LGP2

DHX58
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2RQA, 2W4R, 3EQT
Identifiers
Aliases	DHX58, D11LGP2, D11lgp2e, LGP2, RLR-3, DEXH-box helicase 58
External IDs	MGI: 1931560 HomoloGene: 69371 GeneCards: DHX58
Gene ontology Molecular function • DNA binding • nucleotide binding • helicase activity • zinc ion binding • metal ion binding • protein binding • single-stranded RNA binding • RNA binding • double-stranded RNA binding • hydrolase activity • ATP binding Cellular component • cytoplasm Biological process • negative regulation of MDA-5 signaling pathway • regulation of innate immune response • immune system process • response to virus • positive regulation of RIG-I signaling pathway • defense response to virus • negative regulation of innate immune response • negative regulation of type I interferon production • innate immune response • viral process • positive regulation of MDA-5 signaling pathway • positive regulation of type I interferon production • negative regulation of RIG-I signaling pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	79132	80861
Ensembl	ENSG00000108771	ENSMUSG00000017830
UniProt	Q96C10	Q99J87
RefSeq (mRNA)	NM_024119	NM_030150
RefSeq (protein)	NP_077024	NP_084426.2 NP_084426
Location (UCSC)	Chr 17: 42.1 – 42.11 Mb	Chr 11: 100.69 – 100.7 Mb
PubMed search

2RQA, 2W4R, 3EQT

79132

80861

ENSG00000108771

ENSMUSG00000017830

Q96C10

Q99J87

NM_024119

NM_030150

NP_077024

NP_084426.2
NP_084426

Probable ATP-dependent RNA helicase DHX58 also known as RIG-I-like receptor 3 (RLR-3) or RIG-I-like receptor LGP2 (RLR) is a RIG-I-like receptor dsRNA helicase enzyme that in humans is encoded by the DHX58 gene. The protein encoded by the gene DHX58 is known as LGP2 (Laboratory of Genetics and Physiology 2).

LGP2 was first identified and characterized in the context of mammary tissue in 2001, but its function has been found to be more relevant to the field of innate antiviral immunity. LGP2 has been found to be essential for producing effective antiviral responses against many viruses that are recognized by RIG-I and MDA5.

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