FPR1
entrez
2357
canonical
uniprot
P21462
canonical
ensembl
ENSG00000171051
resolver
ensp
ENSP00000302707
resolver
ensp
ENSP00000470750
resolver
ensp
ENSP00000471493
resolver
ensp
ENSP00000472936
resolver
ensp
ENSP00000551867
resolver
ensp
ENSP00000551868
resolver
ensp
ENSP00000551869
resolver
ensp
ENSP00000600543
resolver
ensp
ENSP00000618453
resolver
ensp
ENSP00000618454
resolver
ensp
ENSP00000618455
resolver
enst
ENST00000304748
resolver
enst
ENST00000594900
resolver
enst
ENST00000595042
resolver
enst
ENST00000600815
resolver
enst
ENST00000881808
resolver
enst
ENST00000881809
resolver
enst
ENST00000881810
resolver
enst
ENST00000930484
resolver
enst
ENST00000948394
resolver
enst
ENST00000948395
resolver
enst
ENST00000948396
resolver
genesymbol
FPR1
resolver
hgnc
HGNC:3826
resolver
uniprot
Q14939
resolver
uniprot
Q7Z6A4
resolver
uniprot
Q86U52
resolver
uniprot
Q9NS48
resolver
uniprot_entry
FPR1_HUMAN
resolver
uniprot_sec
Q14939
resolver
uniprot_sec
Q7Z6A4
resolver
uniprot_sec
Q86U52
resolver
uniprot_sec
Q9NS48
resolver
amino_acid_sequence
METNSSLPTNISGGTPAVSAGYLFLDIITYLVFAVTFVLGVLGNGLVIWVAGFRMTHTVTTISYLNLAVADFCFTSTLPFFMVRKAMGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIALDRCVCVLHPVWTQNHRTVSLAKKVIIGPWVMALLLTLPVIIRVTTVPGKTGTVACTFNFSPWTNDPKERINVAVAMLTVRGIIRFIIGFSAPMSIVAVSYGLIATKIHKQGLIKSSRPLRVLSFVAAAFFLCWSPYQVVALIATVRIRELLQGMYKEIGIAVDVTSALAFFNSCLNPMLYVFMGQDFRERLIHALPASLERALTEDSTQTSDTATNSTLPSAEVELQAK
uniprot
proteins
function
FUNCTION: Pattern recognition G protein-coupled receptor (PRR/GPCR) involved in innate recognition of N-formyl-methionyl peptides derived from invading microbes and host mitochondria as pathogen- and damage-associated molecular patterns (PAMPs and DAMPs). Functions as a sensor of PAMPs and DAMPs released upon microbial infection or tissue damage, triggering immune cell activation and chemotaxis to eliminate pathogens and restore tissue homeostasis (PubMed:24108355, PubMed:25605714, PubMed:35217703, PubMed:36064945). Peptide binding leads to conformational changes coupled to heterotrimeric G(i) protein signaling. Upon GDP to GTP conversion, G(i)-alpha subunit dissociates from G-beta and G-gamma subunits. Free G(i)-alpha subunit inhibits cyclic adenylate cyclase and cAMP synthesis whereas the G-beta and G-gamma dimer activates downstream phospholipase C-beta and phosphoinositide 3-kinase signaling cascades leading to Ca(2+) influx (PubMed:10514456, PubMed:15153520, PubMed:1712023, PubMed:25605714, PubMed:35217703, PubMed:36064945). Displays two affinity states for peptide agonists, low and high, likely accounting for selective signaling of myeloid cell functions at different phases of the inflammatory response. Subnanomolar concentrations of peptide agonists induce myeloid cell chemotaxis, whereas micromolar concentrations trigger degranulation and superoxide production (PubMed:2161213, PubMed:2176894, PubMed:24108355, PubMed:25605714). May recognize a myriad of bacterial signal peptides indicative of an evolutionary conserved detection mechanism in host defense against bacterial infection. Triggers bactericidal functions of neutrophils and phagocytes in response to N-formyl-Met-Leu-Phe (fMLF) which is part of the signal peptide sequences of hundreds distinct bacterial strains (PubMed:25605714). In the homeostatic wound healing response to tissue injury, senses 'necrotaxis' DAMP-type signals released in the form of mitochondria-derived N-formylated peptides and guides neutrophil trafficking toward necrotic cells within the injury site (By similarity). In the context of antitumor immunity, interacts with ANXA1 and guides dendritic cell positioning in close proximity to necrotic tumor cells, allowing for tumor-associated antigen uptake and cross-presentation to T cells (PubMed:24108355, PubMed:26516201). Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing reactive oxygen species (ROS) release (PubMed:25109685). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (PubMed:15210802). Beyond canonical N-terminal formylated peptide agonists, can also be activated by C-terminal amidated peptides, which appear to all share a tripartite structure motif oriented around a carboxyl group (PubMed:24108355, PubMed:25605714). Differential signaling is also defined by receptor oligomerization state. Pro-resolving ligands, such as lipoxin A4 or ANXA1, induce the formation of FPR1:FPR2 heterodimers triggering proapoptotic JNK pathway in neutrophils (PubMed:24108355). {ECO:0000250|UniProtKB:P33766, ECO:0000269|PubMed:10514456, ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:1712023, ECO:0000269|PubMed:2161213, ECO:0000269|PubMed:2176894, ECO:0000269|PubMed:24108355, ECO:0000269|PubMed:25109685, ECO:0000269|PubMed:25605714, ECO:0000269|PubMed:26516201, ECO:0000269|PubMed:35217703, ECO:0000269|PubMed:36064945, ECO:0000303|PubMed:10514456, ECO:0000303|PubMed:1712023, ECO:0000303|PubMed:2161213, ECO:0000303|PubMed:2176894}.; FUNCTION: (Microbial infection) Used by Y. pestis as a receptor on human immune cells. Upon infection, Y. pestis releases N-formyl peptides that activate FPR1-mediated immune signaling and chemotaxis. This leads to Y. pestis docking on FPR1 via the lcrV needle cap protein of its type III secretion system (T3SS) followed by the delivery of effector proteins into host immune cells, ultimately triggering immune cell apoptosis. {ECO:0000269|PubMed:31534221}.
