VL1_HPV58
ID VL1_HPV58 Reviewed; 524 AA.
AC P26535;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 58.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10598;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1656594; DOI=10.1016/0042-6822(91)90791-9;
RA Kirii Y., Iwamoto S., Matsukura T.;
RT "Human papillomavirus type 58 DNA sequence.";
RL Virology 185:424-427(1991).
RN [2]
RP FUNCTION.
RX PubMed=12610160; DOI=10.1128/jvi.77.6.3846-3850.2003;
RA Bousarghin L., Touze A., Sizaret P.Y., Coursaget P.;
RT "Human papillomavirus types 16, 31, and 58 use different endocytosis
RT pathways to enter cells.";
RL J. Virol. 77:3846-3850(2003).
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 ECO:0000269|PubMed:12610160}.
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; D90400; BAA31851.1; -; Genomic_DNA.
DR PIR; G36779; P1WL58.
DR PDB; 5Y9C; X-ray; 3.44 A; A/B/C/D/E=36-524.
DR PDB; 5Y9E; X-ray; 2.04 A; A/B/C/D/E=36-524.
DR PDB; 6IGC; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-524.
DR PDB; 6IGD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-524.
DR PDB; 7DN5; EM; 4.11 A; A/B/C/D/E/F=1-524.
DR PDB; 7DNH; EM; 3.64 A; A/B/C/D/E=1-524.
DR PDB; 7DNK; EM; 6.41 A; A/B/C/D/E=1-524.
DR PDB; 7DNL; EM; 4.19 A; A/B/C/D/E=1-524.
DR PDBsum; 5Y9C; -.
DR PDBsum; 5Y9E; -.
DR PDBsum; 6IGC; -.
DR PDBsum; 6IGD; -.
DR PDBsum; 7DN5; -.
DR PDBsum; 7DNH; -.
DR PDBsum; 7DNK; -.
DR PDBsum; 7DNL; -.
DR SMR; P26535; -.
DR ChEMBL; CHEMBL3562173; -.
DR ABCD; P26535; 1 sequenced antibody.
DR Proteomes; UP000007668; 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..524
FT /note="Major capsid protein L1"
FT /id="PRO_0000133541"
FT REGION 501..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 202
FT /note="Interchain (with C-453)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 453
FT /note="Interchain (with C-202)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6IGD"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5Y9E"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 123..136
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6IGD"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5Y9E"
FT TURN 248..252
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 273..288
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:5Y9C"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 385..407
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:5Y9E"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:5Y9E"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5Y9C"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:5Y9E"
FT HELIX 488..497
FT /evidence="ECO:0007829|PDB:5Y9E"
SQ SEQUENCE 524 AA; 59038 MW; 5DEC95E2878A26DF CRC64;
MVLILCCTLA ILFCVADVNV FHIFLQMSVW RPSEATVYLP PVPVSKVVST DEYVSRTSIY
YYAGSSRLLA VGNPYFSIKS PNNNKKVLVP KVSGLQYRVF RVRLPDPNKF GFPDTSFYNP
DTQRLVWACV GLEIGRGQPL GVGVSGHPYL NKFDDTETSN RYPAQPGSDN RECLSMDYKQ
TQLCLIGCKP PTGEHWGKGV ACNNNAAATD CPPLELFNSI IEDGDMVDTG FGCMDFGTLQ
ANKSDVPIDI CNSTCKYPDY LKMASEPYGD SLFFFLRREQ MFVRHFFNRA GKLGEAVPDD
LYIKGSGNTA VIQSSAFFPT PSGSIVTSES QLFNKPYWLQ RAQGHNNGIC WGNQLFVTVV
DTTRSTNMTL CTEVTKEGTY KNDNFKEYVR HVEEYDLQFV FQLCKITLTA EIMTYIHTMD
SNILEDWQFG LTPPPSASLQ DTYRFVTSQA ITCQKTAPPK EKEDPLNKYT FWEVNLKEKF
SADLDQFPLG RKFLLQSGLK AKPRLKRSAP TTRAPSTKRK KVKK
