ID   NCAP_I07A0              Reviewed;         498 AA.
AC   A8C8J8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-NOV-2023, entry version 57.
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/USA:Texas/UR06-0195/2007 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=455880;
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] OF 1-496.
RA   Spiro D., Sengamalay N., Boyne A., Bera J., Zaborsky J., Subbu V.,
RA   Sparenborg J., Gallagher T., Overton L., Althoff R., Liu X., Ghedin E.,
RA   Sitz J., Katzel D., Neupane R., Shumway M., Koo H., Edelman L., Menegus M.,
RA   Mayer C., Dale S., Bao Y., Bolotov P., Dernovoy D., Kiryutin B.,
RA   Lipman D.J., Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-496.
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CY026214; ABV45930.1; -; Viral_cRNA.
DR   SMR; A8C8J8; -.
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   3: Inferred from homology;
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_0000372933"
FT   REGION          1..21
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"
SQ   SEQUENCE   498 AA;  55955 MW;  8208DD660ED393DF CRC64;
     MASQGTKRSY EQMETDGERQ NATEIRASVG RMIGGIGRFY IQMCTELKLN DYEGRLIQNS
     LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYKRV DGKWVRELVL YDKEEIRRIW
     RQANNGDDAT AGLTHIMIWH SNLNDTTYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
     AAVKGVGTMV LELIRMIKRG INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD
     QVRESRNPGN AEIEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEKEGYSLVG
     VDPFKLLQTS QVYSLIRPNE NPAHKSQLVW MACNSAAFED LRVSSFIRGT RVLPRGKLST
     RGVQIASNEN MDAIVSSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISTQP TFSVQRNLPF
     DKATIMAAFT GNTEGRTSDM RAEIIKMMES ARPEEVSFQG RGVFELSDER ATNPIVPSFD
     MSNEGSYFFG DNAEEYDN
//