VL1_HPV20
ID VL1_HPV20 Reviewed; 516 AA.
AC P50786;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS Human papillomavirus 20.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=31547;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-474.
RX PubMed=7707535; DOI=10.1128/jvi.69.5.3074-3083.1995;
RA Chan S.-Y., Delius H., Halpern A.L., Bernard H.U.;
RT "Analysis of genomic sequences of 95 papillomavirus types: uniting typing,
RT phylogeny, and taxonomy.";
RL J. Virol. 69:3074-3083(1995).
CC -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm
CC diameter. The capsid is composed of 72 pentamers linked to each other
CC by disulfide bonds and associated with L2 proteins. Binds to heparan
CC sulfate proteoglycans on cell surface of basal layer keratinocytes to
CC provide initial virion attachment. This binding mediates a
CC conformational change in the virus capsid that facilitates efficient
CC infection. The virion enters the host cell via endocytosis. During
CC virus trafficking, L1 protein dissociates from the viral DNA and the
CC genomic DNA is released to the host nucleus. The virion assembly takes
CC place within the cell nucleus. Encapsulates the genomic DNA together
CC with protein L2. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC -!- SUBUNIT: Self-assembles into homopentamers. The capsid has an
CC icosahedral symmetry and consists of 72 capsomers, with each capsomer
CC being a pentamer of L1. Interacts with the minor capsid protein L2;
CC this interaction is necessary for viral genome encapsidation. Interacts
CC with protein E2; this interaction enhances E2-dependent replication and
CC transcription activation. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04002}.
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DR EMBL; U31778; AAA79393.1; -; Genomic_DNA.
DR EMBL; U21865; AAA92828.1; -; Genomic_DNA.
DR SMR; P50786; -.
DR Proteomes; UP000008230; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.175.20; -; 2.
DR HAMAP; MF_04002; PPV_L1; 1.
DR InterPro; IPR002210; Capsid_L1_Papillomavir.
DR InterPro; IPR036973; Capsid_L1_sf_Papillomavir.
DR InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR Pfam; PF00500; Late_protein_L1; 1.
DR PRINTS; PR00865; HPVCAPSIDL1.
DR SUPFAM; SSF88648; SSF88648; 1.
PE 3: Inferred from homology;
KW Capsid protein; Disulfide bond; Host nucleus; Host-virus interaction;
KW Late protein; T=7 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..516
FT /note="Major capsid protein L1"
FT /id="PRO_0000133504"
FT DISULFID 175
FT /note="Interchain (with C-444)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 444
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 516 AA; 58434 MW; CC7AF7FF76DBF8B5 CRC64;
MAVWQAASGK VYLPPSTPVA RVQSTDEYVQ RTNIYYHAYS DRLLTVGHPY FNIYDIQGTK
IKVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDKERLV WGCRGIEIGR GQPLGVGSVG
HPLFNKLGDT ENPNSYKGNS TDDRQNVSFD PKQLQMFIIG CAPCLGEHWD RALPCADDVP
NPGSCPPIEL KNTAIQDGDM ADIGYGNLNF KALQENRADV SLDIVNETCK YPDFLKMQND
VYGDSCFFYA RREQCYARHF FVRGGKTGDD IPAGQIDEGS MKNAFYIPPV NNQAQNNLGN
SMYFPTVSGS LVSSDAQLFN RPFWLQRAQG HNNGICWFNQ LFVTVVDNTR NTNFSISVHS
ENTDVSKIQN YDSQKFQEYL RHVEEYEISL ILQLCKVPLT AEVLAQINAM NSNILEEWQL
GFVPAPDNPI HDTYRYINSA ATRCPDKNPP KEREDPYKDL NFWNVDLSER LSLELDQYSL
GRKFLFQAGL QQATVNGTKT VSSKLSTRGV KRKRKQ