VE7_HPV42
ID VE7_HPV42 Reviewed; 93 AA.
AC P27231;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein E7 {ECO:0000255|HAMAP-Rule:MF_04004};
GN Name=E7 {ECO:0000255|HAMAP-Rule:MF_04004};
OS Human papillomavirus 42.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10590;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1309278; DOI=10.1016/0042-6822(92)90091-3;
RA Philipp W., Honore N., Sapp M., Cole S.T., Streeck R.E.;
RT "Human papillomavirus type 42: new sequences, conserved genome
RT organization.";
RL Virology 186:331-334(1992).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M73236; AAA47042.1; ALT_INIT; Genomic_DNA.
DR PIR; F39451; W7WL42.
DR SMR; P27231; -.
DR Proteomes; UP000009122; 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; Transcription;
KW Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..93
FT /note="Protein E7"
FT /id="PRO_0000133440"
FT ZN_FING 53..89
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 25..29
FT /note="LXCXE motif; interaction with host RB1 and
FT TMEM173/STING"
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 93 AA; 10679 MW; 829D1E24071F7AE3 CRC64;
MRGETPTLKD IVLFDIPTCE TPIDLYCYEQ LDSSDEDDQA KQDIQRYRIL CVCTQCYKSV
KLVVQCTEAD IRNLQQMLLG TLDIVCPLCA RVE
