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Protein

Major capsid protein L1

Gene

L1

Organism
Human papillomavirus type 16
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2.UniRule annotation3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Major capsid protein L1UniRule annotation
Gene namesi
Name:L1UniRule annotation
OrganismiHuman papillomavirus type 16
Taxonomic identifieri333760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009251 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • Host nucleus UniRule annotation

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • T=7 icosahedral viral capsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, T=7 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Major capsid protein L1PRO_0000133500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi175 – 175Interchain (with C-428)UniRule annotation1 Publication
Disulfide bondi428 – 428Interchain (with C-175)UniRule annotation1 Publication

Post-translational modificationi

ISGylated by host HERC5, this results in dominant-negative effect on virus infectivity.1 Publication

Keywords - PTMi

Disulfide bond, Ubl conjugation

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Self-assembles into homopentamers. The capsid has an icosahedral symmetry and consists of 72 capsomers, with each capsomer being a pentamer of L1. Interacts with the minor capsid protein L2; this interaction is necessary for viral genome encapsidation. Interacts with protein E2; this interaction enhances E2-dependent replication and transcription activation (PubMed:25911730). Interacts with host KPNA2; this interaction mediates the nuclear localization of L1 capsomers (PubMed:11971900). Interacts with host ITGA6 (PubMed:11341777). Interacts with host SDC1; this interaction promotes efficient infection of keratinocytes (PubMed:26289843).UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA2P522923EBI-7362698,EBI-349938From a different organism.
KPNB1Q149742EBI-7362698,EBI-286758From a different organism.

Protein-protein interaction databases

IntActiP03101. 3 interactions.
MINTiMINT-255544.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Beta strandi29 – 3810Combined sources
Beta strandi42 – 509Combined sources
Beta strandi55 – 573Combined sources
Beta strandi60 – 623Combined sources
Beta strandi71 – 766Combined sources
Turni80 – 823Combined sources
Turni93 – 953Combined sources
Beta strandi96 – 10914Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi125 – 1284Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi153 – 16210Combined sources
Beta strandi165 – 1717Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi188 – 1947Combined sources
Helixi210 – 2134Combined sources
Helixi222 – 2254Combined sources
Beta strandi229 – 2324Combined sources
Helixi234 – 2396Combined sources
Beta strandi247 – 2548Combined sources
Beta strandi256 – 2638Combined sources
Helixi273 – 2753Combined sources
Turni281 – 2844Combined sources
Beta strandi291 – 2966Combined sources
Turni302 – 3043Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi322 – 3243Combined sources
Helixi325 – 3273Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi342 – 3487Combined sources
Helixi357 – 3593Combined sources
Beta strandi360 – 38223Combined sources
Helixi385 – 39410Combined sources
Helixi397 – 4015Combined sources
Helixi414 – 42512Combined sources
Turni440 – 4434Combined sources
Beta strandi447 – 4504Combined sources
Helixi459 – 4613Combined sources
Helixi463 – 47210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZLX-ray3.50A1-505[»]
3J6Relectron microscopy9.10A/B/C/D/E/F9-486[»]
3J7Gelectron microscopy13.60A/B/C/D/E21-474[»]
3J8Velectron microscopy13.90A/B/C/D/E21-474[»]
3J8Welectron microscopy13.00A/B/C/D/E21-474[»]
3J8Zelectron microscopy14.00A/B/C/D/E21-474[»]
3JBAelectron microscopy12.00A/B/C/D/E/F9-486[»]
ProteinModelPortaliP03101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03101.

Family & Domainsi

Sequence similaritiesi

Belongs to the papillomaviridae L1 protein family.UniRule annotation

Phylogenomic databases

KOiK19260.

