ID   VL1_BPV4                Reviewed;         506 AA.
AC   P08341;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 96.
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 4 (Bovine papillomavirus 4).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Xipapillomavirus.
OX   NCBI_TaxID=10562;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3039043; DOI=10.1099/0022-1317-68-8-2117;
RA   Patel K.R., Smith K.T., Campo M.S.;
RT   "The nucleotide sequence and genome organization of bovine papillomavirus
RT   type 4.";
RL   J. Gen. Virol. 68:2117-2128(1987).
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; X05817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B26214; P1WLB4.
DR   SMR; P08341; -.
DR   Proteomes; UP000007613; 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..506
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133478"
FT   REGION          484..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        173
FT                   /note="Interchain (with C-431)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        431
FT                   /note="Interchain (with C-173)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   506 AA;  57903 MW;  F1C5DFDB54FA681E CRC64;
     MSFWVPNSAK LYLPPPTPVT QFLDTDEFVT RTDIFYHTST DRLLFVGHPY FRPKKRRHRC
     CSQMSGSQFR VFRLKFPDPN KFSFPTQDIY NPEKQRLVWA VRGIEICRGQ PLGVGVTGHP
     SFNKFKDAEN LNQNSDQKED DRVNVCMDPK QVQLFIVGCV PCDGEHWDKA QACEPQGPGD
     CPPIELKNTK IQDGEMCDTG FGNMNFAALQ ASKSGAPLDI VDQIVKYPDF LKMGNDPYGN
     SMFFYAKREQ MYVRHLWARA GRVGDDIPTG ESGSPYFLPA TGRGPLPSSV YIGSPSGSLV
     SSDQQIYNRP FWIQRAQGSN NGMCWNNELF VTAVDSTRGT NFSISVHTTD PEVKPQETYT
     ATKFKHYLRH VEEWDLSLIM QLCIVNLTPE SIAYLHNMNE SIIENWNLGF IQPPNDIEDH
     YRFITSLATR CPKKTDTQVK EDPYKDLKFW DVDLTEKFTT NLNQHSLVRK FLFQIGRKAT
     KRSAPKTVTF ENTEGKKAPK RRRKNV