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VL1_HPV41
ID   VL1_HPV41               Reviewed;         534 AA.
AC   P27557;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   23-FEB-2022, entry version 94.
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 41.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Nupapillomavirus.
OX   NCBI_TaxID=10589;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1645904; DOI=10.1016/0168-1702(91)90017-p;
RA   Hirt L., Hirsch-Behnam A., de Villiers E.M.;
RT   "Nucleotide sequence of human papillomavirus (HPV) type 41: an unusual HPV
RT   type without a typical E2 binding site consensus sequence.";
RL   Virus Res. 18:179-190(1991).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA39619.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X56147; CAA39619.1; ALT_INIT; Genomic_DNA.
DR   PIR; H43550; P1WL41.
DR   RefSeq; NP_040294.1; NC_001354.1.
DR   SMR; P27557; -.
DR   PRIDE; P27557; -.
DR   GeneID; 1489283; -.
DR   KEGG; vg:1489283; -.
DR   Proteomes; UP000006367; 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..534
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133525"
FT   REGION          507..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        200
FT                   /note="Interchain (with C-459)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        459
FT                   /note="Interchain (with C-200)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   534 AA;  60950 MW;  61B0E3EA4181511B CRC64;
     MIYILACCAG NVKNANVFIF QMAVWLPGPN RFYLPPQPIQ RTLNTEEYVR RTSTFLHAAT
     DRLLTVGHPF YNITNADGKE VVPKVSSNQF RAFRVRFPNP NTFAFCDKSL FNPDKERLVW
     GIRGIEVSRG QPLGIGVTGN PFFNKFDDAE NPYNGINKNN ITDQGSDSRL SIAFDPKQTQ
     LLIVGAKPAK GEYWDVAATC ENPPLTKADD KCPALELKSS YIEDADMSDI GLGNLNFSTL
     QRNKSDAPLD IVDSICKYPD YLQMIEELYG DHMFFYVRRE ALYARHIMQH AGKMDAEQFP
     TSLYIDSSVE GEKLNSLQRT DRYFMTPSGS LVATEQQLFN RPFWLQRSQG HNNGILWHNE
     AFVTLVDTTR GTNFTISVPE GDASSYNNSK FFEFLRHTEE FQLAFILQLC KVDLTPENLA
     YIHTMDPSII EDWHLAVTSP PNSVLEDHYR YILSIATKCP SKDADDTSTD PYKDLKFWEV
     DLRDRMTEQL DQTPLGRKFL FQTGITQSSS NKRVSTQSTA LTTYRRPTKR RRKA
 
 
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