FPRS4_MOUSE
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 03-AUG-2022, entry version 98.
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 GlyGen; A4FUQ5; 3 sites.
DR PaxDb; A4FUQ5; -.
DR PRIDE; A4FUQ5; -.
DR DNASU; 14291; -.
DR Ensembl; ENSMUST00000095651; ENSMUSP00000093311; ENSMUSG00000048062.
DR GeneID; 14291; -.
DR KEGG; mmu:14291; -.
DR UCSC; uc012alh.1; mouse.
DR CTD; 14291; -.
DR MGI; MGI:1278317; Fpr-rs4.
DR VEuPathDB; HostDB:ENSMUSG00000048062; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; A4FUQ5; -.
DR OMA; ISKFESW; -.
DR OrthoDB; 910274at2759; -.
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 71 CRISPR screens.
DR PRO; PR:A4FUQ5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; A4FUQ5; protein.
DR Bgee; ENSMUSG00000048062; Expressed in gastrula and 1 other tissue.
DR Genevisible; A4FUQ5; 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: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; 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
