ID   VL1_HPV13               Reviewed;         499 AA.
AC   Q02273; Q90075;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 94.
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 13.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10573;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1325697; DOI=10.1016/0042-6822(92)90896-w;
RA   van Ranst M., Fuse A., Fiten P., Beuken E., Pfister H., Burk R.D.,
RA   Opdenakker G.;
RT   "Human papillomavirus type 13 and pygmy chimpanzee papillomavirus type 1:
RT   comparison of the genome organizations.";
RL   Virology 190:587-596(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 331-364.
RX   PubMed=1321168; DOI=10.1128/jcm.30.7.1716-1721.1992;
RA   van den Brule A.J., Snijders P.J., Raaphorst P.M., Schrijnemakers H.F.,
RA   Delius H., Gissmann L., Meijer C.J., Walboomers J.M.;
RT   "General primer polymerase chain reaction in combination with sequence
RT   analysis for identification of potentially novel human papillomavirus
RT   genotypes in cervical lesions.";
RL   J. Clin. Microbiol. 30:1716-1721(1992).
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; X62843; CAA44654.1; -; Genomic_DNA.
DR   EMBL; S40235; AAB22562.1; -; Genomic_DNA.
DR   PIR; H42955; P1WL13.
DR   SMR; Q02273; -.
DR   Proteomes; UP000009107; 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..499
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133497"
FT   REGION          472..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        172
FT                   /note="Interchain (with C-423)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        423
FT                   /note="Interchain (with C-172)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   499 AA;  55773 MW;  AA6D5F7FFFD24759 CRC64;
     MWRPSDNKLY VPPPAPVSKV ITTDAYVTRT NIFYHASSSR LLAVGNPYFP IKKQNKTVVP
     KVSGYQFRVF KVVLPDPNKF ALPDTSIFDS TSQRLVWACT GLEVGRGQPL GVGISGHPLL
     NKYDDVENSA SYAANPGQDN RVNVAMDYKQ TQLCLVGCAP PLGEHWGQGK QCTGVNVQPG
     DCPPLELISS VIQDGDMVDT GFGAMNFAEL QSNKSDVPLD ICTSTCKYPD YLQMAADPYG
     DRLFFYLRKE QMFARHFFNR AGSVGEQIPA ELYVKGSNTL SNSIYYNTPS GSLVSSEAQL
     FNKPYWLQKA QGHNNGICWG NHLFVTVVDT TRSTNMTVCA ATTSSLSDTY KATEYKQYMR
     HVEEFDLQFI FQLCTIKLTA EVMSYIHTMN PTILEDWNFG LSPPPNGTLE DTYRYVQSQA
     ITCQKPTPDK EKQDPYAGLS FWEVNLKEKF SSELDQYPLG RKFLLQTGVQ SRSPIRVGRK
     RAASTSTATP TTRKKAKRK