Q9GLV6

SS
Gene name
DDX58
Protein name
Antiviral innate immune response receptor RIG-I
Names
DEAD box protein 58, Probable ATP-dependent RNA helicase DDX58, RHIV-1, RIG-I-like receptor 1, RLR-1, RNA helicase induced by virus, Retinoic acid-inducible gene 1 protein, RIG-1, Retinoic acid-inducible gene I protein, RIG-I
Species
Sus scrofa (Pig)
KEGG Pathway
EC number
3.6.4.13: Acting on ATP; involved in cellular and subcellular movement
Protein Class

Descriptions

Retinoic-acid-inducible gene-I (RIG-I; also called DDX58) is a cytosolic viral RNA receptor that interacts with MAVS to induce type I interferon-mediated host protective innate immunity against viral infection. The amino-terminal caspase recruitment domains (CARDs) of RIG-I undergo robust ubiquitination induced by TRIM25 that is involved in cell proliferation and antiviral activity in mammalian cells. In resting cells, RIG-I RD (a C-terminal Repressor domain) represses its CARDs signaling. After viral infection, RIG-I RD recognizes 5’-triphosphate double-stranded RNA (dsRNA), which results in a conformational change in the RIG-I protein.

Autoinhibitory domains (AIDs)

795-928 (Repressor domain) SS

Target domain

1-186 (CARD domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9GLV6

Entry ID Method Resolution Chain Position Source
AF-Q9GLV6-F1 Predicted AlphaFoldDB

No variants for Q9GLV6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9GLV6

No associated diseases with Q9GLV6

8 regional properties for Q9GLV6

Type Name Position InterPro Accession
domain Helicase, C-terminal 613 - 779 IPR001650
domain DEAD/DEAH box helicase domain 244 - 409 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 237 - 450 IPR014001
domain RIG-I-like receptor, C-terminal regulatory domain 795 - 928 IPR021673
domain Caspase recruitment domain 1 - 92 IPR031964-1
domain Caspase recruitment domain 100 - 186 IPR031964-2
domain RIG-I-like receptor, C-terminal 456 - 604 IPR041204
domain RIG-I, CARD domain repeat 2 100 - 186 IPR042145

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm
  • Cell projection, ruffle membrane
  • Cytoplasm, cytoskeleton
  • Cell junction, tight junction
  • Colocalized with TRIM25 at cytoplasmic perinuclear bodies
  • Associated with the actin cytoskeleton at membrane ruffles
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
bicellular tight junction An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
ribonucleoprotein complex A macromolecular complex that contains both RNA and protein molecules.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
double-stranded RNA binding Binding to double-stranded RNA.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.
single-stranded RNA binding Binding to single-stranded RNA.
zinc ion binding Binding to a zinc ion (Zn).

14 GO annotations of biological process

Name Definition
antiviral innate immune response A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogens.
cellular response to exogenous dsRNA Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an exogenous double-stranded RNA stimulus.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
positive regulation of defense response to virus by host Any host process that results in the promotion of antiviral immune response mechanisms, thereby limiting viral replication.
positive regulation of interferon-alpha production Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
positive regulation of interferon-beta production Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
positive regulation of interleukin-6 production Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
positive regulation of myeloid dendritic cell cytokine production Any process that activates or increases the frequency, rate, or extent of myeloid dendritic cell cytokine production.
positive regulation of response to cytokine stimulus Any process that increases the rate, frequency, or extent of a response to cytokine stimulus.
positive regulation of tumor necrosis factor production Any process that activates or increases the frequency, rate or extent of tumor necrosis factor production.
regulation of cell migration Any process that modulates the frequency, rate or extent of cell migration.
response to exogenous dsRNA Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an exogenous double-stranded RNA stimulus.
response to virus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus.
RIG-I signaling pathway The series of molecular signals initiated by the binding of viral RNA to a pattern recognition receptor (PRR) RIG-1 (also known as DDX58). RIG-I is a cytoplasmic receptor that detects RNA synthesized during viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q96C10 DHX58 ATP-dependent RNA helicase DHX58 Homo sapiens (Human) PR
Q9BYX4 IFIH1 Interferon-induced helicase C domain-containing protein 1 Homo sapiens (Human) PR
O95786 RIGI Antiviral innate immune response receptor RIG-I Homo sapiens (Human) EV
Q8R5F7 Ifih1 Interferon-induced helicase C domain-containing protein 1 Mus musculus (Mouse) PR
Q6Q899 Ddx58 Antiviral innate immune response receptor RIG-I Mus musculus (Mouse) SS
10 20 30 40 50 60
MTAEQRRNLH AFGDYVRKTL DPTFILSYMA PWFRDDEVQH IQAEKNNKGP TEAASLFLQF
70 80 90 100 110 120
LLELQEEGWF RGFLDALNQA GYCGLCEAIE SWDFQKIEKL EEYRSLLRRL QPEFKTTINP
130 140 150 160 170 180
KDILPEIAEC LISQECEEIL QICSSKGLMA GAEKMVECLL RSDKENWPKT LKLALEKEES
190 200 210 220 230 240
RFSELWMVDK GAEDVKMKDL EDDEMKTCDV QIFYKEEPEN QNLSQNSCSS SAPHTYSPLK
250 260 270 280 290 300
PRKYQLELAL PAQNGKNTII CAPTGCGKTF VSLLICEHHL KKFPRGRKGK VVFFAIQLPV
310 320 330 340 350 360
YEQQKSVFSK HFERLGYKVA GISGATSDTV CVEQIVENSD IIILTPQILV NCLTNGTIPS
370 380 390 400 410 420
LSVFTLMIFD ECHNTSKQHP YNVIMFSYLD RKLGGSSDSL PQVIGLTASV GVGDAKNKAE
430 440 450 460 470 480
ATEYICKLCA SLDTSVIATV RDNLEELEEV VYKPQKFFRK VELRTTDRFK CIISQLMMEI
490 500 510 520 530 540
ESLAKSIFEE LGTITLGGLF QIQNSNFGTQ KYEQWIVKVQ KECAVFQMPD KDKESRICKA
550 560 570 580 590 600
LFSYMSHLRI YNDALIINEH ARMKDALDYL KDFFRNIRAA GFDEIEQDLT QRFEEKLQEL
610 620 630 640 650 660
ESISIDPSNE NPKLRDLCFI LQEEYHLNPE TRTILFVKTR ALVDALKKWI KENPKLSFLK
670 680 690 700 710 720
PSILTGRGKT NQNIGMTLPA QKCVLDTFRT DKDNKILITT SVADEGIDIA QCNLVILYEY
730 740 750 760 770 780
VGNVIKMIQT RGRGRARGSK CFLLTANADL IDKEKMNMYK EEMMNGAILI LQTWDEAVFK
790 800 810 820 830 840
EKIHQIQIRE KIIRDNQGKP EPVPDKKTKK LLCKKCKAFA CYTADIRMVE KCHFTVVGDA
850 860 870 880 890 900
FRERFVSKLH PKPKSFGNIE KRAKIYCARP DCSHDWGIYV RYKAFEMPFI KIESFVVEDI
910 920 930
ATGVQTVHAK WKDFNFEKLS FDAAEMAGGA QDLGLQGMGN