ID   VL1_MMPV1               Reviewed;         501 AA.
AC   P22163;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-SEP-2021, entry version 98.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Macaca mulata papillomavirus 1 (Rhpv 1) (Rhesus papillomavirus type 1).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=2779844;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1847267; DOI=10.1016/0042-6822(91)90519-h;
RA   Ostrow R.S., Labresh K.V., Faras A.J.;
RT   "Characterization of the complete RhPV 1 genomic sequence and an
RT   integration locus from a metastatic tumor.";
RL   Virology 181:424-429(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}.
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DR   EMBL; M60184; AAA79318.1; -; Genomic_DNA.
DR   PIR; H38503; P1WLR1.
DR   RefSeq; NP_043338.1; NC_001678.1.
DR   SMR; P22163; -.
DR   GeneID; 1489013; -.
DR   KEGG; vg:1489013; -.
DR   Proteomes; UP000008169; 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..501
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133559"
FT   REGION          473..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-426)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        426
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   501 AA;  55635 MW;  6E808D8F130E440A CRC64;
     MSMWRPSDSK VYLPPVPVSK VVSTDEYVSR TSIYYHAGSS RLLAVGHPYY AVKKGNNKVS
     VPKVSGLQYR VFRVRLPDPN KFGLPDANFY DPNTQRLVWA CLGVEVGRGQ PLGVGTSGHP
     LLNKLDDTEN GPKVAGGQGA DNRECVSMDY KQTQLCMLGC KPPVGEHWGK GNPCTTGAAG
     DCPALELVNS VIQDGDMVDT GYGAMDFNAL QANKSDVPID ICTSVCKYPD YLKMASDPYG
     DSLFFYLRRE QMFVRHLFNR AGTMGDSVPD DLYIKGSGSN VKLASHVFYP TPSGSMVTSD
     AQLFNKPYWL QKAQGHNNGI CWGNQVFLTV VDTTRSTNMT LCASTASTVT TPYNNESFKE
     YLRHVEEFDL QFIFQLCKVT LNTEVMAYIH SMDASILEDW NFGLQPPPSG SLQDTYRFVT
     SAAITCQKPA PPKEKEDPLA KYTFWEVDLK EKFSADLDQF PLGRKFLLQA GMRARPTLRA
     PKRTASSTSS SSPRKRKRTK R