AC MF_04004; DC Protein; auto TR HAMAP; MF_04004; -; 1; level=0 XX Names: PPV_E7 XX ID VE7 DE RecName: Full=Protein E7; GN Name=E7; XX CC -!- FUNCTION: Plays a role in viral genome replication by driving entry of CC quiescent cells into the cell cycle. Stimulation of progression from G1 CC to S phase allows the virus to efficiently use the cellular DNA CC replicating machinery to achieve viral genome replication. E7 protein CC has both transforming and trans-activating activities. Induces the CC disassembly of the E2F1 transcription factor from RB1, with subsequent CC transcriptional activation of E2F1-regulated S-phase genes. Interferes CC with host histone deacetylation mediated by HDAC1 and HDAC2, leading to CC transcription activation. Plays also a role in the inhibition of both CC antiviral and antiproliferative functions of host interferon alpha. CC Interaction with host TMEM173/STING impairs the ability of CC TMEM173/STING to sense cytosolic DNA and promote the production of type CC I interferon (IFN-alpha and IFN-beta). CC -!- SUBUNIT: Homodimer. Homooligomer. Interacts with host RB1; this CC interaction induces dissociation of RB1-E2F1 complex thereby disrupting CC RB1 activity. Interacts with host EP300; this interaction represses CC EP300 transcriptional activity. Interacts with protein E2; this CC interaction inhibits E7 oncogenic activity. Interacts with host CC TMEM173/STING; this interaction impairs the ability of TMEM173/STING to CC sense cytosolic DNA and promote the production of type I interferon CC (IFN-alpha and IFN-beta). CC -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. Note=Predominantly CC found in the host nucleus. CC -!- DOMAIN: The E7 terminal domain is an intrinsically disordered domain, CC whose flexibility and conformational transitions confer target CC adaptability to the oncoprotein. It allows adaptation to a variety of CC protein targets and exposes the PEST degradation sequence that CC regulates its turnover in the cell. CC -!- PTM: Highly phosphorylated. CC -!- SIMILARITY: Belongs to the papillomaviridae E7 protein family. XX DR Pfam; PF00527; E7; 1; trigger=no DR PIRSF; PIRSF003407; Papvi_E7; 1; trigger=no XX KW Activator KW DNA-binding KW Early protein KW G1/S host cell cycle checkpoint dysregulation by virus KW Host cytoplasm KW Host nucleus KW Host-virus interaction KW Inhibition of host innate immune response by virus KW Inhibition of host interferon signaling pathway by virus KW Metal-binding KW Modulation of host cell cycle by virus KW Transcription KW Transcription regulation KW Viral immunoevasion KW Zinc KW Zinc-finger XX GO GO:0003677; F:DNA binding GO GO:0046872; F:metal ion binding GO GO:0019904; F:protein domain specific binding GO GO:0003700; F:DNA-binding transcription factor activity GO GO:0039645; P:perturbation by virus of host G1/S transition checkpoint GO GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway GO GO:0006351; P:DNA-templated transcription XX FT From: VE7_HPV16 (P03129) FT ZN_FING 58..94 FT REGION Nter..40 FT /note="E7 terminal domain" FT Condition: C-x*-C-x-x-C FT MOTIF 22..26 FT /note="LXCXE motif; interaction with host RB1 and FT TMEM173/STING" FT Condition: L-x-C-x-E FT MOTIF 76..84 FT /note="Nuclear export signal" XX Size: 86-127; Related: None; Template: P03129; Scope: Viruses; Papillomaviridae Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.11 2023/07/28 //