Q99J87 · DHX58_MOUSE
- ProteinATP-dependent RNA helicase DHX58
- GeneDhx58
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids678 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a regulator of RIGI and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to RIGI and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on RIG-I signaling may involve the following mechanisms: competition with RIGI for binding to the viral RNA, binding to RIGI and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by RIGI and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | double-stranded RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | single-stranded RNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | antiviral innate immune response | |
Biological Process | cytoplasmic pattern recognition receptor signaling pathway | |
Biological Process | negative regulation of innate immune response | |
Biological Process | negative regulation of MDA-5 signaling pathway | |
Biological Process | negative regulation of RIG-I signaling pathway | |
Biological Process | negative regulation of type I interferon production | |
Biological Process | positive regulation of MDA-5 signaling pathway | |
Biological Process | positive regulation of RIG-I signaling pathway | |
Biological Process | positive regulation of type I interferon production | |
Biological Process | response to bacterium | |
Biological Process | response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent RNA helicase DHX58
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99J87
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Embryonic lethality at a high frequency. Adult female that survive show an enlarged uterus filled with fluid resulting from vaginal atresia.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | Abolishes IFNB1 production upon infection with various viruses. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000102011 | 1-678 | ATP-dependent RNA helicase DHX58 | |||
Sequence: MELRPYQWEVILPALEGKNIIIWLPTGAGKTRAAAFVAKRHLETVDRGKVVVLVNRVHLVSQHAEEFRRMLDKHWTVTTLSGDMGSRAGFGLMARSHDLLICTAELLQLALNSSEEDEHVELREFSLIVVDECHHTHKDTVYNTILSRYLEQKLKKAEPLPQVLGLTASPGTGGATKLQGAIDHILQLCANLDTCHIMSPKNCYSQLLMHNPKPCKQYDLCQRRAQDPFGDLIKKLMNQIHQQLEMPDLKQQFGTQMYEQQVVQLCKDAAEAGLQEQRVYALHLRRYNDALFIHDTVRARDALDMLQDFYDRERTTKTQMVRAESWLLKLFDDHKNVLGQLAARGPENPKLEMLERILLKQFGSPGHTRGIIFTRTRQTASSLLLWLRQQPCLQTVGIKPQMLIGAGNTSQSTHMTQKDQQEVIQEFRDGILSLLVATSVAEEGLDIAQCNVVVRYGLLTNEISMVQARGRARAGQSVYSFLATEGSREMKRELTNEALEVLMEKAVAAVQKMDPDEFKAKIRDLQQASLVKRAARAAHREIQQGQFLPEHVQLLCINCMVAVGYGSDLRKVEGTHHVNVNPNFSVYYTTSQNPVVINKVFKDWRPGGTIRCSNCGEVWGFQMIYKSVTLPVLKIGSILLETPRGKIQAKKWSRVPFSIPVFDILQDCTQSLSELSLD |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in mammary tissues. Expressed in liver and testis. Expressed at lower level in spleen, embryo, mammary gland and breast tumors.
Induction
By interferon (IFN), virus infection, or intracellular dsRNA.
Gene expression databases
Interaction
Subunit
Monomer in the absence of dsRNA. Homodimer in the presence of dsRNA. Interacts with RIGI (via CARD domain), MAVS/IPS1 and DDX60. Found in a complex with RIGI and IFIH1/MDA5. Interacts with ANKRD17. Directly interacts with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-188 | Helicase ATP-binding | ||||
Sequence: ILPALEGKNIIIWLPTGAGKTRAAAFVAKRHLETVDRGKVVVLVNRVHLVSQHAEEFRRMLDKHWTVTTLSGDMGSRAGFGLMARSHDLLICTAELLQLALNSSEEDEHVELREFSLIVVDECHHTHKDTVYNTILSRYLEQKLKKAEPLPQVLGLTASPGTGGATKLQGAIDHILQL | ||||||
Motif | 131-134 | DECH box | ||||
Sequence: DECH | ||||||
Domain | 353-514 | Helicase C-terminal | ||||
Sequence: MLERILLKQFGSPGHTRGIIFTRTRQTASSLLLWLRQQPCLQTVGIKPQMLIGAGNTSQSTHMTQKDQQEVIQEFRDGILSLLVATSVAEEGLDIAQCNVVVRYGLLTNEISMVQARGRARAGQSVYSFLATEGSREMKRELTNEALEVLMEKAVAAVQKMD | ||||||
Coiled coil | 489-546 | |||||
Sequence: EMKRELTNEALEVLMEKAVAAVQKMDPDEFKAKIRDLQQASLVKRAARAAHREIQQGQ | ||||||
Domain | 542-669 | RLR CTR | ||||
Sequence: IQQGQFLPEHVQLLCINCMVAVGYGSDLRKVEGTHHVNVNPNFSVYYTTSQNPVVINKVFKDWRPGGTIRCSNCGEVWGFQMIYKSVTLPVLKIGSILLETPRGKIQAKKWSRVPFSIPVFDILQDCT | ||||||
Region | 572-655 | RNA-binding | ||||
Sequence: VEGTHHVNVNPNFSVYYTTSQNPVVINKVFKDWRPGGTIRCSNCGEVWGFQMIYKSVTLPVLKIGSILLETPRGKIQAKKWSRV |
Domain
The RLR CTR domain is capable of inhibiting dimerization and signaling of RIGI and also facilitates binding of dsRNA.
Sequence similarities
Belongs to the helicase family. RLR subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length678
- Mass (Da)76,709
- Last updated2011-07-27 v2
- ChecksumD907A30E3AD376A8
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 638 | in Ref. 1; AAK15474/AAK15475 and 3; AAH29209 | ||||
Sequence: I → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF316999 EMBL· GenBank· DDBJ | AAK15474.1 EMBL· GenBank· DDBJ | mRNA | ||
AF317000 EMBL· GenBank· DDBJ | AAK15475.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591469 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC029209 EMBL· GenBank· DDBJ | AAH29209.1 EMBL· GenBank· DDBJ | mRNA |