ID   VL1_HPV31               Reviewed;         504 AA.
AC   P17388;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-JUN-2021, entry version 91.
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 31.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10585;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2545036; DOI=10.1016/0042-6822(89)90545-x;
RA   Goldsborough M.D., Disilvestre D., Temple G.F., Lorincz A.T.;
RT   "Nucleotide sequence of human papillomavirus type 31: a cervical neoplasia-
RT   associated virus.";
RL   Virology 171:306-311(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=12610160; DOI=10.1128/jvi.77.6.3846-3850.2003;
RA   Bousarghin L., Touze A., Sizaret P.Y., Coursaget P.;
RT   "Human papillomavirus types 16, 31, and 58 use different endocytosis
RT   pathways to enter cells.";
RL   J. Virol. 77:3846-3850(2003).
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       ECO:0000269|PubMed:12610160}.
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; J04353; AAA46956.1; -; Genomic_DNA.
DR   PIR; G32444; P1WL31.
DR   SMR; P17388; -.
DR   Proteomes; UP000009116; 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..504
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133515"
FT   REGION          480..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        176
FT                   /note="Interchain (with C-429)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        429
FT                   /note="Interchain (with C-176)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   504 AA;  56352 MW;  B45A306A6B3AB9D2 CRC64;
     MSLWRPSEAT VYLPPVPVSK VVSTDEYVTR TNIYYHAGSA RLLTVGHPYY SIPKSDNPKK
     IVVPKVSGLQ YRVFRVRLPD PNKFGFPDTS FYNPETQRLV WACVGLEVGR GQPLGVGISG
     HPLLNKFDDT ENSNRYAGGP GTDNRECISM DYKQTQLCLL GCKPPIGEHW GKGSPCSNNA
     ITPGDCPPLE LKNSVIQDGD MVDTGFGAMD FTALQDTKSN VPLDICNSIC KYPDYLKMVA
     EPYGDTLFFY LRREQMFVRH FFNRSGTVGE SVPTDLYIKG SGSTATLANS TYFPTPSGSM
     VTSDAQIFNK PYWMQRAQGH NNGICWGNQL FVTVVDTTRS TNMSVCAAIA NSDTTFKSSN
     FKEYLRHGEE FDLQFIFQLC KITLSADIMT YIHSMNPAIL EDWNFGLTTP PSGSLEDTYR
     FVTSQAITCQ KTAPQKPKED PFKDYVFWEV NLKEKFSADL DQFPLGRKFL LQAGYRARPK
     FKAGKRSAPS ASTTTPAKRK KTKK