VL1_HPV53
ID VL1_HPV53 Reviewed; 499 AA.
AC Q05113;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 23-FEB-2022, 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 Human papillomavirus type 53.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333765;
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 300-343.
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; X74482; CAA52595.1; -; Genomic_DNA.
DR EMBL; M96298; AAA47037.1; -; Genomic_DNA.
DR PIR; S36531; S36531.
DR RefSeq; NP_041848.1; NC_001593.1.
DR SMR; Q05113; -.
DR GeneID; 1489468; -.
DR KEGG; vg:1489468; -.
DR Proteomes; UP000009126; 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..499
FT /note="Major capsid protein L1"
FT /id="PRO_0000133536"
FT REGION 472..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 173
FT /note="Interchain (with C-425)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 425
FT /note="Interchain (with C-173)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ SEQUENCE 499 AA; 55722 MW; 5221961A3FDD5A66 CRC64;
MAVWRPSDSK VYLPPTPVSK VITTDAYVKR TTIFYHAGSS RLLTVGHPYY PISKSGKADI
PKVSAFQYRV FRVRLPDPNK FGLPDTNIFN PDQERLVWAC VGLEIGRGQP LGVGVSGHPL
FNRLDDTESS SIAIQDTAPD SRDNVSVDPK QTQLCIIGCA PAIGEHWTKG TACRSTPTTA
GDCPPLELIN SPIEDGDMVD TGFGALNFKA LQESKSDVPL DIVQSTCKYP DYLKMSADAY
GDSMWFYLRR EQLFTRHFFN RAGVIGEEIP NDLYIKGSNG RDPPPSSVYV ATPSGSMITS
EAQLFNKPYW LQRAQGHNNG ICWNNQLFVT VVDTTRNTNM TLSATTQSMS TYNSKQIKQY
VRHAEEYELQ FVFQLCKISL SAEVMAYLHT MNSTLLEDWN IGLSPPVATS LEDKYRYVKS
AAITCQKDQP PPEKQDPLSK YKFWEVNLQN SFSADLDQFP LGRKFLMQVG VRTKPPVSSK
KRSASTTSTS APSSKRKRK
