VE7_PAPVE
ID VE7_PAPVE Reviewed; 102 AA.
AC P11332;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein E7 {ECO:0000255|HAMAP-Rule:MF_04004};
GN Name=E7 {ECO:0000255|HAMAP-Rule:MF_04004};
OS European elk papillomavirus (EEPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Deltapapillomavirus.
OX NCBI_TaxID=10565;
OH NCBI_TaxID=9860; Cervus elaphus (Red deer).
OH NCBI_TaxID=9870; Rangifer tarandus (Reindeer) (Cervus tarandus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3034730; DOI=10.1016/0378-1119(86)90324-0;
RA Ahola H., Bergman P., Stroem A.C., Moreno-Lopez J., Petterson U.;
RT "Organization and expression of the transforming region from the European
RT elk papillomavirus (EEPV).";
RL Gene 50:195-205(1986).
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; M15953; AAA66850.1; -; Genomic_DNA.
DR PIR; B29499; W7WLEP.
DR RefSeq; NP_041302.1; NC_001524.1.
DR SMR; P11332; -.
DR PRIDE; P11332; -.
DR GeneID; 1488988; -.
DR KEGG; vg:1488988; -.
DR Proteomes; UP000009060; 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.
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..102
FT /note="Protein E7"
FT /id="PRO_0000133469"
FT ZN_FING 61..97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT REGION 2..36
FT /note="E7 terminal domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..87
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
SQ SEQUENCE 102 AA; 11228 MW; 1A16531710ECE2C0 CRC64;
MVHGPRTKKH LPPYESPPLT LLLEPVAPVQ QTGIQAPQRK PPSQKGHKKG HKKVYSVTVP
CNGCDKNLEF CARTSSATIL TLQNLLLKDL DFLCSTCETN HG
