VE2_COPV6
ID VE2_COPV6 Reviewed; 385 AA.
AC Q89420;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 107.
DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS Canine oral papillomavirus (strain Y62) (COPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Lambdapapillomavirus.
OX NCBI_TaxID=766192;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8091677; DOI=10.1006/viro.1994.1552;
RA Delius H., van Ranst M.A., Jenson A.B., zur Hausen H., Sundberg J.P.;
RT "Canine oral papillomavirus genomic sequence: a unique 1.5-kb intervening
RT sequence between the E2 and L2 open reading frames.";
RL Virology 204:447-452(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Isegawa N., Ohta M., Shirasawa H., Tokita H., Simizu B., Yamaura A.;
RT "Nucleotide sequence of a canine oral papillomavirus containing a long
RT noncoding region.";
RL Int. J. Oncol. 7:155-159(1995).
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}.
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; D55633; BAA09501.1; -; Genomic_DNA.
DR EMBL; L22695; AAA61747.1; -; Genomic_DNA.
DR RefSeq; NP_056816.1; NC_001619.1.
DR SMR; Q89420; -.
DR GeneID; 1497241; -.
DR KEGG; vg:1497241; -.
DR Proteomes; UP000008788; Genome.
DR Proteomes; UP000097271; 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..385
FT /note="Regulatory protein E2"
FT /id="PRO_0000133244"
FT REGION 1..199
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 189..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..385
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 385 AA; 43095 MW; 4606908D76DD0151 CRC64;
MEKLSEALDL LQEELLSLYE QNSQSLADQS RHWSLLRKEQ VLLYYARGKG IMRIGMQPVP
PQSVSQAKAK QAIEQSLYID SLLHSKYANE PWTLCDTSRE RLVAEPAYTF KKGGKQIDVR
YGDSEENIVR YVLWLDIYYQ DEFDTWEKAH GKLDHKGLSY MHGTQQVYYV DFEEEANKYS
ETGKYEILNQ PTTIPTTSAA GTSGPELPGH SASGSGACSL TPRKGPSRRP GRRSSRFPRR
SGGRGRLGRG GSGELPPQPQ PSSSWSPPSP QQVGSKHQLR TTSSAGGRLG RLLQEAYDPP
VLVLAGDPNS LKCIRYRLSH KHRGLYLGAS TTWKWTSGGD GASKHDRGSA RMLLAFLSDQ
QREDFMDRVT FPKSVRVFRG GLDEL
