ID NCAP_I68A4 Reviewed; 498 AA. AC P22435; Q91MA3; Q91MA4; Q91MA5; Q91MA6; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 2. DT 08-NOV-2023, entry version 99. 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/Hong Kong/1/1968 H3N2). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=506350; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9721; Cetacea (whales). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9709; Phocidae (true seals). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2780295; DOI=10.1093/nar/17.16.6721; RA Reinhardt U., Mandler J., Scholtissek C.; RT "Sequence of the nucleoprotein (NP) gene of the influenza A virus RT reassortant 81/HO, carrying the NP originally derived from A/Hong Kong/1/68 RT (H3N2)."; RL Nucleic Acids Res. 17:6721-6721(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate MA12, Isolate MA20, and Isolate MA20c; RX PubMed=11371620; DOI=10.1073/pnas.111165798; RA Brown E.G., Liu H., Kit L.C., Baird S., Nesrallah M.; RT "Pattern of mutation in the genome of influenza A virus on adaptation to RT increased virulence in the mouse lung: identification of functional RT themes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:6883-6888(2001). 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; X15890; CAA33899.1; -; Genomic_RNA. DR EMBL; AF348180; AAK51722.1; -; Genomic_RNA. DR EMBL; AF348181; AAK51723.1; -; Genomic_RNA. DR EMBL; AF348182; AAK51724.1; -; Genomic_RNA. DR EMBL; AF348183; AAK51725.1; -; Genomic_RNA. DR SMR; P22435; -. DR DIP; DIP-61687N; -. DR IntAct; P22435; 1. DR PRO; PR:P22435; -. DR Proteomes; UP000142359; 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 3: Inferred from homology; KW 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_0000079064" 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" FT VARIANT 34 FT /note="D -> N (in strain: Isolate MA12, Isolate MA20 and FT Isolate MA20c)" FT VARIANT 480 FT /note="D -> N (in strain: Isolate MA20c)" FT CONFLICT 311 FT /note="Q -> H (in Ref. 1; CAA33899)" SQ SEQUENCE 498 AA; 56026 MW; F0AA832B97BC75CC CRC64; MASQGTKRSY EQMETDGERQ NATEIRASVG KMIDGIGRFY IQMCTELKLS DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYKRV DGKWMRELVL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDTTYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRKTRSAYE RMCNILKGKF QTAAQRAMMD QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEKEGYSLVG IDPFKLLQNS QVYSLIRPNE NPAHKSQLVW MACNSAAFED LRVLSFIRGT KVSPRGKLST RGVQIASNEN MDAMESSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP AFSVQRNLPF DKPTIMAAFT GNTEGRTSDM RAEIIRMMEG AKPEEMSFQG RGVFELSDEK AANPIVPSFD MSNEGSYFFG DNAEEYDN //