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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}.
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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
 
 
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