ID FPR2_MOUSE Reviewed; 351 AA.
AC O88536;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 155.
DE RecName: Full=Formyl peptide receptor 2;
DE AltName: Full=Formylpeptide receptor-related sequence 2;
DE AltName: Full=Lipoxin A4 receptor-like protein;
DE AltName: Full=N-formylpeptide receptor-like 2;
GN Name=Fpr2; Synonyms=Fpr-rs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9722950; DOI=10.1006/geno.1998.5376;
RA Gao J.-L., Chen H., Filie J.D., Kozak C.A., Murphy P.M.;
RT "Differential expansion of the N-formylpeptide receptor gene cluster in
RT human and mouse.";
RL Genomics 51:270-276(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=B10.A;
RX PubMed=12218158; DOI=10.4049/jimmunol.169.6.3363;
RA Vaughn M.W., Proske R.J., Haviland D.L.;
RT "Identification, cloning, and functional characterization of a murine
RT lipoxin A4 receptor homologue gene.";
RL J. Immunol. 169:3363-3369(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10477558; DOI=10.1084/jem.190.5.741;
RA Hartt J.K., Barish G., Murphy P.M., Gao J.L.;
RT "N-formylpeptides induce two distinct concentration optima for mouse
RT neutrophil chemotaxis by differential interaction with two N-formylpeptide
RT receptor (FPR) subtypes. Molecular characterization of FPR2, a second mouse
RT neutrophil FPR.";
RL J. Exp. Med. 190:741-747(1999).
RN [6]
RP TISSUE SPECIFICITY, AND LIGAND-BINDING.
RX PubMed=15879124; DOI=10.4049/jimmunol.174.10.6257;
RA Kurosaka K., Chen Q., Yarovinsky F., Oppenheim J.J., Yang D.;
RT "Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes
RT using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2
RT as the receptor and acts as an immune adjuvant.";
RL J. Immunol. 174:6257-6265(2005).
RN [7]
RP TISSUE SPECIFICITY, AND LIGAND-BINDING.
RX PubMed=17237393; DOI=10.4049/jimmunol.178.3.1450;
RA Gao J.L., Guillabert A., Hu J., Le Y., Urizar E., Seligman E., Fang K.J.,
RA Yuan X., Imbault V., Communi D., Wang J.M., Parmentier M., Murphy P.M.,
RA Migeotte I.;
RT "F2L, a peptide derived from heme-binding protein, chemoattracts mouse
RT neutrophils by specifically activating Fpr2, the low-affinity N-
RT formylpeptide receptor.";
RL J. Immunol. 178:1450-1456(2007).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19387439; DOI=10.1038/nature08029;
RA Riviere S., Challet L., Fluegge D., Spehr M., Rodriguez I.;
RT "Formyl peptide receptor-like proteins are a novel family of vomeronasal
RT chemosensors.";
RL Nature 459:574-577(2009).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=19497865; DOI=10.1073/pnas.0904464106;
RA Liberles S.D., Horowitz L.F., Kuang D., Contos J.J., Wilson K.L.,
RA Siltberg-Liberles J., Liberles D.A., Buck L.B.;
RT "Formyl peptide receptors are candidate chemosensory receptors in the
RT vomeronasal organ.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9842-9847(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29138422; DOI=10.1038/s41598-017-15586-0;
RA Park M.Y., Kim H.S., Lee M., Park B., Lee H.Y., Cho E.B., Seong J.Y.,
RA Bae Y.S.;
RT "FAM19A5, a brain-specific chemokine, inhibits RANKL-induced osteoclast
RT formation through formyl peptide receptor 2.";
RL Sci. Rep. 7:15575-15575(2017).
CC -!- FUNCTION: High affinity receptor for N-formyl-methionyl peptides
CC (FMLP), which are powerful neutrophil chemotactic factors
CC (PubMed:12218158, PubMed:10477558, PubMed:19387439). Stimulates
CC chemotaxis in immune cells to site of infection or tissue damage upon
CC recognition of several ligands, such as FMLP, or ligand involved in
CC cell damage, disease or inflammation (PubMed:10477558,
CC PubMed:19497865). Receptor for the chemokine-like protein FAM19A5,
CC mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory
CC effect on TNFSF11/RANKL-induced osteoclast differentiation
CC (PubMed:29138422). {ECO:0000269|PubMed:10477558,
CC ECO:0000269|PubMed:12218158, ECO:0000269|PubMed:19387439,
CC ECO:0000269|PubMed:19497865, ECO:0000269|PubMed:29138422}.
