VE2_PAPVE
ID VE2_PAPVE Reviewed; 415 AA.
AC P11329;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 115.
DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
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 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; M15953; AAA66854.1; -; Genomic_DNA.
DR PIR; D29499; W2WLEP.
DR RefSeq; NP_041306.1; NC_001524.1.
DR SMR; P11329; -.
DR PRIDE; P11329; -.
DR GeneID; 1488990; -.
DR KEGG; vg:1488990; -.
DR Proteomes; UP000009060; 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..415
FT /note="Regulatory protein E2"
FT /id="PRO_0000133247"
FT REGION 1..205
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 221..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..415
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT COMPBIAS 269..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46245 MW; 0B7BF6AEEF0AC80C CRC64;
MKMSAASDHL LAAQETQMQC IEKDSRLLQD HACYWGAVRR EKLLLYAART KGLKTIGCVP
VPPCSVTAEQ AKQAICMQLI VEELLHSPWA KEPWSLTDLS WERYQAAPKG CLKKGARVVE
VEYDGNSSNK TWYTAWSTVY VRGTEEEGWE TAVCAADGQG IYYCAGMSSK VYFETFETDA
RRWSRTGHWT VRDNDVIYHS TFGAPPHSRN DRDCIEGFWS DAGERRGSRG SDTTDRALPY
PAARQSPICR PVRTGENRSR AVHRQAPYSA PSSPGSSVGP DSPSESSRQV PLVLLPGPSD
PAPPSPDSTD VIAEGDKEPE RFSILSKPGG QPCLILSGNG NQAKCYRFRC KRYFREHYQH
ITTTWWTVGE RGSERHGDAC VLVTFKDSSQ RGVFLKRVPL PPGMRAQALT MIADF
