VL1_HPV16
ID VL1_HPV16 Reviewed; 505 AA.
AC P03101; O00530;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 3.
DT 03-AUG-2022, entry version 133.
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 16.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333760;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2990099; DOI=10.1016/0042-6822(85)90214-4;
RA Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G.;
RT "Human papillomavirus type 16 DNA sequence.";
RL Virology 145:181-185(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10423141; DOI=10.1099/0022-1317-80-7-1725;
RA Meissner J.D.;
RT "Nucleotide sequences and further characterization of human papillomavirus
RT DNA present in the CaSki, SiHa and HeLa cervical carcinoma cell lines.";
RL J. Gen. Virol. 80:1725-1733(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10502513; DOI=10.1006/viro.1999.9868;
RA Flores E.R., Allen-Hoffmann B.L., Lee D., Sattler C.A., Lambert P.F.;
RT "Establishment of the human papillomavirus type 16 (HPV-16) life cycle in
RT an immortalized human foreskin keratinocyte cell line.";
RL Virology 262:344-354(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate European German 131;
RA Terai M., Fu L., Ma Z., Burk R.D.;
RT "Cloning and sequencing of non-European human papillomavirus (HPV) variant
RT complete genomes from cervicovaginal cells by an overlapping PCR method.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-345.
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).
RN [6]
RP FUNCTION.
RX PubMed=8553535; DOI=10.1006/viro.1995.0044;
RA Heino P., Dillner J., Schwartz S.;
RT "Human papillomavirus type 16 capsid proteins produced from recombinant
RT Semliki Forest virus assemble into virus-like particles.";
RL Virology 214:349-359(1995).
RN [7]
RP INTERACTION WITH HOST ITGA6.
RX PubMed=11341777; DOI=10.1006/bbrc.2001.4838;
RA Yoon C.S., Kim K.D., Park S.N., Cheong S.W.;
RT "alpha(6) Integrin is the main receptor of human papillomavirus type 16
RT VLP.";
RL Biochem. Biophys. Res. Commun. 283:668-673(2001).
RN [8]
RP INTERACTION WITH HOST KPNA2.
RX PubMed=11971900; DOI=10.1074/jbc.m200724200;
RA Nelson L.M., Rose R.C., Moroianu J.;
RT "Nuclear import strategies of high risk HPV16 L1 major capsid protein.";
RL J. Biol. Chem. 277:23958-23964(2002).
RN [9]
RP DISULFIDE BOND.
RX PubMed=12234916; DOI=10.1093/emboj/cdf494;
RA Modis Y., Trus B.L., Harrison S.C.;
RT "Atomic model of the papillomavirus capsid.";
RL EMBO J. 21:4754-4762(2002).
RN [10]
RP ISGYLATION.
RX PubMed=20542004; DOI=10.1016/j.molcel.2010.05.002;
RA Durfee L.A., Lyon N., Seo K., Huibregtsesend J.M.;
RT "The ISG15 conjugation system broadly targets newly synthesized proteins:
RT implications for the antiviral function of ISG15.";
RL Mol. Cell 38:722-732(2010).
RN [11]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=1660197; DOI=10.1016/0042-6822(91)90533-h;
RA Zhou J., Doorbar J., Sun X.Y., Crawford L.V., McLean C.S., Frazer I.H.;
RT "Identification of the nuclear localization signal of human papillomavirus
RT type 16 L1 protein.";
RL Virology 185:625-632(1991).
RN [12]
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).
RN [13]
RP FUNCTION, AND INTERACTION WITH HOST SDC1.
RX PubMed=26289843; DOI=10.1099/vir.0.000147;
RA Surviladze Z., Sterkand R.T., Ozbun M.A.;
RT "Interaction of human papillomavirus type 16 particles with heparan sulfate
RT and syndecan-1 molecules in the keratinocyte extracellular matrix plays an
RT active role in infection.";
RL J. Gen. Virol. 96:2232-2241(2015).
RN [14]
RP INTERACTION WITH PROTEIN E2.
RX PubMed=25911730; DOI=10.1099/vir.0.000162;
RA Siddiqa A., Leon K.C., James C.D., Bhatti M.F., Roberts S., Parish J.L.;
RT "The human papillomavirus type 16 L1 protein directly interacts with E2 and
RT enhances E2-dependent replication and transcription activation.";
RL J. Gen. Virol. 96:2274-2285(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-505.
RX PubMed=15558545; DOI=10.1002/prot.20311;
RA Shepherd C.M., Reddy V.S.;
RT "Extent of protein-protein interactions and quasi-equivalence in viral
RT capsids.";
RL Proteins 58:472-477(2005).
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, ECO:0000269|PubMed:26289843,
CC ECO:0000269|PubMed:8553535}.
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 (PubMed:25911730). Interacts with host KPNA2;
CC this interaction mediates the nuclear localization of L1 capsomers
CC (PubMed:11971900). Interacts with host ITGA6 (PubMed:11341777).
CC Interacts with host SDC1; this interaction promotes efficient infection
CC of keratinocytes (PubMed:26289843). {ECO:0000255|HAMAP-Rule:MF_04002,
CC ECO:0000269|PubMed:11341777, ECO:0000269|PubMed:11971900,
CC ECO:0000269|PubMed:25911730, ECO:0000269|PubMed:26289843}.
