VE6_PAPVE
ID VE6_PAPVE Reviewed; 135 AA.
AC P11331;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 12-AUG-2020, entry version 86.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
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 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; M15953; AAA66849.1; -; Genomic_DNA.
DR PIR; A29499; W6WLEP.
DR RefSeq; NP_041301.1; NC_001524.1.
DR SMR; P11331; -.
DR GeneID; 1488996; -.
DR KEGG; vg:1488996; -.
DR Proteomes; UP000009060; 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; 1.
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_0000133390"
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; 15870 MW; AE4F1BABC95E0459 CRC64;
MCGECYAYLT CIWCKKGLDK VDAKRCHEKK IRIACRNGKH CAVCTSCLEN GLYLERSLFP
GRPIYPGDLY EPDPWVMFND IRCMYCGGCL TRDEKERHRL FCEDFWIFRH QVRGRCYLCT
RHGSRPPYKE TPAAV