ID   VL1_HPV5B               Reviewed;         525 AA.
AC   P26537;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 5b.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10599;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1649510; DOI=10.1016/0042-6822(91)91013-7;
RA   Yabe Y., Sakai A., Hitsumoto T., Kato H., Ogura H.;
RT   "A subtype of human papillomavirus 5 (HPV-5b) and its subgenomic segment
RT   amplified in a carcinoma: nucleotide sequences and genomic organizations.";
RL   Virology 183:793-798(1991).
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; D90252; BAA14300.1; -; Genomic_DNA.
DR   PIR; G40480; P1WLB5.
DR   SMR; P26537; -.
DR   PRIDE; P26537; -.
DR   Proteomes; UP000007669; 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..525
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133488"
FT   DISULFID        184
FT                   /note="Interchain (with C-453)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        453
FT                   /note="Interchain (with C-184)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   525 AA;  59603 MW;  CC52FB63885C5F3D CRC64;
     MAVWHSANGK VYLPPSTPVA RVQSTDEYIQ RTNIYYHAFS DRLLTVGHPY FNVYNITGDK
     LEVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDKERLV WACRGLEIGR GQPLGVGSTG
     HPYFNKVKDT ENSNAYITFS KDGQNTAFSK DDRLNTSFDP KQIQMFIVGC TPCIGEHWDK
     AVPCAKNDQQ TGLCPPIELK NTYIEDGDMA DIGFGNMNFK ALQDSRSDVS LDIVNETCKY
     PDFLKMQNDI YGDACFFYAR REQCYARHFF VRGGKTGDDI PGAQIDNGTY KNQFYIPGAD
     GQAQKTIGNA MYFPTVSGSL VSSDAQLFNR PFWLQRAQGH NNGILWANQM FITVVDNTRN
     TNFSISVYNQ AGPLKDVADY NAEQFREYQR HVEEYEISLI LQLCKVPLKA EVLAQINAMN
     SSLLEDWQLG FVPTPDNPIQ DTYRYIDSLA TRCPDKNPPK EKEDPYKGLH FWDVDLTERL
     SLDLDQYSLG RKFLFQAGLQ HTTVNGTKAV SYKGSNRGTK RKRKN