ID   VE6_HPV6A               Reviewed;         150 AA.
AC   Q84291;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 83.
DE   RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN   Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS   Human papillomavirus type 6a.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=37122;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7778283; DOI=10.1006/viro.1995.1283;
RA   Hofmann K.J., Cook J.C., Joyce J.G., Brown D.R., Schultz L.D., George H.A.,
RA   Rosolowsky M., Fife K.H., Jansen K.U.;
RT   "Sequence determination of human papillomavirus type 6a and assembly of
RT   virus-like particles in Saccharomyces cerevisiae.";
RL   Virology 209:506-518(1995).
RN   [2]
RP   INTERACTION WITH HUMAN ZYX.
RX   PubMed=11689660; DOI=10.1128/jvi.75.23.11791-11802.2001;
RA   Degenhardt Y.Y., Silverstein S.;
RT   "Interaction of zyxin, a focal adhesion protein, with the E6 protein from
RT   human papillomavirus type 6 results in its nuclear translocation.";
RL   J. Virol. 75:11791-11802(2001).
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. Sequesters tumor suppressor
CC       TP53 in the host cytoplasm and modulates its activity by interacting
CC       with host EP300 that results in the reduction of TP53 acetylation and
CC       activation. In turn, apoptosis induced by DNA damage is inhibited. E6
CC       protects also host keratinocytes from apoptosis by mediating the
CC       degradation of host BAK1. May also inhibit host immune response.
CC       {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 TP53 and EP300; this interaction inhibits TP53
CC       activity. Interacts with human ZYX. {ECO:0000255|HAMAP-Rule:MF_04006,
CC       ECO:0000269|PubMed:11689660}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}.
CC       Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
CC   -!- MISCELLANEOUS: Belongs to the low risk human alphapapillomavirus
CC       family. The cancer-causing human papillomavirus E6 protein has a unique
CC       carboxy terminal PDZ domain containing substrate but low risk E6s do
CC       not possess this domain. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC       {ECO:0000305}.
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; L41216; AAA74211.1; -; Genomic_DNA.
DR   SMR; Q84291; -.
DR   IntAct; Q84291; 17.
DR   MINT; Q84291; -.
DR   Proteomes; UP000007675; 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   1: Evidence at protein level;
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..150
FT                   /note="Protein E6"
FT                   /id="PRO_0000133325"
FT   ZN_FING         31..67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   ZN_FING         104..140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ   SEQUENCE   150 AA;  17290 MW;  AB363E6D233E6BBB CRC64;
     MESANASTSA TTIDQLCKTF NLSMHTLQIN CVFCKNALTT AEIYSYAYKQ LKVLFRGGYP
     YAACACCLEF HGKINQYRHF DYAGYATTVE EETKQDILDV LIRCYLCHKP LCEVEKVKHI
     LTKARFIKLN CTWKGRCLHC WTTCMEDMLP