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Protein

Penton protein

Gene

L2

Organism
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Clathrin-mediated endocytosis of virus by host, 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:
Penton protein
Short name:
CP-P
Alternative name(s):
Penton base protein
Protein III
Gene namesi
ORF Names:L2
OrganismiHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Taxonomic identifieri10515 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008167 Componenti: Genome

Subcellular locationi

  • Virion 1 Publication
  • Host nucleus 1 Publication

  • Note: Located at each vertex of the virion. Present in 60 copies per virion.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, T=25 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Penton proteinPRO_0000221872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei455 – 4551Phosphoserine; by host1 Publication

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP03276.

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with the fiber protein (via N-terminal tail region) (Probable). Interacts with the capsid vertex protein; this interaction binds the penton base to neighboring peripentonal hexons. Interacts (via the cell attachment site RGD) with host heterodimer ITGAV-ITGB5; this interaction promotes virus internalization. Interacts with host WWP1 and WWP2.Curated4 Publications

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni50 – 523Combined sources
Beta strandi55 – 573Combined sources
Beta strandi58 – 603Combined sources
Beta strandi69 – 735Combined sources
Helixi76 – 816Combined sources
Beta strandi82 – 854Combined sources
Beta strandi90 – 945Combined sources
Beta strandi99 – 1013Combined sources
Helixi103 – 1064Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi117 – 12913Combined sources
Turni136 – 1394Combined sources
Beta strandi141 – 15212Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi160 – 16910Combined sources
Helixi177 – 19418Combined sources
Turni195 – 2006Combined sources
Helixi203 – 2053Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi217 – 2204Combined sources
Turni221 – 2244Combined sources
Beta strandi235 – 2428Combined sources
Beta strandi247 – 2493Combined sources
Helixi255 – 2595Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi267 – 2693Combined sources
Beta strandi272 – 2743Combined sources
Helixi275 – 2773Combined sources
Beta strandi282 – 2843Combined sources
Helixi289 – 2946Combined sources
Turni349 – 3535Combined sources
Turni386 – 3883Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi399 – 4057Combined sources
Helixi406 – 4127Combined sources
Turni415 – 4173Combined sources
Helixi419 – 4224Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi436 – 4394Combined sources
Turni442 – 4443Combined sources
Helixi457 – 4593Combined sources
Beta strandi464 – 4674Combined sources
Beta strandi469 – 4757Combined sources
Helixi479 – 4824Combined sources
Helixi483 – 4853Combined sources
Beta strandi487 – 4893Combined sources
Turni495 – 4973Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi512 – 5198Combined sources
Beta strandi522 – 53110Combined sources
Beta strandi533 – 54210Combined sources
Beta strandi554 – 56815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9PX-ray3.30A49-571[»]
1X9TX-ray3.50A49-571[»]
2C6SX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O49-571[»]
2C9Felectron microscopy16.50A/B/C/D/E49-571[»]
2C9Gelectron microscopy9.30A/B/C/D/E49-571[»]
4V4Uelectron microscopy10.00A/B/C/D/E49-571[»]
ProteinModelPortaliP03276.
SMRiP03276. Positions 49-569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03276.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni336 – 34813DisorderedSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi340 – 3423Cell attachment siteSequence analysis

Domaini

The cell attachment RGD motif is exposed at the virion surface and is involved in binding to the integrin heterodimer ITGAV-ITGB5.

