ID A0A1C8Z3U5_9INFA Unreviewed; 498 AA. AC A0A1C8Z3U5; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 29-SEP-2021, entry version 21. DE RecName: Full=Nucleoprotein {ECO:0000256|HAMAP-Rule:MF_04070}; DE AltName: Full=Nucleocapsid protein {ECO:0000256|HAMAP-Rule:MF_04070}; DE Short=Protein N {ECO:0000256|HAMAP-Rule:MF_04070}; GN Name=NP {ECO:0000256|HAMAP-Rule:MF_04070, GN ECO:0000256|RuleBase:RU361251, ECO:0000313|EMBL:AOK93178.1}; OS Influenza A virus (A/duck/Zhejiang/6DK19-MA/2013(H5N2)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1891312 {ECO:0000313|EMBL:AOK93178.1}; RN [1] {ECO:0000313|EMBL:AOK93178.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/duck/Zhejiang/6DK19-MA/2013 {ECO:0000313|EMBL:AOK93178.1}; RX PubMed=27663652; RA Wu H., Peng X., Peng X., Wu N.; RT "Amino acid substitutions involved in the adaptation of a novel highly RT pathogenic H5N2 avian influenza virus in mice."; RL Virol. J. 13:159-159(2016). 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:0000256|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:0000256|HAMAP-Rule:MF_04070}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04070, CC ECO:0000256|RuleBase:RU361251}. Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. 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:0000256|HAMAP-Rule:MF_04070}. CC -!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family. CC {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. 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; KX714307; AOK93178.1; -; Viral_cRNA. 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: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. PE 3: Inferred from homology; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, ECO:0000256|HAMAP- KW Rule:MF_04070}; KW Helical capsid protein {ECO:0000256|ARBA:ARBA00022497, ECO:0000256|HAMAP- KW Rule:MF_04070}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04070}; Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04070}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_04070}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_04070}; KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086, ECO:0000256|HAMAP- KW Rule:MF_04070}; KW Viral penetration into host nucleus {ECO:0000256|ARBA:ARBA00022524, KW ECO:0000256|HAMAP-Rule:MF_04070}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04070}. 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:0000256|HAMAP-Rule:MF_04070" FT MOTIF 198..216 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04070" SQ SEQUENCE 498 AA; 56325 MW; F5AAE38C8A664DA8 CRC64; MASQGTKRSY EQMETGGERQ NATEIRASVG RMISGIGRFY IQMCTELKLS DHEGRLIQNS ITIERMVLSA FDERRNRYLE EHPSAGKDPK KTGGPIYRRR DGKWMRELIL YDKQEIRRIW RQANNGEDAT AGLTHLMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMMD QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGLAVASGYD FEREGYSLVG IDPFRLLQNS QVFSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT RVVPRGQLST RGVQIASNEN METMDSNTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP TFSVQRNLPF ERATIMAAFA GNTEGRTSDM RTEIIRMMES AKPEDVSFQG RGVFELSDEK ATNPIVPSFD MNNEGSYFFG DNAEEYDN //