FPRS3_MOUSE
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 03-AUG-2022, entry version 123.
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 and PubMed:19497865). Expressed in 0.8 % of a subset
CC of sensory neurons located in the apical layer of the vomeronasal
CC organ. Localized in sensory somata as well as dendritic cells. Each
CC neuron 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";
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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 GlyGen; O88537; 2 sites.
DR iPTMnet; O88537; -.
DR PhosphoSitePlus; O88537; -.
DR PaxDb; O88537; -.
DR PRIDE; O88537; -.
DR DNASU; 14290; -.
DR Ensembl; ENSMUST00000071189; ENSMUSP00000071179; ENSMUSG00000060701.
DR GeneID; 14290; -.
DR KEGG; mmu:14290; -.
DR UCSC; uc012alk.1; mouse.
DR CTD; 14290; -.
DR MGI; MGI:1278318; Fpr-rs3.
DR VEuPathDB; HostDB:ENSMUSG00000060701; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; O88537; -.
DR OMA; LACFNSC; -.
DR OrthoDB; 910274at2759; -.
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 73 CRISPR screens.
DR PRO; PR:O88537; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O88537; protein.
DR Genevisible; O88537; 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: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; 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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
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 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
