ID   VL1_HPV39               Reviewed;         505 AA.
AC   P24838;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 95.
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 39.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10588;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1847266; DOI=10.1016/0042-6822(91)90518-g;
RA   Volpers C., Streeck R.E.;
RT   "Genome organization and nucleotide sequence of human papillomavirus type
RT   39.";
RL   Virology 181:419-423(1991).
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; M62849; AAA47056.1; -; Genomic_DNA.
DR   PIR; H38502; P1WL39.
DR   SMR; P24838; -.
DR   PRIDE; P24838; -.
DR   Proteomes; UP000009120; 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_0000133523"
FT   REGION          118..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..143
FT                   /note="Polar residues"
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"
SQ   SEQUENCE   505 AA;  56604 MW;  73854F9F1C56BC8D CRC64;
     MAMWRSSDSM VYLPPPSVAK VVNTDDYVTR TGIYYYAGSS RLLTVGHPYF KVGMNGGRKQ
     DIPKVSAYQY RVFRVTLPDP NKFSIPDASL YNPETQRLVW ACVGVEVGRG QPLGVGISGH
     PLYNRQDDTE NSPFSSTTNK DSRDNVSVDY KQTQLCIIGC VPAIGEHWGK GKACKPNNVS
     TGDCPPLELV NTPIEDGDMI DTGYGAMDFG ALQETKSEVP LDICQSICKY PDYLQMSADV
     YGDSMFFCLR REQLFARHFW NRGGMVGDAI PAQLYIKGTD IRANPGSSVY CPSPSGSMVT
     SDSQLFNKPY WLHKAQGHNN GICWHNQLFL TVVDTTRSTN FTLSTSIESS IPSTYDPSKF
     KEYTRHVEEY DLQFIFQLCT VTLTTDVMSY IHTMNSSILD NWNFAVAPPP SASLVDTYRY
     LQSAAITCQK DAPAPEKKDP YDGLKFWNVD LREKFSLELD QFPLGRKFLL QARVRRRPTI
     GPRKRPAAST SSSSATKHKR KRVSK