Fpr1
entrez
14293
canonical
uniprot
P33766
canonical
ensembl
ENSMUSG00000045551
resolver
ensp
ENSMUSP00000052894
resolver
enst
ENSMUST00000061516
resolver
genesymbol
Fpr1
resolver
uniprot
Q3UV01
resolver
uniprot_entry
FPR1_MOUSE
resolver
uniprot_sec
Q3UV01
resolver
amino_acid_sequence
MDTNMSLLMNKSAVNLMNVSGSTQSVSAGYIVLDVFSYLIFAVTFVLGVLGNGLVIWVAGFRMKHTVTTISYLNLAIADFCFTSTLPFYIASMVMGGHWPFGWFMCKFIYTVIDINLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLAKKVIIVPWICAFLLTLPVIIRLTTVPNSRLGPGKTACTFDFSPWTKDPVEKRKVAVTMLTVRGIIRFIIGFSTPMSIVAICYGLITTKIHRQGLIKSSRPLRVLSFVVAAFFLCWCPFQVVALISTIQVRERLKNMTPGIVTALKITSPLAFFNSCLNPMLYVFMGQDFRERLIHSLPASLERALTEDSAQTSDTGTNLGTNSTSLSENTLNAM
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:18606697, PubMed:25605714, PubMed:8244972, PubMed:9989980). 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 (By similarity) (PubMed:8244972, PubMed:9989980). 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 (By similarity). 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:18606697, PubMed:25605714, PubMed:9989980). 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 (PubMed:20947763). 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:26516201). Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing reactive oxygen species (ROS) release (By similarity). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (By similarity). 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: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 (By similarity). {ECO:0000250|UniProtKB:P21462, ECO:0000269|PubMed:18606697, ECO:0000269|PubMed:20947763, ECO:0000269|PubMed:25605714, ECO:0000269|PubMed:26516201, ECO:0000269|PubMed:8244972, ECO:0000269|PubMed:9989980}.; FUNCTION: (Microbial infection) Used by Y. pestis as a receptor on 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
40327
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; which is necessary for desensitization. {ECO:0000250|UniProtKB:P21462}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17084101
uniprot
proteins
pubmed
18606697
uniprot
proteins
pubmed
19497865
uniprot
proteins
pubmed
20947763
uniprot
proteins
pubmed
25605714
uniprot
proteins
pubmed
26516201
uniprot
proteins
pubmed
31534221
uniprot
proteins
pubmed
8244972
uniprot
proteins
pubmed
9989980
uniprot
proteins
sequence_length
364
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8244972}; Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in presence of its ligand, TAFA4. {ECO:0000250|UniProtKB:P21462}.
uniprot
proteins
transmembrane_region
TRANSMEM 36..58; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 70..91; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 109..129; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 149..170; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 217..237; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 254..277; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 297..316; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins