Skip to main content

Domain

The N-terminus is important for viral particle assembly (PubMed:31009855). The oligomerization region is central (PubMed:15166449). The C-terminus part contains binding regions for the RNA-directed RNA polymerase L and the nucleoprotein (PubMed:26474524).

Function

Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (PubMed:25568210, PubMed:26474524). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (PubMed:26474524). Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA (PubMed:26474524). Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs (PubMed:25568210). Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (PubMed:29489893). Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (By similarity).

Post-translational modifications

Constitutively phosphorylated by host (PubMed:17098979). Phosphorylation at S-116, S-117, S-119, S-232 and S-237 is required for transcription inhibition by M2-2 and viral particle egress (PubMed:26474524). Phosphorylation at S-232 and S-237 increases the affinity of the binding to the nucleoprotein (PubMed:25407889).

Sequence similarities

Belongs to the pneumoviridae phosphoprotein P family.

Cellular localization

  • Virion
  • Host cytoplasm
  • Localizes in cytoplasmic inclusion bodies.

Alternative names

Phosphoprotein, Protein P, P

Target type

Proteins

Molecular weight

27148Da