uniprot
proteins
mass_dalton
38446
uniprot
proteins
mutagenesis
MUTAGEN 81; /note="F->A: Slightly decreases intracellular cAMP reduction upon stimulation with N-formylated fMLF peptide."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 84; /note="R->D: Decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII."; /evidence="ECO:0000269|PubMed:35217703"; MUTAGEN 102; /note="F->A: Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF. Slightly decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 102; /note="F->H: Decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII."; /evidence="ECO:0000269|PubMed:35217703"; MUTAGEN 106; /note="D->A: Abolishes the response to N-formyl peptides fMLF, fMIFL and fMLFII."; /evidence="ECO:0000269|PubMed:35217703, ECO:0000269|PubMed:36064945"; MUTAGEN 106; /note="D->N: Abolishes the response to N-formyl peptides fMLF and fMIFL."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 109; /note="L->A: Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF. Decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 110; /note="F->A: Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 178; /note="F->A: Decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 201; /note="R->A: Abolishes the response to N-formyl peptide fMLF. Decreases intracellular cAMP reduction upon stimulation with N-formyl peptides fMIFL and fMLFII. Abolishes the response to fMIFL; when associated with A-205. Decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:35217703, ECO:0000269|PubMed:36064945"; MUTAGEN 205; /note="R->A: Abolishes the response to N-formyl peptide fMLF. Decreases intracellular cAMP reduction upon stimulation with N-formyl peptides fMIFL and fMLFII. Abolishes the response to fMIFL; when associated with A-201. Slightly decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:35217703, ECO:0000269|PubMed:36064945"; MUTAGEN 257; /note="Y->F: Decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII."; /evidence="ECO:0000269|PubMed:35217703"; MUTAGEN 265; /note="T->A: Decreases the agonist potency of non-formylated WKYMVm peptide."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 277; /note="K->D: No significant effect on intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII."; /evidence="ECO:0000269|PubMed:35217703"; MUTAGEN 283; /note="V->A: No significant effect on intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF."; /evidence="ECO:0000269|PubMed:36064945"; MUTAGEN 291; /note="F->A: Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF."; /evidence="ECO:0000269|PubMed:36064945
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; which is necessary for desensitization. {ECO:0000269|PubMed:10514456}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10514456
uniprot
proteins
pubmed
1445895
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15153520
uniprot
proteins
pubmed
15210802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1612600
uniprot
proteins
pubmed
1712023
uniprot
proteins
pubmed
2161213
uniprot
proteins
pubmed
2176894
uniprot
proteins
pubmed
24108355
uniprot
proteins
pubmed
25109685
uniprot
proteins
pubmed
25605714
uniprot
proteins
pubmed
26516201
uniprot
proteins
pubmed
31534221
uniprot
proteins
pubmed
35217703
uniprot
proteins
pubmed
36064945
uniprot
proteins
pubmed
8224916
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:2176894, ECO:0000269|PubMed:24108355, ECO:0000269|PubMed:25109685, ECO:0000305|PubMed:10514456}; Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in presence of its ligands, fMLP, TAFA4 and CTSG. {ECO:0000269|PubMed:15210802, ECO:0000269|PubMed:25109685}.
uniprot
proteins
transmembrane_region
TRANSMEM 28..50; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 62..83; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 101..121; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 141..162; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 206..226; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 243..266; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 286..305; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins