FPR3
entrez
2359
canonical
uniprot
P25089
canonical
ensembl
ENSG00000187474
resolver
ensp
ENSP00000341821
resolver
ensp
ENSP00000470471
resolver
ensp
ENSP00000571151
resolver
ensp
ENSP00000571152
resolver
ensp
ENSP00000627162
resolver
enst
ENST00000339223
resolver
enst
ENST00000595991
resolver
enst
ENST00000901092
resolver
enst
ENST00000901093
resolver
enst
ENST00000957103
resolver
genesymbol
FPR3
resolver
genesymbol
FPRL2
resolver
genesymbol_syn
FPRL2
resolver
hgnc
HGNC:3828
resolver
uniprot
Q6L5J4
resolver
uniprot_entry
FPR3_HUMAN
resolver
uniprot_entry
Q6L5J4_HUMAN
resolver
amino_acid_sequence
METNFSIPLNETEEVLPEPAGHTVLWIFSLLVHGVTFVFGVLGNGLVIWVAGFRMTRTVNTICYLNLALADFSFSAILPFRMVSVAMREKWPFGSFLCKLVHVMIDINLFVSVYLITIIALDRCICVLHPAWAQNHRTMSLAKRVMTGLWIFTIVLTLPNFIFWTTISTTNGDTYCIFNFAFWGDTAVERLNVFITMAKVFLILHFIIGFSVPMSIITVCYGIIAAKIHRNHMIKSSRPLRVFAAVVASFFICWFPYELIGILMAVWLKEMLLNGKYKIILVLINPTSSLAFFNSCLNPILYVFMGRNFQERLIRSLPTSLERALTEVPDSAQTSNTDTTSASPPEETELQAM
uniprot
proteins
function
FUNCTION: May function as a pattern recognition G protein-coupled receptor (PRR/GPCR) involved in innate recognition of peptides derived from a specific set of bacterial pathogens or host mitochondria as pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) (PubMed:24108355, PubMed:25605714). Low affinity receptor for a restricted repertoire of bacterial N-formylated peptides including fMKKIML from L. monocytogenes and fMPKLNR from V. cholerae. Contrary to FPR1 and FPR2 does not act as a receptor for fMLF peptide (PubMed:15187149, PubMed:25605714). High affinity receptor for N-acetylated F2L peptide derived from the cleavage of heme-binding protein HEBP1. F2L peptide binding may trigger chemotaxis of monocytes and dendritic cells to facilitate tissue repair (PubMed:15623572). Low affinity receptor for N-acetylated Ac2-26 peptide derived from ANXA1, an anti-inflammatory and pro-resolving agonist. Ac2-26 peptide binding can direct myeloid cell chemotaxis within the inflammatory site where ANXA1 is at high concentrations, but it can also lead to receptor desensitization to limit the inflammatory response (PubMed:15187149). Receptor for MT-RNR2/humanin, a mitochondrial-derived peptide that has an anti-inflammatory role in resolution of inflammation (PubMed:15465011). 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:15187149, PubMed:15465011, PubMed:15623572, PubMed:25605714). {ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:15465011, ECO:0000269|PubMed:15623572, ECO:0000269|PubMed:24108355, ECO:0000269|PubMed:25605714}.
uniprot
proteins
mass_dalton
39965
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
15187149
uniprot
proteins
pubmed
15465011
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15623572
uniprot
proteins
pubmed
1612600
uniprot
proteins
pubmed
24108355
uniprot
proteins
pubmed
25605714
uniprot
proteins
pubmed
8198572
uniprot
proteins
sequence_length
353
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15623572, ECO:0000269|PubMed:24108355}; Multi-pass membrane protein {ECO:0000255}. Note=Partially localized intracellularly. {ECO:0000269|PubMed:15623572}.
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 287..306; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins