Fpr2
entrez
14289
canonical
uniprot
O88536
canonical
ensembl
ENSMUSG00000052270
resolver
ensp
ENSMUSP00000065799
resolver
enst
ENSMUST00000064068
resolver
genesymbol
Fpr2
resolver
genesymbol_syn
Fpr-rs2
resolver
uniprot_entry
FPR2_MOUSE
resolver
amino_acid_sequence
MESNYSIHLNGSEVVVYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIVVDVNLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLARKVVVGPWIFALILTLPIFIFLTTVRIPGGDVYCTFNFGSWAQTDEEKLNTAITFVTTRGIIRFLIGFSMPMSIVAVCYGLIAVKINRRNLVNSSRPLRVLTAVVASFFICWFPFQLVALLGTVWFKETLLSGSYKILDMFVNPTSSLAYFNSCLNPMLYVFMGQDFRERFIHSLPYSLERALSEDSGQTSDSSTSSTSPPADIELKAP
uniprot
proteins
function
FUNCTION: Pattern recognition G protein-coupled receptor (GPCR) that recognizes peptides with N-terminal formyl methionine, which are derived from invading pathogens or host mitochondria as pathogen or damage-associated molecular patterns (PAMPs and DAMPs) (PubMed:10477558, PubMed:12218158, PubMed:19387439, PubMed:25605714). Preferentially recognizes longer peptides or peptides with specific sequences such as the phenol-soluble modulin (PSM) family of formylated peptide toxins produced by Staphylococcus aureus (By similarity). Ligand binding causes a conformation change that triggers signaling via G(i)/GNAI1 inhibiting adenylate cyclase activity, leading to decreased intracellular cAMP levels. In addition, can recognize a variety of chemically distinct endogenous ligands including proteins and lipids besides formylpeptides and thereby plays multiple roles in inflammation (PubMed:10477558, PubMed:19497865, PubMed:37056936). Acts as a receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (PubMed:29138422). Acts also as a ceramide membrane receptor, and long-chain ceramides (C14 to C20) binding induces conformational changes that inhibits diet-induced adipose thermogenesis (By similarity). May participate in neuroprotection via interaction with MT-RNR2 and Amyloid-beta protein 42, product of APP (By similarity). Differential signaling is also defined by receptor oligomerization state. Binding of ANXA1 to FPR2 homodimer elicits activation of p38 MAPKinase pathway leading to HSPB1/HSP27 phosphorylation and IL10 production in monocytes. Whereas agonistic activation of FPR1:FPR2 heterodimers signals a proapoptotic JNK pathway in neutrophils (By similarity). {ECO:0000250|UniProtKB:P25090, ECO:0000269|PubMed:10477558, ECO:0000269|PubMed:12218158, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865, ECO:0000269|PubMed:29138422, ECO:0000269|PubMed:37056936}.
uniprot
proteins
mass_dalton
39422
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10477558
uniprot
proteins
pubmed
12218158
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15879124
uniprot
proteins
pubmed
17237393
uniprot
proteins
pubmed
19387439
uniprot
proteins
pubmed
19497865
uniprot
proteins
pubmed
25605714
uniprot
proteins
pubmed
29138422
uniprot
proteins
pubmed
37056936
uniprot
proteins
pubmed
40080544
uniprot
proteins
pubmed
9722950
uniprot
proteins
sequence_length
351
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P25090}. Note=Associates with Amyloid-beta protein 42, product of APP, at the cell surface and the complex is then rapidly internalized. Also internalized in the presence of humanin. {ECO:0000250|UniProtKB:P25090}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..49; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 63..86; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 95..119; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 146..163; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 193..219; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 243..268; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P25090"; TRANSMEM 279..304; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P25090
uniprot
proteins