ID   VL1_HPV15               Reviewed;         507 AA.
AC   Q05137;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   23-FEB-2022, entry version 94.
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 15.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10606;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 312-355.
RX   PubMed=1326639; DOI=10.1128/jvi.66.10.5714-5725.1992;
RA   Chan S.-Y., Bernard H.U., Ong C.K., Chan S.P., Birgit H., Delius H.;
RT   "Phylogenetic analysis of 48 papillomavirus types and 28 subtypes and
RT   variants: a showcase for the molecular evolution of DNA viruses.";
RL   J. Virol. 66:5714-5725(1992).
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; X74468; CAA52511.1; -; Genomic_DNA.
DR   EMBL; M96284; AAA47023.1; -; Genomic_DNA.
DR   PIR; S36478; S36478.
DR   SMR; Q05137; -.
DR   Proteomes; UP000008232; 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..507
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133499"
FT   REGION          122..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-439)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        439
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   507 AA;  57220 MW;  3CF601C0C6229ADA CRC64;
     MTLWLPTTGK VYLPPTPPVA RVQSTDEYVE RTNVFYHAMS DRLLTVGHPY FDVRSVNGGS
     IEVPKVSGNQ YRAFRVTFPD PNRFALADMS VYNPEKERLV WACVGLEIGR GQPLGVGTSG
     HPLFNKVKDT ENNSNYQGNS TDDRQNTSFD PKQVQMFVVG CVPCLGEHWD RALVCESERN
     NQAGKCPPLE LKNTVIEDGD MFDIGFGNIN NKALSVTKSD VSLDIVNETC KYPDFLTMAN
     DVYGDACFFF ARREQCYARH YFVRGGAVGD ALPDAAVNQD HNFYLPAQST QQQNNLANST
     YFPTVSGSLV TSDAQLFNRP FWLRRAQGHN NGILWGNQMF ITVADNTRNT NFTISVTSDG
     NAINEYNSQN IREFLRHVEE YQLSIILQLC KIPLKAEVLT QINAMNSGIL EDWQLGFVPT
     PDNAVQDIYR YIDSKATKCP DAVQPKDKED PFGKYTFWNV DLTEKLSLDL DQYPLGRKFI
     FQAGLQRRPR TIKSSVKVSK GTKRKRT