ID FPRS3_MOUSE Reviewed; 343 AA. AC O88537; A4IF56; E9QL30; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 132. DE RecName: Full=Formyl peptide receptor-related sequence 3; GN Name=Fpr-rs3; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] 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 [5] 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: May have an olfactory function associated with the CC identification of pathogens or of pathogenic states. CC {ECO:0000269|PubMed:19387439}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed exclusively in vomeronasal neurons CC (PubMed:19387439, PubMed:19497865). Expressed in 0.8 % of a subset of CC sensory neurons located in the apical layer of the vomeronasal organ. CC Localized in sensory somata as well as dendritic cells. Each neuron CC appears to express only one receptor gene. CC {ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. 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; AF071181; AAC34586.1; -; Genomic_DNA. DR EMBL; AC166351; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC134352; AAI34353.1; -; mRNA. DR CCDS; CCDS49989.1; -. DR RefSeq; NP_032066.2; NM_008040.2. DR AlphaFoldDB; O88537; -. DR SMR; O88537; -. DR STRING; 10090.ENSMUSP00000071179; -. DR GlyCosmos; O88537; 2 sites, No reported glycans. DR GlyGen; O88537; 2 sites. DR iPTMnet; O88537; -. DR PhosphoSitePlus; O88537; -. DR PaxDb; 10090-ENSMUSP00000071179; -. DR DNASU; 14290; -. DR Ensembl; ENSMUST00000071189.2; ENSMUSP00000071179.2; ENSMUSG00000060701.2. DR GeneID; 14290; -. DR KEGG; mmu:14290; -. DR UCSC; uc012alk.1; mouse. DR AGR; MGI:1278318; -. DR CTD; 14290; -. DR MGI; MGI:1278318; Fpr-rs3. DR VEuPathDB; HostDB:ENSMUSG00000060701; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230438; -. DR HOGENOM; CLU_009579_8_0_1; -. DR InParanoid; O88537; -. DR OMA; LACFNSC; -. DR OrthoDB; 5384006at2759; -. DR PhylomeDB; O88537; -. 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; 14290; 3 hits in 78 CRISPR screens. DR PRO; PR:O88537; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; O88537; Protein. 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; ISO:MGI. 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:0005124; F:scavenger receptor binding; ISO:MGI. DR GO; GO:0038023; F:signaling receptor activity; ISO: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; ISO:MGI. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. 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; IBA:GO_Central. 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 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:SF17; FORMYL PEPTIDE RECEPTOR-RELATED SEQUENCE 3-RELATED; 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. DR Genevisible; O88537; MM. PE 2: Evidence at transcript 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..343 FT /note="Formyl peptide receptor-related sequence 3" FT /id="PRO_0000382023" 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..66 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 67..87 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 88..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..202 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 203..223 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 224..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..280 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 281..301 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 302..343 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..178 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 208..209 FT /note="IG -> NC (in Ref. 1; AAC34586 and 3; AAI34353)" FT /evidence="ECO:0000305" SQ SEQUENCE 343 AA; 38064 MW; B130B0F190D923FF CRC64; MEANSSIPLN GSEVVFYDST TSRVLWILSV IVLSITFVLG VLGNGLVIWV AGFRMAHTVT TICYLNLALG DFSFMVTLPL HIISMVMKGK WLFGWFLCKF VLSIVHINLF VSVFLITLIA MDRCTCVLHP VWVQNHRTVS LARKVIVGAW ILSLLLTLPH FLFLTTVRDA RGEVHCTCNF ESVVANPEEQ LKVSITVSTA TGIISFIIGF SLPMSFIAVC YGLMAAKICR KGFLNSSRPL RVLTAVAISF FMCWFPFQLI ILLGNIWNKE TPSSIHILLN PASTLASFNS CLNPILYVFL GQEFREKLIY SLSASLERAL REDSVLSSGK SSNFSSCPAD SEL //