F2RL1 is a member of the G-protein coupled receptor 1 family of proteins. The encoded cell surface receptor is activated through proteolytic cleavage of its extracellular amino terminus, resulting in a new amino terminus that acts as a tethered ligand that binds to an extracellular loop domain. Activation of the receptor has been shown to stimulate vascular smooth muscle relaxation, dilate blood vessels, increase blood flow, and lower blood pressure. This protein is also important in the inflammatory response, as well as innate and adaptive immunity.
Biological Process
Bblood coagulation Source: InterPro
Cell-cell junction maintenance Source: UniProtKB
Defense response to virus Source: UniProtKB
Establishment of endothelial barrier Source: UniProtKB
G protein-coupled receptor signaling pathway Source: UniProtKB
Inflammatory response Source: UniProtKB-KW
Innate immune response Source: UniProtKB-KW
Leukocyte migration Source: UniProtKB
Leukocyte proliferation Source: UniProtKB
Mature conventional dendritic cell differentiation Source: UniProtKB
Negative regulation of chemokine production Source: UniProtKB
Negative regulation of JNK cascade Source: UniProtKB
Negative regulation of toll-like receptor 3 signaling pathway Source: UniProtKB
Negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Neutrophil activation Source: UniProtKB
Positive regulation of actin filament depolymerization Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of chemokine production Source: UniProtKB
Positive regulation of chemotaxis Source: UniProtKB
Positive regulation of cytokine production involved in immune response Source: UniProtKB
Positive regulation of cytosolic calcium ion concentration Source: UniProtKB
Positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling Pathway Source: GO_Central
Positive regulation of eosinophil degranulation Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
Positive regulation of glomerular filtration Source: UniProtKB
Positive regulation of GTPase activity Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of interferon-gamma production Source: UniProtKB
Positive regulation of interleukin-10 production Source: UniProtKB
Positive regulation of interleukin-1 beta production Source: UniProtKB
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of interleukin-8 production Source: UniProtKB
Positive regulation of JNK cascade Source: UniProtKB
Positive regulation of leukocyte chemotaxis Source: BHF-UCL
Positive regulation of neutrophil mediated killing of gram-negative bacterium Source: UniProtKB
Positive regulation of phagocytosis, engulfment Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of positive chemotaxis Source: BHF-UCL
Positive regulation of pseudopodium assembly Source: UniProtKB
Positive regulation of renin secretion into blood stream Source: UniProtKB
Positive regulation of Rho protein signal transduction Source: UniProtKB
Positive regulation of superoxide anion generation Source: UniProtKB
Positive regulation of toll-like receptor 2 signaling pathway Source: UniProtKB
Positive regulation of toll-like receptor 3 signaling pathway Source: UniProtKB
Positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of blood coagulation Source: BHF-UCL
Regulation of chemokine (C-X-C motif) ligand 2 production Source: UniProtKB
Regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Regulation of JNK cascade Source: UniProtKB
T cell activation involved in immune response Source: UniProtKB
Vasodilation Source: UniProtKB
PTM
A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888). Activating serine proteases include trypsin, mast cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14 (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888, PubMed:23202369). Subsequent cleavage by serine proteases, including neutrophil elastase and cathepsin G, leads to receptor deactivation (PubMed:12594060). At least in part, implicated proteases are also shown to activate the receptor; the glycosylation status of the receptor is thought to contribute to the difference (PubMed:12171601). In addition to conventional trypsin-like proteases activated by other proteases and glycosidases derived from bacteria, fungi and insects (PubMed:11447194, PubMed:11441110, PubMed:17404307, PubMed:18474671, PubMed:19864598). Activated by serine protease allergens such as dust mite Der p3 and Der p9 and mold Pen c13 (PubMed:11441110, PubMed:17404307). Activated by P.gingivalis arginine-specific (trypsin-like) cysteine proteinases called gingipains (PubMed:11447194). Activated by S.griseus exogenous chitinase (PubMed:18474671). Activated by A.alternata aspartate protease; the cleavage generates non-conventional processed forms (PubMed:19864598).
N-glycosylated and sialylated.
Multiple phosphorylated on serine and threonine residues in the cytoplasmic region upon receptor activation.
Monoubiquitinated by CBL at the plasma membrane and in early endosomes; not required for receptor endocytosis but for translocation to late endosomes or lysosomes. Deubiquitination involves STAMBP and USP8; required for lysosomal trafficking and receptor degradation.
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