ID   VL1_PAPVE               Reviewed;         501 AA.
AC   P11326;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, 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   European elk papillomavirus (EEPV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=10565;
OH   NCBI_TaxID=9860; Cervus elaphus (Red deer).
OH   NCBI_TaxID=9870; Rangifer tarandus (Reindeer) (Cervus tarandus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Eriksson A.;
RL   Submitted (AUG-1987) to the EMBL/GenBank/DDBJ databases.
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; M15953; AAA66861.1; -; Genomic_DNA.
DR   PIR; A94457; P1WLEP.
DR   RefSeq; NP_041313.1; NC_001524.1.
DR   SMR; P11326; -.
DR   GeneID; 1488995; -.
DR   KEGG; vg:1488995; -.
DR   Proteomes; UP000009060; 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; -; 1.
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..501
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133558"
FT   DISULFID        173
FT                   /note="Interchain (with C-428)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        428
FT                   /note="Interchain (with C-173)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   501 AA;  56460 MW;  7452CCCB4964A6F6 CRC64;
     MAFWQPSQRL YLPPTPVTKV LCSEQYIRRK DVFYHGETER MLTVGHPYYE IKQSGSGKTI
     PKVSPNQYRV FRILLPDPNQ FALPDKAMYD PSKERLVWAV VGVQVSRGQP LGGSVSGHSY
     QNTLIDAENV SKKVNAQGTD DRKQGGMDVK QQQILLLGCT PAIGEYWTTA RPCVTDRPET
     GSCPPIELKN KPIEDGDMMD IGFGAANFKE LNATKSDLPL DIAKDICLYP DYLKMTEEAA
     GNSMFFFARK EQVYVRHIWS RGGTDKEMPP EAYFLKPKGG DQTQKMPSIL FGVPSGSLVS
     TDGQLFNRPY WLFRAQGMNN GICWLNQLFV TVGDNTRGTT LTITVPTSGS PLTEYDTSKF
     NVFQRHVEEY KLAFVFQLCS VTLSPETVSH LQGLMPSILE HWDINMQPPT SSILEDTYRY
     LESPATKCAD NVTPMGPEDP YAGLKFWEVN LKERLSLDLD QFPLGRRFLA QQGLGCSTRK
     RVAPVPKVTE KRIVRKRRKG N