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Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

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

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/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Taxonomic identifieri381518 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000000834 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Host nucleus, Virion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3706556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000791131 – 498NucleoproteinAdd BLAST498

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.1 Publication

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 (By similarity).By similarity

Structurei

Secondary structure

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 47Combined sources26
Helixi51 – 54Combined sources4
Helixi57 – 72Combined sources16
Beta strandi75 – 78Combined sources4
Beta strandi95 – 100Combined sources6
Beta strandi103 – 108Combined sources6
Helixi113 – 123Combined sources11
Turni124 – 126Combined sources3
Helixi130 – 147Combined sources18
Helixi151 – 155Combined sources5
Turni156 – 158Combined sources3
Helixi161 – 166Combined sources6
Turni168 – 171Combined sources4
Turni178 – 180Combined sources3
Helixi181 – 183Combined sources3
Helixi186 – 199Combined sources14
Beta strandi200 – 202Combined sources3
Beta strandi204 – 210Combined sources7
Helixi211 – 229Combined sources19
Helixi233 – 243Combined sources11
Helixi250 – 263Combined sources14
Helixi278 – 286Combined sources9
Helixi291 – 294Combined sources4
Helixi301 – 309Combined sources9
Beta strandi313 – 316Combined sources4
Helixi322 – 333Combined sources12
Helixi341 – 348Combined sources8
Helixi355 – 357Combined sources3
Beta strandi371 – 373Combined sources3
Beta strandi375 – 378Combined sources4
Beta strandi384 – 390Combined sources7
Helixi422 – 428Combined sources7
Beta strandi433 – 435Combined sources3
Helixi439 – 449Combined sources11
Beta strandi456 – 458Combined sources3
Beta strandi460 – 465Combined sources6
Beta strandi470 – 472Combined sources3
Turni487 – 490Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZDPX-ray2.69A/B/C1-498[»]
4BBLelectron microscopy18.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X8-498[»]
4IRYX-ray2.80A/B1-401[»]
A/B430-498[»]
5B7BX-ray3.00A/B/C/D/E/F1-498[»]
ProteinModelPortaliP15682.
SMRiP15682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1 – 18Unconventional nuclear localization signalBy similarityAdd BLAST18
Motifi198 – 216Bipartite nuclear localization signalBy similarityAdd BLAST19

Sequence similaritiesi

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P15682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS
60 70 80 90 100
DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV
110 120 130 140 150
DGKWMRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR
160 170 180 190 200
TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG
210 220 230 240 250
INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMVD QVRESRNPGN
260 270 280 290 300
AEFEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
310 320 330 340 350
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT
360 370 380 390 400
KVVPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR
410 420 430 440 450
ASSGQISIQP TFSVQRNLPF DRPTIMAAFT GNTEGRTSDM RTEIIRLMES
460 470 480 490
ARPEDVSFQG RGVFELSDEK AASPIVPSFD MSNEGSYFFG DNAEEYDN
Length:498
Mass (Da):56,244
Last modified:April 1, 1990 - v1
Checksum:i27AA1703050AA877
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30746 Genomic RNA. Translation: AAA43452.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30746 Genomic RNA. Translation: AAA43452.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZDPX-ray2.69A/B/C1-498[»]
4BBLelectron microscopy18.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X8-498[»]
4IRYX-ray2.80A/B1-401[»]
A/B430-498[»]
5B7BX-ray3.00A/B/C/D/E/F1-498[»]
ProteinModelPortaliP15682.
SMRiP15682.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL3706556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Entry informationi

Entry nameiNCAP_I33A0
AccessioniPrimary (citable) accession number: P15682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.