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Gene and Protein Information | ||||||
class A G protein-coupled receptor | ||||||
Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | 7 | 351 | 19q13.41 | FPR2 | formyl peptide receptor 2 | 4,69 |
Mouse | 7 | 351 | 17 A3.2 | Fpr2 | formyl peptide receptor 2 | 34,97 |
Rat | 7 | 351 | 1q12 | Fpr2 | formyl peptide receptor 2 | 14,68 |
Database Links | |
Specialist databases | |
GPCRdb | fpr2_human (Hs), fpr2_mouse (Mm) |
Other databases | |
Alphafold | P25090 (Hs), O88536 (Mm) |
ChEMBL Target | CHEMBL4227 (Hs), CHEMBL4739842 (Mm) |
Ensembl Gene | ENSG00000171049 (Hs), ENSMUSG00000052270 (Mm), ENSRNOG00000042605 (Rn) |
Entrez Gene | 2358 (Hs), 14289 (Mm), 690158 (Rn) |
Human Protein Atlas | ENSG00000171049 (Hs) |
KEGG Gene | hsa:2358 (Hs), mmu:14289 (Mm), rno:690158 (Rn) |
OMIM | 136538 (Hs) |
Pharos | P25090 (Hs) |
RefSeq Nucleotide | NM_001462 (Hs), NM_008042 (Mm) |
RefSeq Protein | NP_001453 (Hs), NP_032068 (Mm) |
UniProtKB | P25090 (Hs), O88536 (Mm) |
Wikipedia | FPR2 (Hs) |
Natural/Endogenous Ligands |
annexin I {Sp: Human} , annexin I {Sp: Mouse} , annexin I {Sp: Rat} |
aspirin triggered lipoxin A4 |
aspirin-triggered resolvin D1 |
CRAMP {Sp: Mouse} |
humanin {Sp: Human} |
LL-37 {Sp: Human} |
LXA4 |
PrP106-126 |
resolvin D1 |
serum amyloid A {Sp: Human} |
Potency order of endogenous and other ligands |
LXA4 = aspirin triggered lipoxin A4 = ATLa2 = resolvin D1 > LTC4 = LTD4 >> 15-deoxy-LXA4 >> fMet-Leu-Phe [17,26,29,39,97] |
Download all structure-activity data for this target as a CSV file
Agonists | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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View species-specific agonist tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Agonist Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Listed above are major FPR2/ALX agonists and several agonists for mouse Fpr2 (Fpr-rs2). They are grouped into several classes: 1. Bacteria-derived formyl peptides: The classic tripeptide fMet-Leu-Phe is a low affinity agonist for FPR2/ALX and is not an activator for mouse Fpr2. The PSMα3 peptide from highly pathogenic S. aureus has a pEC50 value of 8.67 and is one of the most potent bacterial formyl peptides for FPR2/ALX. 2. Mitochondria-derived formyl peptides: fMet-Met-Tyr-Ala-Leu-Phe (ND6), fMet-Leu-Lys-Leu-Ile-Val (ND4), and fMet-Tyr-Phe-Ile-Asn-Ile-Leu-Thr-Leu (ND1) are endogenous agonists for FPR2/ALX [83]. 3. Lipid mediators: resolvin D1 (RvD1) and lipoxin A4 (LXA4). LXA4 is highly potent in triggering anti-inflammatory functions in animal models. Cell-based studies suggest that FPR2/ALX is a receptor for LXA4 in several published reports [13,26,28], but others failed to identify LXA4-induced GPCR responses [31,40,78]. One of the reasons could be agonist (LXA4) batch difference. A recent study [54] showed that RvD1 and LXA4 selectively activate the beta-arrestin pathway, suggesting that RvD1 and LXA4 might be partial agonists or biased agonists at ALX/FPR2. See [40] for a different outcome in β-arrestin translocation by LXA4. 4. Host-derived non-amyloidogenic peptides: This class includes SHAAGtide, LL-37, CCL-23, humanin, and uPAR(88-274)/D2D3. Annexin and derived peptides are also host-derived non-amyloidogenic peptides, but some of these peptides are less selective between FPR1 and FPR2/ALX. 5. Host-derived amyloidogenic peptides: SAA and Aβ[1-42] are two agonists in this class. They also bind and activate other receptors. 6. HIV-1 envelope peptides: These are T21/DP107, N36, F peptide, and V3 peptide. 7. Prion peptide: PrP (106-126) is the only member of this class, derived from prion proteins. 8. Peptides identified from library screen: This class is represented by WKYMVm and MMK-1. Other peptides with lower potency or affinity are not shown. 