ID   VL1_HPV12               Reviewed;         517 AA.
AC   P36733;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 89.
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 12.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10604;
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).
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; X74466; CAA52501.1; -; Genomic_DNA.
DR   PIR; S36543; S36543.
DR   SMR; P36733; -.
DR   PRIDE; P36733; -.
DR   Proteomes; UP000009106; 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..517
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133496"
FT   REGION          497..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-444)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        444
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   517 AA;  58923 MW;  30E10F551A5CFDDE CRC64;
     MAVWQAAHGK VYLPPSTPVA RVQSTDEYIQ RTNIYYHANT DRLLTVGHPY FNVYDNTGKK
     LEVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDRERLV WACRGLEISR GQPLGVGSTG
     HPYFNKIKDT ENSNNYATGS KDDRQNTSFD PKQIQMFIVG CTPCVGEHWE KALPCGDAPA
     ENGVCPPIEL KNTFIEDGDM ADIGFGNMNF KTLQQNRSDV SLDIVNETCK YPDFLKMQND
     VYGDACFFYA RREQCYARHF FVRGGKTGDD IPDAQIDDGN MKNQYYIPGA QDQSQKDIGN
     AMYFPTVSGS LVSSDAQLFN RPFWLQRAQG HNNGILWANQ MFVTVVDNTR NTNFSISIYS
     DNQNVHDIPN YDSQKFREYL RHVEEYEISL ILQLCKVPLK AEVLAQINAM NSSLLEDWQL
     GFVPTPDNPI HDTYRYIESL ATRCPDKNPP KEKPDPYDGL SFWTVDMTER LSLDLDQYSL
     GRKFLFQAGL QQTTVNGTTK SSSYRSSIRG TKRKRKN