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P03418

- NCAP_HRSVA

UniProt

P03418 - NCAP_HRSVA

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Protein

Nucleoprotein

Gene

N

Organism
Human respiratory syncytial virus A (strain A2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.1 Publication

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. suppression by virus of host PKR activity Source: UniProtKB-KW
  2. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host PKR by virus, Viral immunoevasion

Keywords - Ligandi

RNA-binding, Viral nucleoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoprotein
Short name:
Protein N
Alternative name(s):
Nucleocapsid protein
Gene namesi
Name:N
OrganismiHuman respiratory syncytial virus A (strain A2)
Taxonomic identifieri11259 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaePneumovirinaePneumovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007678: Genome

Subcellular locationi

GO - Cellular componenti

  1. helical viral capsid Source: UniProtKB-KW
  2. host cell cytoplasm Source: UniProtKB-KW
  3. ribonucleoprotein complex Source: UniProtKB-KW
  4. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Host cytoplasm, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391NucleoproteinPRO_0000142652Add
BLAST

Interactioni

Subunit structurei

Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. In nucleocapsid, interacts with the protein P and thereby positions the polymerase on the template. Interacts with protein M2-1; this interaction allows the association of nucleocapsid with the matrix protein, supposely to shut down virus transcriptase activity and initiate assembly and budding.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAVSM1QCQ23EBI-6930799,EBI-6930883From a different organism.

Protein-protein interaction databases

IntActiP03418. 4 interactions.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910
Beta strandi33 – 353
Helixi38 – 403
Helixi41 – 5313
Helixi62 – 7413
Helixi76 – 8611
Beta strandi92 – 943
Beta strandi97 – 1048
Beta strandi107 – 1148
Beta strandi117 – 1193
Helixi121 – 14222
Turni147 – 1493
Helixi155 – 16915
Helixi170 – 1734
Helixi179 – 18810
Helixi191 – 1966
Helixi202 – 21514
Helixi217 – 23014
Helixi238 – 24811
Turni249 – 2546
Helixi256 – 26611
Helixi270 – 2734
Helixi275 – 29420
Helixi295 – 3006
Turni301 – 3055
Helixi307 – 3126
Helixi318 – 33013
Helixi344 – 35714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WJ8X-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-391[»]
2YHMX-ray3.60A/B/C/D/E/F/G/H/I/J1-375[»]
4BKKelectron microscopy-B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-391[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03418.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR004930. Pneumo_ncap.
[Graphical view]
PfamiPF03246. Pneumo_ncap. 1 hit.
[Graphical view]
ProDomiPD006438. Pneumo_ncap. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P03418-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALSKVKLND TLNKDQLLSS SKYTIQRSTG DSIDTPNYDV QKHINKLCGM
60 70 80 90 100
LLITEDANHK FTGLIGMLYA MSRLGREDTI KILRDAGYHV KANGVDVTTH
110 120 130 140 150
RQDINGKEMK FEVLTLASLT TEIQINIEIE SRKSYKKMLK EMGEVAPEYR
160 170 180 190 200
HDSPDCGMII LCIAALVITK LAAGDRSGLT AVIRRANNVL KNEMKRYKGL
210 220 230 240 250
LPKDIANSFY EVFEKHPHFI DVFVHFGIAQ SSTRGGSRVE GIFAGLFMNA
260 270 280 290 300
YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
310 320 330 340 350
YHILNNPKAS LLSLTQFPHF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA
360 370 380 390
KAYAEQLKEN GVINYSVLDL TAEELEAIKH QLNPKDNDVE L
Length:391
Mass (Da):43,451
Last modified:April 1, 1988 - v1
Checksum:iD06E84F4F88D382B
GO

Sequence cautioni

The sequence CAA24906.1 differs from that shown. Reason: Frameshift at position 376.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671V → I in strain: Cold-passage attenuated.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11486 Genomic RNA. Translation: AAB59852.1.
X00001 Genomic RNA. Translation: CAA24906.1. Frameshift.
U50362 Genomic RNA. Translation: AAB86658.1.
U50363 Genomic RNA. Translation: AAB86670.1.
U63644 Genomic RNA. Translation: AAC55964.1.
AF035006 Genomic RNA. Translation: AAC14896.1.
PIRiA04026. VHNZ.
A23316. VHNZ1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11486 Genomic RNA. Translation: AAB59852.1 .
X00001 Genomic RNA. Translation: CAA24906.1 . Frameshift.
U50362 Genomic RNA. Translation: AAB86658.1 .
U50363 Genomic RNA. Translation: AAB86670.1 .
U63644 Genomic RNA. Translation: AAC55964.1 .
AF035006 Genomic RNA. Translation: AAC14896.1 .
PIRi A04026. VHNZ.
A23316. VHNZ1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WJ8 X-ray 3.29 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-391 [» ]
2YHM X-ray 3.60 A/B/C/D/E/F/G/H/I/J 1-375 [» ]
4BKK electron microscopy - B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-391 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03418. 4 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03418.

Family and domain databases

InterProi IPR004930. Pneumo_ncap.
[Graphical view ]
Pfami PF03246. Pneumo_ncap. 1 hit.
[Graphical view ]
ProDomi PD006438. Pneumo_ncap. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  1. "Correct sequence for the major nucleocapsid protein mRNA of respiratory syncytial virus."
    Collins P.L., Anderson K., Langer S.J., Wertz G.W.
    Virology 146:69-77(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Amino acid sequence of human respiratory syncytial virus nucleocapsid protein."
    Elango N., Venkatesan S.
    Nucleic Acids Res. 11:5941-5951(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "A cold-passaged, attenuated strain of human respiratory syncytial virus contains mutations in the F and L genes."
    Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.
    Virology 208:478-484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  4. "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged human respiratory syncytial virus vaccine candidate results from the acquisition of a single mutation in the polymerase (L) gene."
    Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.
    Virus Genes 13:269-273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  5. "Nucleotide sequence analysis of the respiratory syncytial virus subgroup A cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated virus vaccine candidate."
    Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.
    Virology 225:419-422(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  6. "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations from cold-passaged RSV is attenuated in chimpanzees."
    Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.
    J. Virol. 72:4467-4471(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  7. "Increased expression of the N protein of respiratory syncytial virus stimulates minigenome replication but does not alter the balance between the synthesis of mRNA and antigenome."
    Fearns R., Peeples M.E., Collins P.L.
    Virology 236:188-201(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is essential for protein function."
    Hardy R.W., Wertz G.W.
    J. Virol. 74:5880-5885(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH M2-1.
  9. "Identification of temperature-sensitive mutations in the phosphoprotein of respiratory syncytial virus that are likely involved in its interaction with the nucleoprotein."
    Lu B., Brazas R., Ma C.H., Kristoff T., Cheng X., Jin H.
    J. Virol. 76:2871-2880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P.

Entry informationi

Entry nameiNCAP_HRSVA
AccessioniPrimary (citable) accession number: P03418
Secondary accession number(s): P88810
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: October 29, 2014
This is version 68 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

External Data

Dasty 3