ID   NCAP_INCJH              Reviewed;         556 AA.
AC   Q9IMP6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04070};
DE   AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04070};
DE            Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04070};
GN   Name=NP {ECO:0000255|HAMAP-Rule:MF_04070};
OS   Influenza C virus (strain C/Johannesburg/1/1966).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX   NCBI_TaxID=100673;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Crescenzo-Chaigne B.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2-556.
RX   PubMed=10600605; DOI=10.1006/viro.1999.0059;
RA   Crescenzo-Chaigne B., Naffakh N., van der Werf S.;
RT   "Comparative analysis of the ability of the polymerase complexes of
RT   influenza viruses type A, B and C to assemble into functional RNPs that
RT   allow expression and replication of heterotypic model RNA templates in
RT   vivo.";
RL   Virology 265:342-353(1999).
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:0000255|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:0000255|HAMAP-Rule:MF_04070}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04070}.
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:0000255|HAMAP-Rule:MF_04070}.
CC   -!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04070}.
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DR   EMBL; AF170573; AAF89736.2; -; Genomic_RNA.
DR   SMR; Q9IMP6; -.
DR   Proteomes; UP000138885; 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; Helical capsid protein; Host nucleus;
KW   Host-virus interaction; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Viral penetration into host nucleus; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..556
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000269908"
FT   REGION          516..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  62739 MW;  E9D35FEF246821B9 CRC64;
     MSDRRQNRKT PDEQRKANAL IINENIEAYI AICKEVGLNG DEMLILENGI AIEKAIRICC
     DGKYQEKREK KAREAQRADS NFNADSIGIR LVKRAGSGTN ITYHAVVELT SRSRIVQILK
     SHWGNELNRA KIAGKRLGFS ALFASNLEAI IYQRGRNAAR RNGSAELFTL TQGAGIETRY
     KWIMEKHIGI GVLIADAKGL INGKREGKKG VDANVKLRAG TTGSPLERAM QGIEKKAFPG
     PLRALARRVV KANYNDAREA LNVIAEASLL LKPQITNKMT MPWCMWLAAR LTLKDEFANF
     CAYAGRRAFE VFNIAMEKIG ICSFQGTIMN DDEIESIEDK AQVLMMACFG LAYEDFSLVS
     AMVSHPLKLR NRMKIGNFRV GEKVSTVLSP LLRFTRWAEF AQRFALQTNT SREGAQISNS
     AVFAVERKIT TDVQRVEELL NKVQAHEDEP LQTLYKKVRE QISIIGRNKS EIKEFLGSSM
     YDLNDQEKQN PINFRSGAHP FFFEFDPDYN PIRVKRPKKP IAKRNSNISR LEEEGMDENS
     EIGQAKKMKP LDQLAK