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Nucleoprotein (Nucleocapsid protein) (Protein N)

 NCAP_I34A1              Reviewed;         498 AA.
P03466; Q20N34; Q58NB3; Q67228; Q80AB4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
25-OCT-2017, entry version 108.
RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04070};
AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04070};
Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04070};
Name=NP {ECO:0000255|HAMAP-Rule:MF_04070};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7292985; DOI=10.1016/0042-6822(81)90223-3;
Winter G., Fields S.;
"The structure of the gene encoding the nucleoprotein of human
influenza virus A/PR/8/34.";
Virology 114:423-428(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6166474; DOI=10.1111/j.1432-1033.1981.tb05341.x;
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
"Complete nucleotide sequence of the nucleoprotein gene from the human
influenza strain A/PR/8/34 (HON1).";
Eur. J. Biochem. 116:347-353(1981).
[3]
ERRATUM, AND SEQUENCE REVISION.
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
Eur. J. Biochem. 116:645-645(1981).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16136460; DOI=10.1086/444546;
van Baalen C.A., Kwa D., Verschuren E.J., Reedijk M.L., Boon A.C.,
de Mutsert G., Rimmelzwaan G.F., Osterhaus A.D., Gruters R.A.;
"Fluorescent antigen-transfected target cell cytotoxic T lymphocyte
assay for ex vivo detection of antigen-specific cell-mediated
cytotoxicity.";
J. Infect. Dis. 192:1183-1190(2005).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[8]
SUBCELLULAR LOCATION.
PubMed=9770415; DOI=10.1006/viro.1998.9329;
Weber F., Kochs G., Gruber S., Haller O.;
"A classical bipartite nuclear localization signal on Thogoto and
influenza A virus nucleoproteins.";
Virology 250:9-18(1998).
[9]
SUBCELLULAR LOCATION.
PubMed=9971805;
Digard P., Elton D., Bishop K., Medcalf E., Weeds A., Pope B.;
"Modulation of nuclear localization of the influenza virus
nucleoprotein through interaction with actin filaments.";
J. Virol. 73:2222-2231(1999).
[10]
SUBUNIT, AND MUTAGENESIS OF ARG-199; ARG-416 AND PHE-479.
PubMed=10405371; DOI=10.1006/viro.1999.9818;
Elton D., Medcalf E., Bishop K., Digard P.;
"Oligomerization of the influenza virus nucleoprotein: identification
of positive and negative sequence elements.";
Virology 260:190-200(1999).
[11]
RNA-BINDING, AND MUTAGENESIS OF ARG-8; TRP-104; TRP-120; TRP-139;
TYR-148; ARG-150; ARG-156; ARG-175; ARG-199; ARG-204; TRP-207;
ARG-208; ARG-213; ARG-267; TRP-330; TRP-386; ARG-391; PHE-412 AND
ARG-416.
PubMed=10438825;
Elton D., Medcalf L., Bishop K., Harrison D., Digard P.;
"Identification of amino acid residues of influenza virus
nucleoprotein essential for RNA binding.";
J. Virol. 73:7357-7367(1999).
[12]
INTERACTION WITH HUMAN XPO1.
PubMed=11119609; DOI=10.1128/JVI.75.1.408-419.2001;
Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R.,
McCauley J., Digard P.;
"Interaction of the influenza virus nucleoprotein with the cellular
CRM1-mediated nuclear export pathway.";
J. Virol. 75:408-419(2001).
-!- FUNCTION: Encapsidates the negative strand viral RNA, protecting
it from nucleases. The encapsidated genomic RNA is termed the
ribonucleoprotein (RNP) and serves as template for transcription
and replication. The RNP needs to be localized in the host nucleus
to start an infectious cycle, but is too large to diffuse through
the nuclear pore complex. NP comprises at least 2 nuclear
localization signals that are responsible for the active RNP
import into the nucleus through cellular importin alpha/beta
pathway. Later in the infection, nclear export of RNPs are
mediated through viral proteins NEP interacting with M1 which
binds nucleoproteins. It is possible that nucleoprotein binds
directly host exportin-1/XPO1 and plays an active role in RNPs
nuclear export. M1 interaction with RNP seems to hide
nucleoprotein's nuclear localization signals. Soon after a virion
infects a new cell, M1 dissociates from the RNP under
acidification of the virion driven by M2 protein. Dissociation of
M1 from RNP unmasks nucleoprotein's nuclear localization signals,
targeting the RNP to the nucleus. {ECO:0000255|HAMAP-
Rule:MF_04070}.
-!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind host
exportin-1/XPO1. Binds to viral genomic RNA. Protein-RNA contacts
are mediated by a combination of electrostatic interactions
between positively charged residues and the phosphate backbone and
planar interactions between aromatic side chains and bases.
{ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:10405371}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2547640, EBI-2547640;
O43707:ACTN4 (xeno); NbExp=2; IntAct=EBI-2547640, EBI-351526;
O60684:KPNA6 (xeno); NbExp=5; IntAct=EBI-2547640, EBI-359923;
P03485:M; NbExp=2; IntAct=EBI-2547640, EBI-2547543;
P03433:PA; NbExp=3; IntAct=EBI-2547640, EBI-2547616;
P03431:PB1; NbExp=5; IntAct=EBI-2547640, EBI-2547514;
P03428:PB2; NbExp=3; IntAct=EBI-2547640, EBI-2547475;
Q8WV44:TRIM41 (xeno); NbExp=5; IntAct=EBI-2547640, EBI-725997;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04070,
ECO:0000269|PubMed:9770415, ECO:0000269|PubMed:9971805}.
-!- PTM: Late in virus-infected cells, may be cleaved from a 56-kDa
protein to a 53-kDa protein by a cellular caspase. This cleavage
might be a marker for the onset of apoptosis in infected cells or
have a specific function in virus host interaction.
{ECO:0000255|HAMAP-Rule:MF_04070}.
-!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family.
{ECO:0000255|HAMAP-Rule:MF_04070}.
-----------------------------------------------------------------------
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EMBL; V01084; CAA24268.1; -; Genomic_RNA.
EMBL; J02147; AAA43467.1; -; Genomic_RNA.
EMBL; AF389119; AAM75159.1; -; Genomic_RNA.
EMBL; EF467822; ABO21710.1; -; Genomic_RNA.
EMBL; AY936882; AAX39501.1; -; Genomic_RNA.
EMBL; CY009447; ABD77679.1; -; Genomic_RNA.
RefSeq; NP_040982.1; NC_002019.1.
PDB; 2BST; X-ray; 2.10 A; C=383-391.
PDB; 2WFS; EM; 12.00 A; A/B/C/D/E/F/G/H/I=8-498.
PDB; 4NQV; X-ray; 2.39 A; M/N/O/P/Q/R=44-52.
PDB; 4ZDU; X-ray; 2.30 A; B=2-15.
PDBsum; 2BST; -.
PDBsum; 2WFS; -.
PDBsum; 4NQV; -.
PDBsum; 4ZDU; -.
ProteinModelPortal; P03466; -.
SMR; P03466; -.
DIP; DIP-43998N; -.
IntAct; P03466; 149.
MINT; MINT-3375097; -.
GeneID; 956531; -.
KEGG; vg:956531; -.
KO; K19391; -.
OrthoDB; VOG0900006S; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-192814; vRNA Synthesis.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-192869; cRNA Synthesis.
Reactome; R-HSA-192905; vRNP Assembly.
EvolutionaryTrace; P03466; -.
PRO; PR:P03466; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000109386; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; TAS:Reactome.
GO; GO:0019070; P:viral genome maturation; TAS:Reactome.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0019076; P:viral release from host cell; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
HAMAP; MF_04070; INFV_NCAP; 1.
InterPro; IPR002141; Flu_NP.
Pfam; PF00506; Flu_NP; 1.
1: Evidence at protein level;
3D-structure; Capsid protein; Complete proteome;
Helical capsid protein; Host nucleus; Host-virus interaction;
Reference proteome; Ribonucleoprotein; RNA-binding;
Viral nucleoprotein; Viral penetration into host nucleus; Virion;
Virus entry into host cell.
CHAIN 1 498 Nucleoprotein.
/FTId=PRO_0000079092.
MOTIF 1 18 Unconventional nuclear localization
signal. {ECO:0000255|HAMAP-
Rule:MF_04070}.
MOTIF 198 216 Bipartite nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04070}.
MUTAGEN 8 8 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 104 104 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 120 120 W->A: Partial loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 139 139 W->A: Partial loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 148 148 Y->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 150 150 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 156 156 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 175 175 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 199 199 R->A: 60% loss of Homomultimerization
affinity. No effect on RNA-binding
activity. {ECO:0000269|PubMed:10405371,
ECO:0000269|PubMed:10438825}.
MUTAGEN 204 204 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 207 207 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 208 208 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 213 213 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 267 267 R->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 330 330 W->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 386 386 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 391 391 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 412 412 F->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 416 416 R->A: Complete loss of
Homomultimerization. Complete loss of
RNA-binding activity.
{ECO:0000269|PubMed:10405371,
ECO:0000269|PubMed:10438825}.
MUTAGEN 479 479 F->A: 2-fold increase of self
association.
{ECO:0000269|PubMed:10405371}.
CONFLICT 135 135 H -> N (in Ref. 1; CAA24268).
CONFLICT 247 247 N -> D (in Ref. 1; CAA24268).
CONFLICT 353 353 L -> V (in Ref. 1; CAA24268).
CONFLICT 425 425 I -> V (in Ref. 1; CAA24268).
CONFLICT 430 430 N -> T (in Ref. 1; CAA24268).
HELIX 10 13 {ECO:0000244|PDB:4ZDU}.
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


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