ID   VL1_HPV49               Reviewed;         509 AA.
AC   P36742;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-DEC-2020, entry version 89.
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 49.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10616;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(1994).
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; X74480; CAA52584.1; -; Genomic_DNA.
DR   PIR; S36572; S36572.
DR   RefSeq; NP_041837.1; NC_001591.1.
DR   SMR; P36742; -.
DR   PRIDE; P36742; -.
DR   GeneID; 1489446; -.
DR   KEGG; vg:1489446; -.
DR   Proteomes; UP000009124; 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..509
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133532"
FT   DISULFID        177
FT                   /note="Interchain (with C-439)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        439
FT                   /note="Interchain (with C-177)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   509 AA;  57475 MW;  CBBD384899431689 CRC64;
     MTSLWLPATG KVYLPPSTPV ARVQSTDEYI QRTDIYYHAN SDRLLTVGHP YFDVRDTADN
     SKILVPKVSG NQYRAFRLLL PDPNRFALVD MNIYNPEKER LVWACRGLEI GRGQPLGVGT
     TGHPLFNKVK DTENANNYIV TSKDDRQDTS FDPKQVQMFI IGCTPCMGEY WDAAKPCDAD
     AGQGKCPPLE LINSVIQDGD MIDIGFGNIN NKTLSVNRSD VSLDIVNDIC KYPDFLKMAN
     DIYGDACFFY ARREQCYARH FFVRGGNVGD AIPNTAVGQD NNYILPAASQ QAQNTLGSSI
     YFPTVSGSLV STDAQLFNRP FWLQRAQGHN NGICWENQLF ITVADNTRNT NFTISVSTDG
     QTPTEYDSTK VREFLRHVEE YEISIILQLC KVPLEPEVLA QINAMNSSIL ENWQLGFVPT
     PDNPIHDTYR YLTSQATRCP DKQPAPERKD PYEQYNFWTV DLTEKLSLDL DQYSLGRKFL
     FQAGLQRASR VSKSSAARAS TRGIKRKRR