ID L7P6F3_9INFA Unreviewed; 498 AA. AC L7P6F3; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 10-APR-2019, entry version 36. 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:AFO83401.1}; OS Influenza A virus (A/duck/Guangxi/GXd-3/2009(H6N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Negarnaviricota; Polyploviricotina; Insthoviricetes; Articulavirales; OC Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1208725 {ECO:0000313|EMBL:AFO83401.1, ECO:0000313|Proteomes:UP000117558}; RN [1] {ECO:0000313|EMBL:AFO83401.1, ECO:0000313|Proteomes:UP000117558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/duck/Guangxi/GXd-3/2009 {ECO:0000313|EMBL:AFO83401.1}; RA Xie Z., Zhou C., Peng Y., Liu J., Pang Y., Deng X., Xie Z., Xie L., RA Fan Q.; RT "Genetic Characterization of H6 Subtype Avian Influenza Virus."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Encapsidates the negative strand viral RNA, protecting CC it from nucleases. The encapsidated genomic RNA is termed the CC ribonucleoprotein (RNP) and serves as template for transcription CC and replication. The RNP needs to be localized in the host nucleus CC to start an infectious cycle, but is too large to diffuse through CC the nuclear pore complex. NP comprises at least 2 nuclear CC localization signals that are responsible for the active RNP CC import into the nucleus through cellular importin alpha/beta CC pathway. Later in the infection, nclear export of RNPs are CC mediated through viral proteins NEP interacting with M1 which CC binds nucleoproteins. It is possible that nucleoprotein binds CC directly host exportin-1/XPO1 and plays an active role in RNPs CC nuclear export. M1 interaction with RNP seems to hide CC nucleoprotein's nuclear localization signals. Soon after a virion CC infects a new cell, M1 dissociates from the RNP under CC acidification of the virion driven by M2 protein. Dissociation of CC M1 from RNP unmasks nucleoprotein's nuclear localization signals, CC targeting the RNP to the nucleus. {ECO:0000256|HAMAP- CC Rule:MF_04070, ECO:0000256|SAAS:SAAS00966143}. CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind host CC exportin-1/XPO1. Binds to viral genomic RNA. Protein-RNA contacts CC are mediated by a combination of electrostatic interactions CC between positively charged residues and the phosphate backbone and CC planar interactions between aromatic side chains and bases. CC {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|SAAS:SAAS00966136}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04070, ECO:0000256|RuleBase:RU361251, CC ECO:0000256|SAAS:SAAS00966152}. Virion {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 CC protein to a 53-kDa protein by a cellular caspase. This cleavage CC might be a marker for the onset of apoptosis in infected cells or CC have a specific function in virus host interaction. CC {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 ECO:0000256|SAAS:SAAS00966161}. 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; JX297580; AFO83401.1; -; Viral_cRNA. DR Proteomes; UP000117558; 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: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|HAMAP-Rule:MF_04070, KW ECO:0000256|RuleBase:RU361251, ECO:0000256|SAAS:SAAS00966151}; KW Complete proteome {ECO:0000313|Proteomes:UP000117558}; KW Helical capsid protein {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966174}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|RuleBase:RU361251, ECO:0000256|SAAS:SAAS00966147}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966156}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966134}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966163}; KW Viral nucleoprotein {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|RuleBase:RU361251, ECO:0000313|EMBL:AFO83401.1}; KW Viral penetration into host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966166}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|RuleBase:RU361251, ECO:0000256|SAAS:SAAS00966164}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04070, KW ECO:0000256|SAAS:SAAS00966165}. FT MOTIF 1 18 Unconventional nuclear localization FT signal. {ECO:0000256|HAMAP-Rule: FT MF_04070}. FT MOTIF 198 216 Bipartite nuclear localization signal. FT {ECO:0000256|HAMAP-Rule:MF_04070}. SQ SEQUENCE 498 AA; 56238 MW; FC2C78F8DC4A8FB8 CRC64; MASQGTKRSY EQMETGGERQ NATEIRASVG RMVGGIGRFY IQMCTELKLS DYEGRLIQNS ITIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPVYRRR DGKWMRELIL YDKEEIRRIW RQANNGEEAT AGLTHLMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMMD QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGLAVASGYD FEREGYSLVG IDPFRLLQNS QVFSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT RVVPRGQLST RGVQIASNEN VETMDSSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP TFSVQRNLPF ERATIMAAFT GNTEGRTSDM RTEIIRMMES AKPEDVSFQG RGVFELSDEK ATNPIVPSFD MSKEGSYFFG DNAEEYDN //