A0A5J6AAY5 · A0A5J6AAY5_RUBV
- ProteinStructural polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1063 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells.
Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement.
Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell Golgi membrane | |
Cellular Component | host cell mitochondrion | |
Cellular Component | membrane | |
Cellular Component | T=4 icosahedral viral capsid | |
Cellular Component | viral envelope | |
Cellular Component | viral nucleocapsid | |
Cellular Component | virion membrane | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Biological Process | clathrin-dependent endocytosis of virus by host cell | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | virion attachment to host cell |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameStructural polyprotein
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Hepelivirales > Matonaviridae > Rubivirus > Rubivirus rubellae
Accessions
- Primary accessionA0A5J6AAY5
Subcellular Location
UniProt Annotation
GO Annotation
Host Golgi apparatus membrane ; Single-pass type I membrane protein
Virion membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 1032-1056 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Heterodimer with spike glycoprotein E1.
Heterodimer with spike glycoprotein E2.
Homodimer; further assembles into homooligomer. Interacts with human C1QBP. Interacts (via N-terminus) with protease/methyltransferase p150.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | |||
Region | 1-131 | Disordered | |||
Compositional bias | 37-62 | Basic and acidic residues | |||
Domain | 301-567 | Rubella membrane glycoprotein E2 | |||
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,063
- Mass (Da)114,898
- Last updated2019-12-11 v1
- ChecksumE074EED4F006E583
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | |||
Compositional bias | 37-62 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MK787188 EMBL· GenBank· DDBJ | QBZ96522.1 EMBL· GenBank· DDBJ | Genomic RNA |