FPRS7_MOUSE
ID FPRS7_MOUSE Reviewed; 338 AA.
AC Q71MR7; G3X9N8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Formyl peptide receptor-related sequence 7;
GN Name=Fpr-rs7;
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 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 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 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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in vomeronasal organ
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 Each neuron appears to express only one receptor gene. Expressed in
CC heart, liver, lung, spleen smooth muscle and pancreas
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";
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DR EMBL; AF437513; AAN63621.1; -; Genomic_DNA.
DR EMBL; AC121539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466644; EDL38007.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71MR7; -.
DR SMR; Q71MR7; -.
DR STRING; 10090.ENSMUSP00000093297; -.
DR GlyGen; Q71MR7; 3 sites.
DR iPTMnet; Q71MR7; -.
DR PhosphoSitePlus; Q71MR7; -.
DR PaxDb; Q71MR7; -.
DR PRIDE; Q71MR7; -.
DR Ensembl; ENSMUST00000095637; ENSMUSP00000093297; ENSMUSG00000071276.
DR MGI; MGI:2448177; Fpr-rs7.
DR VEuPathDB; HostDB:ENSMUSG00000071276; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q71MR7; -.
DR OMA; GQNFQKR; -.
DR PhylomeDB; Q71MR7; -.
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 PRO; PR:Q71MR7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q71MR7; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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 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..338
FT /note="Formyl peptide receptor-related sequence 7"
FT /id="PRO_0000382026"
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..338
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 CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 147
FT /note="L -> F (in Ref. 1; AAN63621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38141 MW; 4C995F285CCE2577 CRC64;
MEANFSIPQN GSEVVFYDST TSRVICIFLV VVLSITFLLG VIGNGLVIYV AGFRMTHTVT
TICYLNLALS DFSYMTSLPF QITSIVMNGE WLFGWFLCKF VHMIINVNLF LSIFLITFIA
MDRCICVLHP VWAQNHRTVN LARKVILGSW ILVLMLIFPH FFFLTTVKDE SGKVHCICNF
ESWAATPEEQ VNMSMTVSLI SVTLSFIVGF SIPMIFIVIC YGLMAAKIGR RGLVNSSRPL
RVLTAVAFSF FVCWFPFQLI FLLGNIGNKE TQNNIDAWVN PASTLASFNS CLNPILYVFL
GQQFRERLIY SLSASLERAL REDSALNSDK IRNLSSQT
