VE6_HPV49
ID VE6_HPV49 Reviewed; 138 AA.
AC P36813;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 82.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS Human papillomavirus type 49.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10616;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA Delius H., Hofmann B.;
RT "Primer-directed sequencing of human papillomavirus types.";
RL Curr. Top. Microbiol. Immunol. 186:13-31(1994).
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; X74480; CAA52579.1; -; Genomic_DNA.
DR PIR; S36567; S36567.
DR RefSeq; NP_041832.1; NC_001591.1.
DR PDB; 6SMV; X-ray; 2.14 A; A=1-138.
DR PDBsum; 6SMV; -.
DR SMR; P36813; -.
DR GeneID; 1489444; -.
DR KEGG; vg:1489444; -.
DR Proteomes; UP000009124; 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 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; Transcription;
KW Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..138
FT /note="Protein E6"
FT /id="PRO_0000133367"
FT ZN_FING 25..61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 98..134
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:6SMV"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6SMV"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6SMV"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6SMV"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6SMV"
SQ SEQUENCE 138 AA; 16202 MW; 69AD429D88C08ADB CRC64;
MARPVKVCEL AHHLNIPIWE VLLPCNFCTG FLTYQELLEF DYKDFNLLWK DGFVFGCCAA
CAYRSAYHEF TNYHQEIVVG IEIEGRAAAN IAEIVVRCLI CLKRLDLLEK LDICAQHREF
HRVRNRWKGV CRHCRVIE
