VE7_BPV1
ID VE7_BPV1 Reviewed; 127 AA.
AC P06933;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein E7 {ECO:0000255|HAMAP-Rule:MF_04004};
GN Name=E7 {ECO:0000255|HAMAP-Rule:MF_04004};
OS Bovine papillomavirus type 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Deltapapillomavirus.
OX NCBI_TaxID=337052;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6289124; DOI=10.1038/299529a0;
RA Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.;
RT "The primary structure and genetic organization of the bovine
RT papillomavirus type 1 genome.";
RL Nature 299:529-534(1982).
RN [2]
RP COMPARATIVE ANALYSIS OF HUMAN TYPE 1A AND BOVINE TYPE 1 GENOMES.
RX PubMed=6302319; DOI=10.1128/jvi.46.2.557-566.1983;
RA Danos O., Engel L.W., Chen E.Y., Yaniv M., Howley P.M.;
RT "Comparative analysis of the human type 1a and bovine type 1 papillomavirus
RT genomes.";
RL J. Virol. 46:557-566(1983).
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 -!- INTERACTION:
CC P06933; A2AN08: Ubr4; Xeno; NbExp=2; IntAct=EBI-7730971, EBI-4285947;
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; X02346; CAB46510.1; -; Genomic_DNA.
DR PIR; D18151; W7WLEB.
DR RefSeq; NP_056738.1; NC_001522.1.
DR IntAct; P06933; 2.
DR MINT; P06933; -.
DR GeneID; 1489018; -.
DR KEGG; vg:1489018; -.
DR Proteomes; UP000006567; 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:0019904; F:protein domain specific binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
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 GO; GO:0019087; P:transformation of host cell by virus; IDA:CACAO.
DR HAMAP; MF_04004; PPV_E7; 1.
DR InterPro; IPR000148; Papilloma_E7.
DR Pfam; PF00527; E7; 1.
PE 1: Evidence at protein level;
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..127
FT /note="Protein E7"
FT /id="PRO_0000133392"
FT ZN_FING 82..118
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT REGION 2..56
FT /note="E7 terminal domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT REGION 23..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..108
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
SQ SEQUENCE 127 AA; 13637 MW; B2FA82C37F8DE9BE CRC64;
MVQGPNTHRN LDDSPAGPLL ILSPCAGTPT RSPAAPDAPD FRLPCHFGRP TRKRGPTTPP
LSSPGKLCAT GPRRVYSVTV CCGNCGKELT FAVKTSSTSL LGFEHLLNSD LDLLCPRCES
RERHGKR
