ID   VL1_HPV10               Reviewed;         531 AA.
AC   P36732;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 95.
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 10.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=333759;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-29 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; X74465; CAA52494.1; -; Genomic_DNA.
DR   PIR; S36537; S36537.
DR   RefSeq; NP_041746.1; NC_001576.1.
DR   SMR; P36732; -.
DR   GeneID; 1489377; -.
DR   KEGG; vg:1489377; -.
DR   Proteomes; UP000009105; 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..531
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133494"
FT   REGION          511..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        203
FT                   /note="Interchain (with C-456)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        456
FT                   /note="Interchain (with C-203)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   531 AA;  59011 MW;  EDC9BA0DCA7A67F6 CRC64;
     MAGISIFGLL PFTSPDIVAV NVSHIFLQMA LWRSSDNLVY LPPTPVSKVL STDDYVTRTN
     IYYYAGTSRL LTVGHPYFPI PKSSNNKVDV PKVSAFQYRV FRVRLPDPNK FGLPDARIYN
     PDAERLVWAC TGVEVGRGQP LGVGLSGHPL YNKLEDTENS NIAHGPIGQD SRDNISVDNK
     QTQLCIIGCT PPMGEHWGKG TPCRNPPAQG DCPPLELITS PIQDGDMVDT GYGAMDFTAL
     QLNKSDVPID ICQSTCKYPD YLGMAAEPYG DSMFFYLRRE QLFARHFFNR ASAVGDAIPD
     TFILKSNGGG RDVGSAVYSP TPSGSMVTSE AQLFNKPYWL RRAQGHNNGI CWANQLFVTV
     VDTTRSTNMC LCVPSEASPA TTYDATKFKE YLRHGEEYDL QFIFQLCKVT LTPDIMAYLH
     TMNSSLLEDW NFGLTLPPST SLEDTYRFLS SSAITCQKDT PPTEKQDPYA KLNFWDVDLK
     DRFSLDLSQF PLGRKFLLQL GVRSRSAVSV RKRPATSATG STAAKRKRTK K