ID   NCAP_I76A7              Reviewed;         498 AA.
AC   P26074; Q67225;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-NOV-2023, entry version 84.
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 A virus (strain A/New Jersey/8/1976 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=379756;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2041090; DOI=10.1128/jvi.65.7.3704-3714.1991;
RA   Gorman O.T., Bean W.J., Kawaoka Y., Donatelli I., Guo Y., Webster R.G.;
RT   "Evolution of influenza A virus nucleoprotein genes: implications for the
RT   origins of H1N1 human and classical swine viruses.";
RL   J. Virol. 65:3704-3714(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1536092; DOI=10.1016/0168-1702(92)90091-m;
RA   Altmuller A., Kunerl M., Muller K., Hinshaw V.S., Fitch W.M.,
RA   Scholtissek C.;
RT   "Genetic relatedness of the nucleoprotein (NP) of recent swine, turkey, and
RT   human influenza A virus (H1N1) isolates.";
RL   Virus Res. 22:79-87(1992).
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}.
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; M63754; AAA52253.1; -; Genomic_RNA.
DR   EMBL; M76606; AAA73108.1; -; mRNA.
DR   SMR; P26074; -.
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:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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.
DR   SUPFAM; SSF161003; flu NP-like; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Helical capsid protein; Host nucleus;
KW   Host-virus interaction; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Viral penetration into host nucleus; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..498
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000079088"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..18
FT                   /note="Unconventional nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04070"
FT   MOTIF           198..216
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04070"
FT   CONFLICT        195
FT                   /note="G -> R (in Ref. 2; AAA73108)"
FT   CONFLICT        404
FT                   /note="D -> G (in Ref. 2; AAA73108)"
FT   CONFLICT        483
FT                   /note="N -> Y (in Ref. 2; AAA73108)"
SQ   SEQUENCE   498 AA;  56005 MW;  34AB4786570E78EB CRC64;
     MASQGTKRSY EQMETGGERQ DATEIRASVG RMIGGIGRFY IQMCTELKLS DYEGRLIQNS
     ITIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYKRI DGKWMRELIL YDKEEIRRVW
     RQANNGEDAT AGLTHIMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
     AAVKGVGTIA MELIGMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMMD
     QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGLAVASGHD FEREGYSLVG
     IDPFKLLQNS QVFSLIRPNE NPAHKSQLVW MACHSAAFED LRVSGFIRGK KVVPRGRLST
     RGVQIASNEN VEAMDSSTLE LRSRYWAIRT RSGGNTNQQK ASADQISVQP TFSVQRNLPF
     ERATVMAAFI GDNEGRTSDM RTEIIRMMES AKPEDLSFQG RGVFELSDEK ATNPIVPSFD
     MNNEGSYFFG DNAEEYDN
//