ID A0A1X9YLL5_9PAPI Unreviewed; 107 AA. AC A0A1X9YLL5; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 25-OCT-2017, entry version 3. DE RecName: Full=Major capsid protein L1 {ECO:0000256|RuleBase:RU361248}; DE Flags: Fragment; GN Name=L1 {ECO:0000256|RuleBase:RU361248}; OS Human papillomavirus type 6. OC Viruses; dsDNA viruses, no RNA stage; Papillomaviridae; OC Alphapapillomavirus. OX NCBI_TaxID=31552 {ECO:0000313|EMBL:ARS33698.1}; RN [1] {ECO:0000313|EMBL:ARS33698.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HPV/EGY/2015/ZI-11 {ECO:0000313|EMBL:ARS33698.1}; RA Hamza I.A., Hamza H.; RT "Circulation of human papillomavirus in Egypt."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 CC nm diameter. The capsid is composed of 72 pentamers linked to each CC other by disulfide bonds and associated with L2 proteins. Binds to CC heparan sulfate proteoglycans on cell surface of basal layer CC keratinocytes to provide initial virion attachment. This binding CC mediates a conformational change in the virus capsid that CC facilitates efficient infection. The virion enters the host cell CC via endocytosis. During virus trafficking, L1 protein dissociates CC from the viral DNA and the genomic DNA is released to the host CC nucleus. The virion assembly takes place within the cell nucleus. CC Encapsulates the genomic DNA together with protein L2. CC {ECO:0000256|RuleBase:RU361248}. CC -!- SUBUNIT: Self-assembles into homopentamers. The capsid has an CC icosahedral symmetry and consists of 72 capsomers, with each CC capsomer being a pentamer of L1. Interacts with the minor capsid CC protein L2; this interaction is necessary for viral genome CC encapsidation. {ECO:0000256|RuleBase:RU361248}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|RuleBase:RU361248}. CC -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family. CC {ECO:0000256|RuleBase:RU361248}. 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; KY848437; ARS33698.1; -; Genomic_DNA. DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR Gene3D; 2.60.175.20; -; 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 SUPFAM; SSF88648; SSF88648; 1. PE 3: Inferred from homology; KW Capsid protein {ECO:0000256|RuleBase:RU361248}; KW Host-virus interaction {ECO:0000256|RuleBase:RU361248}; KW Late protein {ECO:0000256|RuleBase:RU361248}; KW T=7 icosahedral capsid protein {ECO:0000256|RuleBase:RU361248}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU361248}; KW Virion {ECO:0000256|RuleBase:RU361248}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU361248}. FT NON_TER 1 1 {ECO:0000313|EMBL:ARS33698.1}. FT NON_TER 107 107 {ECO:0000313|EMBL:ARS33698.1}. SQ SEQUENCE 107 AA; 12302 MW; 8BFA5538B5220744 CRC64; RSTNMTLCAS VTTSSTYTNS DYKEYMRHVE EYDLQFIFQL CSITLSAEVM AYIHTMNPSV LEDWNFGLSP PPNGTLEDTY RYVQSQAITC QKPTPEKQKP DPYKNLS //