FPR2
entrez
2358
canonical
uniprot
P25090
canonical
ensembl
ENSG00000171049
resolver
ensp
ENSP00000340191
resolver
ensp
ENSP00000468876
resolver
ensp
ENSP00000468897
resolver
enst
ENST00000340023
resolver
enst
ENST00000598776
resolver
enst
ENST00000598953
resolver
genesymbol
FPR2
resolver
genesymbol_syn
FPRH1
resolver
genesymbol_syn
FPRL1
resolver
genesymbol_syn
LXA4R
resolver
hgnc
HGNC:3827
resolver
uniprot
A8K3E2
resolver
uniprot_entry
FPR2_HUMAN
resolver
uniprot_sec
A8K3E2
resolver
amino_acid_sequence
METNFSTPLNEYEEVSYESAGYTVLRILPLVVLGVTFVLGVLGNGLVIWVAGFRMTRTVTTICYLNLALADFSFTATLPFLIVSMAMGEKWPFGWFLCKLIHIVVDINLFGSVFLIGFIALDRCICVLHPVWAQNHRTVSLAMKVIVGPWILALVLTLPVFLFLTTVTIPNGDTYCTFNFASWGGTPEERLKVAITMLTARGIIRFVIGFSLPMSIVAICYGLIAAKIHKKGMIKSSRPLRVLTAVVASFFICWFPFQLVALLGTVWLKEMLFYGKYKIIDILVNPTSSLAFFNSCLNPMLYVFVGQDFRERLIHSLPTSLERALSEDSAPTNDTAANSASPPAETELQAM
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:1374236, PubMed:25605714, PubMed:35217703). 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 (PubMed:30098280). Ligand binding causes a conformation change that triggers signaling via G(i)/GNAI1 inhibiting adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:40080544). In addition, can recognize a variety of chemically distinct endogenous ligands including proteins and lipids besides formylpeptides and thereby plays multiple roles in inflammation. 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 (By similarity). Acts also as a ceramide membrane receptor, and long-chain ceramides (C14 to C20) binding induces conformational changes that inhibits diet-induced adipose thermogenesis (PubMed:40080544). Participates in neuroprotection via interaction with humanin/MT-RNR2 and Amyloid-beta protein 42, product of APP (PubMed:11689470, PubMed:35365641). 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. {ECO:0000250|UniProtKB:O88536, ECO:0000269|PubMed:1374236, ECO:0000269|PubMed:15465011, ECO:0000269|PubMed:24108355, ECO:0000269|PubMed:25605714, ECO:0000269|PubMed:35217703, ECO:0000269|PubMed:35365641, ECO:0000269|PubMed:40080544, ECO:0000269|PubMed:9547339}.
uniprot
proteins
mass_dalton
38964
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11689470
uniprot
proteins
pubmed
1373134
uniprot
proteins
pubmed
1374236
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
1511907
uniprot
proteins
pubmed
15465011
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1612600
uniprot
proteins
pubmed
24108355
uniprot
proteins
pubmed
25605714
uniprot
proteins
pubmed
30098280
uniprot
proteins
pubmed
35217703
uniprot
proteins
pubmed
35365641
uniprot
proteins
pubmed
40080544
uniprot
proteins
pubmed
7505609
uniprot
proteins
pubmed
9151906
uniprot
proteins
pubmed
9547339
uniprot
proteins
sequence_length
351
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11689470, ECO:0000269|PubMed:15465011, ECO:0000269|PubMed:24108355}; Multi-pass membrane protein. Note=Associates with Amyloid-beta protein 42, product of APP, at the cell surface and the complex is then rapidly internalized (PubMed:11689470). Also internalized in the presence of humanin (PubMed:15465011). {ECO:0000269|PubMed:11689470, ECO:0000269|PubMed:15465011}.
uniprot
proteins
transmembrane_region
TRANSMEM 28..49; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 61..86; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 95..119; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 146..163; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 193..219; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 243..268; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35217703"; TRANSMEM 279..304; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35217703
uniprot
proteins