ID   VL1_HPV38               Reviewed;         510 AA.
AC   P50814; Q80913;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   23-FEB-2022, entry version 86.
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 38.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=37959;
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 373-468.
RX   PubMed=7707535; DOI=10.1128/jvi.69.5.3074-3083.1995;
RA   Chan S.-Y., Delius H., Halpern A.L., Bernard H.U.;
RT   "Analysis of genomic sequences of 95 papillomavirus types: uniting typing,
RT   phylogeny, and taxonomy.";
RL   J. Virol. 69:3074-3083(1995).
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; U31787; AAA79456.1; -; Genomic_DNA.
DR   EMBL; U21875; AAA92836.1; -; Genomic_DNA.
DR   SMR; P50814; -.
DR   Proteomes; UP000009166; 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_0000133522"
FT   REGION          128..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-438)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        438
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   CONFLICT        419
FT                   /note="T -> A (in Ref. 2; AAA92836)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  57692 MW;  0FB61C7A2082E949 CRC64;
     MTLWLPASGK IYLPPTPPVA RVQSTDEYVE RTDIYYHATS DRLLTVGHPY FDVRSQDGQK
     IEVPKVSGNQ YRSFRVTFPD PNKFALADMS VYDPDKYRLV WACKGLEIGR GQPLGVGTTG
     HPLFNKVRDT ENSSNYQNTS TDDRQNTSFD PKQVQMFIIG CTPCLGEYWD KAPVCDNAGD
     QTGLCPPLEL KNSVIEDGDM FDIGFGNINN KTLSFNRSDV SLDIVNETCK YPDFLTMSND
     VYGDSCFFFV RREQCYARHY FVRGGAVGDA IPDGTVNQNH NYYLPAKNGQ GQRTLGNSTY
     FPTVSGSLVT SDAQLFNRPF WLQRAQGHNN GILWGNQMFV TVADNTRNTN FTISVSTENG
     GAQEYDSANI REYLRHVEEY QLSFILQLCK VPLNAEVLTQ INAMNSGILE NWQLGFVPTP
     DNSVHDTYRY ITSKATKCPD AVPETEKEDP FGQYTFWNVD MTEKLSLDLD QYPLGRKFLF
     QAGLQTARTR AVKRPLVRKS SKSVKRKRTQ