ID   VL1_HPV04               Reviewed;         516 AA.
AC   Q07860;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   23-FEB-2022, entry version 93.
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 4.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Gammapapillomavirus.
OX   NCBI_TaxID=10617;
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; X70827; CAA50163.1; -; Genomic_DNA.
DR   RefSeq; NP_040895.1; NC_001457.1.
DR   SMR; Q07860; -.
DR   PRIDE; Q07860; -.
DR   GeneID; 1489455; -.
DR   KEGG; vg:1489455; -.
DR   Proteomes; UP000009253; 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_0000133486"
FT   REGION          129..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..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;  58462 MW;  FF2615FE732B3CCF CRC64;
     MSSWLSTTGK VYLPPAQPVA RVLETDEYIT GTSLYFHAGT ERLLTVGHPY FPVKDVQEPH
     KVLVPKVSGS QFRVFRFNLP DPNRFALIDN GFYDSDHERL VWKLRGIEIG RGGPLGIGTT
     GHPLYNKFGD TENPNGYKKQ SDDNRQDVSL DPKQTQMFII GCTPAIGEHW DKAEPCPSPA
     PQQGDCPPIE LVNSYIQDGD MCDIGFGAFN FKALQADKSS APLDVIATVC KWPDFLKMGK
     DIYGDSLFFF GRREQLYARH FFVRAGTMGD ALPEPFEATS DYFIGAQNQQ DQYTLGPHIY
     VGTPSGSLVS SESQLFNRPY WLNRAQGTNN GICWDNQLFV TLVDNTHNTN FTISVKSDGA
     NDNYQYKASD FKQYLRHIEE FEMEFIFQLC KVPLTADVMA HLNVMNPNIL DNWQLNFVPP
     PPSGIEDQYR FLQSRATRCP TQTPATEKED PYKDLSFWVV DLSERFSSEL SQFSLGRRFL
     YQSGLINGSL KRKRIISSSH AQTNTKRSAK RKRSLK