P03418 (NCAP_HRSVA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nucleoprotein Short name=Protein N Alternative name(s): Nucleocapsid protein | ||
| Gene names |
| ||
| Organism | Human respiratory syncytial virus A (strain A2) [Complete proteome] | ||
| Taxonomic identifier | 11259 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Pneumovirinae › Pneumovirus › ![]() | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 391 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.7 |
| Subunit structure | 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. Ref.8 Ref.9 |
| Subcellular location | |
| Sequence similarities | Belongs to the paramyxoviruses nucleocapsid family. |
| Sequence caution | The sequence CAA24906.1 differs from that shown. Reason: Frameshift at position 376. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Inhibition of host PKR by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Viral immunoevasion |
| Cellular component | Host cytoplasm Virion |
| Ligand | RNA-binding Viral nucleoprotein |
| Molecular function | Ribonucleoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | suppression by virus of host PKR activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathwayInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complexInferred from electronic annotation. Source: UniProtKB-KW viral nucleocapsidInferred from electronic annotation. Source: InterPro |
| Molecular_function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 391 | 391 | Nucleoprotein | PRO_0000142652 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 267 | 1 | V → I in strain: Cold-passage attenuated. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 10 – 19 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 35 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 38 – 40 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 41 – 53 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 74 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 76 – 86 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 92 – 94 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 97 – 104 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 107 – 114 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 119 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 142 | 22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 147 – 149 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 155 – 169 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 170 – 173 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 179 – 188 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 191 – 196 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 202 – 215 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 217 – 230 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 238 – 248 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 249 – 254 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 256 – 266 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 270 – 273 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 275 – 294 | 20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 295 – 300 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 301 – 305 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 307 – 312 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 318 – 330 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 344 – 357 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||
| PIR | VHNZ. A04026. VHNZ1. A23316. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR004930. Pneumo_ncap. [Graphical view] | ||||||||||||||||||
| Pfam | PF03246. Pneumo_ncap. 1 hit. [Graphical view] | ||||||||||||||||||
| ProDom | PD006438. Pneumo_ncap. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P03418. | ||||||||||||||||||
Entry information
| Entry name | NCAP_HRSVA | ||||||||
| Accession | Primary (citable) accession number: P03418 Secondary accession number(s): P88810 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
