NCAP_I34A0
ID NCAP_I34A0 Reviewed; 498 AA.
AC P12604; Q67279; Q67280; Q67281;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 4.
DT 02-JUN-2021, entry version 91.
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/Fowl plague virus/Rostock/8/1934 H7N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=392810;
OH NCBI_TaxID=8782; Aves.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX DOI=10.1016/0168-1702(84)90053-4;
RA Tomley F.M., Roditi I.J.;
RT "Nucleotide sequence of RNA segment 5, encoding the nucleoprotein, of
RT influenza A/FPV/Rostock/34.";
RL Virus Res. 1:625-630(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2718389; DOI=10.1016/0042-6822(89)90353-x;
RA Gammelin M., Mandler J., Scholtissek C.;
RT "Two subtypes of nucleoproteins (NP) of influenza A viruses.";
RL Virology 170:71-80(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant ts19, Mutant ts81, Revertant 19R, and Revertant 81R;
RX PubMed=2705330; DOI=10.1016/0168-1702(89)90058-0;
RA Mandler J., Scholtissek C.;
RT "Localization of the temperature-sensitive defect in the nucleoprotein of
RT an influenza A/FPV/Rostock/34 virus.";
RL Virus Res. 12:113-121(1989).
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; M21937; AAA43116.1; -; Genomic_RNA.
DR EMBL; M22576; AAB59744.1; -; Genomic_RNA.
DR EMBL; M24556; AAA64422.1; -; Genomic_RNA.
DR EMBL; M24557; AAA64423.1; -; Genomic_RNA.
DR EMBL; M24660; AAA64424.1; -; Genomic_RNA.
DR PIR; A42757; A42757.
DR SMR; P12604; -.
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; 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_0000079047"
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"
FT VARIANT 162
FT /note="R -> K (in strain: Mutant ts19)"
FT VARIANT 332
FT /note="A -> T (in strain: Mutant ts81 and Revertant 81R)"
FT VARIANT 363
FT /note="V -> A (in strain: Mutant ts19 and Revertant 19R)"
FT CONFLICT 201
FT /note="I -> M (in Ref. 1; AAA43116)"
FT CONFLICT 284
FT /note="A -> T (in Ref. 1; AAA43116)"
FT CONFLICT 318
FT /note="P -> S (in Ref. 1; AAA43116)"
FT CONFLICT 359
FT /note="S -> P (in Ref. 1; AAA43116)"
SQ SEQUENCE 498 AA; 56249 MW; EF494BABCCF57144 CRC64;
MASQGTKRSY EQMETGGERQ NATEIRASVG RMVSGIGRFY IQMCTELKLS DYEGRLIQNS
ITIERMVLSA FDERRNRYLE EHPSAGKDPK KTGGPIYRRR DGKWVRELIL YDKEEIRRIW
RQANNGEDAT AGLTHLMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMMD
QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGLAVASGYD FEREGYSLVG
IDPFRLLQNS QVFSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT RVVPRGQLST
RGVQIASNEN METMDSSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP TFSVQRNLPF
ERATIMAAFT GNTEGRTSDM RTEIIRMMES ARPEDVSFQG RGVFELSDEK ATSPIVPSLD
MSNEGSYFFG DNAEEYDN
