VL1_HPV08
ID VL1_HPV08 Reviewed; 514 AA.
AC P06417;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 23-FEB-2022, entry version 92.
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 type 8.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10579;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009874; DOI=10.1128/jvi.58.2.626-634.1986;
RA Fuchs P.G., Iftner T., Weninger J., Pfister H.;
RT "Epidermodysplasia verruciformis-associated human papillomavirus 8: genomic
RT sequence and comparative analysis.";
RL J. Virol. 58:626-634(1986).
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; M12737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03642; P1WL8.
DR SMR; P06417; -.
DR Proteomes; UP000009103; 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..514
FT /note="Major capsid protein L1"
FT /id="PRO_0000133492"
FT REGION 127..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175
FT /note="Interchain (with C-443)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 443
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 514 AA; 58562 MW; 22860386CB9FE9CA CRC64;
MAVWQSATGK VYLPPSTPVA RVQSTDEYIQ RTNIYYHANT DRLLTVGHPY FNVYNNNGDT
LQVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDKERLV WACRGLEISR GQPLGVGSTG
HPYFNKVKDT ENSNSYTTTS TDDRQNTSFD PKQIQMFIVG CTPCIGEHWE KAIPCAEDQQ
QGLCPPIELK NTVIEDGDMA DIGFGNMNFK TLQQNRSDVS LDIVNEICKY PDFLKMQNDV
YGDACFFYAR REQCYARHFF VRGGKTGDDI PAAQIDDGMM KNQYYIPGGQ DQSQKDIGNA
MYFPTVSGSL VSSDAQLFNR PFWLQRAQGH NNGILWANQM FVTVVDNTRN TNFSISVYTE
NGELKNITDY KSTQFREYLR HVEEYEISLI LQLCKIPLKA DVLAQINAMN SSLLEEWQLG
FVPTPDTPIH DTYRYIDSLA TRCPDKSPPK EKPDPYAKFN FWNVDLTERL SLDLDQYSLG
RKFLFQAGLQ QTTVNGTKSI SRGSVRGTKR KRKN