ID   VL1_HPV47               Reviewed;         514 AA.
AC   P22424;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   23-FEB-2022, entry version 91.
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 47.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10594;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2162112; DOI=10.1016/0042-6822(90)90500-q;
RA   Kiyono T., Adachi A., Ishibashi M.;
RT   "Genome organization and taxonomic position of human papillomavirus type 47
RT   inferred from its DNA sequence.";
RL   Virology 177:401-405(1990).
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; M32305; AAA46982.1; -; Genomic_DNA.
DR   PIR; G35324; P1WL47.
DR   SMR; P22424; -.
DR   Proteomes; UP000008697; 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_0000133530"
FT   REGION          495..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-442)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        442
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   514 AA;  58283 MW;  E0F753F851EAE0F0 CRC64;
     MAVWHSANGK VYLPPSTPVA RVQSTDEYIQ RTNIYYHANT DRLLTVGHPY FNVYNNNGTT
     LEVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDKERLV WACRGLEIGR GQPLGVGSTG
     HPYFNKVKDT ENSNSYITNS KDDRQDTSFD PKQIQMFIVG CTPCIGEHWD KAEPCGEQQT
     GLCPPIELKN TYIQDGDMAD IGFGNINFKA LQHSRSDVSL DIVNETCKYP DFLKMQNDVY
     GDACFFYARR EQCYARHFFV RGGKTGDDIP GAQVGNGNMK NQFYIPGATG QAQSTIGNAM
     YFPTVSGSLV SSDAQLFNRP FWLQRAQGHN NGILWANQMF VTVVDNTRNT NFSISVYSQA
     GDIKDIQDYN ADNFREYQRH VEEYEISVIL QLCKVPLKAE VLAQINAMNS SLLEEWQLGF
     VPTPDNPIQD TYRYLESLAT RCPEKSPPKE KVDPYKGLNF WDVDMTERLS LDLDQYSLGR
     KFLFQAGLQQ TTVNGTKTTP YRGSIRGTKR KRKN