ID   VL1_BPV1                Reviewed;         495 AA.
AC   P03103;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 99.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Bovine papillomavirus type 1.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=337052;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6289124; DOI=10.1038/299529a0;
RA   Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.;
RT   "The primary structure and genetic organization of the bovine
RT   papillomavirus type 1 genome.";
RL   Nature 299:529-534(1982).
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; X02346; CAB46515.1; -; Genomic_DNA.
DR   PIR; A03644; P1WLB.
DR   RefSeq; NP_056744.1; NC_001522.1.
DR   PDB; 3IYJ; EM; 4.20 A; A/B/C/D/E/F=1-495.
DR   PDBsum; 3IYJ; -.
DR   SMR; P03103; -.
DR   DIP; DIP-59517N; -.
DR   GeneID; 1489016; -.
DR   KEGG; vg:1489016; -.
DR   EvolutionaryTrace; P03103; -.
DR   Proteomes; UP000006567; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Disulfide bond; Host nucleus;
KW   Host-virus interaction; Late protein; Reference proteome;
KW   T=7 icosahedral capsid protein; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   CHAIN           1..495
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133475"
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"
SQ   SEQUENCE   495 AA;  55551 MW;  EA4B379D1CDD1C51 CRC64;
     MALWQQGQKL YLPPTPVSKV LCSETYVQRK SIFYHAETER LLTIGHPYYP VSIGAKTVPK
     VSANQYRVFK IQLPDPNQFA LPDRTVHNPS KERLVWAVIG VQVSRGQPLG GTVTGHPTFN
     ALLDAENVNR KVTTQTTDDR KQTGLDAKQQ QILLLGCTPA EGEYWTTARP CVTDRLENGA
     CPPLELKNKH IEDGDMMEIG FGAANFKEIN ASKSDLPLDI QNEICLYPDY LKMAEDAAGN
     SMFFFARKEQ VYVRHIWTRG GSEKEAPTTD FYLKNNKGDA TLKIPSVHFG SPSGSLVSTD
     NQIFNRPYWL FRAQGMNNGI AWNNLLFLTV GDNTRGTNLT ISVASDGTPL TEYDSSKFNV
     YHRHMEEYKL AFILELCSVE ITAQTVSHLQ GLMPSVLENW EIGVQPPTSS ILEDTYRYIE
     SPATKCASNV IPAKEDPYAG FKFWNIDLKE KLSLDLDQFP LGRRFLAQQG AGCSTVRKRR
     ISQKTSSKPA KKKKK