ID   VL1_HPV22               Reviewed;         510 AA.
AC   P50788;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   23-FEB-2022, entry version 88.
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 22.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=37954;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Delius H.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-464.
RX   PubMed=7707535; DOI=10.1128/jvi.69.5.3074-3083.1995;
RA   Chan S.-Y., Delius H., Halpern A.L., Bernard H.U.;
RT   "Analysis of genomic sequences of 95 papillomavirus types: uniting typing,
RT   phylogeny, and taxonomy.";
RL   J. Virol. 69:3074-3083(1995).
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; U31780; AAA79407.1; -; Genomic_DNA.
DR   EMBL; U21866; AAA92829.1; -; Genomic_DNA.
DR   SMR; P50788; -.
DR   Proteomes; UP000009111; 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..510
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133506"
FT   REGION          126..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..510
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-434)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        434
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   510 AA;  57744 MW;  252E564317A45A47 CRC64;
     MTLWLPTSGK IYLPPTPPVA RVQNTDEYVE RTDIYYHAIS DRLLTVGHPY FDVRSSDGAK
     IEVPKVSGNQ FRAFRVTFPD PNKFALGDMT IHDPERYRLV WACKGLEIGR GQPLGVGTTG
     HPLFNKLHDT ENPTERQEGT SDDRRNVSFD PKQVQMFIIG CIPCLGEYWD KAPVCEDAGS
     QVGLCPPLEL KNGVIEDGDM FDIGFGNINN KTLSFNRSDV SLDIVNEICK YPDFLTMSND
     VYGDSCFFCA RREQCYARHN FVRGGLVGDA IPDDAVQQDH KYYLPAASQT ALENSTYFPT
     VSGSLVTSDA QLFNRPFWLK RAQGHNNGIL WNNQMFVTVA DNTRNTNFSI SVASDGTTVN
     YDAKKIREFM RHVEEYQLSF ILQLCRIPLE AEVLTQINAM NHGILENWQL GFVPTPDNSV
     HDTYRYLQSK ATKCPDAVPD TQKEDPFGQY TFWNVDMSEK LSLDLDQYPL GRKFLFQSGL
     QRARASARVS VKRSATRKTS KTVKRRKLTS