VL1_HPV54
ID VL1_HPV54 Reviewed; 497 AA.
AC P50819; Q81024;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 23-FEB-2022, entry version 96.
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 54.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=1671798;
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 310-460.
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; U37488; AAA79193.1; -; Genomic_DNA.
DR EMBL; U12501; AAA67245.1; -; Genomic_DNA.
DR RefSeq; NP_043294.1; NC_001676.1.
DR SMR; P50819; -.
DR PRIDE; P50819; -.
DR GeneID; 1497438; -.
DR KEGG; vg:1497438; -.
DR Proteomes; UP000007665; 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; -; 1.
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..497
FT /note="Major capsid protein L1"
FT /id="PRO_0000133537"
FT REGION 473..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 171
FT /note="Interchain (with C-421)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 421
FT /note="Interchain (with C-171)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT CONFLICT 313
FT /note="Q -> H (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> L (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="I -> T (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="T -> A (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="N -> T (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="F -> Y (in Ref. 2; AAA67245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55840 MW; A6F7A815F8476A4B CRC64;
MWRPSENKVY LPPTPVSKVV STDEYVTRTS IYYHASSSRL LAVGHPYFKV QKTNNKQSIP
KVSGYQYRVF RVQLPDPNKF GLPDPSLYNP ETQRLVWACT GVEVGRGQPL GLGLSGHPLL
NKLDDTENAP KYVGAGADNR ENVSMDYKQT QLCILGCTPP IGEHWAKGNL CTPNTLAAGD
CPPLELVNSY IQDGDMVDIG FGAMDFKTLQ TSKSEVPLDV ATSICKYPDY LKMAAEAYGD
SLFFYLRREQ MFVRHMLNRA GTMGEPVPND LYIKKSSGNL DSSIYAATPS GSMVTSEYQI
FNKPYWLQRA QGQNNGICWG NQVFLTVVDT TRSTNLTLCA TASTQDSFNN SDFREYIRHV
EEYDLQFIFQ LCTITLTADV MAYIHGMNPT ILEDWNFGIT PPATSSLEDT YRFVQSQAIA
CQKNNAPAKE KEDPYSKFNF WTVDLKERFS SDLDQFPLGR KFLLQAGLRA RPRLRPVKRA
APSSSKGTAR KRAKTKR
