ID   VL1_HPV60               Reviewed;         508 AA.
AC   P50821; Q80947;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   23-FEB-2022, entry version 86.
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 60.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Gammapapillomavirus.
OX   NCBI_TaxID=40540;
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 372-467.
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; U31792; AAA79491.1; -; Genomic_DNA.
DR   EMBL; U21876; AAA92837.1; -; Genomic_DNA.
DR   RefSeq; NP_043443.1; NC_001693.1.
DR   SMR; P50821; -.
DR   GeneID; 1403644; -.
DR   KEGG; vg:1403644; -.
DR   Proteomes; UP000120507; 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..508
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133542"
FT   DISULFID        178
FT                   /note="Interchain (with C-437)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        437
FT                   /note="Interchain (with C-178)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   508 AA;  57828 MW;  3149549895534D00 CRC64;
     MALWLQTAGQ LYLPPSKPVA RVLSTDEYVQ PTNLVFHTGT DRMLIVGHPY FDIIDSGSNN
     ITVPKCSGNQ FRVMRLLFPD PNKFAMIDRA VFNPERERLV WRLEGLEIGR GGPLGIGTSG
     HPLFNKYGDT ENPAAYPLKQ NNGDDNRMDV SMDPKQMQLF IVGCKPATGE HWDIAKPCDP
     APAKGSCPPI KLTQSIIQDG EMCDTGFGNA NFITLQEDKS GVPLDITNEI CKYPDLLKMT
     KDIYGDAVFF FGKREQIYSR HYFVRGGIDG DSLPDSGYYL APQTDKPQNN LGGYSYFPTP
     SGSVASSDNQ LFNRPYWLHR AQGANNGICW GNQLFITIVD NTRNTNLSIS VYKQDAAIDN
     RYKYKQEDFR QYLRHTEEYE VELILRLCKV PLNPDVLAHL NVMDKNILED WQLSFVPPPP
     QGIEDAYRYI MSQATMCPTD VPNTEREDPY KQYTFWTIDL QERFSNELSQ FSLGKRYLYQ
     YGLLNGRKRS ASSFVTKKSK TVKRKRTK