NCAP_I34A1
ID NCAP_I34A1 Reviewed; 498 AA.
AC P03466; Q20N34; Q58NB3; Q67228; Q80AB4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 130.
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/Puerto Rico/8/1934 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=211044;
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=7292985; DOI=10.1016/0042-6822(81)90223-3;
RA Winter G., Fields S.;
RT "The structure of the gene encoding the nucleoprotein of human influenza
RT virus A/PR/8/34.";
RL Virology 114:423-428(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6166474; DOI=10.1111/j.1432-1033.1981.tb05341.x;
RA van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
RT "Complete nucleotide sequence of the nucleoprotein gene from the human
RT influenza strain A/PR/8/34 (HON1).";
RL Eur. J. Biochem. 116:347-353(1981).
RN [3]
RP ERRATUM OF PUBMED:6166474, AND SEQUENCE REVISION.
RA van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
RL Eur. J. Biochem. 116:645-645(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11779399; DOI=10.1098/rstb.2001.0979;
RA Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
RA Garcia-Sastre A., Palese P.;
RT "Plasmid-only rescue of influenza A virus vaccine candidates.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
RX PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
RA de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
RA Osterhaus A.D.M.E., Fouchier R.A.M.;
RT "Efficient generation and growth of influenza virus A/PR/8/34 from eight
RT cDNA fragments.";
RL Virus Res. 103:155-161(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16136460; DOI=10.1086/444546;
RA van Baalen C.A., Kwa D., Verschuren E.J., Reedijk M.L., Boon A.C.,
RA de Mutsert G., Rimmelzwaan G.F., Osterhaus A.D., Gruters R.A.;
RT "Fluorescent antigen-transfected target cell cytotoxic T lymphocyte assay
RT for ex vivo detection of antigen-specific cell-mediated cytotoxicity.";
RL J. Infect. Dis. 192:1183-1190(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT "The NIAID influenza genome sequencing project.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9770415; DOI=10.1006/viro.1998.9329;
RA Weber F., Kochs G., Gruber S., Haller O.;
RT "A classical bipartite nuclear localization signal on Thogoto and influenza
RT A virus nucleoproteins.";
RL Virology 250:9-18(1998).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9971805; DOI=10.1128/jvi.73.3.2222-2231.1999;
RA Digard P., Elton D., Bishop K., Medcalf E., Weeds A., Pope B.;
RT "Modulation of nuclear localization of the influenza virus nucleoprotein
RT through interaction with actin filaments.";
RL J. Virol. 73:2222-2231(1999).
RN [10]
RP SUBUNIT, AND MUTAGENESIS OF ARG-199; ARG-416 AND PHE-479.
RX PubMed=10405371; DOI=10.1006/viro.1999.9818;
RA Elton D., Medcalf E., Bishop K., Digard P.;
RT "Oligomerization of the influenza virus nucleoprotein: identification of
RT positive and negative sequence elements.";
RL Virology 260:190-200(1999).
RN [11]
RP RNA-BINDING, AND MUTAGENESIS OF ARG-8; TRP-104; TRP-120; TRP-139; TYR-148;
RP ARG-150; ARG-156; ARG-175; ARG-199; ARG-204; TRP-207; ARG-208; ARG-213;
RP ARG-267; TRP-330; TRP-386; ARG-391; PHE-412 AND ARG-416.
RX PubMed=10438825; DOI=10.1128/jvi.73.9.7357-7367.1999;
RA Elton D., Medcalf L., Bishop K., Harrison D., Digard P.;
RT "Identification of amino acid residues of influenza virus nucleoprotein
RT essential for RNA binding.";
RL J. Virol. 73:7357-7367(1999).
RN [12]
RP INTERACTION WITH HUMAN XPO1.
RX PubMed=11119609; DOI=10.1128/jvi.75.1.408-419.2001;
RA Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J.,
RA Digard P.;
RT "Interaction of the influenza virus nucleoprotein with the cellular CRM1-
RT mediated nuclear export pathway.";
RL J. Virol. 75:408-419(2001).
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, ECO:0000269|PubMed:10405371}.
CC -!- INTERACTION:
CC P03466; P03485: M; NbExp=2; IntAct=EBI-2547640, EBI-2547543;
CC P03466; P03466: NP; NbExp=2; IntAct=EBI-2547640, EBI-2547640;
CC P03466; P03433: PA; NbExp=3; IntAct=EBI-2547640, EBI-2547616;
CC P03466; P03431: PB1; NbExp=5; IntAct=EBI-2547640, EBI-2547514;
CC P03466; P03428: PB2; NbExp=3; IntAct=EBI-2547640, EBI-2547475;
CC P03466; O43707: ACTN4; Xeno; NbExp=2; IntAct=EBI-2547640, EBI-351526;
CC P03466; O60684: KPNA6; Xeno; NbExp=5; IntAct=EBI-2547640, EBI-359923;
CC P03466; Q8WV44: TRIM41; Xeno; NbExp=5; IntAct=EBI-2547640, EBI-725997;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:9770415,
CC ECO:0000269|PubMed:9971805}.
