ID   VL1_HPV6A               Reviewed;         500 AA.
AC   P69898; P03100;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 71.
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 6a.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=37122;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7778283; DOI=10.1006/viro.1995.1283;
RA   Hofmann K.J., Cook J.C., Joyce J.G., Brown D.R., Schultz L.D., George H.A.,
RA   Rosolowsky M., Fife K.H., Jansen K.U.;
RT   "Sequence determination of human papillomavirus type 6a and assembly of
RT   virus-like particles in Saccharomyces cerevisiae.";
RL   Virology 209:506-518(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; L41216; AAA74218.1; -; Genomic_DNA.
DR   PDB; 6L31; EM; 4.18 A; A/B/C/D/E/F=22-468.
DR   PDBsum; 6L31; -.
DR   SMR; P69898; -.
DR   Proteomes; UP000007675; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Disulfide bond; Host nucleus;
KW   Host-virus interaction; 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..500
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133489"
FT   REGION          475..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        171
FT                   /note="Interchain (with C-423)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        423
FT                   /note="Interchain (with C-171)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   500 AA;  55597 MW;  B6168D0F76A287F7 CRC64;
     MWRPSDSTVY VPPPNPVSKV VATDAYVTRT NIFYHASSSR LLAVGHPYFS IKRANKTVVP
     KVSGYQYRVF KVVLPDPNKF ALPDSSLFDP TTQRLVWACT GLEVGRGQPL GVGVSGHPFL
     NKYDDVENSG SGGNPGQDNR VNVGMDYKQT QLCMVGCAPP LGEHWGKGKQ CTNTPVQAGD
     CPPLELITSV IQDGDMVDTG FGAMNFADLQ TNKSDVPIDI CGTTCKYPDY LQMAADPYGD
     RLFFFLRKEQ MFARHFFNRA GEVGEPVPDT LIIKGSGNRT SVGSSIYVNT PSGSLVSSEA
     QLFNKPYWLQ KAQGHNNGIC WGNQLFVTVV DTTRSTNMTL CASVTTSSTY TNSDYKEYMR
     HVEEYDLQFI FQLCSITLSA EVMAYIHTMN PSVLEDWNFG LSPPPNGTLE DTYRYVQSQA
     ITCQKPTPEK EKPDPYKNLS FWEVNLKEKF SSELDQYPLG RKFLLQSGYR GRSSIRTGVK
     RPAVSKASAA PKRKRAKTKR