O55777 · V_HENDH
- ProteinNon-structural protein V
- GeneP/V/C
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids457 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Blocks the type I interferon signaling pathway by interacting with host STAT1 and STAT2 and thereby inhibiting their phosphorylation and subsequent nuclear translocation. Efficiently blocks the type II interferon signaling pathway (By similarity).
Miscellaneous
The P/V/C gene has two overlapping open reading frames. One encodes the P/V/W proteins and the other the C protein.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 406 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 425 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 429 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 441 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 443 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 446 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 450 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 453 | Zn2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell | |
Cellular Component | host cell cytoplasm | |
Molecular Function | importin-alpha family protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | small GTPase binding | |
Biological Process | intracellular transport of virus | |
Biological Process | response to leptomycin B | |
Biological Process | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity | |
Biological Process | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity | |
Biological Process | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity | |
Biological Process | symbiont-mediated suppression of host type I interferon-mediated signaling pathway | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameNon-structural protein V
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Paramyxoviridae > Orthoparamyxovirinae > Henipavirus > Henipavirus hendraense
- Virus hosts
Accessions
- Primary accessionO55777
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000236014 | 1-457 | Non-structural protein V | ||
Modified residue | 257 | Phosphoserine; by host | |||
Modified residue | 350 | Phosphoserine; by host | |||
Keywords
- PTM
Interaction
Subunit
Interacts with host IFIH1/MDA5, DHX58/LGP2, STAT1 and STAT2.
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 26-104 | Disordered | |||
Compositional bias | 73-94 | Polar residues | |||
Region | 193-403 | Disordered | |||
Compositional bias | 293-314 | Basic and acidic residues | |||
Compositional bias | 340-354 | Basic and acidic residues | |||
Compositional bias | 360-377 | Polar residues | |||
Sequence similarities
Belongs to the paramyxoviruses V protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length457
- Mass (Da)50,648
- Last updated1998-06-01 v1
- Checksum15C63B4FF638587D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 73-94 | Polar residues | |||
Compositional bias | 293-314 | Basic and acidic residues | |||
Compositional bias | 340-354 | Basic and acidic residues | |||
Compositional bias | 360-377 | Polar residues | |||
RNA Editing
Edited at position 407
Partially edited. RNA editing at this position consists of an insertion of one or two guanine nucleotides. The sequence displayed here is the V protein, derived from the +1G edited RNA. The unedited RNA gives rise to the P protein (AC O55778), the +2G edited RNA gives rise to the W protein (AC P0C1C6)
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF010304 EMBL· GenBank· DDBJ | AAC04241.1 EMBL· GenBank· DDBJ | mRNA | ||
AF017149 EMBL· GenBank· DDBJ | AAC83189.1 EMBL· GenBank· DDBJ | Genomic RNA |