FPRS6_MOUSE
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 25-MAY-2022, entry version 114.
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 and PubMed:19497865). Expressed in 1.2 % of a subset
CC of sensory neurons located in the apical layer of the vomeronasal
CC organ. Each neuron appears to express only one receptor gene. Expressed
CC in 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";
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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 GlyGen; Q3SXG2; 2 sites.
DR iPTMnet; Q3SXG2; -.
DR PhosphoSitePlus; Q3SXG2; -.
DR PaxDb; Q3SXG2; -.
DR PRIDE; Q3SXG2; -.
DR DNASU; 321020; -.
DR Ensembl; ENSMUST00000095636; ENSMUSP00000093296; ENSMUSG00000071275.
DR GeneID; 321020; -.
DR KEGG; mmu:321020; -.
DR UCSC; uc008apy.1; mouse.
DR CTD; 321020; -.
DR MGI; MGI:2448176; Fpr-rs6.
DR VEuPathDB; HostDB:ENSMUSG00000071275; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q3SXG2; -.
DR OMA; IVINGEW; -.
DR OrthoDB; 910274at2759; -.
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 70 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: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: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 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
