ID   VE7_HPV65               Reviewed;          98 AA.
AC   Q07859;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein E7 {ECO:0000255|HAMAP-Rule:MF_04004};
GN   Name=E7 {ECO:0000255|HAMAP-Rule:MF_04004};
OS   Human papillomavirus 65.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Gammapapillomavirus.
OX   NCBI_TaxID=28312;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8389082; DOI=10.1006/viro.1993.1320;
RA   Egawa K., Delius H., Matsukura T., Kawashima M., de Villiers E.M.;
RT   "Two novel types of human papillomavirus, HPV 63 and HPV 65: comparisons of
RT   their clinical and histological features and DNA sequences to other HPV
RT   types.";
RL   Virology 194:789-799(1993).
RN   [2]
RP   REVIEW.
RX   PubMed=11921304; DOI=10.1002/rmv.340;
RA   Lee C., Cho Y.;
RT   "Interactions of SV40 large T antigen and other viral proteins with
RT   retinoblastoma tumour suppressor.";
RL   Rev. Med. Virol. 12:81-92(2002).
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. Also plays 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). {ECO:0000255|HAMAP-
CC       Rule:MF_04004}.
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). {ECO:0000255|HAMAP-Rule:MF_04004}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004}.
CC       Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004}. Note=Predominantly
CC       found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004}.
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. {ECO:0000255|HAMAP-Rule:MF_04004}.
CC   -!- PTM: Highly phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04004}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E7 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04004}.
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DR   EMBL; X70829; CAA50172.1; -; Genomic_DNA.
DR   SMR; Q07859; -.
DR   Proteomes; UP000007672; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-UniRule.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04004; PPV_E7; 1.
DR   InterPro; IPR000148; Papilloma_E7.
DR   Pfam; PF00527; E7; 1.
DR   PIRSF; PIRSF003407; Papvi_E7; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Early protein;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW   Host nucleus; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus; Metal-binding;
KW   Modulation of host cell cycle by virus; Oncogene; Reference proteome;
KW   Transcription; Transcription regulation; Viral immunoevasion; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..98
FT                   /note="Protein E7"
FT                   /id="PRO_0000133458"
FT   ZN_FING         53..90
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT   REGION          1..42
FT                   /note="E7 terminal domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT   MOTIF           71..79
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
SQ   SEQUENCE   98 AA;  11062 MW;  98C2A51327ECFE62 CRC64;
     MRGAAPRVAD LNLELNDLVL PINLLSEEVL QPSDDESEAP EEELFPFRID TCCYRCEVNV
     RITLFAVEFG LRALEQLIVD GKLTFCCTTC ARTLRNGR