ID   VL1_HPV67               Reviewed;         529 AA.
AC   P50825; O90730;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Human papillomavirus 67.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=37120;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9857984; DOI=10.1023/a:1008002905588;
RA   Kirii Y., Matsukura T.;
RT   "Nucleotide sequence and phylogenetic classification of human
RT   papillomavirus type 67.";
RL   Virus Genes 17:117-121(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-495.
RX   PubMed=7963696; DOI=10.1093/infdis/170.5.1077;
RA   Bernard H.U., Chan S.-Y., Manos M.M., Ong C.K., Villa L.L., Delius H.,
RA   Peyton C.L., Bauer H.M., Wheeler C.M.;
RT   "Identification and assessment of known and novel human papillomaviruses by
RT   polymerase chain reaction amplification, restriction fragment length
RT   polymorphisms, nucleotide sequence, and phylogenetic algorithms.";
RL   J. Infect. Dis. 170:1077-1085(1994).
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; D21208; BAA28859.1; -; Genomic_DNA.
DR   EMBL; U12492; AAA67236.1; -; Genomic_DNA.
DR   SMR; P50825; -.
DR   Proteomes; UP000171341; 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..529
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133549"
FT   REGION          506..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        205
FT                   /note="Interchain (with C-457)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        457
FT                   /note="Interchain (with C-205)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   CONFLICT        375
FT                   /note="C -> Y (in Ref. 2; AAA67236)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="E -> G (in Ref. 2; AAA67236)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        491
FT                   /note="F -> Y (in Ref. 2; AAA67236)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   529 AA;  59426 MW;  9750C245F1BC6C07 CRC64;
     MYLFMVVILF YTLVIFYVAG VNGFHIFLQM SVWRPSEATV YLPPVPVSKV VSTDEYVSRT
     SIYYYAGSSR LLAVGHPYFS IPNPSNTKKV LVPKVSGLQY RVFRVRLPDP NKFGFPDTSF
     YNPDTQRLVW ACVGIEIGRG QPLGVGISGH PLLNKFDDTE TNNKYPSQPG TDNRECLSMD
     AKQTQLCIIG CKPPTGEHWG KGTPCSGNSN GPGACPPLEL MNTVIEDGDM IDTGFGCMDF
     KSLQANKSDV PLDICTSICK YPDYLGMASE AYGDSLFFFL RREQMFVRHL FNRAGKLGED
     VPTDLYFKGS ANTSALQTSA FFPTPSGSMV SSESQLFNKP YWLQRAQGHN NGICWGNQIF
     VTVVDTTRST NMTLCSEEKS EATYKNENFK EYLRHVEEYD LQFIFQLCKI SLTANVMQYI
     HTMNPDILED WQFGLTPPPS GNLQDTYRFV TSQAITCQKT SPPTAKEDPL KKYSFWEINL
     KEKFSADLDQ FPLGRKFLLQ AGFTAKPKLK RSSPSSSSSS SAKRKKVKR