| Full protein name | ATP-dependent RNA helicase laf-1;DEAD-box RNA helicase laf-1 |
| Gene name | laf-1;Y71H2AM.19 |
| Species | Caenorhabditis elegans |
| Localization | Cytoplasm; Cytoplasmic granule. |
| Description | LAF-1, an ATP-dependent DDX3 RNA helicase found in P granules, plays a role in RNA remodeling, but is not required for RNA unwinding. Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA. This process is also dependent upon ATP; ATP reduces binding to RNA and subsequently diminishes RNA annealing. Promotes liquid-liquid phase separation of P granules, which is a process important for intracellular organization and stress granule assembly. The purely viscous properties highly tunable by salt and RNA concentration. RNA decreases viscosity and increases molecular dynamics within the droplet. LAF-1 is comprised of an intrinsically disordered RGG domain at its N terminus, followed by a helicase domain and disordered C-terminal domain. The N-terminal, arginine/glycine rich, intrinsically disordered protein (IDP) domain of LAF-1 is necessary and sufficient for both phase separation and RNA-protein interactions. The C-terminal of LAF-1 (LAF-1^C) contains a R/G/Q rich domain，which doesn’t undergo phase transitions along, while the WT LAF-1 and LAF-1^RGG does. |
| GO term | GO:0005524; ATP binding; IEA:UniProtKB-KW. GO:0140603; ATP hydrolysis activity; IEA:RHEA. GO:0008186; ATPase, acting on RNA; IDA:UniProtKB. GO:0042802; identical protein binding; IDA:UniProtKB. GO:0003723; RNA binding; IBA:GO_Central. GO:0003724; RNA helicase activity; IBA:GO_Central. GO:0033592; RNA strand annealing activity; IMP:UniProtKB. |
| Full sequence length | 708 |
| Database linked | MobiDB :D0PV95 DisProt :DP01113 |
| IDR Region | 1 708 |
| LCR Region | 1 708 |