ID   VL1_HPV03               Reviewed;         532 AA.
AC   P36731;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-JUN-2021, 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   Human papillomavirus 3.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10614;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(1994).
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   -!- CAUTION: It is uncertain whether Met-1 or Met-29 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; X74462; CAA52474.1; -; Genomic_DNA.
DR   PIR; S36554; S36554.
DR   SMR; P36731; -.
DR   Proteomes; UP000007706; 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..532
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133485"
FT   REGION          512..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        203
FT                   /note="Interchain (with C-457)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        457
FT                   /note="Interchain (with C-203)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   532 AA;  59194 MW;  A0AFB87DBEE98B27 CRC64;
     MAGIFIYGLS PSFCPDVVAV NVSHIFLQMA LWRSSDNLVY LPPTPVSKVL STDDYVTRTN
     IYYYAGSSRL LTVGHPYFAI PKSSNSKMDI PKVSAFQYRV FRVRLPDPNK FGLPDARIYN
     PDAERLVWAC TGVEVGRGLP LGVGLSGHPL YNKLDDTENS NIAHGDIGKD SRDNISVDNK
     QTQLCIVGCT PPMGEHWGKG TPCKQNASPG DCPPLELITA PIQDGDMVDT GYGAMDFGNL
     QSNKSDVPLD ICQTTCKYPD YLGMAAEPYG DSMFFYLRKE QLFARHFLNR AGMAGDTVPD
     ALYIKGDSQS GGRDKIGSAV YCPTPSGSMV TSETQLFNKP YWLRRAQGHN NGICWANQLF
     VTVVDTTRST NMTLCVSTET SATYDATKFK EYLRHGEEYD LQFIFQLCKV TLTPEIMAYL
     HTMNSTLLED WNFGLTLPPS TSLEDTYRFL TSSAITCQKD APPTEKQDPY AKLNFWDVDL
     KDRFSLDLSQ FPLGRKFLMQ LGVGTRSSIS VRKRSATTTS RTAAAKRKRT KK