ID   VL1_BPV2                Reviewed;         497 AA.
AC   P06458;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   23-FEB-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   Bos taurus papillomavirus 2 (Bovine papillomavirus 2).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=2758382;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2981958; DOI=10.1099/0022-1317-66-1-187;
RA   Potter H.L., Meinke W.J.;
RT   "Nucleotide sequence of bovine papillomavirus type 2 late region.";
RL   J. Gen. Virol. 66:187-193(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Groff D.E., Mitra R., Lancaster W.D.;
RL   Submitted (MAY-1988) to the EMBL/GenBank/DDBJ databases.
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; X01768; CAA25908.1; -; Genomic_DNA.
DR   EMBL; M20219; AAA66840.1; -; Genomic_DNA.
DR   PIR; A31169; P1WLB2.
DR   SMR; P06458; -.
DR   Proteomes; UP000007612; 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; -; 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; 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..497
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133476"
FT   DISULFID        171
FT                   /note="Interchain (with C-426)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        426
FT                   /note="Interchain (with C-171)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   CONFLICT        176
FT                   /note="L -> I (in Ref. 1; CAA25908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="N -> D (in Ref. 1; CAA25908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="L -> V (in Ref. 1; CAA25908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="K -> R (in Ref. 1; CAA25908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   497 AA;  55595 MW;  674728E3A884A068 CRC64;
     MALWQQGQKL YLPPTPVSKV LCSETYVQRK SIFYHAETER LLTVGHPYYQ VTVGDKTVPK
     VSANQFRVFK IQLPDPNQFA LPDRTVHNPS KERLVWAVIG VQVSRGQPLG GTVTGHPTFN
     ALLDAENVNR KVTAQTTDDR KQTGLDAKQQ QILLLGCTPA EGEYWTTARP CVTDRLENGA
     CPPLELKNKH IEDGDMMEIG FGAADFKTLN ASKSDLPLDI QNEICLYPDY LKMAEDAAGN
     SMFFFARKEQ VYVRHIWTRG GSEKEAPSKD FYLKNGRGEE TLKIPSVHFG SPSGSLVSTD
     NQIFNRPYWL FRAQGMNNGI AWNNLLFLTV GDNTRGTNLS ISVAADGNAL SEYDTGKFNL
     YHRHMEEYKL AFILELCSVE ITAQTLSHLQ GLMPSVLQNW EIGVQPPASS ILEDTYRYIE
     SPATKCASNV IPPKEDPYAG LKFWSIDLKE KLSLDLDQFP LGRRFLAQQG AGCSTVRKRA
     VATRNSSKPA KRKKIKA