VE6_OVPVD
ID VE6_OVPVD Reviewed; 135 AA.
AC P03128;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
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 major role in the induction and maintenance of
CC cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-
CC protein ligase and modulates its activity. Protects host keratinocytes
CC from apoptosis by mediating the degradation of host BAK1. May also
CC inhibit host immune response. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC -!- SUBUNIT: Forms homodimers. Interacts with ubiquitin-protein ligase
CC UBE3A/E6-AP; this interaction stimulates UBE3A ubiquitin activity.
CC Interacts with host BAK1. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000305}.
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DR EMBL; M11910; AAA66841.1; -; Genomic_DNA.
DR PIR; A03687; W6WLDP.
DR RefSeq; NP_041293.1; NC_001523.1.
DR SMR; P03128; -.
DR GeneID; 1488979; -.
DR KEGG; vg:1488979; -.
DR Proteomes; UP000009185; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 Gene3D; 3.30.240.40; -; 2.
DR HAMAP; MF_04006; HPV_E6; 1.
DR InterPro; IPR001334; E6.
DR InterPro; IPR038575; E6_sf.
DR Pfam; PF00518; E6; 1.
DR SUPFAM; SSF161229; SSF161229; 2.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Early protein; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Metal-binding; Modulation of host cell apoptosis by virus;
KW Reference proteome; Transcription; Transcription regulation;
KW Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..135
FT /note="Protein E6"
FT /id="PRO_0000133389"
FT ZN_FING 11..47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 83..119
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ SEQUENCE 135 AA; 15624 MW; 7B02C68266430C4B CRC64;
MSADYYEHLY CVFCYCVLGK VEARRCYDKK IRTVVRGGLR CAVCTACLEK GLYLERVLNA
PQPVYQGSIE EPDPFIQKAC IRCMYCGGIL TRDEKDRHRY FEELYVIFRN QVLGRCYTCT
RHGMCSAPYR ANATG