ID   VL1_HPV07               Reviewed;         505 AA.
AC   Q05136;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
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 7.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10620;
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 300-343.
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; M96293; AAA47032.1; -; Genomic_DNA.
DR   EMBL; X74463; CAA52481.1; -; Genomic_DNA.
DR   EMBL; M96300; AAA47039.1; -; Genomic_DNA.
DR   PIR; S36589; S36589.
DR   RefSeq; NP_041859.1; NC_001595.1.
DR   SMR; Q05136; -.
DR   GeneID; 1489474; -.
DR   KEGG; vg:1489474; -.
DR   Proteomes; UP000008226; 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..505
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133491"
FT   REGION          474..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        173
FT                   /note="Interchain (with C-427)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        427
FT                   /note="Interchain (with C-173)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   505 AA;  56276 MW;  1D126BA00EC4D9A3 CRC64;
     MWQLNENQVY LPPPTPVATI VSTDEYVQRT SLYYHAGSTR LLTIGHPYFE LKKPNGDVSV
     PKVSGHQYRV FRVRLPDPNK FGLSDTSLFN SETQRLVWAC VGVEVGRGQP LGVGISGHPY
     FNKDEDVENS SVYGTVPGQD SRENVAMDYK QTQLCIVGCT PPIGEYWGMG TPCNASKVSP
     GDCPVLELKS EVIEDGDMVD AGFGAMDFAS LQANKSDVPL DLCTSISKYP DYLGMAAEPY
     GNSLFFFLRR EQMFVRHFFN RAGTTGDSVP NDLYITGSSN RASIAGSIYY STPSGSLVTS
     DSQIFNKPLW IQKAQGHNNG ICFGNQLFVT VVDTTRSTNL TLCAATQSPT PTPYDNSKFK
     EYLRHGEEFD LQFIFQLCVI TLNAEVMTYI HAMDSSLLDD WNFKIGPPAS ATLEDTYRFL
     TNKAIACQRD APPKEKEDPY KKYKFWEVNL TEKFSSQLDQ FPLGRKFLMQ AGLRTGPKFK
     SRKRPAPTSS SSSGSVTPKR KKTKR