ID   VL1_HPV30               Reviewed;         508 AA.
AC   Q02515;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 99.
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 30.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10611;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-352.
RX   PubMed=1326639; DOI=10.1128/jvi.66.10.5714-5725.1992;
RA   Chan S.-Y., Bernard H.U., Ong C.K., Chan S.P., Birgit H., Delius H.;
RT   "Phylogenetic analysis of 48 papillomavirus types and 28 subtypes and
RT   variants: a showcase for the molecular evolution of DNA viruses.";
RL   J. Virol. 66:5714-5725(1992).
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; X74474; CAA52548.1; -; Genomic_DNA.
DR   EMBL; M96279; AAA47018.1; -; Genomic_DNA.
DR   PIR; S36508; S36508.
DR   SMR; Q02515; -.
DR   Proteomes; UP000009155; 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..508
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133514"
FT   REGION          481..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        182
FT                   /note="Interchain (with C-434)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        434
FT                   /note="Interchain (with C-182)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   508 AA;  56667 MW;  62F359F257714748 CRC64;
     MFPIFLQMAV WRPSETKVYL PPTPVSKVVP TDAYVKRTNI FYHAGSSRLL AVGHPYYSIS
     KAGNSKTDVP KVSAFQYRVF RVRLPDPNKF GLPDTNVFNP EQERLVWACV GLEIGRGQPL
     GVGVSGNPLF NKLDDTESST IANQDTAEDS RDNISVDPKQ TQLCIIGCTP AIGEHWAKGT
     ACRSAPPAQG DCPPLELVNS PIQDGDMVDI GFGAMDFKTL QESKSDVPLD ISQSTCKYPD
     YLKMSADAYG DSMWFYLRRE QLFARHYFNR AGAIGEQLPS TLYIKGTNNR DPPPSSVYVA
     TPSGSMVTSE AQLFNKPYWL QRAQGHNNGI CWGNQVFVTV VDTTRNTNMT ISATTQTLST
     YNSSQIKQYV RHVEEYELQF VFQLCKISLS AETMAYLHTM NSTLLEGWNI GLSPPAATSL
     EDKYRYVKSL AITCQKDQPP AEKEDPLAKY KFWDVNLQDS FSADLDQFPL GRKFLMQLGV
     RTKPSTTTKK RSAPSSSTST PSAKRKRR