}.
HELIX 161 163 {ECO:0000244|PDB:4EKF}.
HELIX 164 181 {ECO:0000244|PDB:4EKF}.
HELIX 183 187 {ECO:0000244|PDB:4EKF}.
HELIX 189 195 {ECO:0000244|PDB:4EKF}.
TURN 198 201 {ECO:0000244|PDB:4EKF}.
SEQUENCE 204 AA; 23087 MW; E43C7DDF14A589A2 CRC64;
MGSSEQELKA IVKDLGCGPY FLGTYDKRFP GFVSPHKLAC AIVNTAGRET GGVHWMAFAW
NPRSKTCYLF EPFGFSDQRL KQVYQFEYES LLRRSAIASS PDRCITLEKS TQSVQGPNSA
ACGLFCCMFL HAFANWPQTP MDHNPTMNLI TGVPNSMLNS PQVQPTLRRN QEQLYSFLER
HSPYFRSHSA QIRSATSFCH LKNM


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Pathways :
WP2199: Seed Development
WP470: Proteasome Degradation
WP1929: Thrombin signalling through proteinase activated receptors (PARs)

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Bibliography :
[12793204] Adenain, the adenovirus endoprotease (a review).
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