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VL1_HPV27
ID   VL1_HPV27               Reviewed;         594 AA.
AC   P36736; Q81959;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 89.
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 27.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=333752;
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 L1; 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,
CC       ECO:0000305}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04002, ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-110 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X74473; CAA52541.1; -; Genomic_DNA.
DR   EMBL; X74473; CAA52542.1; ALT_INIT; Genomic_DNA.
DR   PIR; S36502; S36502.
DR   SMR; P36736; -.
DR   Proteomes; UP000009114; 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..594
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133511"
FT   DISULFID        282
FT                   /note="Interchain (with C-533)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        533
FT                   /note="Interchain (with C-282)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   594 AA;  67099 MW;  946BA35505DDC0A8 CRC64;
     MMFMLILMSC SHWTITTQPL AAPWLIPRYL PPLHLHCEGP LQPLSRVVLM CLCILGLILN
     HPLFLVWGPS FLWLHRCHPL FTYLGGIIIY CQVISCGLND VNVSTISLQM ALWRPNESKV
     YLPPTPVSKV ISTDVYVTRT NVYYHGGSSR LLTVGHPYYS IKKGSNNRLA VPKVSGYQYR
     VFHVKLPDPN KFGLPDADLY DPDTQRLLWA CVGVEVGRGQ PLGVGVSGHP YYNRQDDTEN
     AHTLDSAEDG RENISMDYKQ TQLFILGCKP SIGEHWSKGT TCNGSSAAGD CPPLQFTNST
     IEDGDMVETG FGALDFATLQ SNRSDVPLDI CTNVCKYPDY LKMAAEPYGD SMFFSLRREQ
     MFTRHFFNRA GKMGDTIPDE LYIKSTTISD PGSHVYTSTP SGSMVSSEQQ LFNKPYWLRR
     AQGHNNGMCW GNRIFLTVVD TTRSTNVSLC AAEVSDNTNY KATNFKEYLR HMEEYDLQFI
     FQLCKITLTP EIMAYIHNMD PQLLEDWNFG VPPPPSASLQ DTYRYLQSQA ITCQKPTPPK
     TPTDPYANMT FWDVDLRESF SMDLDQFPLG RKFLLQRGTT PTVSRKRTAV GRGH
 
 
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