ID   VL1_HPV40               Reviewed;         505 AA.
AC   P36740;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-NOV-2023, entry version 97.
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 40.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus; Alphapapillomavirus 8.
OX   NCBI_TaxID=10615;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X74478; CAA52572.1; -; Genomic_DNA.
DR   PIR; S36560; S36560.
DR   SMR; P36740; -.
DR   Proteomes; UP000009121; 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; Major capsid L1 (late) superfamily, Papillomavirus; 1.
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; Group I dsDNA viruses; 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_0000133524"
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;  56376 MW;  7D88D4162C8A48E1 CRC64;
     MWQLNENQVY LPPPTPVATI VSTDEYVQRT SLYYHAGSAR LLTIGHPYFE LKKPNGDISV
     PKVSGHQYRV FRVRLPDPNK FGLSDTSLFN SETQRLVWAC VGVEVGRGQP LGVGVSGHPY
     FNKDEDVENS SAYGTGPGQD SRENVAMDYK QTQLCMLGCT PPIGEYWGKG TPCNASRVTL
     GDCPVLELKT EVIQDGDMVD TGFGAMDFAS LQANKSDVPL DLCTSISKYP DYLGMAAEPY
     GNSLFFFLRR EQMFVRHFFN RAGTTGDSVP TDLYITGTSG RTPIAGSIYY STPSGSLVTS
     DSQIFNKPLW IQKAQGHNNG ICFGNQLFVT VVDTTRSTNL TLCAATQSPT PTPYNNSNFK
     EYLRHGEEFD LQFIFQLCVI TLNAEVMTYI HAMDPTLLED WNFKIAPPAS ASLEDTYRFL
     TNKAIACQRD APPKVREDPY KKYKFWDVNL TERFSSQLDQ FPLGRKFLMQ AGVRAGPRFK
     SRKRPAPSSS SSSKPVTPKR KKTKR
//