ID NCAP_I96A3 Reviewed; 498 AA. AC Q07FI1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 08-NOV-2023, entry version 60. DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04070}; DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04070}; DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04070}; GN Name=NP {ECO:0000255|HAMAP-Rule:MF_04070}; OS Influenza A virus (strain A/China:Nanchang/11/1996 H1N1). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=394786; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y., RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.; RT "The NIAID influenza genome sequencing project."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RG The NIAID Influenza Genome Sequencing Consortium; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Encapsidates the negative strand viral RNA, protecting it CC from nucleases. The encapsidated genomic RNA is termed the CC ribonucleoprotein (RNP) and serves as template for transcription and CC replication. The RNP needs to be localized in the host nucleus to start CC an infectious cycle, but is too large to diffuse through the nuclear CC pore complex. NP comprises at least 2 nuclear localization signals that CC are responsible for the active RNP import into the nucleus through CC cellular importin alpha/beta pathway. Later in the infection, nclear CC export of RNPs are mediated through viral proteins NEP interacting with CC M1 which binds nucleoproteins. It is possible that nucleoprotein binds CC directly host exportin-1/XPO1 and plays an active role in RNPs nuclear CC export. M1 interaction with RNP seems to hide nucleoprotein's nuclear CC localization signals. Soon after a virion infects a new cell, M1 CC dissociates from the RNP under acidification of the virion driven by M2 CC protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear CC localization signals, targeting the RNP to the nucleus. CC {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind host CC exportin-1/XPO1. Binds to viral genomic RNA. Protein-RNA contacts are CC mediated by a combination of electrostatic interactions between CC positively charged residues and the phosphate backbone and planar CC interactions between aromatic side chains and bases. CC {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host CC nucleus {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- PTM: Late in virus-infected cells, may be cleaved from a 56-kDa protein CC to a 53-kDa protein by a cellular caspase. This cleavage might be a CC marker for the onset of apoptosis in infected cells or have a specific CC function in virus host interaction. {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family. CC {ECO:0000255|HAMAP-Rule:MF_04070}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CY016239; ABI95265.1; -; Other_RNA. DR PDB; 4NQX; X-ray; 2.00 A; M/N/O/P/Q/R=44-52. DR PDBsum; 4NQX; -. DR SMR; Q07FI1; -. DR PRO; PR:Q07FI1; -. DR Proteomes; UP000008586; Genome. DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule. DR HAMAP; MF_04070; INFV_NCAP; 1. DR InterPro; IPR002141; Flu_NP. DR Pfam; PF00506; Flu_NP; 1. DR SUPFAM; SSF161003; flu NP-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Helical capsid protein; Host nucleus; KW Host-virus interaction; Ribonucleoprotein; RNA-binding; KW Viral nucleoprotein; Viral penetration into host nucleus; Virion; KW Virus entry into host cell. FT CHAIN 1..498 FT /note="Nucleoprotein" FT /id="PRO_0000372944" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1..18 FT /note="Unconventional nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04070" FT MOTIF 198..216 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04070" SQ SEQUENCE 498 AA; 55983 MW; 1AA4BC8CF3BEF649 CRC64; MASQGTKRSY EQMETDGERQ NATEIRASVG RMIGGIGRFY IQMCTELKLN DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYKRV DGKWVRELVL YDKEEIRRIW RQANNGDDAT AGLTHIMIWH SNLNDTTYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV LELIRMIKRG INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQRAMMD QVRESRNPGN AEIEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEKEGYSLVG VDPFKLLQTS QVYSLIRPNE NPAHKSQLVW MACNSAAFED LRVSSFIRGT RVLPRGKLST RGVQIASNEN MDAIVSSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISTQP TFSVQRNLPF DKTTIMAAFT GNAEGRTSDM RAEIIKMMES ARPEEVSFQG RGVFELSDER ATNPIVPSFD MSNEGSYFFG DNAEEYDN //