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; V01084; CAA24268.1; -; Genomic_RNA.
DR EMBL; J02147; AAA43467.1; -; Genomic_RNA.
DR EMBL; AF389119; AAM75159.1; -; Genomic_RNA.
DR EMBL; EF467822; ABO21710.1; -; Genomic_RNA.
DR EMBL; AY936882; AAX39501.1; -; Genomic_RNA.
DR EMBL; CY009447; ABD77679.1; -; Genomic_RNA.
DR RefSeq; NP_040982.1; NC_002019.1.
DR PDB; 2BST; X-ray; 2.10 A; C=383-391.
DR PDB; 2WFS; EM; 12.00 A; A/B/C/D/E/F/G/H/I=8-498.
DR PDB; 4NQV; X-ray; 2.39 A; M/N/O/P/Q/R=44-52.
DR PDB; 4ZDU; X-ray; 2.30 A; B=2-15.
DR PDB; 5NPZ; X-ray; 1.43 A; C=252-260.
DR PDB; 5NQ3; X-ray; 1.57 A; C/F=252-260.
DR PDB; 5V5O; X-ray; 2.24 A; A/B=198-216.
DR PDBsum; 2BST; -.
DR PDBsum; 2WFS; -.
DR PDBsum; 4NQV; -.
DR PDBsum; 4ZDU; -.
DR PDBsum; 5NPZ; -.
DR PDBsum; 5NQ3; -.
DR PDBsum; 5V5O; -.
DR SMR; P03466; -.
DR DIP; DIP-43998N; -.
DR IntAct; P03466; 150.
DR MINT; P03466; -.
DR ABCD; P03466; 2 sequenced antibodies.
DR GeneID; 956531; -.
DR KEGG; vg:956531; -.
DR Reactome; R-HSA-168255; Influenza Infection.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
DR Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
DR Reactome; R-HSA-168298; Release.
DR Reactome; R-HSA-168302; Budding.
DR Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
DR Reactome; R-HSA-192814; vRNA Synthesis.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-192869; cRNA Synthesis.
DR Reactome; R-HSA-192905; vRNP Assembly.
DR EvolutionaryTrace; P03466; -.
DR PRO; PR:P03466; -.
DR Proteomes; UP000009255; Genome.
DR Proteomes; UP000116373; Genome.
DR Proteomes; UP000170967; Genome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; 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..498
FT /note="Nucleoprotein"
FT /id="PRO_0000079092"
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 MUTAGEN 8
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 104
FT /note="W->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 120
FT /note="W->A: Partial loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 139
FT /note="W->A: Partial loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 148
FT /note="Y->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 150
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 156
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 175
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 199
FT /note="R->A: 60% loss of Homomultimerization affinity. No
FT effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10405371,
FT ECO:0000269|PubMed:10438825"
FT MUTAGEN 204
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 207
FT /note="W->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 208
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 213
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 267
FT /note="R->A: Complete loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 330
FT /note="W->A: Complete loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 386
FT /note="W->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 391
FT /note="R->A: No effect on RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 412
FT /note="F->A: Complete loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10438825"
FT MUTAGEN 416
FT /note="R->A: Complete loss of Homomultimerization. Complete
FT loss of RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:10405371,
FT ECO:0000269|PubMed:10438825"
FT MUTAGEN 479
FT /note="F->A: 2-fold increase of self association."
FT /evidence="ECO:0000269|PubMed:10405371"
FT CONFLICT 135
FT /note="H -> N (in Ref. 1; CAA24268)"
FT CONFLICT 247
FT /note="N -> D (in Ref. 1; CAA24268)"
FT CONFLICT 353
FT /note="L -> V (in Ref. 1; CAA24268)"
FT CONFLICT 425
FT /note="I -> V (in Ref. 1; CAA24268)"
FT CONFLICT 430
FT /note="N -> T (in Ref. 1; CAA24268)"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:4ZDU"
SQ SEQUENCE 498 AA; 56210 MW; 4F750FEF05D6E668 CRC64;
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS DYEGRLIQNS
LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV NGKWMRELIL YDKEEIRRIW
RQANNGDDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
AAVKGVGTMV MELVRMIKRG INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD
QVRESRNPGN AEFEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT KVLPRGKLST
RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISIQP TFSVQRNLPF
DRTTIMAAFN GNTEGRTSDM RTEIIRMMES ARPEDVSFQG RGVFELSDEK AASPIVPSFD
MSNEGSYFFG DNAEEYDN
