ID   VL1_HPV51               Reviewed;         504 AA.
AC   P26536; Q90081;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 51.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10595;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1649326; DOI=10.1128/jvi.65.8.4216-4225.1991;
RA   Lungu O., Crum C.P., Silverstein S.J.;
RT   "Biologic properties and nucleotide sequence analysis of human
RT   papillomavirus type 51.";
RL   J. Virol. 65:4216-4225(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-369.
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; M62877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S40272; AAB22568.1; -; Genomic_DNA.
DR   PIR; G40415; P1WL51.
DR   SMR; P26536; -.
DR   Proteomes; UP000009125; 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..504
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133534"
FT   REGION          476..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-428)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        428
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   504 AA;  56315 MW;  4D5940CB31ED9646 CRC64;
     MALWRTNDSK VYLPPAPVSR IVNTEEYITR TGIYYYAGSS RLITLGHPYF PIPKTSTRAA
     IPKVSAFQYR VFRVQLPDPN KFGLPDPNLY NPDTDRLVWG CVGVEVGRGQ PLGVGLSGHP
     LFNKYDDTEN SRIANGNAQQ DVRDNTSVDN KQTQLCIIGC APPIGEHWGI GTTCKNTPVP
     PGDCPPLELV SSVIQDGDMI DTGFGAMDFA ALQATKSDVP LDISQSVCKY PDYLKMSADT
     YGNSMFFHLR REQIFARHYY NKLVGVGEDI PNDYYIKGSG NGRDPIESYI YSATPSGSMI
     TSDSQIFNKP YWLHRAQGHN NGICWNNQLF ITCVDTTRST NLTISTATAA VSPTFTPSNF
     KQYIRHGEEY ELQFIFQLCK ITLTTEVMAY LHTMDPTILE QWNFGLTLPP SASLEDAYRF
     VRNAATSCQK DTPPQAKPDP LAKYKFWDVD LKERFSLDLD QFALGRKFLL QVGVQRKPRP
     GLKRPASSAS SSSSSSAKRK RVKK