ID   L7QGV3_9INFA            Unreviewed;       498 AA.
AC   L7QGV3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   16-OCT-2013, entry version 7.
DE   SubName: Full=Nucleocapsid protein;
DE   Flags: Fragment;
GN   Name=NP;
OS   Influenza A virus (A/elephant seal/California/2/2010(H1N1)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=1263915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/elephant seal/California/2/2010;
RX   PubMed=23690933;
RA   Goldstein T., Mena I., Anthony S.J., Medina R., Robinson P.W.,
RA   Greig D.J., Costa D.P., Lipkin W.I., Garcia-Sastre A., Boyce W.M.;
RT   "Pandemic H1N1 Influenza Isolated from Free-Ranging Northern Elephant
RT   Seals in 2010 off the Central California Coast.";
RL   PLoS ONE 8:E62259-E62259(2013).
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).
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DR   EMBL; KC222503; AGA19351.1; -; Viral_cRNA.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-KW.
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.
FT   NON_TER     498    498
SQ   SEQUENCE   498 AA;  56009 MW;  23476CB9A166A4D3 CRC64;
     MASQGTKRSY EQMETGGERQ DATEIRASVG RMIGGIGRFY IQMCTELKLS DYDGRLIQNS
     ITIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRI NGKWMRELIL YDKEEIRRVW
     RQANNGEDAT AGLTHIMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
     AAVKGVGTIA MELIRMIKRG INDRNFWRGE NGRRTRVAYE RMCNILKGKF QTAAQRAMMD
     QVRESRNPGN AEIEDLIFLT RSALILRGSV AHKSCLPACV YGLAVASGHD FEREGYSLVG
     IDPFKLLQNS QVVSLMRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGK KVIPRGKLST
     RGVQVASNEN VETMDSNTLE LRSRYWAIRT RSGGNTNQQK ASAGQISVQP TFSVQRNLPF
     ERATVMAAFS GNNEGRTSDM RTEVIRMMES AKPEDLSFQG RGVFELSDEK ATNPIVPSFD
     MSNEGSYFFG DNAEEYDS
//