ID   VL1_COPV6               Reviewed;         503 AA.
AC   Q89828;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 91.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Canine oral papillomavirus (strain Y62) (COPV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Lambdapapillomavirus.
OX   NCBI_TaxID=766192;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8076829; DOI=10.1016/0378-1119(94)90303-4;
RA   Isegawa N., Nakano K., Ohta M., Shirasawa H., Tokita H., Simizu B.;
RT   "Cloning and sequencing of the L1 gene of canine oral papillomavirus.";
RL   Gene 146:261-265(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8091677; DOI=10.1006/viro.1994.1552;
RA   Delius H., van Ranst M.A., Jenson A.B., zur Hausen H., Sundberg J.P.;
RT   "Canine oral papillomavirus genomic sequence: a unique 1.5-kb intervening
RT   sequence between the E2 and L2 open reading frames.";
RL   Virology 204:447-452(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Isegawa N., Ohta M., Shirasawa H., Tokita H., Simizu B., Yamaura A.;
RT   "Nucleotide sequence of a canine oral papillomavirus containing a long
RT   noncoding region.";
RL   Int. J. Oncol. 7:155-159(1995).
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; D55633; BAA09503.1; -; Genomic_DNA.
DR   EMBL; D26115; BAA05111.1; -; Genomic_DNA.
DR   EMBL; L22695; AAA61750.1; -; Genomic_DNA.
DR   RefSeq; NP_056819.1; NC_001619.1.
DR   SMR; Q89828; -.
DR   PRIDE; Q89828; -.
DR   GeneID; 1497245; -.
DR   KEGG; vg:1497245; -.
DR   Proteomes; UP000008788; Genome.
DR   Proteomes; UP000097271; 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..503
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133555"
FT   REGION          270..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        178
FT                   /note="Interchain (with C-431)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        431
FT                   /note="Interchain (with C-178)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   503 AA;  57310 MW;  1355F2C354DCA789 CRC64;
     MAVWLPAQNK FYLPPQPSTK VLSTDEYVSR TNIFYHASSE RLLTVGHPFY EIYKEERSEE
     VIVPKVSPNQ YRVFRLLLPD PNNFAFGDKS LFDPEKERLV WGLRGLEIGR GQPLGISVTG
     HPTFDRYNDV ENPNKNLAGH GGGTDSRVNM GLDPKQTQMF MIGCKPALGE HWSLTRWCTG
     QVHTAGQCPP IELRNTTIED GDMVDIGFGA MDFKALQHYK SGVPIDIVNS ACKYPDYLKM
     ANEPYGDRCF FFVRREQLYA RHIMSRSGTQ GLEPVPKDTY ATREDNNIGT TNYFSTPSGS
     LVSSEGQLFN RPYWIQRSQG KNNGIAWGNQ LFLTVVDNTR GTPLTINIGQ QDKPEEGNYV
     PSSYRTYLRH VEEYEVSIIV QLCKVKLSPE NLAIIHTMDP NIIEDWHLNV TPPSGTLDDT
     YRYINSLATK CPTNIPPKTN VDPFADFKFW EVDLKDKMTE QLDQTPLGRK FLFQTNVLRP
     RSVKVRSTSH VSVKRKAVKR KRK