ID   VL1_CRPVK               Reviewed;         505 AA.
AC   P03102;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 95.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Cottontail rabbit papillomavirus (strain Kansas) (CRPV) (Papillomavirus
OS   sylvilagi).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Kappapapillomavirus.
OX   NCBI_TaxID=31553;
OH   NCBI_TaxID=9988; Sylvilagus floridanus (Cottontail rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2984661; DOI=10.1073/pnas.82.6.1580;
RA   Giri I., Danos O., Yaniv M.;
RT   "Genomic structure of the cottontail rabbit (Shope) papillomavirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1580-1584(1985).
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; K02708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A03643; P1WLRB.
DR   SMR; P03102; -.
DR   Proteomes; UP000008787; 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..505
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133556"
FT   REGION          479..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175
FT                   /note="Interchain (with C-434)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        434
FT                   /note="Interchain (with C-175)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   505 AA;  57933 MW;  50FF168D8A2F5A38 CRC64;
     MAVWLSTQNK FYLPPQPVTK IPSTDEYVTR TNVFYYASSD RLLTVGHPYY EIRDKGTMLV
     PKVSPNQYRV FRIKLPDPNK FAFGDKQLYD PEKERLVWCL RGIEVNRGQP LGVSVTGNPI
     FNKFDDVENP TKYYNNHADQ QDYRKSMAFD PKQVQLLMLG CVPATGEHWA QAKQCAEDPP
     QQTDCPPIEL VNTVIEDGDM CEIGFGAMDH KTLQASLSEV PLELAQSISK YPDYLKMQKD
     QFGDSMFFYA RREQMYARHF FSRAGGDKEN VKSRAYIKRT QMQGEANANI ATDNYCITPS
     GSLVSSDSQV FNRAYWLQKA QGMNNGVCWD NQIFVTVVDN TRGTILSLVT KSKEQIKKTH
     GKTVHFSSYL RHVEEYELQF VLQLCKVKLT PENLSYLHSM HPTIIDNWQL SVSAQPSGTL
     EDQYRYLQSI ATKCPPPEPP KENTDPYKNY KFWEVDLSEK LSDQLDQYPL GRKFLNQSGL
     QRIGTKRPAP APVSIVKSSK RKRRT