VL1_HPV26
ID VL1_HPV26 Reviewed; 503 AA.
AC P36735;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 26.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333762;
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; X74472; CAA52535.1; -; Genomic_DNA.
DR PIR; S36549; S36549.
DR RefSeq; NP_041787.1; NC_001583.1.
DR SMR; P36735; -.
DR PRIDE; P36735; -.
DR GeneID; 1496948; -.
DR KEGG; vg:1496948; -.
DR Proteomes; UP000009113; 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..503
FT /note="Major capsid protein L1"
FT /id="PRO_0000133510"
FT REGION 476..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 174
FT /note="Interchain (with C-429)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 429
FT /note="Interchain (with C-174)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 503 AA; 56328 MW; A0706D12F425BE80 CRC64;
MALWRTSDSK VYLPPTPVSR VVNTDEYVTR TGIYYYAGSS RLLTLGHPYF SIPKTGQKAE
IPKVSAYQYR VFRVHLPDPN KFGLPDPQLY NPDTERLVWA CVGVEVGRGQ PLGIGLSGHP
LFNKLDDTEN SHLATVNADT DNRDNVSVDN KQTQLCIIGC TPPLGEHWGI GTICKNTQTQ
RGDCPPLELI SSIIEDGDMI DTGFGAMDFT ALQATKSDVP IDISQSTCKY PDYLKMSADT
YGNSMFFFLR REQLFARHFY NKAGAVGDAI PTTLYIKGAE SGREPPTSSI YSATPSGSMV
TSDAQLFNKP YWLQRAQGHN NGICWGNQLF VTCVDTTRST NLTISTLSAA SASTPFKPSD
YKQFIRHGEE YELQFIFQLC KITLTTDVMA YIHLMNASIL EDWNFGLTLP PTASLEDAYR
FIKNSATTCQ RNAPPVPKED PFQKFKFWDV DLKEKFSIDL DQFPLGRKFM LQAGIQRRPK
LGTKRPLSST SSSTKRKKRK LTK