ID   VL1_HPV42               Reviewed;         502 AA.
AC   P27233;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
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 42.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10590;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1309278; DOI=10.1016/0042-6822(92)90091-3;
RA   Philipp W., Honore N., Sapp M., Cole S.T., Streeck R.E.;
RT   "Human papillomavirus type 42: new sequences, conserved genome
RT   organization.";
RL   Virology 186:331-334(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA47048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M73236; AAA47048.1; ALT_INIT; Genomic_DNA.
DR   PIR; G39451; P1WL42.
DR   SMR; P27233; -.
DR   Proteomes; UP000009122; 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..502
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133526"
FT   REGION          478..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-427)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        427
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   502 AA;  56166 MW;  ED8083E650A1EA2E CRC64;
     MSVWRPSDNK VYLPPPPVSK VVSTDEYVQR TNYFYHASSS RLLVVGHPYY SITKRPNKTS
     IPKVSGLQYR VFRVRLPDPN KFTLPETNLY NPETQRMVWA CVGLEVGRGQ PLGVGISGHP
     LLNKLDDTEN APTYGGGPGT DNRENVSMDY KQTQLCLVGC KPAIGEHWGK GTACTPQSNG
     DCPPLELKNS FIQDGDMVDV GFGALDFGAL QSSKAEVPLD IVNSITKYPD YLKMSAEAYG
     DSMFFFLRRE QMFVRHLFNR AGAIGEPVPD ELYTKAANNA SGRHNLGSSI YYPTPSGSMV
     TSDAQLFNKP YWLQQAQGHN NGICWGNQLF LTVVDTTRST NMTLCATATS GDTYTAANFK
     EYLRHAEEYD VQFIFQLCKI TLTVEVMSYI HNMNPNILEE WNVGVAPPPS GTLEDSYRYV
     QSEAIRCQAK VTTPEKKDPY SDFWFWEVNL SEKFSTDLDQ FPLGRKFLLQ AGLRARPKLS
     VGKRKASTAK SVSSAKRKKT HK