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P03276 (PEN3_ADE02) Reviewed, UniProtKB/Swiss-Prot

Last modified April 5, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Penton protein
Alternative name(s):
Penton base protein
Virion component III
pIII
Gene names
Name:PIII
OrganismHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) [Complete proteome]
Taxonomic identifier10515 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in virus clathrin-mediated internalization through the binding to host integrin heterodimer alphaV-beta5 (ITGAV-ITGB5). In primary receptor (CXADR)-negative cells, also mediates virus attachment to host cell By similarity. Binding to integrins ITGAV-ITGB5 also seems to be linked to macropinocytosis uptake of the virus. Ref.4

Subunit structure

Interacts with host WWP1 and WWP2. Interacts (via cell attachment site RGD) with host heterodimer ITGAV-ITGB5 By similarity. Ref.3

Sequence similarities

Belongs to the adenoviridae pIII family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Penton protein
PRO_0000221872

Regions

Motif340 – 3423Cell attachment site Potential

Secondary structure

1 ........................................................................................ 571
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03276 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E9807342982B1BC7

FASTA57163,255
        10         20         30         40         50         60 
MQRAAMYEEG PPPSYESVVS AAPVAAALGS PFDAPLDPPF VPPRYLRPTG GRNSIRYSEL 

        70         80         90        100        110        120 
APLFDTTRVY LVDNKSTDVA SLNYQNDHSN FLTTVIQNND YSPGEASTQT INLDDRSHWG 

       130        140        150        160        170        180 
GDLKTILHTN MPNVNEFMFT NKFKARVMVS RSLTKDKQVE LKYEWVEFTL PEGNYSETMT 

       190        200        210        220        230        240 
IDLMNNAIVE HYLKVGRQNG VLESDIGVKF DTRNFRLGFD PVTGLVMPGV YTNEAFHPDI 

       250        260        270        280        290        300 
ILLPGCGVDF THSRLSNLLG IRKRQPFQEG FRITYDDLEG GNIPALLDVD AYQASLKDDT 

       310        320        330        340        350        360 
EQGGDGAGGG NNSGSGAEEN SNAAAAAMQP VEDMNDHAIR GDTFATRAEE KRAEAEAAAE 

       370        380        390        400        410        420 
AAAPAAQPEV EKPQKKPVIK PLTEDSKKRS YNLISNDSTF TQYRSWYLAY NYGDPQTGIR 

       430        440        450        460        470        480 
SWTLLCTPDV TCGSEQVYWS LPDMMQDPVT FRSTSQISNF PVVGAELLPV HSKSFYNDQA 

       490        500        510        520        530        540 
VYSQLIRQFT SLTHVFNRFP ENQILARPPA PTITTVSENV PALTDHGTLP LRNSIGGVQR 

       550        560        570 
VTITDARRRT CPYVYKALGI VSPRVLSSRT F

« Hide

References

[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: 6334081] [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: 6094534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-571.
[3]"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: 12450395] [Abstract]
Cited for: INTERACTION WITH WWP1 AND WWP2.
[4]"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: 12221069] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01917 Genomic DNA. Translation: AAA92211.1.
PIRXZAD32. A03847.
RefSeqAP_000170.1. AC_000007.1.
NP_040521.1. NC_001405.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9PX-ray3.30A49-571[»]
1X9TX-ray3.50A49-571[»]
2BLDelectron microscopy10.00A/B/C/D/E49-571[»]
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[»]
ProteinModelPortalP03276.
SMRP03276. Positions 49-569.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2652996.

Phylogenomic databases

ProtClustDBCLSP2513879.

Family and domain databases

InterProIPR002605. Adeno_Penton_B.
[Graphical view]
PfamPF01686. Adeno_Penton_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEN3_ADE02
AccessionPrimary (citable) accession number: P03276
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 5, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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