Overview
| Uniprot ID | O95786 |
|---|
| Protein Name | Antiviral innate immune response receptor RIG-I |
|---|
| Gene Name | RIGI |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 851 |
SRPHPKPKQFSSFEK |
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 (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). 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 (PubMed:28469175, PubMed:31006531). 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 (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.74). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration
Protein Sequence
10
MTTEQRRSLQ
20
AFQDYIRKTL
30
DPTYILSYMA
40
PWFREEEVQY
50
IQAEKNNKGP
60
MEAATLFLKF
70
LLELQEEGWF
80
RGFLDALDHA
90
GYSGLYEAIE
100
SWDFKKIEKL
110
EEYRLLLKRL
120
QPEFKTRIIP
130
TDIISDLSEC
140
LINQECEEIL
150
QICSTKGMMA
160
GAEKLVECLL
170
RSDKENWPKT
180
LKLALEKERN
190
KFSELWIVEK
200
GIKDVETEDL
210
EDKMETSDIQ
220
IFYQEDPECQ
230
NLSENSCPPS
240
EVSDTNLYSP
250
FKPRNYQLEL
260
ALPAMKGKNT
270
IICAPTGCGK
280
TFVSLLICEH
290
HLKKFPQGQK
300
GKVVFFANQI
310
PVYEQQKSVF
320
SKYFERHGYR
330
VTGISGATAE
340
NVPVEQIVEN
350
NDIIILTPQI
360
LVNNLKKGTI
370
PSLSIFTLMI
380
FDECHNTSKQ
390
HPYNMIMFNY
400
LDQKLGGSSG
410
PLPQVIGLTA
420
SVGVGDAKNT
430
DEALDYICKL
440
CASLDASVIA
450
TVKHNLEELE
460
QVVYKPQKFF
470
RKVESRISDK
480
FKYIIAQLMR
490
DTESLAKRIC
500
KDLENLSQIQ
510
NREFGTQKYE
520
QWIVTVQKAC
530
MVFQMPDKDE
540
ESRICKALFL
550
YTSHLRKYND
560
ALIISEHARM
570
KDALDYLKDF
580
FSNVRAAGFD
590
EIEQDLTQRF
600
EEKLQELESV
610
SRDPSNENPK
620
LEDLCFILQE
630
EYHLNPETIT
640
ILFVKTRALV
650
DALKNWIEGN
660
PKLSFLKPGI
670
LTGRGKTNQN
680
TGMTLPAQKC
690
ILDAFKASGD
700
HNILIATSVA
710
DEGIDIAQCN
720
LVILYEYVGN
730
VIKMIQTRGR
740
GRARGSKCFL
750
LTSNAGVIEK
760
EQINMYKEKM
770
MNDSILRLQT
780
WDEAVFREKI
790
LHIQTHEKFI
800
RDSQEKPKPV
810
PDKENKKLLC
820
RKCKALACYT
830
ADVRVIEECH
840
YTVLGDAFKE
850
CFVSRPHPKP
860
KQFSSFEKRA
870
KIFCARQNCS
880
HDWGIHVKYK
890
TFEIPVIKIE
900
SFVVEDIATG
910
VQTLYSKWKD
920
FHFEKIPFDP
AEMSK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015629 |
actin cytoskeleton |
| Cellular Component |
GO:0005923 |
bicellular tight junction |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:1990904 |
ribonucleoprotein complex |
| Cellular Component |
GO:0032587 |
ruffle membrane |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0003690 |
double-stranded DNA binding |
| Molecular Function |
GO:0003725 |
double-stranded RNA binding |
| Molecular Function |
GO:0005525 |
GTP binding |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0038187 |
pattern recognition receptor activity |
| Molecular Function |
GO:0003724 |
RNA helicase activity |
| Molecular Function |
GO:0003727 |
single-stranded RNA binding |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0140374 |
antiviral innate immune response |
| Biological Process |
GO:0071360 |
cellular response to exogenous dsRNA |
| Biological Process |
GO:0002753 |
cytoplasmic pattern recognition receptor signaling pathway |
| Biological Process |
GO:0051607 |
defense response to virus |
| Biological Process |
GO:0009597 |
detection of virus |
| Biological Process |
GO:0010467 |
gene expression |
| Biological Process |
GO:0045087 |
innate immune response |
| Biological Process |
GO:0002230 |
positive regulation of defense response to virus by host |
| Biological Process |
GO:0010628 |
positive regulation of gene expression |
| Biological Process |
GO:0032725 |
positive regulation of granulocyte macrophage colony-stimulating factor production |
| Biological Process |
GO:0032727 |
positive regulation of interferon-alpha production |
| Biological Process |
GO:0032728 |
positive regulation of interferon-beta production |
| Biological Process |
GO:0032755 |
positive regulation of interleukin-6 production |
| Biological Process |
GO:0032757 |
positive regulation of interleukin-8 production |
| Biological Process |
GO:0002735 |
positive regulation of myeloid dendritic cell cytokine production |
| Biological Process |
GO:0060760 |
positive regulation of response to cytokine stimulus |
| Biological Process |
GO:0045944 |
positive regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0032760 |
positive regulation of tumor necrosis factor production |
| Biological Process |
GO:0030334 |
regulation of cell migration |
| Biological Process |
GO:0034344 |
regulation of type III interferon production |
| Biological Process |
GO:0043330 |
response to exogenous dsRNA |
| Biological Process |
GO:0009615 |
response to virus |
| Biological Process |
GO:0039529 |
RIG-I signaling pathway |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.