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

P03281 (CAP9_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:
Hexon-interlacing protein
Alternative name(s):
Protein IX
Gene names
ORF Names:IX
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 length140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Structural component of the virion that presumably stabilizes the groups of hexons but is dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus. Ref.5

Subunit structure

Homotrimer. Interacts with hexon protein; this interaction tethers the hexons together. Self-interacts with adjacent proteins. Interacts with kinesin light chain KLC1; this interaction leads to capsid disruption at the nuclear pore complex during virus entry into host cell. Ref.5

Subcellular location

Virion. Host nucleus Probable. Note: Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion. Ref.5

Induction

Expressed in the intermediate phase of the viral replicative cycle.

Domain

Three N-terminal domains of hexon-interlacing protein form triskelions between hexon capsomers.

Miscellaneous

This protein is only encoded by mastadenoviruses, and may therefore play a role in mammals tropism.

Sequence similarities

Belongs to the adenoviridae hexon-interlacing protein family.

Ontologies

Keywords
   Biological processHost-virus interaction
Virus entry into host cell
   Cellular componentCapsid protein
Host nucleus
Virion
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processviral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 140140Hexon-interlacing protein
PRO_0000221846

Regions

Coiled coil97 – 13337 Potential

Amino acid modifications

Modified residue1351Phosphoserine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P03281 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DAFD4045CAB616FB

FASTA14014,458
        10         20         30         40         50         60 
MSTNSFDGSI VSSYLTTRMP PWAGVRQNVM GSSIDGRPVL PANSTTLTYE TVSGTPLETA 

        70         80         90        100        110        120 
ASAAASAAAA TARGIVTDFA FLSPLASSAA SRSSARDDKL TALLAQLDSL TRELNVVSQQ 

       130        140 
LLDLRQQVSA LKASSPPNAV 

« Hide

References

[1]"The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens starting at different AUG triplets."
Bos J.L., Polder L.J., Bernards R., Schrier P.I., van den Elsen P.J., van der Eb A.J., van Ormondt H.
Cell 27:121-131(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of adenovirus type 5 early region E1: the region between map positions 8.0 (HindIII site) and 11.8 (SmaI site)."
Maat J., van Beveren C.P., van Ormondt H.
Gene 10:27-38(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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].
[4]"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].
[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, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEXON PROTEIN.
[6]"Latest insights on adenovirus structure and assembly."
San Martin C.
Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. No translation available.
X02996 Genomic DNA. Translation: CAA26746.1.
PIRSXAD95. A03853.
RefSeqAP_000200.1. AC_000008.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-Q/R/S/T1-140[»]
ProteinModelPortalP03281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29895N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005641. Hexon_assoc_IX.
[Graphical view]
PfamPF03955. Adeno_PIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03281.

Entry information

Entry nameCAP9_ADE05
AccessionPrimary (citable) accession number: P03281
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 53 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