DDX58

DEAD (Asp-Glu-Ala-Asp) box polypeptide 58

Rendering based on PDB 2QFB.

Available structures
PDB	2QFB, 2QFD, 2RMJ, 3LRN, 3LRR, 3NCU, 3OG8

Identifiers

Symbols

DDX58; DKFZp434J1111; DKFZp686N19181; FLJ13599; RIG-I

External IDs

OMIM: 609631 MGI: 2442858 HomoloGene: 32215 GeneCards: DDX58 Gene

EC number

3.6.4.13

Gene Ontology
Molecular function	• nucleotide binding • double-stranded RNA binding • helicase activity • protein binding • ATP binding • ATP-dependent helicase activity • zinc ion binding • hydrolase activity, acting on acid anhydrides • metal ion binding
Cellular component	• cytoplasm • cytosol • cytosol
Biological process	• positive regulation of defense response to virus by host • detection of virus • negative regulation of type I interferon production • positive regulation of interferon-alpha production • positive regulation of interferon-beta production • positive regulation of interferon-beta production • positive regulation of transcription factor import into nucleus • innate immune response • positive regulation of transcription from RNA polymerase II promoter • positive regulation of sequence-specific DNA binding transcription factor activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 9:
32.46 – 32.53 Mb

Chr 4:
40.15 – 40.19 Mb

PubMed search

[1]

[2]

Probable ATP-dependent RNA helicase DDX58 is an enzyme that in humans is encoded by the DDX58 gene. It codes for a protein called retinoic acid-inducible gene 1 protein (or RIG-I), also known as DEAD-box protein 58 (DDX58), which is a cell receptor found in the cytoplasm of cells. RIG-I is part of the RIG-I-like receptor (RLR) family, which also includes MDA5 and LGP2, and functions as a pattern recognition receptor that is a sensor for viruses. DDX58 and MDA5 are involved in activating MAVS and triggering an antiviral response. ^[1]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. This gene encodes a protein containing RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.^[2]

References

^ Hou, F; Sun, L, Zheng, H, Skaug, B, Jiang, QX, Chen, ZJ (2011 Aug 5). "MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response.". Cell 146 (3): 448–61. doi:10.1016/j.cell.2011.06.041. PMC 3179916. PMID 21782231. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3179916.
^ "Entrez Gene: DDX58 DEAD (Asp-Glu-Ala-Asp) box polypeptide 58". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23586.

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Imaizumi T, Hatakeyama M, Yamashita K, et al. (2004). "Interferon-gamma induces retinoic acid-inducible gene-I in endothelial cells.". Endothelium 11 (3-4): 169–73. doi:10.1080/10623320490512156. PMID 15370293.
Sakaki H, Imaizumi T, Matsumiya T, et al. (2005). "Retinoic acid-inducible gene-I is induced by interleukin-1beta in cultured human gingival fibroblasts.". Oral Microbiol. Immunol. 20 (1): 47–50. doi:10.1111/j.1399-302X.2005.00181.x. PMID 15612946.
Sumpter R, Loo YM, Foy E, et al. (2005). "Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I.". J. Virol. 79 (5): 2689–99. doi:10.1128/JVI.79.5.2689-2699.2005. PMC 548482. PMID 15708988. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=548482.
Li K, Chen Z, Kato N, et al. (2005). "Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes.". J. Biol. Chem. 280 (17): 16739–47. doi:10.1074/jbc.M414139200. PMID 15737993.
Breiman A, Grandvaux N, Lin R, et al. (2005). "Inhibition of RIG-I-dependent signaling to the interferon pathway during hepatitis C virus expression and restoration of signaling by IKKepsilon.". J. Virol. 79 (7): 3969–78. doi:10.1128/JVI.79.7.3969-3978.2005. PMC 1061556. PMID 15767399. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1061556.
Zhao C, Denison C, Huibregtse JM, et al. (2005). "Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways.". Proc. Natl. Acad. Sci. U.S.A. 102 (29): 10200–5. doi:10.1073/pnas.0504754102. PMC 1177427. PMID 16009940. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1177427.
Yoneyama M, Kikuchi M, Matsumoto K, et al. (2005). "Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity.". J. Immunol. 175 (5): 2851–8. PMID 16116171.
Seth RB, Sun L, Ea CK, Chen ZJ (2005). "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3.". Cell 122 (5): 669–82. doi:10.1016/j.cell.2005.08.012. PMID 16125763.
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DDX58

Function

References

Further reading