ID   VL1_HPV2A               Reviewed;         510 AA.
AC   P25486;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 93.
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 2a.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10584;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1964523; DOI=10.1016/0168-1702(90)90091-o;
RA   Hirsch-Behnam A., Delius H., de Villiers E.M.;
RT   "A comparative sequence analysis of two human papillomavirus (HPV) types 2a
RT   and 57.";
RL   Virus Res. 18:81-98(1990).
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; X55964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S15620; S15620.
DR   SMR; P25486; -.
DR   Proteomes; UP000007710; 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..510
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133484"
FT   REGION          489..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        188
FT                   /note="Interchain (with C-438)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        438
FT                   /note="Interchain (with C-188)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   510 AA;  57194 MW;  83509AFB9DAF70D9 CRC64;
     MSCGLNDVNV STISLQMALW RPNESKVYLP PTPVSKVIST DVYVTRTNVY YHGGSSRLLT
     VGHPYYSIKK SNNKVAVPKV SGYQYRVFHV KLPDPNKFGL PDADLYDPDT QRLLWACVGV
     EVGRGQPLGV GVSGHPYYNR LDDTENAHTP DTADDGRENI SMDYKQTQLF ILGCKPPIGE
     HWSKGTTCNG SSAAGDCPPL QFTNTTIEDG DMVETGFGAL DFATLQSNKS DVPLDICTNT
     CKYPDYLKMA AEPYGDSMFF SLRREQMFTR HFFNLGGKMG DTIPDELYIK STSVPTPGSH
     VYTSTPSGSM VSSEQQLFNK PYWLRRAQGH NNGMCWGNRV FLTVVDTTRS TNVSLCATEA
     SDTNYKATNF KEYLRHMEEY DLQFIFQLCK ITLTPEIMAY IHNMDPQLLE DWNFGVPPPP
     SASLQDTYRY LQSQAITCQK PTPPKTPTDP YASLTFWDVD LSESFSMDLD QFPLGRKFLL
     QRGAMPTVSR KRAAVSGTTP PTSKRKRVRR