ID   VL1_HPV65               Reviewed;         516 AA.
AC   Q07874;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-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 65.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Gammapapillomavirus.
OX   NCBI_TaxID=28312;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8389082; DOI=10.1006/viro.1993.1320;
RA   Egawa K., Delius H., Matsukura T., Kawashima M., de Villiers E.M.;
RT   "Two novel types of human papillomavirus, HPV 63 and HPV 65: comparisons of
RT   their clinical and histological features and DNA sequences to other HPV
RT   types.";
RL   Virology 194:789-799(1993).
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; X70829; CAA50177.1; -; Genomic_DNA.
DR   SMR; Q07874; -.
DR   PRIDE; Q07874; -.
DR   Proteomes; UP000007672; 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; Reference proteome; 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_0000133547"
FT   REGION          128..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        176
FT                   /note="Interchain (with C-439)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        439
FT                   /note="Interchain (with C-176)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   516 AA;  58649 MW;  B2F1F797911BFBF9 CRC64;
     MASWLSAKGK VYLPPAQPVA RVLETDEYIT GTSLYFHAGT ERLLTVGHPY FPVKDVQDQH
     KVLVPKVSGS QYRVFRFYLP DPNRFALIDN GFYDSDHERL VWRLRGIEIG RGGPLGIGTT
     GHPLYNKFGD SENPNGYRKQ SDDNRQDVSL DPKQTQMFII GCTPAIGEHW DKAEPCASPV
     PQPGDCPPIE LVNTYIEDGD MCDIGFGAFN FKALQQDKSS APLDVVATMC KWPDFLKMSK
     DVYGDSLFFY GRREQLYARH FFVRAGAMGD ALPEPFEVKT DYWIPAQEGQ DQNTLGPHIY
     IGTPSGSLVS SESQLFNRPY WLNRAQGTNN GICWDNQLFV TLVDNTHNTN FTISVKTEAA
     DESYKYKAGD FKQYLRHIEE FEMEFIFQLC TVPLTADVMA HLNVMNPNIL DNWQLNFVPP
     PPSGIEDQYR FIQSRATRCP TQSPSTEKED PYKDLSFWGV DLTERFSSEL SQFSLGRRFL
     YQSGLINGTL KRKRTINSQA PTSIKRSAKR KRSIKQ