Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P24936 (CAP8_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 47. 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:
Pre-hexon-linking protein
Alternative name(s):
Pre-protein VIII
Short name=pVIII

Cleaved into the following 2 chains:

  1. Hexon-linking protein-N
    Alternative name(s):
    12.1 kDa protein VIII
    Protein VIII-N
  2. Hexon-linking protein-C
    Alternative name(s):
    7.6 kDa protein VIII
    Protein VIII-C
Gene names
ORF Names:L4
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 length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hexon-linking protein: Structural component of the virion that lashes peripentonal hexons to the hexons situated in the facets thanks to its interaction with the capsid vertex protein. Also binds together hexons of different facets. Ref.5

Subunit structure

Interacts with the capsid vertex protein; this interaction allows tethering of the hexons surrounding the penton base to those situated in the central plate of the facet. Interacts with hexon protein; this interaction lashes hexons together, each copy of hexon-linking protein being bound to 4 hexon trimers. Ref.5

Subcellular location

Pre-hexon-linking protein: Host nucleus Probable Ref.5.

Hexon-linking protein-N: Virion. Note: Located on the inner side of the capsid shell. Present in around 120 copies per virion. Ref.5

Hexon-linking protein-C: Virion. Note: Located on the inner side of the capsid shell. Present in around 120 copies per virion. Ref.5

Induction

Expressed in the late phase of the viral replicative cycle.

Post-translational modification

Cleaved by the viral protease during virion maturation causing the middle segment to be shed from the capsid Probable.

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 hexon-linking protein family.

Ontologies

Keywords
   Cellular componentCapsid protein
Host nucleus
Virion
   Developmental stageLate protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Pre-hexon-linking protein
PRO_0000421131
Peptide1 – 111111Hexon-linking protein-N Potential
PRO_0000036495
Propeptide112 – 15746 Potential
PRO_0000421132
Peptide158 – 22770Hexon-linking protein-C Potential
PRO_0000036496

Sites

Site111 – 1122Cleavage; by viral protease Potential
Site131 – 1322Cleavage; by viral protease Potential
Site157 – 1582Cleavage; by viral protease Potential

Amino acid modifications

Modified residue641Phosphothreonine; by host By similarity
Modified residue1181Phosphoserine; by host By similarity
Modified residue1741Phosphoserine; by host By similarity

Experimental info

Sequence conflict1601P → S no nucleotide entry Ref.2

Secondary structure

.......... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24936 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: C1CACF31E6F5E5D5

FASTA22724,687
        10         20         30         40         50         60 
MSKEIPTPYM WSYQPQMGLA AGAAQDYSTR INYMSAGPHM ISRVNGIRAH RNRILLEQAA 

        70         80         90        100        110        120 
ITTTPRNNLN PRSWPAALVY QESPAPTTVV LPRDAQAEVQ MTNSGAQLAG GFRHRVRSPG 

       130        140        150        160        170        180 
QGITHLTIRG RGIQLNDESV SSSLGLRPDG TFQIGGAGRP SFTPRQAILT LQTSSSEPRS 

       190        200        210        220 
GGIGTLQFIE EFVPSVYFNP FSGPPGHYPD QFIPNFDAVK DSADGYD 

« Hide

References

[1]"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].
[2]"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].
[3]"Latest insights on adenovirus structure and assembly."
San Martin C.
Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[4]"Visualization of alpha-helices in a 6-angstrom resolution cryoelectron microscopy structure of adenovirus allows refinement of capsid protein assignments."
Saban S.D., Silvestry M., Nemerow G.R., Stewart P.L.
J. Virol. 80:12049-12059(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE VIRAL PARTICLE, PROTEOLYTIC PROCESSING.
[5]"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, PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CAPSID VERTEX PROTEIN AND HEXON PROTEIN.
[6]"Crystal structure of human adenovirus at 3.5 A resolution."
Reddy V.S., Natchiar S.K., Stewart P.L., Nemerow G.R.
Science 329:1071-1075(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. Translation: AAA96413.1.
PIRSXAD85. E39449.
RefSeqAP_000217.1. AC_000008.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VSZX-ray3.50R/S1-227[»]
3IYNelectron microscopy-O/P1-227[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000646. Adeno_PVIII.
[Graphical view]
PfamPF01310. Adeno_PVIII. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24936.

Entry information

Entry nameCAP8_ADE05
AccessionPrimary (citable) accession number: P24936
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 3, 2013
This is version 47 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