CC -!- SUBUNIT: Interacts with Amyloid-beta protein 42, product of APP; the
CC interaction takes place at the cell surface and the complex is then
CC rapidly internalized. {ECO:0000250|UniProtKB:P25090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25090};
CC Multi-pass membrane protein {ECO:0000305}. Note=Associates with
CC Amyloid-beta protein 42, product of APP, at the cell surface and the
CC complex is then rapidly internalized. {ECO:0000250|UniProtKB:P25090}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in neutrophils. Not detected in
CC vomeronasal neurons. {ECO:0000269|PubMed:10477558,
CC ECO:0000269|PubMed:15879124, ECO:0000269|PubMed:17237393,
CC ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}.
CC -!- DISRUPTION PHENOTYPE: Blocks Fam19a5-stimulated macrophage chemotaxis
CC and phosphorylation of Erk1 and Akt1 (PubMed:29138422). Suppression of
CC Fam19a5-mediated inhibition of Rankl-induced osteoclast differentiation
CC (PubMed:29138422). {ECO:0000269|PubMed:29138422}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF071180; AAC34585.1; -; Genomic_DNA.
DR EMBL; AY138248; AAN06932.1; -; Genomic_DNA.
DR EMBL; CH466642; EDL20513.1; -; Genomic_DNA.
DR EMBL; BC117066; AAI17067.1; -; mRNA.
DR CCDS; CCDS28419.1; -.
DR RefSeq; NP_032065.1; NM_008039.2.
DR AlphaFoldDB; O88536; -.
DR SMR; O88536; -.
DR BioGRID; 199733; 1.
DR STRING; 10090.ENSMUSP00000065799; -.
DR BindingDB; O88536; -.
DR ChEMBL; CHEMBL4739842; -.
DR GuidetoPHARMACOLOGY; 223; -.
DR GlyCosmos; O88536; 2 sites, No reported glycans.
DR GlyGen; O88536; 2 sites.
DR PhosphoSitePlus; O88536; -.
DR MaxQB; O88536; -.
DR PaxDb; 10090-ENSMUSP00000065799; -.
DR ProteomicsDB; 267407; -.
DR DNASU; 14289; -.
DR Ensembl; ENSMUST00000064068.5; ENSMUSP00000065799.5; ENSMUSG00000052270.8.
DR GeneID; 14289; -.
DR KEGG; mmu:14289; -.
DR UCSC; uc008apu.1; mouse.
DR AGR; MGI:1278319; -.
DR CTD; 2358; -.
DR MGI; MGI:1278319; Fpr2.
DR VEuPathDB; HostDB:ENSMUSG00000052270; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; O88536; -.
DR OMA; VYCTFNF; -.
DR OrthoDB; 5384006at2759; -.
DR PhylomeDB; O88536; -.
DR TreeFam; TF330976; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14289; 2 hits in 76 CRISPR screens.
DR PRO; PR:O88536; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O88536; Protein.
DR Bgee; ENSMUSG00000052270; Expressed in granulocyte and 70 other cell types or tissues.
DR ExpressionAtlas; O88536; baseline and differential.
DR Genevisible; O88536; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IDA:MGI.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
DR GO; GO:0005124; F:scavenger receptor binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0050918; P:positive chemotaxis; IGI:ARUK-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISO:MGI.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:ARUK-UCL.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1.
DR PANTHER; PTHR24225:SF0; N-FORMYL PEPTIDE RECEPTOR 2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00526; FMETLEUPHER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Formyl peptide receptor 2"
FT /id="PRO_0000382022"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 325..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 351 AA; 39422 MW; B16BCE7FA9AA8F43 CRC64;
MESNYSIHLN GSEVVVYDST ISRVLWILSM VVVSITFFLG VLGNGLVIWV AGFRMPHTVT
TIWYLNLALA DFSFTATLPF LLVEMAMKEK WPFGWFLCKL VHIVVDVNLF GSVFLIALIA
LDRCICVLHP VWAQNHRTVS LARKVVVGPW IFALILTLPI FIFLTTVRIP GGDVYCTFNF
GSWAQTDEEK LNTAITFVTT RGIIRFLIGF SMPMSIVAVC YGLIAVKINR RNLVNSSRPL
RVLTAVVASF FICWFPFQLV ALLGTVWFKE TLLSGSYKIL DMFVNPTSSL AYFNSCLNPM
LYVFMGQDFR ERFIHSLPYS LERALSEDSG QTSDSSTSST SPPADIELKA P
//
