ID L7P6F3_9INFA Unreviewed; 498 AA. AC L7P6F3; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 22-JAN-2014, entry version 8. DE SubName: Full=Nucleocapsid protein; GN Name=NP; OS Influenza A virus (A/duck/Guangxi/GXd-3/2009(H6N2)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=1208725; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/duck/Guangxi/GXd-3/2009; 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 nucleus to CC start an infectious cycle, but is too large to diffuse through the CC nuclear pore complex. NP comprises at least 2 nuclear localization CC signals and is responsible of the active RNP import into the CC nucleus through the cellular importin alpha/beta pathway. Later in CC the infection, nucleus export of RNP are mediated through viral CC proteins NEP interacting with M1 which binds nucleoproteins. It is CC possible that the nucleoprotein binds directly exportin-1 (XPO1) CC and plays an active role in RNP nuclear export. M1 interaction CC with RNP seems to hide nucleoprotein's nuclear localization CC signals. Soon after a virion infects a new cell, M1 dissociates CC from the RNP under acidification of the virion driven by M2 CC protein. Dissociation of M1 from RNP unmask nucleoprotein's CC nuclear localization signals, targeting the RNP to the nucleus (By CC similarity). CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind human CC exportin-1. 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 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus (By similarity). 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 GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW. 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-KW. DR InterPro; IPR002141; Flu_NP. DR Pfam; PF00506; Flu_NP; 1. PE 3: Inferred from homology; KW Capsid protein; Helical capsid protein; Host nucleus; KW Host-virus interaction; RNA-binding; Viral nucleoprotein; KW Viral penetration into host nucleus; Virion; KW Virus entry into host cell. 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 //