9. Synthetic compounds which are FPR2/ALX-specific agonists: Quin-C1, N`-Phenylurea derivatives (AG-26, AG-09/37, AG-09/38, AG-09/42, and AG-09/43), 2-(N-piperazinyl) acetamide derivatives (AG-09/3, AG-09/4, AG-09/73 through AG-09/77, and AG-09/82), and acetohydrazide derivatives (AG-09/7, AG-09/92, AG-09/96, AG-09/101, and AG-09/102). Selected chiral 6-methyl-2, 4-disubstituted pyridazin-3(2H)-compounds are potent mixed FPR1/FPR2/ALX agonists, among which R-(-)-forms generally exhibited higher activity than the S-(+)-enantiomers [16]. Pyrazolone, 4-iodo-substituted compound no. 43 activates FPR2/ALX and mouse Fpr1. Mouse Fpr2 shares most of its binding properties with human FPR2/ALX. One of the differences is the inability for the mouse Fpr2 to bind and interact with most formylpeptides tested. The exceptions are long peptides such as fMLFII, fMMYALF (from mitochondria), fMIVIL (from L. monocytogenes), which are better agonists with reasonably good EC50 in most functional assays. Hp(2-20), a peptide from H. pylori induced a rise in intracellular calcium levels in cells tranfected with FPR2/ALX; however the efficacy of this peptide was greater at FPRL2-expressing cells [5]. |
Antagonists | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Antagonist Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
The available FPR2/ALX antagonists are very limited at this time. The recently identified compound (1754-31) is one of the most potent FPR2/ALX antagonists. None of the FPR2/ALX antagonists are found to have inverse agonistic activity. t-Boc-FLFLF is shown in some publications as an antagonist for both FPR1 and FPR2/ALX. In a recent publication, its antagonistic activity is found to be more selective for FPR1 than FPR2/ALX [71]. |
Allosteric Modulators | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Allosteric Modulator Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||
PBP10 is a cell-permeable, rhodamine B-coupled polyphosphoinositide-binding peptide based on gelsolin a.a. 160-169. PBP10 inhibits neutrophil degranulation and superoxide generation induced by FPR2/ALX agonists but not FPR1 agonists. However, PBP10 does not affect agonist-induced calcium mobilization, suggesting that it is an allosteric modulator of FPR2/ALX mediated functions [30,33]. |
Immunopharmacology Comments |
Formyl peptide receptor type 2 (FPR2/ALX) activation by lipoxin A4 and annexin 1 has been linked to resolution of inflammation, via upregulation of anti-inflammatory cytokines including IL-10. Resolvin D1-mediated activation of FPR2/ALX appears to resolve salivary gland inflammation in a mouse model of Sjögren syndrome [101]. FPR2/ALX receptor agonism is a new therapeutic concept that is being investigated for the development of novel non-steroidal anti-inflammatory agents as modulators of pathological dysregulated inflammation [6-7]. Since endogenous pro-resolving mediators like lipoxin A4 are highly unstable, investigators are designing lipoxin mimetics with improved physicochemical properties [18]. |
Immuno Process Associations | ||
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Primary Transduction Mechanisms | |
Transducer | Effector/Response |
Gi/Go family |
Phospholipase C stimulation Phospholipase A2 stimulation Phospholipase D stimulation |
References: 26-27,48,57,73-74 |
Secondary Transduction Mechanisms | |
Transducer | Effector/Response |
Gq/G11 family |
Phospholipase C stimulation Phospholipase A2 stimulation Phospholipase D stimulation Other - See Comments |
Comments: FPR2/ALX joins a small group of chemoattractant/chemokine receptors which share a mechanism of using CD38-dependent cyclic ADP ribose for calcium flux and chemotaxis. Many of these receptors also couple to Gq in addition to Gi proteins. | |
References: 73-74 |
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Xenobiotics Influencing Gene Expression | ||||||||||
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Phenotypes, Alleles and Disease Models | Mouse data from MGI | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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General Comments |
The nomenclature for this receptor is outlined in the 2022 NC-IUPHAR review by Qin et al. [80]. It is important to validate chemical structures of LXA4, ATL and RvD1 before carrying out receptor assays because these ligands are chemically fragile and require precise working conditions at the bench. Also, it is noteworthy that LXA4 and RvD1 are subject to rapid metabolic conversion by mammalian cells and cell lines. |
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