ID   VL1_HPV55               Reviewed;         501 AA.
AC   P50820; Q80940;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 83.
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 type 55.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=37114;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Delius H.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 312-462.
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; U31791; AAA79484.1; -; Genomic_DNA.
DR   EMBL; U12494; AAA67238.1; -; Genomic_DNA.
DR   SMR; P50820; -.
DR   PRIDE; P50820; -.
DR   Proteomes; UP000152738; 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..501
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133538"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        172
FT                   /note="Interchain (with C-425)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        425
FT                   /note="Interchain (with C-172)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   501 AA;  55787 MW;  0DBC4D47E552E968 CRC64;
     MWRPSENQVY VPPPAPVSKV ITTDAYVKRT NIVYHASSSR LLAVGNPYFA IRPANKTLVP
     KVSGFQYRVF KVVLPDPNKF ALPDTSIYDP TTQRLVWACI GLEVGRGQPL GVGISGHPLL
     NKLDDVENSA SYAASPGQDN RVNVAMDYKQ TQLCLVGCAP PLGEHWGKGK PCNNGSVNSG
     DCPPLELITS VIEDGDMVDT GFGAMNFAEL QPNKSDVPLD ICTATCKYPD YLQMAADPYG
     DRLFFYLRKE QMFARHFFNR AGTVGEDIPQ DLVFKGATKS TVPNAIYFNT PSGSLVSSET
     QLFNKPFWLQ RAQGHNNGIC WGNQLFVTVV DTTRSTNMTI CAATTQSPST TYNSTEYKQY
     MRHVEEFDLQ FMFQLCSITL TAEVMAYLHT MNPGILEQWN FGLSPPPNGT LEDKYRYVQS
     QAITCQKPPP EKAKQDPYAK LSFWEVDLRE KFSSELDQYP LGRKFLLQTG VQARSSVRVG
     RKRPASAATS SSSKPKRSRK K