ID   Q5V913_9INFB            Unreviewed;       560 AA.
AC   Q5V913;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   26-FEB-2008, entry version 17.
DE   Nucleoprotein.
GN   Name=NP;
OS   Influenza B virus (B/Memphis/13/03).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus B.
OX   NCBI_TaxID=289331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B/Memphis/13/03;
RX   PubMed=15542634; DOI=10.1128/JVI.78.23.12817-12828.2004;
RA   McCullers J.A., Saito T., Iverson A.R.;
RT   "Multiple genotypes of influenza B virus circulated between 1979 and
RT   2003.";
RL   J. Virol. 78:12817-12828(2004).
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 (Potential). Nucleus (By similarity).
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DR   EMBL; AY582031; AAU94830.1; -; Genomic_RNA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR002141; Flu_NP.
DR   Pfam; PF00506; Flu_NP; 1.
PE   3: Inferred from homology;
KW   Host-virus interaction; Nucleus; RNA-binding; Ribonucleoprotein;
KW   Viral nucleoprotein; Virion.
SQ   SEQUENCE   560 AA;  61554 MW;  A44C459463E051D9 CRC64;
     MSNMDIDGIN TGTIDKAPEE ITSGTSGTTR PIIRPATLAP PSNKRTRNPS PERATTISEA
     DVGRKTQKKQ TPTEIKKSVY NMVVKLGEFY NQMMVKAGLN DDMERNLIQN AHAVERILLA
     ATDDKKTEFQ KKKNARDVKE GKEEIDHNKT GGTFYKMVRD DKTIYFSPIR VTFLKEEVKT
     MYKTTMGSDG FSGLNHIMIG HSQMNDVCFQ RSKALKRVGL DPSLISTFAG STLPRRSGAT
     GVAIKGGGTL VAEAIRFIGR AMADRGLLRD IKAKTAYEKI LLNLKNKCSA PQQKALVDQV
     IGSRNPGIAD IEDLTLLARS MVVVRPSVAS KVVLPISIYA KIPQLGFNVE EYSMVGYEAM
     ALYNMATPVS ILRVGDDAKD KSQLFFMSCF GAAYEDLRVL SALTGTEFKP RSALKCKGFH
     VPAKEQVEGM GAALMSIKLQ FWAPMTRSGG NEVGGDGGSG QISCSPVFAV ERPIALSKQA
     VRRMLSMNIE GRDADVKGNL LKMMNDSMAK KTNGNAFIGK KMFQISDKNK TNPVEIPIKQ
     TIPNFFFGRD TAEDYDDLDY
//