CC -!- INTERACTION:
CC P03101; P52292: KPNA2; Xeno; NbExp=3; IntAct=EBI-7362698, EBI-349938;
CC P03101; Q14974: KPNB1; Xeno; NbExp=2; IntAct=EBI-7362698, EBI-286758;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC -!- PTM: ISGylated by host HERC5, this results in dominant-negative effect
CC on virus infectivity. {ECO:0000269|PubMed:20542004}.
CC -!- MISCELLANEOUS: HPV16, in comparison to HPV types 6 and 11, is more
CC often associated with malignant genital cancers in humans.
CC -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04002}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1dzl";
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DR EMBL; K02718; AAA46943.1; -; Genomic_DNA.
DR EMBL; AF001600; AAC31789.1; -; Genomic_DNA.
DR EMBL; AF125673; AAD33259.1; -; Genomic_DNA.
DR EMBL; AF536179; AAQ10719.1; -; Genomic_DNA.
DR EMBL; M96285; AAA47024.1; -; Genomic_DNA.
DR EMBL; A06331; CAA00546.1; -; Unassigned_DNA.
DR PIR; A03640; P1WLHS.
DR PDB; 1DZL; X-ray; 3.50 A; A=1-505.
DR PDB; 3J6R; EM; 9.10 A; A/B/C/D/E/F=9-486.
DR PDB; 3J7G; EM; 13.60 A; A/B/C/D/E=21-474.
DR PDB; 3J8V; EM; 13.90 A; A/B/C/D/E=21-474.
DR PDB; 3J8W; EM; 13.00 A; A/B/C/D/E=21-474.
DR PDB; 3J8Z; EM; 14.00 A; A/B/C/D/E=21-474.
DR PDB; 3JBA; EM; 12.00 A; A/B/C/D/E/F=9-486.
DR PDB; 5KEP; EM; 4.30 A; A/B/C/D/E/F=3-485.
DR PDB; 5KEQ; EM; 4.30 A; A/B/C/D/E/F=3-485.
DR PDB; 6BSP; EM; 4.70 A; C/D/E/F/G/H=12-480.
DR PDB; 6BT3; EM; 4.70 A; I/J/K/L/M/N=1-503.
DR PDB; 7CN2; EM; 3.43 A; A/B/C/D/E/F=1-505.
DR PDB; 7KZF; EM; 3.10 A; A/B/C/D/E/F=1-503.
DR PDBsum; 1DZL; -.
DR PDBsum; 3J6R; -.
DR PDBsum; 3J7G; -.
DR PDBsum; 3J8V; -.
DR PDBsum; 3J8W; -.
DR PDBsum; 3J8Z; -.
DR PDBsum; 3JBA; -.
DR PDBsum; 5KEP; -.
DR PDBsum; 5KEQ; -.
DR PDBsum; 6BSP; -.
DR PDBsum; 6BT3; -.
DR PDBsum; 7CN2; -.
DR PDBsum; 7KZF; -.
DR SMR; P03101; -.
DR BioGRID; 4263561; 1.
DR IntAct; P03101; 3.
DR MINT; P03101; -.
DR BindingDB; P03101; -.
DR ChEMBL; CHEMBL3562172; -.
DR PRIDE; P03101; -.
DR ABCD; P03101; 5 sequenced antibodies.
DR EvolutionaryTrace; P03101; -.
DR Proteomes; UP000009251; Genome.
DR Proteomes; UP000106302; Genome.
DR Proteomes; UP000137623; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IMP:CACAO.
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; Ubl conjugation;
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..505
FT /note="Major capsid protein L1"
FT /id="PRO_0000133500"
FT REGION 480..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175
FT /note="Interchain (with C-428)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002,
FT ECO:0000269|PubMed:12234916"
FT DISULFID 428
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002,
FT ECO:0000269|PubMed:12234916"
FT CONFLICT 202
FT /note="D -> H (in Ref. 1; AAA46943)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> T (in Ref. 1; AAA46943)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="Missing (in Ref. 1; AAA46943)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="D -> DD (in Ref. 1; AAA46943)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7CN2"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7KZF"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:7CN2"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1DZL"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:7CN2"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 247..261
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1DZL"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 360..382
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:7CN2"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:7KZF"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:7KZF"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:7CN2"
SQ SEQUENCE 505 AA; 56278 MW; D426CEC3DCE6B0E2 CRC64;
MSLWLPSEAT VYLPPVPVSK VVSTDEYVAR TNIYYHAGTS RLLAVGHPYF PIKKPNNNKI
LVPKVSGLQY RVFRIHLPDP NKFGFPDTSF YNPDTQRLVW ACVGVEVGRG QPLGVGISGH
PLLNKLDDTE NASAYAANAG VDNRECISMD YKQTQLCLIG CKPPIGEHWG KGSPCTNVAV
NPGDCPPLEL INTVIQDGDM VDTGFGAMDF TTLQANKSEV PLDICTSICK YPDYIKMVSE
PYGDSLFFYL RREQMFVRHL FNRAGAVGEN VPDDLYIKGS GSTANLASSN YFPTPSGSMV
TSDAQIFNKP YWLQRAQGHN NGICWGNQLF VTVVDTTRST NMSLCAAIST SETTYKNTNF
KEYLRHGEEY DLQFIFQLCK ITLTADVMTY IHSMNSTILE DWNFGLQPPP GGTLEDTYRF
VTSQAIACQK HTPPAPKEDP LKKYTFWEVN LKEKFSADLD QFPLGRKFLL QAGLKAKPKF
TLGKRKATPT TSSTSTTAKR KKRKL
