VL1_HPV14
ID VL1_HPV14 Reviewed; 518 AA.
AC P36734;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 87.
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 14.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10605;
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; X74467; CAA52505.1; -; Genomic_DNA.
DR PIR; S36472; S36472.
DR SMR; P36734; -.
DR Proteomes; UP000009108; 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..518
FT /note="Major capsid protein L1"
FT /id="PRO_0000133498"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 177
FT /note="Interchain (with C-446)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 446
FT /note="Interchain (with C-177)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 518 AA; 58905 MW; 86CE1695CEA833DA CRC64;
MAVWQAASGK VYLPPSTPVA RVQSTDEYVQ RTNIYYHAYS DRLLTVGHPY FNIYDVQSAK
IKVPKVSGNQ HRVFRLKLPD PNRFALADMS VYNPDKERLV WACRGIEIGR GQPLGVGSVG
HPLFNKVGDT ENPNSYRQQA NSTDDRQNVS FDPKQLQMFI IGCAPCMGEH WDRALPCVED
KPPPGSCPPI ELKNTVIEDG DMADIGYGNL NFKALQENRS DVSLDIVNEI CKYPDFLKMQ
NDVYGDSCFF YARREQCYAR HFFVRGGKTG DDIPAAQVDE GSLKNVYYIP PMTNQPQNNI
GNAMYFPTVS GSLVSSDAQL FNRPFWLQRA QGHNNGICWF NQLFVTVVDN TRNTNFSISV
SSENTEVSKI DNYTSQKFQE YLRHVEEYEM SLILQLCKIP LTAEVLAQIN AMNSNILEEW
QLGFVPAPDN PIHDTYRYIE SAATRCPDKN PPKEREDPYK NFNFWNVDLT ERLSLDLDQY
SLGRKFLFQA GLQQSTVNGT KTVSTRGSIK GIKRKRKN