ID   VL1_HPV82               Reviewed;         503 AA.
AC   Q9IR52;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-JUN-2021, entry version 85.
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 82.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=129724;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10618284; DOI=10.1128/cdli.7.1.91-95.2000;
RA   Kino N., Sata T., Sato Y., Sugase M., Matsukura T.;
RT   "Molecular cloning and nucleotide sequence analysis of a novel human
RT   papillomavirus (type 82) associated with vaginal intraepithelial
RT   neoplasia.";
RL   Clin. Diagn. Lab. Immunol. 7:91-95(2000).
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; AB027021; BAA90742.1; -; Genomic_DNA.
DR   SMR; Q9IR52; -.
DR   Proteomes; UP000145193; 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..503
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133553"
FT   REGION          476..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-429)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        429
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   503 AA;  56210 MW;  526E427B3A2C6CC3 CRC64;
     MALWRTNDSK VYLPPAPVSR IVNTEEYITR TGIYYYAGSS RLITLGHPYF SIPKTNTRAE
     IPKVSAFQYR VFRVQLPDPN KFGLPDPNLF NPDTDRLVWG CVGVEVGRGQ PLGVGLSGHP
     LFNKYDDTEN SRFANGNDQQ DVRDNISVDN KQTQLCIIGC APPIGEHWAT GTTCKNVPVP
     QGDCPPLELV STVIEDGDMV DTGFGAMDFA NLQATKSDVP LDIAQSVCKY PDYLKMSADT
     YGNSMFFHLR REQIFARHYY NKAGVVGDAI PDKAYIKGTG AGRDPISSYI YSATPSGSMI
     TSDSQIFNKP YWLHRAQGHN NGICWNNQLF ITCVDTTKST NLTISTAVTP SVAQTFTPAN
     FKQYIRHGEE YELQFIFQLC KITLTTEIMA YLHTMDSTIL EQWNFGLTLP PSASLEDAYR
     FVKNAATSCH KDSPPQAKED PLAKYKFWNV DLKERFSLDL DQFALGRKFL LQIGAQRKPR
     PGLKRPAPSS SASSSAKRKR VKK