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P03466

- NCAP_I34A1

UniProt

P03466 - NCAP_I34A1

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Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 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 and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP 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 unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: Reactome
  2. intracellular transport of virus Source: Reactome
  3. receptor-mediated endocytosis of virus by host cell Source: Reactome
  4. uncoating of virus Source: Reactome
  5. viral entry into host cell Source: Reactome
  6. viral genome maturation Source: Reactome
  7. viral genome packaging Source: Reactome
  8. viral life cycle Source: Reactome
  9. viral penetration into host nucleus Source: UniProtKB-KW
  10. viral process Source: Reactome
  11. viral release from host cell Source: Reactome
  12. viral transcription Source: Reactome
  13. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Host-virus interaction, Viral penetration into host nucleus, Virus entry into host cell

Keywords - Ligandi

RNA-binding, Viral nucleoprotein

Enzyme and pathway databases

ReactomeiREACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
REACT_6212. Budding.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_9434. vRNP Assembly.
REACT_9491. Viral mRNA Translation.
REACT_9497. vRNA Synthesis.
REACT_9527. cRNA Synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoprotein
Alternative name(s):
Nucleocapsid protein
Short name:
Protein N
Gene namesi
Name:NP
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000009255: Genome

Subcellular locationi

Virion Curated. Host nucleus 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. Golgi membrane Source: Reactome
  5. helical viral capsid Source: UniProtKB-KW
  6. host cell nucleus Source: UniProtKB-KW
  7. nucleoplasm Source: Reactome
  8. plasma membrane Source: Reactome
  9. ribonucleoprotein complex Source: UniProtKB-KW
  10. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi104 – 1041W → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi120 – 1201W → A: Partial loss of RNA-binding activity. 1 Publication
Mutagenesisi139 – 1391W → A: Partial loss of RNA-binding activity. 1 Publication
Mutagenesisi148 – 1481Y → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi150 – 1501R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi156 – 1561R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi175 – 1751R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi199 – 1991R → A: 60% loss of Homomultimerization affinity. No effect on RNA-binding activity. 2 Publications
Mutagenesisi204 – 2041R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi207 – 2071W → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi208 – 2081R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi213 – 2131R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi267 – 2671R → A: Complete loss of RNA-binding activity. 1 Publication
Mutagenesisi330 – 3301W → A: Complete loss of RNA-binding activity. 1 Publication
Mutagenesisi386 – 3861W → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi391 – 3911R → A: No effect on RNA-binding activity. 1 Publication
Mutagenesisi412 – 4121F → A: Complete loss of RNA-binding activity. 1 Publication
Mutagenesisi416 – 4161R → A: Complete loss of Homomultimerization. Complete loss of RNA-binding activity. 2 Publications
Mutagenesisi479 – 4791F → A: 2-fold increase of self association. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498NucleoproteinPRO_0000079092Add
BLAST

Post-translational modificationi

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 (By similarity).By similarity

Interactioni

Subunit structurei

Homomultimerizes to form the nucleocapsid. May bind human exportin-1. 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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN4O437072EBI-2547640,EBI-351526From a different organism.
MP034852EBI-2547640,EBI-2547543

Protein-protein interaction databases

IntActiP03466. 21 interactions.
MINTiMINT-3375097.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BSTX-ray2.10C383-391[»]
2WFSelectron microscopy12.00A/B/C/D/E/F/G/H/I8-498[»]
4NQVX-ray2.39M/N/O/P/Q/R44-52[»]
ProteinModelPortaliP03466.
SMRiP03466. Positions 22-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03466.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1 – 1818Unconventional nuclear localization signalAdd
BLAST
Motifi198 – 21619Bipartite nuclear localization signalAdd
BLAST

