ID   VE2_OVPVD               Reviewed;         416 AA.
AC   P03123;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN   Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS   Odocoileus virginianus papillomavirus 1 (DPV) (Deer papillomavirus).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=2772504;
OH   NCBI_TaxID=9874; Odocoileus virginianus (White-tailed deer).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2993669; DOI=10.1128/jvi.56.1.85-91.1985;
RA   Groff D.E., Lancaster W.D.;
RT   "Molecular cloning and nucleotide sequence of deer papillomavirus.";
RL   J. Virol. 56:85-91(1985).
CC   -!- FUNCTION: Plays a role in the initiation of viral DNA replication. A
CC       dimer of E2 interacts with a dimer of E1 in order to improve
CC       specificity of E1 DNA binding activity. Once the complex recognizes and
CC       binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also
CC       regulates viral transcription through binding to the E2RE response
CC       element (5'-ACCNNNNNNGGT-3') present in multiple copies in the
CC       regulatory regions of the viral genome. Activates or represses
CC       transcription depending on E2RE's position with regards to proximal
CC       promoter elements including the TATA-box. Repression occurs by
CC       sterically hindering the assembly of the transcription initiation
CC       complex. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SUBUNIT: Binds DNA as homodimer. Interacts with protein E1; this
CC       interaction greatly increases E1 DNA-binding activity. Interacts with
CC       protein L1; this interaction enhances E2-dependent replication and
CC       transcription activation. Interacts with protein L2; this interaction
CC       inhibits E2 transcriptional activity but not DNA replication function
CC       E2. Interacts with protein E7; this interaction inhibits E7 oncogenic
CC       activity. Interacts with host TAF1; this interaction modulates E2-
CC       dependent transcriptional regulation. Interacts with host BRD4; this
CC       interaction mediates E2 transcriptional activation function.
CC       Additionally, the interaction with host BRD4 on mitotic chromosomes
CC       mediates tethering of the viral genome. Interacts with host TOPBP1;
CC       this interaction is required for optimal viral DNA replication.
CC       {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04001}.
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DR   EMBL; M11910; AAA66844.1; -; Genomic_DNA.
DR   PIR; A03673; W2WLDP.
DR   RefSeq; NP_041296.1; NC_001523.1.
DR   SMR; P03123; -.
DR   GeneID; 1488982; -.
DR   KEGG; vg:1488982; -.
DR   Proteomes; UP000009185; Genome.
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:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.30; -; 1.
DR   Gene3D; 2.170.200.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_04001; PPV_E2; 1.
DR   InterPro; IPR035975; E2/EBNA1_C_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR000427; Papillomavirus_E2_C.
DR   InterPro; IPR001866; Papillomavirus_E2_N.
DR   InterPro; IPR033668; Reg_prot_E2.
DR   InterPro; IPR036050; Regulatory_protein_E2_N.
DR   InterPro; IPR042503; Regulatory_protein_E2_N_1.
DR   InterPro; IPR042504; Regulatory_protein_E2_N_2.
DR   Pfam; PF00511; PPV_E2_C; 1.
DR   Pfam; PF00508; PPV_E2_N; 1.
DR   SUPFAM; SSF51332; SSF51332; 1.
DR   SUPFAM; SSF54957; SSF54957; 1.
PE   3: Inferred from homology;
KW   Activator; DNA replication; DNA-binding; Early protein; Host nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..416
FT                   /note="Regulatory protein E2"
FT                   /id="PRO_0000133246"
FT   REGION          1..203
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   REGION          190..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..416
FT                   /note="DNA-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   COMPBIAS        255..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46259 MW;  79064F8017368693 CRC64;
     MSAAKEQLLA AQETQMTLIE KDSTDLKDHI DSWGPVRREH GLLYAARHKG LIWLGLNPVP
     PCSVKCLEAR QAIEMQLLGN SLKESPWCNE PWSLCDLSWG RYQAPPAETL KKGARLVEVE
     YDGSSTNKTW YTAWNSLYLR KPDEEGWETA TGGADADGLF YTTMSGTRVY YELFERDAAR
     YSTTGTWTVR DNDRTYHSHS APSHSRETIE GLWNSGGRER GRPTNSPDRA VLHTPPGGNT
     VHGPVRACEN RGRSINRPTP YSTPQSPRSG VGPDTTSPLP SPVPQNPRCV SLPDGFGRGE
     EDNPPSPDQH DVIPNPQPKE PRFSLFGSSG GLPCLLISGT GNQVKCYSFR VKRWHRDKYH
     HCTTTWWAVG EQGSERPGDA TVIVTFKDQS QRSMFLQQVP LPPGMSAHGV TMTVDF