Family and domain databases

Gene3Di2.60.175.20. 1 hit.
HAMAPiMF_04002. PPV_L1.
InterProiIPR002210. Capsid_L1_Papillomavir.
IPR011222. dsDNA_vir_gr_I_capsid.
[Graphical view]
PfamiPF00500. Late_protein_L1. 1 hit.
[Graphical view]
PRINTSiPR00865. HPVCAPSIDL1.
SUPFAMiSSF88648. SSF88648. 1 hit.

Sequencei

Sequence statusi: Complete.

P03101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLWLPSEAT VYLPPVPVSK VVSTDEYVAR TNIYYHAGTS RLLAVGHPYF
60 70 80 90 100
PIKKPNNNKI LVPKVSGLQY RVFRIHLPDP NKFGFPDTSF YNPDTQRLVW
110 120 130 140 150
ACVGVEVGRG QPLGVGISGH PLLNKLDDTE NASAYAANAG VDNRECISMD
160 170 180 190 200
YKQTQLCLIG CKPPIGEHWG KGSPCTNVAV NPGDCPPLEL INTVIQDGDM
210 220 230 240 250
VDTGFGAMDF TTLQANKSEV PLDICTSICK YPDYIKMVSE PYGDSLFFYL
260 270 280 290 300
RREQMFVRHL FNRAGAVGEN VPDDLYIKGS GSTANLASSN YFPTPSGSMV
310 320 330 340 350
TSDAQIFNKP YWLQRAQGHN NGICWGNQLF VTVVDTTRST NMSLCAAIST
360 370 380 390 400
SETTYKNTNF KEYLRHGEEY DLQFIFQLCK ITLTADVMTY IHSMNSTILE
410 420 430 440 450
DWNFGLQPPP GGTLEDTYRF VTSQAIACQK HTPPAPKEDP LKKYTFWEVN
460 470 480 490 500
LKEKFSADLD QFPLGRKFLL QAGLKAKPKF TLGKRKATPT TSSTSTTAKR

KKRKL
Length:505
Mass (Da):56,278
Last modified:January 20, 2016 - v3
Checksum:iD426CEC3DCE6B0E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021D → H in AAA46943 (PubMed:2990099).Curated
Sequence conflicti266 – 2661A → T in AAA46943 (PubMed:2990099).Curated
Sequence conflicti423 – 4231Missing in AAA46943 (PubMed:2990099).Curated
Sequence conflicti439 – 4391D → DD in AAA46943 (PubMed:2990099).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46943.1.
AF001600 Genomic DNA. Translation: AAC31789.1.
AF125673 Genomic DNA. Translation: AAD33259.1.
AF536179 Genomic DNA. Translation: AAQ10719.1.
M96285 Genomic DNA. Translation: AAA47024.1.
A06331 Unassigned DNA. Translation: CAA00546.1.
PIRiA03640. P1WLHS.
RefSeqiNP_041332.1. NC_001526.2.

Genome annotation databases

GeneIDi1489082.
KEGGivg:1489082.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46943.1.
AF001600 Genomic DNA. Translation: AAC31789.1.
AF125673 Genomic DNA. Translation: AAD33259.1.
AF536179 Genomic DNA. Translation: AAQ10719.1.
M96285 Genomic DNA. Translation: AAA47024.1.
A06331 Unassigned DNA. Translation: CAA00546.1.
PIRiA03640. P1WLHS.
RefSeqiNP_041332.1. NC_001526.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZLX-ray3.50A1-505[»]
3J6Relectron microscopy9.10A/B/C/D/E/F9-486[»]
3J7Gelectron microscopy13.60A/B/C/D/E21-474[»]
3J8Velectron microscopy13.90A/B/C/D/E21-474[»]
3J8Welectron microscopy13.00A/B/C/D/E21-474[»]
3J8Zelectron microscopy14.00A/B/C/D/E21-474[»]
3JBAelectron microscopy12.00A/B/C/D/E/F9-486[»]
ProteinModelPortaliP03101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03101. 3 interactions.
MINTiMINT-255544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489082.
KEGGivg:1489082.

Phylogenomic databases

KOiK19260.

