ID FPRS6_MOUSE Reviewed; 339 AA. AC Q3SXG2; Q71MR8; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Formyl peptide receptor-related sequence 6; GN Name=Fpr-rs6; 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], AND TISSUE SPECIFICITY. RC STRAIN=129S6/SvEvTac; RX PubMed=12459252; DOI=10.1016/s0378-1119(02)01012-0; RA Wang Z.-G., Ye R.D.; RT "Characterization of two new members of the formyl peptide receptor gene RT family from 129S6 mice."; RL Gene 299:57-63(2002). RN [2] 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 [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: May have an olfactory function associated with the CC identification of pathogens or of pathogenic states. CC {ECO:0000269|PubMed:19387439}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed exclusively in vomeronasal tissue CC (PubMed:19387439, PubMed:19497865). Expressed in 1.2 % of a subset of CC sensory neurons located in the apical layer of the vomeronasal organ. CC Each neuron appears to express only one receptor gene. Expressed in CC brain, spleen, skeletal muscle and at high level in testis CC (PubMed:12459252). {ECO:0000269|PubMed:12459252, 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; AF437512; AAN63620.1; -; Genomic_DNA. DR EMBL; BC104318; AAI04319.1; -; mRNA. DR EMBL; BC104319; AAI04320.1; -; mRNA. DR CCDS; CCDS28423.1; -. DR RefSeq; NP_796290.2; NM_177316.2. DR AlphaFoldDB; Q3SXG2; -. DR SMR; Q3SXG2; -. DR STRING; 10090.ENSMUSP00000093296; -. DR GlyCosmos; Q3SXG2; 2 sites, No reported glycans. DR GlyGen; Q3SXG2; 2 sites. DR iPTMnet; Q3SXG2; -. DR PhosphoSitePlus; Q3SXG2; -. DR PaxDb; 10090-ENSMUSP00000093296; -. DR DNASU; 321020; -. DR Ensembl; ENSMUST00000095636.2; ENSMUSP00000093296.2; ENSMUSG00000071275.2. DR GeneID; 321020; -. DR KEGG; mmu:321020; -. DR UCSC; uc008apy.1; mouse. DR AGR; MGI:2448176; -. DR CTD; 321020; -. DR MGI; MGI:2448176; Fpr-rs6. DR VEuPathDB; HostDB:ENSMUSG00000071275; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230438; -. DR HOGENOM; CLU_009579_8_0_1; -. DR InParanoid; Q3SXG2; -. DR OMA; ECAIKEE; -. DR OrthoDB; 5384006at2759; -. DR PhylomeDB; Q3SXG2; -. 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; 321020; 2 hits in 75 CRISPR screens. DR PRO; PR:Q3SXG2; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q3SXG2; 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: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. PE 2: Evidence at transcript level; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..339 FT /note="Formyl peptide receptor-related sequence 6" FT /id="PRO_0000382025" FT TOPO_DOM 1..23 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 24..44 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 45..62 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 63..85 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 86..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..198 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 220..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..339 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 32 FT /note="V -> I (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="T -> A (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" FT CONFLICT 107 FT /note="V -> I (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="T -> A (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="T -> P (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="T -> I (in Ref. 1; AAN63620)" FT /evidence="ECO:0000305" SQ SEQUENCE 339 AA; 38154 MW; CFC144FB2E388A62 CRC64; MEANFSIPQN GSEVVFYDST TSRVICIFLV VVLSITFLLG VIGNGLVIYV AGFRMTHTVT TICYLNLALS DFSYMASLPF QITSIVMNGE WLFGWFLCKF VHMIINVNLF LSIFLITFIA MDRCICVLHP VWAQNHRTVN VATKVIFGAW ILVLMLIFPH CIFVTTVKDE SGKVHCICNF ESWAATPEEQ VKVSMTVSLI SVTISFIIGF SIPMIFIVIC YGLMAAKIGR RGFVNSSRPL RVLTAVAISF FVCWFPFQLI FLLGNIGNKE TQNNIDTWVN TASTLASFNS CLNPILYVFL GQQFRERLIY SLSASLERAL REDSALNSDK TRNLSSQRL //