FPRS1_MOUSE
ID FPRS1_MOUSE Reviewed; 351 AA.
AC O08790; O88535;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Formyl peptide receptor-related sequence 1;
DE AltName: Full=FMLP-related receptor I;
DE Short=FMLP-R-I;
DE AltName: Full=Formyl peptide receptor related sequence 1;
DE AltName: Full=Formyl peptide receptor-like 1;
DE AltName: Full=Lipoxin A4 receptor;
DE Short=LXA4 receptor;
DE AltName: Full=N-formyl peptide receptor 2;
DE AltName: Full=N-formyl peptide receptor 3;
GN Name=Fpr-s1; Synonyms=Fpr2, Fpr3, Fprl1, Lxa4r;
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 [MRNA], LIGAND-BINDING, AND TISSUE SPECIFICITY.
RC TISSUE=Neutrophil, and Spleen;
RX PubMed=9151906; DOI=10.1084/jem.185.9.1693;
RA Takano T., Fiore S., Maddox J.F., Brady H.R., Petasis N.A., Serhan C.N.;
RT "Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 stable analogues are
RT potent inhibitors of acute inflammation: evidence for anti-inflammatory
RT receptors.";
RL J. Exp. Med. 185:1693-1704(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
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 [3]
RP TISSUE SPECIFICITY, AND FUNCTION.
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 [4]
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).
CC -!- FUNCTION: Low affinity receptor for N-formyl-methionyl peptides.
CC Receptor for lipoxin A4. May have an olfactory function associated with
CC the identification of pathogens or of pathogenic states.
CC {ECO:0000269|PubMed:19387439}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in vomeronasal neurons
CC (PubMed:19387439 and PubMed:19497865). Expressed in 0.6 % of a subset
CC of sensory neurons located in the basal layer of the vomeronasal organ.
CC Each neuron appears to express only one receptor gene. Expressed mostly
CC in neutrophils, followed by spleen and lung and expressed at very low
CC levels in heart and liver (PubMed:19387439).
CC {ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865,
CC ECO:0000269|PubMed:9151906, ECO:0000269|PubMed:9722950}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A sickly smell - Issue 114
CC of February 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/114";
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; U78299; AAC53198.1; -; mRNA.
DR EMBL; AF071179; AAC34584.1; -; Genomic_DNA.
DR CCDS; CCDS28420.1; -.
DR RefSeq; NP_032068.2; NM_008042.2.
DR AlphaFoldDB; O08790; -.
DR SMR; O08790; -.
DR STRING; 10090.ENSMUSP00000093316; -.
DR BindingDB; O08790; -.
DR ChEMBL; CHEMBL3407315; -.
DR GuidetoPHARMACOLOGY; 224; -.
DR GlyGen; O08790; 2 sites.
DR PaxDb; O08790; -.
DR PRIDE; O08790; -.
DR DNASU; 14294; -.
DR Ensembl; ENSMUST00000054871; ENSMUSP00000093316; ENSMUSG00000079700.
DR Ensembl; ENSMUST00000115565; ENSMUSP00000111227; ENSMUSG00000079700.
DR GeneID; 14294; -.
DR KEGG; mmu:14294; -.
DR UCSC; uc008apv.1; mouse.
DR CTD; 2359; -.
DR MGI; MGI:1194495; Fpr3.
DR VEuPathDB; HostDB:ENSMUSG00000079700; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; O08790; -.
DR OMA; RVIMGLW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; O08790; -.
DR TreeFam; TF330976; -.
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 BioGRID-ORCS; 14294; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Fpr3; mouse.
DR PRO; PR:O08790; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O08790; protein.
DR Bgee; ENSMUSG00000079700; Expressed in lumbar dorsal root ganglion and 6 other tissues.
DR Genevisible; O08790; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; ISO:MGI.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IBA:GO_Central.
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:0006935; P:chemotaxis; TAS:MGI.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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-related sequence 1"
FT /id="PRO_0000069453"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..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..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..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..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
FT CONFLICT 3
FT /note="T -> S (in Ref. 1; AAC53198)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="P -> H (in Ref. 1; AAC53198)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="D -> E (in Ref. 1; AAC53198)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="I -> V (in Ref. 1; AAC53198)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..145
FT /note="Missing (in Ref. 2; AAC34584)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="T -> Y (in Ref. 2; AAC34584)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="F -> S (in Ref. 2; AAC34584)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> M (in Ref. 2; AAC34584)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Q -> P (in Ref. 2; AAC34584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39523 MW; 295618B0ED0F98D6 CRC64;
METNYSIPLN GSDVVIYDST ISRVLWILSM VVVSITFFLG VLGNGLVIWV AGFRMPHTVT
TIWYLNLALA DFSFTATLPF LLVEMAMKEK WPFGWFLCKL VHIAVDVNLF GSVFLIAVIA
LDRCICVLHP VWAQNHRTVS LARNVVVGSW IFALILTLPL FLFLTTVRDA RGDVHCRLSF
VSWGNSVEER LNTAITFVTT RGIIRFIVSF SLPMSFVAIC YGLITTKIHK KAFVNSSRPF
RVLTGVVASF FICWFPFQLV ALLGTVWLKE MQFSGSYKII GRLVNPTSSL AFFNSCLNPI
LYVFMGQDFQ ERLIHSLSSR LQRALSEDSG HISDTRTNLA SLPEDIEIKA I