Sequence similaritiesi

Belongs to the adenoviridae penton family.Curated

Family and domain databases

InterProiIPR002605. Adeno_Penton_B.
[Graphical view]
PfamiPF01686. Adeno_Penton_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRAAMYEEG PPPSYESVVS AAPVAAALGS PFDAPLDPPF VPPRYLRPTG
60 70 80 90 100
GRNSIRYSEL APLFDTTRVY LVDNKSTDVA SLNYQNDHSN FLTTVIQNND
110 120 130 140 150
YSPGEASTQT INLDDRSHWG GDLKTILHTN MPNVNEFMFT NKFKARVMVS
160 170 180 190 200
RSLTKDKQVE LKYEWVEFTL PEGNYSETMT IDLMNNAIVE HYLKVGRQNG
210 220 230 240 250
VLESDIGVKF DTRNFRLGFD PVTGLVMPGV YTNEAFHPDI ILLPGCGVDF
260 270 280 290 300
THSRLSNLLG IRKRQPFQEG FRITYDDLEG GNIPALLDVD AYQASLKDDT
310 320 330 340 350
EQGGDGAGGG NNSGSGAEEN SNAAAAAMQP VEDMNDHAIR GDTFATRAEE
360 370 380 390 400
KRAEAEAAAE AAAPAAQPEV EKPQKKPVIK PLTEDSKKRS YNLISNDSTF
410 420 430 440 450
TQYRSWYLAY NYGDPQTGIR SWTLLCTPDV TCGSEQVYWS LPDMMQDPVT
460 470 480 490 500
FRSTSQISNF PVVGAELLPV HSKSFYNDQA VYSQLIRQFT SLTHVFNRFP
510 520 530 540 550
ENQILARPPA PTITTVSENV PALTDHGTLP LRNSIGGVQR VTITDARRRT
560 570
CPYVYKALGI VSPRVLSSRT F
Length:571
Mass (Da):63,255
Last modified:July 21, 1986 - v1
Checksum:iE9807342982B1BC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92211.1.
PIRiA03847. XZAD32.
RefSeqiAP_000170.1. AC_000007.1.
NP_040521.1. NC_001405.1.

Genome annotation databases

GeneIDi2652996.
KEGGivg:2652996.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with an ad2 N-terminal fiber peptide

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92211.1.
PIRiA03847. XZAD32.
RefSeqiAP_000170.1. AC_000007.1.
NP_040521.1. NC_001405.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9PX-ray3.30A49-571[»]
1X9TX-ray3.50A49-571[»]
2C6SX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O49-571[»]
2C9Felectron microscopy16.50A/B/C/D/E49-571[»]
2C9Gelectron microscopy9.30A/B/C/D/E49-571[»]
4V4Uelectron microscopy10.00A/B/C/D/E49-571[»]
ProteinModelPortaliP03276.
SMRiP03276. Positions 49-569.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP03276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652996.
KEGGivg:2652996.

Miscellaneous databases

EvolutionaryTraceiP03276.

Family and domain databases

InterProiIPR002605. Adeno_Penton_B.
[Graphical view]
PfamiPF01686. Adeno_Penton_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "DNA sequences from the adenovirus 2 genome."
    Roberts R.J., O'Neill K.E., Yen C.E.
    J. Biol. Chem. 259:13968-13975(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genes encoding the core proteins of adenovirus type 2."
    Alestroem P., Akusjaervi G., Lager M., Yeh-kai L., Pettersson U.
    J. Biol. Chem. 259:13980-13985(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-571.
  3. Cited for: PROTEIN SEQUENCE OF 453-473, PHOSPHORYLATION AT SER-455.
  4. "A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein."
    van Raaij M.J., Mitraki A., Lavigne G., Cusack S.
    Nature 401:935-938(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE FIBER PROTEIN.
  5. "Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases."
    Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.
    Biochemistry 41:14299-14305(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWP1 AND WWP2.
  6. "Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake."
    Meier O., Boucke K., Hammer S.V., Keller S., Stidwill R.P., Hemmi S., Greber U.F.
    J. Cell Biol. 158:1119-1131(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative cells."
    Lyle C., McCormick F.
    Virol. J. 7:148-148(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST ITGAV-ITGB5 HETERODIMER.
    Strain: Human adenovirus C serotype 5.
  8. "Latest insights on adenovirus structure and assembly."
    San Martin C.
    Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks."
    Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.
    Science 329:1038-1043(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CAPSID VERTEX PROTEIN.
    Strain: Human adenovirus C serotype 5.
  10. "The structure of the human adenovirus 2 penton."
    Zubieta C., Schoehn G., Chroboczek J., Cusack S.
    Mol. Cell 17:121-135(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 49-571.
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 49-571.
    Strain: Human adenovirus C serotype 5.
  12. "Structural and biochemical characterization of a human adenovirus 2/12 penton base chimera."
    Zubieta C., Blanchoin L., Cusack S.
    FEBS J. 273:4336-4345(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 49-571.

Entry informationi

Entry nameiCAPSP_ADE02
AccessioniPrimary (citable) accession number: P03276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.