VE6_BPV1
ID VE6_BPV1 Reviewed; 137 AA.
AC P06931;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-JUN-2021, entry version 114.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS Bovine papillomavirus type 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Deltapapillomavirus.
OX NCBI_TaxID=337052;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6289124; DOI=10.1038/299529a0;
RA Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.;
RT "The primary structure and genetic organization of the bovine
RT papillomavirus type 1 genome.";
RL Nature 299:529-534(1982).
RN [2]
RP COMPARATIVE ANALYSIS OF HUMAN TYPE 1A AND BOVINE TYPE 1 GENOMES.
RX PubMed=6302319; DOI=10.1128/jvi.46.2.557-566.1983;
RA Danos O., Engel L.W., Chen E.Y., Yaniv M., Howley P.M.;
RT "Comparative analysis of the human type 1a and bovine type 1 papillomavirus
RT genomes.";
RL J. Virol. 46:557-566(1983).
RN [3]
RP IDENTIFICATION OF PROTEIN.
RX PubMed=2996134; DOI=10.1126/science.2996134;
RA Androphy E.J., Schiller J.T., Lowy D.R.;
RT "Identification of the protein encoded by the E6 transforming gene of
RT bovine papillomavirus.";
RL Science 230:442-445(1985).
RN [4]
RP INTERACTION WITH HUMAN FBLN1, AND INHIBITION OF E6-MEDIATED TRANSFORMATION.
RX PubMed=12200142; DOI=10.1016/s0006-291x(02)02041-7;
RA Du M., Fan X., Hong E., Chen J.J.;
RT "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1.";
RL Biochem. Biophys. Res. Commun. 296:962-969(2002).
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. Interacts with human FBLN1.
CC {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:12200142}.
CC -!- INTERACTION:
CC P06931; P49023: PXN; Xeno; NbExp=3; IntAct=EBI-7281937, EBI-702209;
CC P06931; P49024: PXN; Xeno; NbExp=5; IntAct=EBI-7281937, EBI-2896280;
CC P06931; Q05086: UBE3A; Xeno; NbExp=2; IntAct=EBI-7281937, EBI-954357;
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; X02346; CAB46509.1; -; Genomic_DNA.
DR PIR; C18151; W6WLEB.
DR RefSeq; NP_056737.1; NC_001522.1.
DR PDB; 3PY7; X-ray; 2.29 A; A=1-137.
DR PDBsum; 3PY7; -.
DR SMR; P06931; -.
DR DIP; DIP-41442N; -.
DR IntAct; P06931; 7.
DR MINT; P06931; -.
DR GeneID; 1489017; -.
DR KEGG; vg:1489017; -.
DR Proteomes; UP000006567; 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:0008270; F:zinc ion binding; IDA:BHF-UCL.
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 3D-structure; Activator; DNA-binding; Early protein; Host cytoplasm;
KW Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus; Metal-binding;
KW Modulation of host cell apoptosis by virus; Reference proteome;
KW Transcription; Transcription regulation; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..137
FT /note="Protein E6"
FT /id="PRO_0000133315"
FT ZN_FING 17..53
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 90..127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:3PY7"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3PY7"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:3PY7"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3PY7"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3PY7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3PY7"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3PY7"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3PY7"
SQ SEQUENCE 137 AA; 15850 MW; 36FADDDA55444566 CRC64;
MDLKPFARTN PFSGLDCLWC REPLTEVDAF RCMVKDFHVV IREGCRYGAC TICLENCLAT
ERRLWQGVPV TGEEAELLHG KTLDRLCIRC CYCGGKLTKN EKHRHVLFNE PFCKTRANII
RGRCYDCCRH GSRSKYP
