UniProt functional annotation for P03418



	UniProt functional annotation for P03418

UniProt code: P03418.

Organism: Human respiratory syncytial virus A (strain A2).

Taxonomy: Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.

Function: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases (PubMed:23677789, PubMed:19965480, PubMed:31229488). RNA replication depends on the availability of soluble nucleoprotein (PubMed:9299631, PubMed:22623798). The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication (PubMed:22623798). Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (PubMed:32878896). May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs (PubMed:22623778). {ECO:0000269|PubMed:19965480, ECO:0000269|PubMed:22623778, ECO:0000269|PubMed:22623798, ECO:0000269|PubMed:23677789, ECO:0000269|PubMed:31229488, ECO:0000269|PubMed:32878896, ECO:0000269|PubMed:9299631}.

Subunit: Homomultimerizes to form the nucleocapsid (PubMed:23677789, PubMed:19965480). Binds to viral genomic RNA. Interacts (via N- terminus) with the phosphoprotein P (via C-terminus); the phosphorylated phosphoprotein P binds to N-RNA complex (PubMed:26474524, PubMed:17170452, PubMed:22623798, PubMed:25407889, PubMed:11861854, PubMed:12368320, PubMed:28031463). When in a monomeric RNA-free form, interacts with the phosphoprotein (via N-terminus) (PubMed:25568210, PubMed:30626736). Interacts with protein M2-1; this interaction allows the association of nucleocapsid with the matrix protein (PubMed:10846068). Interacts with host EIF2AK2/PKR; this interaction inhibits EIF2AK2 phosphorylation of EIF2S1 and blocks EIF2AK2-mediated translation shutoff (PubMed:20519500). Interacts with host EIF1AX; this interaction recruits EIF1AX to the viral replication complex to facilitate viral genomic RNA synthesis and virus production (PubMed:25479059). Interacts with host NF-kappa-B; this interation sequesters NF-kappa-B in inclusion bodies (By similarity). {ECO:0000250|UniProtKB:P22677, ECO:0000269|PubMed:10846068, ECO:0000269|PubMed:11861854, ECO:0000269|PubMed:12368320, ECO:0000269|PubMed:17170452, ECO:0000269|PubMed:19965480, ECO:0000269|PubMed:20519500, ECO:0000269|PubMed:22623798, ECO:0000269|PubMed:23677789, ECO:0000269|PubMed:25407889, ECO:0000269|PubMed:25479059, ECO:0000269|PubMed:25568210, ECO:0000269|PubMed:26474524, ECO:0000269|PubMed:28031463, ECO:0000269|PubMed:30626736}.

Subcellular location: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}.

Ptm: Tyrosine phosphorylation modulates viral transcription and replication. {ECO:0000269|PubMed:22019509}.

Similarity: Belongs to the paramyxoviruses nucleocapsid family. {ECO:0000305}.

Sequence caution: Sequence=CAA24906.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Human respiratory syncytial virus A (strain A2).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.



Function:		Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases (PubMed:23677789, PubMed:19965480, PubMed:31229488). RNA replication depends on the availability of soluble nucleoprotein (PubMed:9299631, PubMed:22623798). The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication (PubMed:22623798). Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (PubMed:32878896). May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs (PubMed:22623778). {ECO:0000269\|PubMed:19965480, ECO:0000269\|PubMed:22623778, ECO:0000269\|PubMed:22623798, ECO:0000269\|PubMed:23677789, ECO:0000269\|PubMed:31229488, ECO:0000269\|PubMed:32878896, ECO:0000269\|PubMed:9299631}.


Subunit:		Homomultimerizes to form the nucleocapsid (PubMed:23677789, PubMed:19965480). Binds to viral genomic RNA. Interacts (via N- terminus) with the phosphoprotein P (via C-terminus); the phosphorylated phosphoprotein P binds to N-RNA complex (PubMed:26474524, PubMed:17170452, PubMed:22623798, PubMed:25407889, PubMed:11861854, PubMed:12368320, PubMed:28031463). When in a monomeric RNA-free form, interacts with the phosphoprotein (via N-terminus) (PubMed:25568210, PubMed:30626736). Interacts with protein M2-1; this interaction allows the association of nucleocapsid with the matrix protein (PubMed:10846068). Interacts with host EIF2AK2/PKR; this interaction inhibits EIF2AK2 phosphorylation of EIF2S1 and blocks EIF2AK2-mediated translation shutoff (PubMed:20519500). Interacts with host EIF1AX; this interaction recruits EIF1AX to the viral replication complex to facilitate viral genomic RNA synthesis and virus production (PubMed:25479059). Interacts with host NF-kappa-B; this interation sequesters NF-kappa-B in inclusion bodies (By similarity). {ECO:0000250\|UniProtKB:P22677, ECO:0000269\|PubMed:10846068, ECO:0000269\|PubMed:11861854, ECO:0000269\|PubMed:12368320, ECO:0000269\|PubMed:17170452, ECO:0000269\|PubMed:19965480, ECO:0000269\|PubMed:20519500, ECO:0000269\|PubMed:22623798, ECO:0000269\|PubMed:23677789, ECO:0000269\|PubMed:25407889, ECO:0000269\|PubMed:25479059, ECO:0000269\|PubMed:25568210, ECO:0000269\|PubMed:26474524, ECO:0000269\|PubMed:28031463, ECO:0000269\|PubMed:30626736}.
Subcellular location:		Virion {ECO:0000305}. Host cytoplasm {ECO:0000269\|PubMed:17703289, ECO:0000269\|PubMed:32878896}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269\|PubMed:17703289, ECO:0000269\|PubMed:32878896}.
Ptm:		Tyrosine phosphorylation modulates viral transcription and replication. {ECO:0000269\|PubMed:22019509}.
Similarity:		Belongs to the paramyxoviruses nucleocapsid family. {ECO:0000305}.
Sequence caution:		Sequence=CAA24906.1; Type=Frameshift; Evidence={ECO:0000305};