G9G843 · G9G843_9ADEN
- ProteinHexon-interlacing protein
- GeneIX
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids142 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Structural component of the virion that acts as a cement protein on the capsid exterior and forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons. 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.
Miscellaneous
This protein is only encoded by mastadenoviruses, and may therefore play a role in mammals tropism.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleus | |
Cellular Component | viral capsid, decoration | |
Molecular Function | hexon binding | |
Biological Process | symbiont entry into host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameHexon-interlacing protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Human mastadenovirus E
Accessions
- Primary accessionG9G843
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
Expression
Induction
Expressed in the intermediate phase of the viral replicative cycle.
Interaction
Subunit
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.
Family & Domains
Features
Showing features for coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 104-131 | |||||
Sequence: LLLLMAQLEALTQRLGELTQQVAQLQEQ |
Domain
Three N-terminal domains of hexon-interlacing protein form triskelions between hexon capsomers.
Sequence similarities
Belongs to the adenoviridae hexon-interlacing protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length142
- Mass (Da)14,459
- Last updated2012-02-22 v1
- ChecksumF4E6AFBB3B35C163
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JN254802 EMBL· GenBank· DDBJ | AEW43609.1 EMBL· GenBank· DDBJ | Genomic DNA |