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P12538 (CAPSP_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penton protein

Short name=CP-P
Alternative name(s):
Penton base protein
Protein III
Gene names
ORF Names:L2
OrganismHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) [Complete proteome]
Taxonomic identifier28285 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

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

General annotation (Comments)

Function

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. Ref.4 Ref.6

Subunit structure

Interacts (via the cell attachment site RGD) with host heterodimer ITGAV-ITGB5; this interaction promotes virus internalization. Interacts with host WWP1 and WWP2 By similarity. 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. Ref.4 Ref.6

Subcellular location

Virion. Host nucleus Probable. Note: Located at each vertex of the virion. Present in 60 copies per virion. Ref.6

Induction

Expressed in the late phase of the viral replicative cycle.

Domain

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

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 By similarity.

Sequence similarities

Belongs to the adenoviridae penton family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Penton protein
PRO_0000221873

Regions

Region336 – 34813Disordered Potential
Motif340 – 3423Cell attachment site Potential

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P12538 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 89D77207F2786802

FASTA57163,293
        10         20         30         40         50         60 
MRRAAMYEEG 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 RLPTKDNQVE 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 
EQGGGGAGGS NSSGSGAEEN 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 FRSTRQISNF PVVGAELLPV HSKSFYNDQA 

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

       550        560        570 
VTITDARRRT CPYVYKALGI VSPRVLSSRT F 

« Hide

References

[1]"Determination of the nucleotide sequence for the penton-base gene of human adenovirus type 5."
Neumann R., Chroboczek J., Jacrot B.
Gene 69:153-157(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
Chroboczek J., Bieber F., Jacrot B.
Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"De novo derivation of proteomes from transcriptomes for transcript and protein identification."
Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.
Nat. Methods 9:1207-1211(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-571.
[4]"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.
[5]"A quasi-atomic model of human adenovirus type 5 capsid."
Fabry C.M., Rosa-Calatrava M., Conway J.F., Zubieta C., Cusack S., Ruigrok R.W., Schoehn G.
EMBO J. 24:1645-1654(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 49-571.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. No translation available.
M22141 Genomic DNA. Translation: AAA42519.1.
PIRXZADH5. JT0337.
RefSeqAP_000206.1. AC_000008.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VSZX-ray3.50N1-571[»]
3IYNelectron microscopy-M1-571[»]
3IZOelectron microscopy-A/B/C/D/E1-571[»]
ProteinModelPortalP12538.
SMRP12538. Positions 49-569.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Other

EvolutionaryTraceP12538.

Entry information

Entry nameCAPSP_ADE05
AccessionPrimary (citable) accession number: P12538
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references