VL1_HPV17
ID VL1_HPV17 Reviewed; 507 AA.
AC Q02514;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-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 Human papillomavirus 17.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10607;
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 312-355.
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; X74469; CAA52517.1; -; Genomic_DNA.
DR EMBL; M96286; AAA47025.1; -; Genomic_DNA.
DR PIR; S36484; S36484.
DR SMR; Q02514; -.
DR Proteomes; UP000006932; 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..507
FT /note="Major capsid protein L1"
FT /id="PRO_0000133501"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175
FT /note="Interchain (with C-439)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 439
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 507 AA; 57293 MW; 72BE26C24ECC6EE8 CRC64;
MTLWLPTTGK VYLPPTPPVA RVQSTDEYVE RTNIFYHAMS DRLLTVGHPF YDVRSTDGLR
IEVPKVSGNQ YRAFRVTLPD PNKFALADMS VYNPEKERLV WACAGLEIGR GQPLGVGTTG
HPLFNKLRDT ENNSSYQGGS TDDRQNTSFD PKQVQMFVVG CVPCIGEHWD RAPVCENEQN
NQTGLCPPLE LKNTVIEDGD MVDIGFGNIN NKVLSFNKSD VSLDIVNETC KYPDFLSMAN
DVYGDACFFF ARREQCYARH YFVRGGNVGD AVPDGSVNQD HKFYLPAQTG QQQRTLGNST
YFPTVSGSLV TSDAQLFNRP FWLRRAQGHN NGILWGNQIF VTVADNTRNT NFSISVSTEA
GAVTEYNSQN IREYLRHVEE YQLSFILQLC KIPLKAEVLT QINAMNSGIL EDWQLGFVPT
PDNPVHDIYR YINSKATKCP DAVVEKEKED PFAKYTFWNV NLTEKLSLDL DQYPLGRKFI
FQSGLQARPR TIRTSVKVPK GIKRKRS