ID   FPRS4_MOUSE             Reviewed;         323 AA.
AC   A4FUQ5; A4QMY2; E9QPJ4; O88538;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Formyl peptide receptor-related sequence 4;
DE   AltName: Full=N-formylpeptide receptor-like 4;
GN   Name=Fpr-rs4;
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; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in 0.6 % of a subset of sensory neurons
CC       located in the apical layer of the vomeronasal organ. 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";
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DR   EMBL; AF071182; AAC34587.1; -; Genomic_DNA.
DR   EMBL; AC171405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115534; AAI15535.1; -; mRNA.
DR   EMBL; BC115535; AAI15536.1; -; mRNA.
DR   CCDS; CCDS49968.1; -.
DR   RefSeq; NP_032067.2; NM_008041.2.
DR   AlphaFoldDB; A4FUQ5; -.
DR   SMR; A4FUQ5; -.
DR   STRING; 10090.ENSMUSP00000093311; -.
DR   GlyCosmos; A4FUQ5; 3 sites, No reported glycans.
DR   GlyGen; A4FUQ5; 3 sites.
DR   PaxDb; 10090-ENSMUSP00000093311; -.
DR   DNASU; 14291; -.
DR   Ensembl; ENSMUST00000095651.2; ENSMUSP00000093311.2; ENSMUSG00000048062.5.
DR   GeneID; 14291; -.
DR   KEGG; mmu:14291; -.
DR   UCSC; uc012alh.1; mouse.
DR   AGR; MGI:1278317; -.
DR   CTD; 14291; -.
DR   MGI; MGI:1278317; Fpr-rs4.
DR   VEuPathDB; HostDB:ENSMUSG00000048062; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01020000230438; -.
DR   HOGENOM; CLU_009579_8_0_1; -.
DR   InParanoid; A4FUQ5; -.
DR   OMA; ISKFESW; -.
DR   OrthoDB; 5384006at2759; -.
DR   PhylomeDB; A4FUQ5; -.
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; 14291; 4 hits in 76 CRISPR screens.
DR   PRO; PR:A4FUQ5; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; A4FUQ5; Protein.
DR   Bgee; ENSMUSG00000048062; Expressed in gastrula and 1 other cell type or tissue.
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.
DR   Genevisible; A4FUQ5; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..323
FT                   /note="Formyl peptide receptor-related sequence 4"
FT                   /id="PRO_0000382024"
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..323
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        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        98..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        23
FT                   /note="R -> S (in Ref. 1; AAC34587 and 3; AAI15536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="A -> V (in Ref. 1; AAC34587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="V -> M (in Ref. 1; AAC34587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="V -> I (in Ref. 1; AAC34587)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   323 AA;  36294 MW;  17803E937AD10D9F CRC64;
     MEVNISMPLN GSEVVFYDST TSRVLWILSL VVLFITFVLG VLGNGLVIWV AGFQMAHTVT
     TVSYLNLALS DLSFMATLPL HIISMVMRGK WLFGWFLCKL VHIIANINLF VSIFLITLIA
     MDRCICVLCP VWSQNHRTVS LARKVVLGAW IFALLLTLPH FLFLTTVRDA RGDVYCISKF
     ESWVATSEEQ LKVSVIAATA SGIINFIIGF SMPMSFIAIC YGLMAAKICR RGFVNSSRPL
     RVLTAVAVSF FVCWFPFQLI MLLGNIFNNE TLSIIHMLVN PANTLASFNS CLNPILYVFL
     GQEFRDRLIY SLYASLERAL RED
//