P19715 (NSP5_ROTP5) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 46. History...
Names and origin
|Protein names||Recommended name:|
Non-structural protein 5
|Organism||Rotavirus A (strain Pig/United States/OSU/1977 G5-P9-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))|
|Taxonomic identifier||10915 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus ›|
|Virus host||Sus scrofa (Pig) [TaxID: 9823]|
|Sequence length||197 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Involved in genome replication. Plays a crucial role, together with NSP2, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where core-like replication intermediates are assembled and RNA replication takes place. May regulate NSP2-RNA interactions during genome replication, since NSP5 competes with RNA for the same binding site on the NSP2 octamer. Binds to either ssRNA or dsRNA with similar affinities. Displays ATPase and autokinase activities By similarity.
Magnesium for ATPase activity.
Homodimer. Interacts with VP1. Interacts with VP2. Interacts with NSP2; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories. Interacts with NSP6 By similarity. Ref.4
Hyperphosphorylated on serine residues, when in dimeric form. Ser-67 phosphorylation by CK1 is required for the hyperphosphorylation of NSP5 dimer. Impaired phosphorylation is associated with a profound morphological change in virus factories and a moderate decrease in virus replication. Ref.3 Ref.5
Belongs to the rotavirus A NSP5 family.
|Cellular component||Host cytoplasm|
|Gene Ontology (GO)|
|Biological_process||viral genome replication|
Inferred from electronic annotation. Source: InterPro
|Cellular_component||host cell cytoplasm|
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: InterProRNA binding
Inferred from electronic annotation. Source: UniProtKB-KWmagnesium ion binding
Inferred from electronic annotation. Source: InterPronucleotide binding
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 197||197||Non-structural protein 5||PRO_0000149638|
|Region||1 – 48||48||Interaction with VP1 By similarity|
|Region||188 – 197||10||Homodimerization and interaction with NSP6 By similarity|
|Compositional bias||2 – 101||100||Ser-rich|
|Metal binding||92||1||Magnesium Potential|
Amino acid modifications
|Modified residue||67||1||Phosphoserine; by host CK1 By similarity|
|Modified residue||153||1||Phosphoserine; by host By similarity|
|Modified residue||155||1||Phosphoserine; by host By similarity|
|Modified residue||163||1||Phosphoserine; by host By similarity|
|Modified residue||165||1||Phosphoserine; by host By similarity|
|||"Porcine OSU rotavirus segment II sequence shows common features with the viral gene of human origin."|
Gonzalez S.A., Burrone O.R.
Nucleic Acids Res. 17:6402-6402(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine."|
Gonzalez S.A., Burrone O.R.
Virology 182:8-16(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
|||"Phosphorylation generates different forms of rotavirus NSP5."|
Afrikanova I., Miozzo M.C., Giambiagi S., Burrone O.R.
J. Gen. Virol. 77:2059-2065(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
|||"Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation."|
Eichwald C., Rodriguez J.F., Burrone O.R.
J. Gen. Virol. 85:625-634(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NSP2.
|||"Impaired hyperphosphorylation of rotavirus NSP5 in cells depleted of casein kinase 1alpha is associated with the formation of viroplasms with altered morphology and a moderate decrease in virus replication."|
Campagna M., Budini M., Arnoldi F., Desselberger U., Allende J.E., Burrone O.R.
J. Gen. Virol. 88:2800-2810(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF PHOSPHORYLATION BY CK1.
|X15519 Genomic RNA. Translation: CAA33540.1.|
|PIR||VHXRPU. A34009. |
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR002512. Rotavirus_A/C_NSP5. |
|Pfam||PF01525. Rota_NS26. 1 hit. |
|PIRSF||PIRSF004006. Rota_NS26. 1 hit. |
|Accession||Primary (citable) accession number: P19715|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families