ID   VL1_HPV62               Reviewed;         503 AA.
AC   P50823; Q676U6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 87.
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 62.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=334210;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15346342; DOI=10.1086/423855;
RA   Fu L., Terai M., Matsukura T., Herrero R., Burk R.D.;
RT   "Codetection of a mixed population of candHPV62 containing wild-type and
RT   disrupted E1 open-reading frame in a 45-year-old woman with normal
RT   cytology.";
RL   J. Infect. Dis. 190:1303-1309(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-466.
RX   PubMed=7963696; DOI=10.1093/infdis/170.5.1077;
RA   Bernard H.U., Chan S.-Y., Manos M.M., Ong C.K., Villa L.L., Delius H.,
RA   Peyton C.L., Bauer H.M., Wheeler C.M.;
RT   "Identification and assessment of known and novel human papillomaviruses by
RT   polymerase chain reaction amplification, restriction fragment length
RT   polymorphisms, nucleotide sequence, and phylogenetic algorithms.";
RL   J. Infect. Dis. 170:1077-1085(1994).
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; AY395706; AAR32252.1; -; Genomic_DNA.
DR   EMBL; U12499; AAA67243.1; -; Genomic_DNA.
DR   SMR; P50823; -.
DR   PRIDE; P50823; -.
DR   Proteomes; UP000102297; 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..503
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133544"
FT   REGION          475..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-428)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        428
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   CONFLICT        356
FT                   /note="K -> T (in Ref. 2; AAA67243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421..422
FT                   /note="LQ -> FE (in Ref. 2; AAA67243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430..436
FT                   /note="KGAASPS -> RGLPTR (in Ref. 2; AAA67243)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  56551 MW;  7F23BD7BDBB20F3D CRC64;
     MAMWRPGDGK VYLPPTPVSK VLSTDTYVTR TNLFYYGGSS RLLTVGHPYC TLQVGQGKRA
     TIPKVSGYQY RVFRVKLPDP NKFTLPDATL YNPDTERMVW ACRGIEVGRG QPLGVGTSGH
     PLYNRLDDTE NTSLLAAAND DSRDNISVDY KQTQLLIVGC KPPIGEHWTK GTLCPNAAPA
     PTECPPLEFK NTTIQDGDMV ETGYGAIDFK SLQESKSEVP LDICTSTCKY PDYLQMAAEP
     YGDCMFFCLR REQMFARHFF NRHGTMGEAL PTDLYMKGTP GSDRQMPGSY IYAPTPSGSM
     VSSDSQLFNK PYWLQRAQGH NNGICWFNEL FVTVVDTTRS TNFTICTAST AAAEYKATNF
     REFLRHTEEF DLQFIFQLCK IQLTPEIMAY LHNMNKDLLD DWNFGVLPPP STSLDETYHY
     LQSRAITCQK GAASPSPKVD PYAQMTFWTV DLKDKLSTDL DQFPLGRKFL LQAGSRPRSV
     AVSRKRSAPT KQSPTSAKRK RRK