VL1_HPV52
ID VL1_HPV52 Reviewed; 529 AA.
AC Q05138;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 02-JUN-2021, entry version 90.
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 52.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10618;
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 333-376.
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; X74481; CAA52590.1; -; Genomic_DNA.
DR EMBL; M96297; AAA47036.1; -; Genomic_DNA.
DR PIR; S36578; S36578.
DR PDB; 6IGF; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J=1-529.
DR PDBsum; 6IGF; -.
DR SMR; Q05138; -.
DR PRIDE; Q05138; -.
DR Proteomes; UP000008692; 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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Disulfide bond; Host nucleus;
KW Host-virus interaction; Late protein; Reference proteome;
KW T=7 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..529
FT /note="Major capsid protein L1"
FT /id="PRO_0000133535"
FT REGION 507..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204
FT /note="Interchain (with C-458)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 458
FT /note="Interchain (with C-204)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6IGF"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 125..138
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6IGF"
FT TURN 251..255
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 276..291
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 390..412
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:6IGF"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6IGF"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:6IGF"
SQ SEQUENCE 529 AA; 59469 MW; 77F7DB5CA9664C53 CRC64;
MVQILFYILV IFYYVAGVNV FHIFLQMSVW RPSEATVYLP PVPVSKVVST DEYVSRTSIY
YYAGSSRLLT VGHPYFSIKN TSSGNGKKVL VPKVSGLQYR VFRIKLPDPN KFGFPDTSFY
NPETQRLVWA CTGLEIGRGQ PLGVGISGHP LLNKFDDTET SNKYAGKPGI DNRECLSMDY
KQTQLCILGC KPPIGEHWGK GTPCNNNSGN PGDCPPLQLI NSVIQDGDMV DTGFGCMDFN
TLQASKSDVP IDICSSVCKY PDYLQMASEP YGDSLFFFLR REQMFVRHFF NRAGTLGDPV
PGDLYIQGSN SGNTATVQSS AFFPTPSGSM VTSESQLFNK PYWLQRAQGH NNGICWGNQL
FVTVVDTTRS TNMTLCAEVK KESTYKNENF KEYLRHGEEF DLQFIFQLCK ITLTADVMTY
IHKMDATILE DWQFGLTPPP SASLEDTYRF VTSTAITCQK NTPPKGKEDP LKDYMFWEVD
LKEKFSADLD QFPLGRKFLL QAGLQARPKL KRPASSAPRT STKKKKVKR
