UniProt functional annotation for P18272



	UniProt functional annotation for P18272

UniProt code: P18272.

Organism: Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).

Taxonomy: Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.

Function: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:26119732, PubMed:25865894, PubMed:30333622, PubMed:16719918). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:26119732, PubMed:25865894). Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released (PubMed:29144446). The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm (PubMed:22247782). Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid (PubMed:30333622). Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription (PubMed:29290611, PubMed:27755595). Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1 (PubMed:28794491, PubMed:30301857). {ECO:0000269|PubMed:16719918, ECO:0000269|PubMed:22247782, ECO:0000269|PubMed:25865894, ECO:0000269|PubMed:26119732, ECO:0000269|PubMed:27755595, ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29144446, ECO:0000269|PubMed:29290611, ECO:0000269|PubMed:30301857, ECO:0000269|PubMed:30333622}.

Subunit: Homooligomer. Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. Interacts with VP35 and VP30 to form the nucleocapsid (PubMed:12191476, PubMed:26119732, PubMed:25865894, PubMed:25910597, PubMed:27755595). Interacts with host PPP2R5C; this interaction leads to VP30 dephosphorylation and viral transcription (PubMed:29290611). Interacts with VP24; this interaction facilitates nucleocapsid assembly and genome packaging (PubMed:12191476, PubMed:28794491, PubMed:29144446, PubMed:29339477). Interacts with matrix protein VP40; this interaction allows recruitment of the nucleocapsid into progeny virions (PubMed:17229682). Interacts with host STAU1 (PubMed:30301857). Interacts with host NXF1 (via RNA-binding domain); this interaction recruits NXF1 to the inclusion bodies were viral replication takes place, probably to export viral mRNA-NXF1 complexes from these sites (PubMed:31940815). {ECO:0000269|PubMed:12191476, ECO:0000269|PubMed:17229682, ECO:0000269|PubMed:25865894, ECO:0000269|PubMed:25910597, ECO:0000269|PubMed:26119732, ECO:0000269|PubMed:27755595, ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29144446, ECO:0000269|PubMed:29290611, ECO:0000269|PubMed:29339477, ECO:0000269|PubMed:30301857, ECO:0000269|PubMed:31940815}.

Subcellular location: Virion {ECO:0000269|PubMed:16719918}. Host cytoplasm {ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29290611}.

Domain: Comprizes a N-terminal arm involved in oligomerization, a NP core region involved in RNA binding, a disordered region follwoed by a C-terminal tail involved in protein-protein interactions (PubMed:25865894, PubMed:30333622). During oligomerization, NP N- terminal arm binds to a neighbor NP thereby displacing VP35 bound to monomeric NP (PubMed:30333622). {ECO:0000269|PubMed:25865894, ECO:0000269|PubMed:30333622}.

Ptm: Phosphorylated by host. {ECO:0000269|PubMed:16571791}.

Ptm: O-glycosylated by host. {ECO:0000269|PubMed:16571791}.

Ptm: Acetylated by host EP300 in vitro. {ECO:0000269|PubMed:30205953}.

Similarity: Belongs to the filoviruses nucleoprotein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.



Function:		Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:26119732, PubMed:25865894, PubMed:30333622, PubMed:16719918). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:26119732, PubMed:25865894). Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released (PubMed:29144446). The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm (PubMed:22247782). Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid (PubMed:30333622). Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription (PubMed:29290611, PubMed:27755595). Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1 (PubMed:28794491, PubMed:30301857). {ECO:0000269\|PubMed:16719918, ECO:0000269\|PubMed:22247782, ECO:0000269\|PubMed:25865894, ECO:0000269\|PubMed:26119732, ECO:0000269\|PubMed:27755595, ECO:0000269\|PubMed:28794491, ECO:0000269\|PubMed:29144446, ECO:0000269\|PubMed:29290611, ECO:0000269\|PubMed:30301857, ECO:0000269\|PubMed:30333622}.


Subunit:		Homooligomer. Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. Interacts with VP35 and VP30 to form the nucleocapsid (PubMed:12191476, PubMed:26119732, PubMed:25865894, PubMed:25910597, PubMed:27755595). Interacts with host PPP2R5C; this interaction leads to VP30 dephosphorylation and viral transcription (PubMed:29290611). Interacts with VP24; this interaction facilitates nucleocapsid assembly and genome packaging (PubMed:12191476, PubMed:28794491, PubMed:29144446, PubMed:29339477). Interacts with matrix protein VP40; this interaction allows recruitment of the nucleocapsid into progeny virions (PubMed:17229682). Interacts with host STAU1 (PubMed:30301857). Interacts with host NXF1 (via RNA-binding domain); this interaction recruits NXF1 to the inclusion bodies were viral replication takes place, probably to export viral mRNA-NXF1 complexes from these sites (PubMed:31940815). {ECO:0000269\|PubMed:12191476, ECO:0000269\|PubMed:17229682, ECO:0000269\|PubMed:25865894, ECO:0000269\|PubMed:25910597, ECO:0000269\|PubMed:26119732, ECO:0000269\|PubMed:27755595, ECO:0000269\|PubMed:28794491, ECO:0000269\|PubMed:29144446, ECO:0000269\|PubMed:29290611, ECO:0000269\|PubMed:29339477, ECO:0000269\|PubMed:30301857, ECO:0000269\|PubMed:31940815}.
Subcellular location:		Virion {ECO:0000269\|PubMed:16719918}. Host cytoplasm {ECO:0000269\|PubMed:28794491, ECO:0000269\|PubMed:29290611}.
Domain:		Comprizes a N-terminal arm involved in oligomerization, a NP core region involved in RNA binding, a disordered region follwoed by a C-terminal tail involved in protein-protein interactions (PubMed:25865894, PubMed:30333622). During oligomerization, NP N- terminal arm binds to a neighbor NP thereby displacing VP35 bound to monomeric NP (PubMed:30333622). {ECO:0000269\|PubMed:25865894, ECO:0000269\|PubMed:30333622}.
Ptm:		Phosphorylated by host. {ECO:0000269\|PubMed:16571791}.
Ptm:		O-glycosylated by host. {ECO:0000269\|PubMed:16571791}.
Ptm:		Acetylated by host EP300 in vitro. {ECO:0000269\|PubMed:30205953}.
Similarity:		Belongs to the filoviruses nucleoprotein family. {ECO:0000305}.