ID   VE6_HPVME               Reviewed;         158 AA.
AC   P27962;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   23-FEB-2022, entry version 79.
DE   RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN   Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS   Human papillomavirus type ME180.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; unclassified Papillomaviridae.
OX   NCBI_TaxID=10602;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1716694; DOI=10.1128/jvi.65.10.5564-5568.1991;
RA   Reuter S., Delius H., Kahn T., Hofmann B., zur Hausen H., Schwarz E.;
RT   "Characterization of a novel human papillomavirus DNA in the cervical
RT   carcinoma cell line ME180.";
RL   J. Virol. 65:5564-5568(1991).
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; M73258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C40509; W6WLPR.
DR   SMR; P27962; -.
DR   IntAct; P27962; 1.
DR   MINT; P27962; -.
DR   PRIDE; P27962; -.
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; Transcription;
KW   Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..158
FT                   /note="Protein E6"
FT                   /id="PRO_0000133318"
FT   ZN_FING         32..68
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   ZN_FING         105..141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   MOTIF           156..158
FT                   /note="PDZ-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ   SEQUENCE   158 AA;  18739 MW;  2B1F406B563F05FC CRC64;
     MALFHNPEER PYKLPDLCRT LDTTLHDVTI DCVYCRRQLQ RTEVYEFAFG DLNVVYRDGV
     PLAACQSCIK FYAKIRELRY YSESVYATTL ETITNTKLYD LSIRCMCCLK PLSPAEKLRH
     LNSKRRFHKI AGNFTGQCRH CWTSKREDRR RTRQETQV