VL1_BPV5
ID VL1_BPV5 Reviewed; 494 AA.
AC P50806; Q705G5; Q8BDG2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 23-FEB-2022, entry version 87.
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 5.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Epsilonpapillomavirus.
OX NCBI_TaxID=40537;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H., de Villiers E.M.;
RT "Sequencing of the complete genomes of BPV 3, BPV 5 and BPV 6.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12208979; DOI=10.1128/jvi.76.19.10020-10023.2002;
RA Terai M., DeSalle R., Burk R.D.;
RT "Lack of canonical E6 and E7 open reading frames in bird papillomaviruses:
RT Fringilla coelebs papillomavirus and Psittacus erithacus timneh
RT papillomavirus.";
RL J. Virol. 76:10020-10023(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-453.
RX PubMed=7707535; DOI=10.1128/jvi.69.5.3074-3083.1995;
RA Chan S.-Y., Delius H., Halpern A.L., Bernard H.U.;
RT "Analysis of genomic sequences of 95 papillomavirus types: uniting typing,
RT phylogeny, and taxonomy.";
RL J. Virol. 69:3074-3083(1995).
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; AJ620206; CAF05676.1; -; Genomic_DNA.
DR EMBL; AF457465; AAN09929.1; -; Genomic_DNA.
DR EMBL; U21863; AAA92826.1; -; Genomic_DNA.
DR RefSeq; NP_694435.1; NC_004195.1.
DR SMR; P50806; -.
DR GeneID; 955406; -.
DR KEGG; vg:955406; -.
DR Proteomes; UP000008785; Genome.
DR Proteomes; UP000185273; 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; Reference proteome; 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..494
FT /note="Major capsid protein L1"
FT /id="PRO_0000133479"
FT REGION 475..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 170
FT /note="Interchain (with C-424)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 424
FT /note="Interchain (with C-170)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT CONFLICT 156..157
FT /note="QS -> CT (in Ref. 2; AAN09929)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="S -> Y (in Ref. 3; AAA92826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55973 MW; CB6F78A089075D5B CRC64;
MAVWQQQGQR LYFPPNPVTK VLCTESYVKR TSIFYHGETE RLLTVGHPYW KIPEQNIPKV
SGNQYRVFRV QLPDPNQFAL PDKNLHNPAK ERLVWAILGL QVSRGQPLGA PVTGNQLFNV
WTDAENVTAK RALPGSDDRK QLGMDVKQTQ MLLIGQSPAI GEYWGKAIPC EGKQPKAGDC
PPIELKNKPI EDGDMMDIGF GACDWKDFSQ NLSDVPLDLI NSKSLYPDYL KMAEDSLGNS
CFFYARREQV YVRHVYSRGG EQKEAIPKDM TLPQQVPDNK DTSFTFMGTP SGSLVSTDGQ
LFNRPYWLYQ AQGLNNGVCW DNELFITVGD NSRGGVFTIS VPVDDRKPEQ YNSANMNIYC
RHVEEYKLAV ILELCSVELT SETVAYLQTV NPSVLEKWEV GVNPPPATVL EDTYRYQESK
AIKCIDQTAA AKKDKYENLS FWNIDLREKL SADLDQYPLG RRFLAQNGIT CSRKRLRPAS
TKKSTTNKKR KTSR
