Rigi
entrez
230073
canonical
uniprot
Q6Q899
canonical
ensembl
ENSMUSG00000040296
resolver
ensp
ENSMUSP00000042433
resolver
genesymbol
Rigi
resolver
genesymbol_syn
Ddx58
resolver
uniprot
A1L0V6
resolver
uniprot
A2AP28
resolver
uniprot
Q8C320
resolver
uniprot
Q8C5I3
resolver
uniprot
Q8C7T2
resolver
uniprot_entry
A1L0V6_MOUSE
resolver
uniprot_entry
RIGI_MOUSE
resolver
uniprot_sec
A2AP28
resolver
uniprot_sec
Q8C320
resolver
uniprot_sec
Q8C5I3
resolver
uniprot_sec
Q8C7T2
resolver
amino_acid_sequence
MTAEQRQNLQAFRDYIKKILDPTYILSYMSSWLEDEEVQYIQAEKNNKGPMEAASLFLQYLLKLQSEGWFQAFLDALYHAGYCGLCEAIESWDFQKIEKLEEHRLLLRRLEPEFKATVDPNDILSELSECLINQECEEIRQIRDTKGRMAGAEKMAECLIRSDKENWPKVLQLALEKDNSKFSELWIVDKGFKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNPGPPSEASSNNLHSPLKPRNYQLELALPAKKGKNTIICAPTGCGKTFVSLLICEHHLKKFPCGQKGKVVFFANQIPVYEQQATVFSRYFERLGYNIASISGATSDSVSVQHIIEDNDIIILTPQILVNNLNNGAIPSLSVFTLMIFDECHNTSKNHPYNQIMFRYLDHKLGESRDPLPQVVGLTASVGVGDAKTAEEAMQHICKLCAALDASVIATVRDNVAELEQVVYKPQKISRKVASRTSNTFKCIISQLMKETEKLAKDVSEELGKLFQIQNREFGTQKYEQWIVGVHKACSVFQMADKEEESRVCKALFLYTSHLRKYNDALIISEDAQMTDALNYLKAFFHDVREAAFDETERELTRRFEEKLEELEKVSRDPSNENPKLRDLYLVLQEEYHLKPETKTILFVKTRALVDALKKWIEENPALSFLKPGILTGRGRTNRATGMTLPAQKCVLEAFRASGDNNILIATSVADEGIDIAECNLVILYEYVGNVIKMIQTRGRGRARDSKCFLLTSSADVIEKEKANMIKEKIMNESILRLQTWDEMKFGKTVHRIQVNEKLLRDSQHKPQPVPDKENKKLLCGKCKNFACYTADIRVVETSHYTVLGDAFKERFVCKPHPKPKIYDNFEKKAKIFCAKQNCSHDWGIFVRYKTFEIPVIKIESFVVEDIVSGVQNRHSKWKDFHFERIQFDPAEMSV
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines. Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments. The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms. Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons. Ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Sendai virus (SeV), Rhabdoviridae and Flaviviridae. It also detects rotavirus and orthoreovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome. Detects dsRNA produced from non-self dsDNA by RNA polymerase III. May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:16039576, ECO:0000269|PubMed:16625202, ECO:0000269|PubMed:17942531, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.
uniprot
proteins
mass_dalton
105975
uniprot
proteins
mutagenesis
MUTAGEN 813; /note="K->R: Greatly decreases 'K-48'-linked ubiquitination."; /evidence="ECO:0000269|PubMed:23374343
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-771 results in inhibition of its activity while dephosphorylation at these sites results in its activation. {ECO:0000250|UniProtKB:O95786}.; PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response. {ECO:0000250|UniProtKB:O95786}.; PTM: Sumoylated, probably by MUL1; inhibiting its polyubiquitination. {ECO:0000250|UniProtKB:O95786}.; PTM: Acetylated in response to RNA virus infection. Deacetylated by HDAC6 in the presence of viral mRNAs which is required for detection of viral RNA by RIGI. {ECO:0000250|UniProtKB:O95786}.; PTM: Ubiquitinated. 'Lys-63' ubiquitination by RNF135, which occurs after RNA-binding and homodimerization, releases the autoinhibition of the CARD domains by the RLR CTR domain, an essential step in the activation of the RIG-I signaling pathway. Also ubiquitinated by TRIM4. Also undergoes 'Lys-48' ubiquitination by RNF125 that leads to proteasomal degradation. 'Lys-48' ubiquitination follows viral infection and is enhanced by 'Lys-63'-linked ubiquitination of the CARD domains that promotes interaction with VCP/p97 and subsequent recruitment of RNF125 (By similarity). Within a negative feedback loop involving SIGLEC10 and PTPN11, 'Lys-48' ubiquitination at Lys-813 by CBL also elicits the proteasomal degradation of RIGI (PubMed:23374343). Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'- and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor (By similarity). Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation (By similarity). Deubiquitinated by USP27X that cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (By similarity). Deubiquitinated by USP3 that also cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (By similarity). {ECO:0000250|UniProtKB:O95786, ECO:0000269|PubMed:23374343}.; PTM: Degraded via selective autophagy following interaction with Irgm1. Irgm1 promotes RIGI recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:O95786}.
uniprot
proteins
protein_family
Helicase family
uniprot
proteins
protein_family
RLR subfamily
uniprot
proteins
pubmed
16039576
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16625202
uniprot
proteins
pubmed
17942531
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19576794
uniprot
proteins
pubmed
19609254
uniprot
proteins
pubmed
19631370
uniprot
proteins
pubmed
20950133
uniprot
proteins
pubmed
21175414
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21496944
uniprot
proteins
pubmed
21616437
uniprot
proteins
pubmed
21884169
uniprot
proteins
pubmed
21979817
uniprot
proteins
pubmed
23374343
uniprot
proteins
pubmed
29259080
uniprot
proteins
sequence_length
926
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles. {ECO:0000250}.
uniprot
proteins