Sequence similaritiesi

Family and domain databases

InterProiIPR002141. Flu_NP.
[Graphical view]
PfamiPF00506. Flu_NP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03466-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS
60 70 80 90 100
DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV
110 120 130 140 150
NGKWMRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR
160 170 180 190 200
TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELVRMIKRG
210 220 230 240 250
INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD QVRESRNPGN
260 270 280 290 300
AEFEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
310 320 330 340 350
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT
360 370 380 390 400
KVLPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR
410 420 430 440 450
ASAGQISIQP TFSVQRNLPF DRTTIMAAFN GNTEGRTSDM RTEIIRMMES
460 470 480 490
ARPEDVSFQG RGVFELSDEK AASPIVPSFD MSNEGSYFFG DNAEEYDN
Length:498
Mass (Da):56,210
Last modified:September 11, 2007 - v2
Checksum:i4F750FEF05D6E668
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351H → N in CAA24268. (PubMed:7292985)Curated
Sequence conflicti247 – 2471N → D in CAA24268. (PubMed:7292985)Curated
Sequence conflicti353 – 3531L → V in CAA24268. (PubMed:7292985)Curated
Sequence conflicti425 – 4251I → V in CAA24268. (PubMed:7292985)Curated
Sequence conflicti430 – 4301N → T in CAA24268. (PubMed:7292985)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01084 Genomic RNA. Translation: CAA24268.1.
J02147 Genomic RNA. Translation: AAA43467.1.
AF389119 Genomic RNA. Translation: AAM75159.1.
EF467822 Genomic RNA. Translation: ABO21710.1.
AY936882 Genomic RNA. Translation: AAX39501.1.
CY009447 Genomic RNA. Translation: ABD77679.1.
RefSeqiNP_040982.1. NC_002019.1.

Genome annotation databases

GeneIDi956531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01084 Genomic RNA. Translation: CAA24268.1 .
J02147 Genomic RNA. Translation: AAA43467.1 .
AF389119 Genomic RNA. Translation: AAM75159.1 .
EF467822 Genomic RNA. Translation: ABO21710.1 .
AY936882 Genomic RNA. Translation: AAX39501.1 .
CY009447 Genomic RNA. Translation: ABD77679.1 .
RefSeqi NP_040982.1. NC_002019.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BST X-ray 2.10 C 383-391 [» ]
2WFS electron microscopy 12.00 A/B/C/D/E/F/G/H/I 8-498 [» ]
4NQV X-ray 2.39 M/N/O/P/Q/R 44-52 [» ]
ProteinModelPortali P03466.
SMRi P03466. Positions 22-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03466. 21 interactions.
MINTi MINT-3375097.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956531.

Enzyme and pathway databases

Reactomei REACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
REACT_6212. Budding.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_9434. vRNP Assembly.
REACT_9491. Viral mRNA Translation.
REACT_9497. vRNA Synthesis.
REACT_9527. cRNA Synthesis.

Miscellaneous databases

EvolutionaryTracei P03466.

Family and domain databases

InterProi IPR002141. Flu_NP.
[Graphical view ]
Pfami PF00506. Flu_NP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The structure of the gene encoding the nucleoprotein of human influenza virus A/PR/8/34."
    Winter G., Fields S.
    Virology 114:423-428(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Complete nucleotide sequence of the nucleoprotein gene from the human influenza strain A/PR/8/34 (HON1)."
    van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.
    Eur. J. Biochem. 116:347-353(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. Erratum
    van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.
    Eur. J. Biochem. 116:645-645(1981)
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  5. "Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
    de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
    Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
  6. "Fluorescent antigen-transfected target cell cytotoxic T lymphocyte assay for ex vivo detection of antigen-specific cell-mediated cytotoxicity."
    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.
    J. Infect. Dis. 192:1183-1190(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  8. "A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins."
    Weber F., Kochs G., Gruber S., Haller O.
    Virology 250:9-18(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments."
    Digard P., Elton D., Bishop K., Medcalf E., Weeds A., Pope B.
    J. Virol. 73:2222-2231(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements."
    Elton D., Medcalf E., Bishop K., Digard P.
    Virology 260:190-200(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF ARG-199; ARG-416 AND PHE-479.
  11. "Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding."
    Elton D., Medcalf L., Bishop K., Harrison D., Digard P.
    J. Virol. 73:7357-7367(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, 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.
  12. "Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway."
    Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J., Digard P.
    J. Virol. 75:408-419(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN XPO1.

Entry informationi

Entry nameiNCAP_I34A1
AccessioniPrimary (citable) accession number: P03466
Secondary accession number(s): Q20N34
, Q58NB3, Q67228, Q80AB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 11, 2007
Last modified: October 29, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3