ID   VL1_HPV61               Reviewed;         505 AA.
AC   P50822; Q80954;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   02-JUN-2021, entry version 93.
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 61.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=37116;
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 317-468.
RX   PubMed=7963696; DOI=10.1093/infdis/170.5.1077;
RA   Bernard H.U., Chan S.-Y., Manos M.M., Ong C.K., Villa L.L., Delius H.,
RA   Peyton C.L., Bauer H.M., Wheeler C.M.;
RT   "Identification and assessment of known and novel human papillomaviruses by
RT   polymerase chain reaction amplification, restriction fragment length
RT   polymorphisms, nucleotide sequence, and phylogenetic algorithms.";
RL   J. Infect. Dis. 170:1077-1085(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U31793; AAA79498.1; -; Genomic_DNA.
DR   EMBL; U12500; AAA67244.1; -; Genomic_DNA.
DR   RefSeq; NP_043450.1; NC_001694.1.
DR   SMR; P50822; -.
DR   PRIDE; P50822; -.
DR   GeneID; 1403318; -.
DR   KEGG; vg:1403318; -.
DR   Proteomes; UP000007670; 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..505
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133543"
FT   REGION          476..505
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"
FT   CONFLICT        374
FT                   /note="Q -> P (in Ref. 2; AAA67244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="Q -> L (in Ref. 2; AAA67244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   505 AA;  56710 MW;  EB56C4A60E94C853 CRC64;
     MALWRPGDGK VYLPPTPVSK VISTDRYVQR TNLFYYGGSS RLLTVGHPYC SLQLDGLQGK
     KNTIPKVSGY QYRVFRVQLP DPNKFALPDG TLYNPDTERM VWACRGIEVG RGQPLGVGTS
     GHPLYNRLDD TENTTLLVAE SSDSRDNVSV DYKQTQLLIV GCKPPIGEHW TKGTACANPA
     PRPTDCPPLE FTNTTIQDGD MVETGYGAID FAALQENKSE VPLDICTTIC KYPDYLQMAA
     EPYGDCMFFC LRREQMFARH FFNRQGVMGE ALPDSYYLKG ANDKAAPGSY IYSPTPSGSM
     VSSDSQLFNK PYWLQRAQGH NNGICWFNEL FVTVVDTTRS TNLTICTATS PPVSEYKATS
     FREYLRHTEE FDLQFIFQLC KIHLTPEIMA YLHNMNKALL DDWNFGVVPP PSTSLEDTYR
     FLQSRAITCQ KGAAAPPPKE DRYAKLSFWT VDLRDKFSTD LDQFPLGRKF LLQAGPRSVS
     VSRKRAAPSS TPTSSPATKR KKRKQ