VE7_HPV31
ID VE7_HPV31 Reviewed; 98 AA.
AC P17387;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, 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 31.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10585;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2545036; DOI=10.1016/0042-6822(89)90545-x;
RA Goldsborough M.D., Disilvestre D., Temple G.F., Lorincz A.T.;
RT "Nucleotide sequence of human papillomavirus type 31: a cervical neoplasia-
RT associated virus.";
RL Virology 171:306-311(1989).
RN [2]
RP FUNCTION, INTERACTION WITH HUMAN RB1; HDAC1 AND HDAC1, AND MUTAGENESIS OF
RP CYS-61; LEU-67; SER-71; 82-LEU-LEU-83; CYS-91 AND CYS-94.
RX PubMed=15016876; DOI=10.1128/jvi.78.7.3533-3541.2004;
RA Longworth M.S., Laimins L.A.;
RT "The binding of histone deacetylases and the integrity of zinc finger-like
RT motifs of the E7 protein are essential for the life cycle of human
RT papillomavirus type 31.";
RL J. Virol. 78:3533-3541(2004).
CC -!- FUNCTION: E7 protein has both transforming and trans-activating
CC activities. Disrupts the function of host retinoblastoma protein
CC RB1/pRb, which is a key regulator of the cell cycle. Induces the
CC disassembly of the E2F1 transcription factors from RB1, with subsequent
CC transcriptional activation of E2F1-regulated S-phase genes.
CC Inactivation of the ability of RB1 to arrest the cell cycle is critical
CC for cellular transformation, uncontrolled cellular growth and
CC proliferation induced by viral infection. Stimulation of progression
CC from G1 to S phase allows the virus to efficiently use the cellular DNA
CC replicating machinery to achieve viral genome replication. Interferes
CC with histone deacetylation mediated by HDAC1 and HDAC2, leading to
CC activation of transcription. {ECO:0000269|PubMed:15016876}.
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 ---------------------------------------------------------------------------
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; J04353; AAA46951.1; -; Genomic_DNA.
DR PIR; B32444; W7WL31.
DR SMR; P17387; -.
DR IntAct; P17387; 3.
DR MINT; P17387; -.
DR Proteomes; UP000009116; 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 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..98
FT /note="Protein E7"
FT /id="PRO_0000133429"
FT ZN_FING 58..94
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT REGION 1..40
FT /note="E7 terminal domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT MOTIF 22..26
FT /note="LXCXE motif; interaction with host RB1 and
FT TMEM173/STING"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT MOTIF 76..84
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04004"
FT MUTAGEN 61
FT /note="C->A: No effect on the binding to HDAC1 and HDAC2.
FT Reduced copy number of episomes. Impaired production of
FT late transcripts."
FT /evidence="ECO:0000269|PubMed:15016876"
FT MUTAGEN 67
FT /note="L->R: Complete loss of binding to HDAC1 and HDAC2.
FT Complete loss of episomes. Impaired production of late
FT transcripts."
FT /evidence="ECO:0000269|PubMed:15016876"
FT MUTAGEN 71
FT /note="S->C: No effect on the binding to HDAC1 and HDAC2."
FT /evidence="ECO:0000269|PubMed:15016876"
FT MUTAGEN 82..83
FT /note="LL->RR: No effect on the binding to HDAC1 and HDAC2.
FT Impaired production of late transcripts."
FT /evidence="ECO:0000269|PubMed:15016876"
FT MUTAGEN 91
FT /note="C->G: Reduced binding to HDAC1 and HDAC2. Reduced
FT copy number of episomes. Impaired production of late
FT transcripts."
FT /evidence="ECO:0000269|PubMed:15016876"
FT MUTAGEN 94
FT /note="C->A: No effect on the binding to HDAC1 and HDAC2.
FT Reduced copy number of episomes. Impaired production of
FT late transcripts."
FT /evidence="ECO:0000269|PubMed:15016876"
SQ SEQUENCE 98 AA; 10918 MW; 793B7F5BC7324E9B CRC64;
MRGETPTLQD YVLDLQPEAT DLHCYEQLPD SSDEEDVIDS PAGQAEPDTS NYNIVTFCCQ
CKSTLRLCVQ STQVDIRILQ ELLMGSFGIV CPNCSTRL
