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P03418

- NCAP_HRSVA

UniProt

P03418 - NCAP_HRSVA

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
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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. protein binding Source: IntAct
    2. 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

    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-SubCell
    3. ribonucleoprotein complex Source: UniProtKB-KW
    4. viral nucleocapsid Source: UniProtKB-KW

    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

    MALSKVKLND TLNKDQLLSS SKYTIQRSTG DSIDTPNYDV QKHINKLCGM    50
    LLITEDANHK FTGLIGMLYA MSRLGREDTI KILRDAGYHV KANGVDVTTH 100
    RQDINGKEMK FEVLTLASLT TEIQINIEIE SRKSYKKMLK EMGEVAPEYR 150
    HDSPDCGMII LCIAALVITK LAAGDRSGLT AVIRRANNVL KNEMKRYKGL 200
    LPKDIANSFY EVFEKHPHFI DVFVHFGIAQ SSTRGGSRVE GIFAGLFMNA 250
    YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF 300
    YHILNNPKAS LLSLTQFPHF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA 350
    KAYAEQLKEN GVINYSVLDL TAEELEAIKH QLNPKDNDVE L 391
    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 1, 2014
    This is version 67 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