VL1_HPV34
ID VL1_HPV34 Reviewed; 528 AA.
AC P36738;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 91.
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 34.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333764;
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}.
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; X74476; CAA52560.1; -; Genomic_DNA.
DR PIR; S36520; S36520.
DR RefSeq; NP_041812.1; NC_001587.1.
DR SMR; P36738; -.
DR GeneID; 1489433; -.
DR KEGG; vg:1489433; -.
DR Proteomes; UP000009171; 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; 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..528
FT /note="Major capsid protein L1"
FT /id="PRO_0000133518"
FT REGION 504..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 200
FT /note="Interchain (with C-453)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 453
FT /note="Interchain (with C-200)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 528 AA; 59048 MW; A3F92CA480B43703 CRC64;
MGPILYCILA CMSFHANVNV CHIFLQMWRP TEAKVYLPPV SVSKVVSTEE YVTRTNIYYY
AGSTRLLAVG HPYYPIKDTN GKRKIAVPKV SGLQYRVFRI RLPDPNKFGF PDASFYNPDK
ERLVWACAGV EVGRGQPLGI GTSGNPFMNK LEDTENAAKY IGGNIADSRE CMSVDYKQTQ
LCIVGCKPPL GEHWGTGTPC GTQNAGECPP LELKNTTIQD GDMIDVGFGA MDFKALQANK
SDVPIDISNT ICKYPDYLGM AADPYGDSMW FYIRREQMFV RHLFNRAGTV GDAIPDDLMI
KGTGNTASPS SCVFYPTPSG SMVSSDAQIF NKPYWLQKAQ GQNNGICWHN QLFLTVVDTT
RSTNFSVCVG TQSTSTTAPY ANSNFKEYLR HAEEYDLQFV FQLCKINLTT DVMTYIHSMS
SSILEQWNFG LTPPPSGTLE ETYRYVTSQA ITCQRPQPPK ETEDPYGKMT FWEVDLKEKF
SAELDQFALG RKFLLQLGMR ARPRLQASKR SAPSSSSTAP KKKRAKRI