Miscellaneous databases

EvolutionaryTraceiP03101.

Family and domain databases

Gene3Di2.60.175.20. 1 hit.
HAMAPiMF_04002. PPV_L1.
InterProiIPR002210. Capsid_L1_Papillomavir.
IPR011222. dsDNA_vir_gr_I_capsid.
[Graphical view]
PfamiPF00500. Late_protein_L1. 1 hit.
[Graphical view]
PRINTSiPR00865. HPVCAPSIDL1.
SUPFAMiSSF88648. SSF88648. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequences and further characterization of human papillomavirus DNA present in the CaSki, SiHa and HeLa cervical carcinoma cell lines."
    Meissner J.D.
    J. Gen. Virol. 80:1725-1733(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Establishment of the human papillomavirus type 16 (HPV-16) life cycle in an immortalized human foreskin keratinocyte cell line."
    Flores E.R., Allen-Hoffmann B.L., Lee D., Sattler C.A., Lambert P.F.
    Virology 262:344-354(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning and sequencing of non-European human papillomavirus (HPV) variant complete genomes from cervicovaginal cells by an overlapping PCR method."
    Terai M., Fu L., Ma Z., Burk R.D.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Isolate European German 131.
  5. "Phylogenetic analysis of 48 papillomavirus types and 28 subtypes and variants: a showcase for the molecular evolution of DNA viruses."
    Chan S.-Y., Bernard H.U., Ong C.K., Chan S.P., Birgit H., Delius H.
    J. Virol. 66:5714-5725(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-345.
  6. "Human papillomavirus type 16 capsid proteins produced from recombinant Semliki Forest virus assemble into virus-like particles."
    Heino P., Dillner J., Schwartz S.
    Virology 214:349-359(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "alpha(6) Integrin is the main receptor of human papillomavirus type 16 VLP."
    Yoon C.S., Kim K.D., Park S.N., Cheong S.W.
    Biochem. Biophys. Res. Commun. 283:668-673(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST ITGA6.
  8. "Nuclear import strategies of high risk HPV16 L1 major capsid protein."
    Nelson L.M., Rose R.C., Moroianu J.
    J. Biol. Chem. 277:23958-23964(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST KPNA2.
  9. "Atomic model of the papillomavirus capsid."
    Modis Y., Trus B.L., Harrison S.C.
    EMBO J. 21:4754-4762(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  10. "The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15."
    Durfee L.A., Lyon N., Seo K., Huibregtsesend J.M.
    Mol. Cell 38:722-732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.
  11. "Identification of the nuclear localization signal of human papillomavirus type 16 L1 protein."
    Zhou J., Doorbar J., Sun X.Y., Crawford L.V., McLean C.S., Frazer I.H.
    Virology 185:625-632(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR LOCALIZATION SIGNAL.
  12. "Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells."
    Bousarghin L., Touze A., Sizaret P.Y., Coursaget P.
    J. Virol. 77:3846-3850(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Interaction of human papillomavirus type 16 particles with heparan sulfate and syndecan-1 molecules in the keratinocyte extracellular matrix plays an active role in infection."
    Surviladze Z., Sterkand R.T., Ozbun M.A.
    J. Gen. Virol. 96:2232-2241(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST SDC1.
  14. "The human papillomavirus type 16 L1 protein directly interacts with E2 and enhances E2-dependent replication and transcription activation."
    Siddiqa A., Leon K.C., James C.D., Bhatti M.F., Roberts S., Parish J.L.
    J. Gen. Virol. 96:2274-2285(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN E2.
  15. "Extent of protein-protein interactions and quasi-equivalence in viral capsids."
    Shepherd C.M., Reddy V.S.
    Proteins 58:472-477(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-505.

Entry informationi

Entry nameiVL1_HPV16
AccessioniPrimary (citable) accession number: P03101
Secondary accession number(s): O00530
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 20, 2016
Last modified: May 11, 2016
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.