ID   VL1_PCPV1               Reviewed;         502 AA.
AC   Q02274;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, 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   Pygmy chimpanzee papillomavirus type 1 (PCPV-1).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10576;
OH   NCBI_TaxID=9597; Pan paniscus (Pygmy chimpanzee) (Bonobo).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1325697; DOI=10.1016/0042-6822(92)90896-w;
RA   van Ranst M., Fuse A., Fiten P., Beuken E., Pfister H., Burk R.D.,
RA   Opdenakker G.;
RT   "Human papillomavirus type 13 and pygmy chimpanzee papillomavirus type 1:
RT   comparison of the genome organizations.";
RL   Virology 190:587-596(1992).
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; X62844; CAA44662.1; -; Genomic_DNA.
DR   SMR; Q02274; -.
DR   Proteomes; UP000000469; 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; 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..502
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133554"
FT   REGION          478..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        172
FT                   /note="Interchain (with C-426)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        426
FT                   /note="Interchain (with C-172)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   502 AA;  55718 MW;  A22D1980EEA94BA3 CRC64;
     MWRPSDNKLY VPPPAPVSKV ITTDAYVTRT KIFYHASSSR LLAVGNPYFP IRKGNKTIVP
     KVSGFQFRVF KIVLPDPNKF ALPDTSIFDS TSQRLVWACI GLEVGRGQPL GVGISGHPLL
     NKFDDVENSA SYAVNPGQDN RVNVAMDYKQ TQLCLVGCAP PLGEHWGKGT QCSGVSVQDG
     DCPPLELVTS VIQDGDMVDT GFGAMDFAQL QSNKSDVPLD ICTATCKYPD YLQMAADPYG
     DRLFFSLRKE QMFARHFFNR AGTVGEQIPE DLLVKGTTSR ATVSSTIYFN TPSGSLVSSE
     AQLFNKPYWL HKAQGHNNGI CWGNTLFVTV VDTTRSTNMT VCASTTSSPS ATYTASEYKQ
     YMRHVEEFDL QFIFQLCSIK LTAEVMAYIH TMNPTVLEEW NFGLSPPPNG TLEDTYRYVQ
     SQAITCQKPT PDKEKQDPYA GLSFWEVNLK EKFSSELDQY PLGRKFLLQT GVQTTSFARA
     GTKRAASTSS STPTTRKRVK RK