ID   VL1_HPVME               Reviewed;         505 AA.
AC   P27964;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   02-JUN-2021, entry version 81.
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 ME180.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; unclassified Papillomaviridae.
OX   NCBI_TaxID=10602;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1716694; DOI=10.1128/jvi.65.10.5564-5568.1991;
RA   Reuter S., Delius H., Kahn T., Hofmann B., zur Hausen H., Schwarz E.;
RT   "Characterization of a novel human papillomavirus DNA in the cervical
RT   carcinoma cell line ME180.";
RL   J. Virol. 65:5564-5568(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}.
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; M73258; AAF14010.1; -; Genomic_DNA.
DR   PIR; B40509; P1WLPR.
DR   SMR; P27964; -.
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_0000133482"
FT   REGION          126..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-429)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        429
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   505 AA;  56805 MW;  595DE493B708207B CRC64;
     MALWRSSDNM VYLPPPSVAK VVNTDDYVTR TGIYYYAGTS RLLTVGHPYF KVPMSGGRKQ
     DIPKVSAYQY RVFRISLPDP NKFSLPESTL YNPDTQRLVW ACVGVEIGRG QPLGVGLSGH
     PLYNRLDDTE NSPFSSNKNP KDSRDNVSVD YKQTQLCIIG CVPAIGEHWA KGKSCKPSNV
     QPGDCPPLEL VNTPIQDGDM IDTGYGAMDF STLQETKSEV PLDICQSVCK YPDYLQMSAD
     VYGDSMFFCL RREQLFARHF WNRGGMVGDT IPTELYIKGT DIRDSPSSYV YAPSPSGSMV
     SSDSQLFNKP YWLHKAQGHN NGICWHNQLF LTVVDTTRST NFTLSTTTES AVPNIYDPNK
     FKEYIRHVEE YDLQFIFQLC TITLSTDVMS YIHTMNPAIL DDWNFGVAPP PSASLVDTYR
     YLQSAAITCQ KDAPAPTKKD PYDGLNFWNV NLKEKFSSEL DQFPLGRKFL LQAGVRRRPT
     IGPRKRPATA TTASTSKHKR KRVSK