ID  Q89462;
PN  Nucleoprotein;
GN  N;
OS  1980491;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: Q89462;
DR  PDB: 2IC6;
DR  PDB: 2IC9;
DR  PDB: 5E05;
DR  PDB: 5E06;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000269|PubMed:15254200, ECO:0000269|PubMed:15650206, ECO:0000269|PubMed:16775315, ECO:0000269|PubMed:16971445, ECO:0000269|PubMed:18971945, ECO:0000269|PubMed:19047634, ECO:0000269|PubMed:20164193, ECO:0000269|PubMed:20844026, ECO:0000269|PubMed:21378500, ECO:0000269|PubMed:25062117, ECO:0000269|PubMed:27261891, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTLKEVQDNITLHEQQLVTARQKLKDAERAVELDPDDVNKSTLQSRRAAVSALETKLGELKRELADLIAAQKLASKPVD
SQ  PTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKSIGLYILSFALPIILKALYMLSTRGRQTIKENKGTRIRFK
SQ  DDSSYEEVNGIRKPRHLYVSMPTAQSTMKADEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFSFFVKDWMERIDDFL
SQ  AARCPFLPEQKDPRDAALATNRAYFITRQLQVDESKVSDIEDLIADARAESATIFADIATPHSVWVFACAPDRCPPTALY
SQ  VAGMPELGAFFAILQDMRNTIMASKSVGTSEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMSHWGREAVNHFHLGDD
SQ  MDPELRELAQTLVDIKVREISNQEPLKL
//