FPR1_MOUSE
ID FPR1_MOUSE Reviewed; 364 AA.
AC P33766; Q3UV01;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=fMet-Leu-Phe receptor;
DE Short=fMLP receptor;
DE AltName: Full=N-formyl peptide receptor;
DE Short=FPR;
DE AltName: Full=N-formylpeptide chemoattractant receptor;
GN Name=Fpr1;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8244972; DOI=10.1016/s0021-9258(19)74405-6;
RA Gao J.-L., Murphy P.M.;
RT "Species and subtype variants of the N-formyl peptide chemotactic receptor
RT reveal multiple important functional domains.";
RL J. Biol. Chem. 268:25395-25401(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 REVIEW.
RX PubMed=17084101; DOI=10.1016/j.cytogfr.2006.09.009;
RA Migeotte I., Communi D., Parmentier M.;
RT "Formyl peptide receptors: a promiscuous subfamily of G protein-coupled
RT receptors controlling immune responses.";
RL Cytokine Growth Factor Rev. 17:501-519(2006).
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: High affinity receptor for N-formyl-methionyl peptides
CC (fMLP), which are powerful neutrophil chemotactic factors. Binding of
CC fMLP to the receptor stimulates intracellular calcium mobilization and
CC superoxide anion release. This response is mediated via a G-protein
CC that activates a phosphatidylinositol-calcium second messenger system.
CC Receptor for TAFA4, mediates its effects on chemoattracting
CC macrophages, promoting phagocytosis and increasing ROS release (By
CC similarity). Receptor for cathepsin CTSG, leading to increased
CC phagocyte chemotaxis (By similarity). {ECO:0000250|UniProtKB:P21462,
CC ECO:0000269|PubMed:8244972}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8244972};
CC Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in
CC presence of its ligand, TAFA4. {ECO:0000250|UniProtKB:P21462}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils, dendritic cells,
CC microglia, spleen, lung and liver. Low level of expression in the
CC vomeronasal organ. {ECO:0000269|PubMed:19497865}.
CC -!- PTM: Phosphorylated; which is necessary for desensitization.
CC {ECO:0000250|UniProtKB:P21462}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L22181; AAA16110.1; -; Unassigned_DNA.
DR EMBL; AK137714; BAE23472.1; -; mRNA.
DR EMBL; CH466642; EDL20512.1; -; Genomic_DNA.
DR CCDS; CCDS28418.1; -.
DR PIR; A49542; A49542.
DR RefSeq; NP_038549.1; NM_013521.2.
DR AlphaFoldDB; P33766; -.
DR SMR; P33766; -.
DR STRING; 10090.ENSMUSP00000052894; -.
DR BindingDB; P33766; -.
DR ChEMBL; CHEMBL1770037; -.
DR GuidetoPHARMACOLOGY; 222; -.
DR GlyGen; P33766; 3 sites.
DR iPTMnet; P33766; -.
DR PhosphoSitePlus; P33766; -.
DR MaxQB; P33766; -.
DR PaxDb; P33766; -.
DR PRIDE; P33766; -.
DR ProteomicsDB; 267406; -.
DR Antibodypedia; 19049; 439 antibodies from 33 providers.
DR DNASU; 14293; -.
DR Ensembl; ENSMUST00000061516; ENSMUSP00000052894; ENSMUSG00000045551.
DR GeneID; 14293; -.
DR KEGG; mmu:14293; -.
DR UCSC; uc008apt.1; mouse.
DR CTD; 2357; -.
DR MGI; MGI:107443; Fpr1.
DR VEuPathDB; HostDB:ENSMUSG00000045551; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P33766; -.
DR OMA; GWFMCKF; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P33766; -.
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 Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14293; 4 hits in 73 CRISPR screens.
DR PRO; PR:P33766; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P33766; protein.
DR Bgee; ENSMUSG00000045551; Expressed in granulocyte and 21 other tissues.
DR Genevisible; P33766; 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:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IDA:MGI.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
DR GO; GO:0005124; F:scavenger receptor binding; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; TAS: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; IDA:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR InterPro; IPR027345; Formyl_pep_1/2_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF15; PTHR24225:SF15; 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; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="fMet-Leu-Phe receptor"
FT /id="PRO_0000069446"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 364 AA; 40327 MW; 2F59193CF1D74DB2 CRC64;
MDTNMSLLMN KSAVNLMNVS GSTQSVSAGY IVLDVFSYLI FAVTFVLGVL GNGLVIWVAG
FRMKHTVTTI SYLNLAIADF CFTSTLPFYI ASMVMGGHWP FGWFMCKFIY TVIDINLFGS
VFLIALIALD RCICVLHPVW AQNHRTVSLA KKVIIVPWIC AFLLTLPVII RLTTVPNSRL
GPGKTACTFD FSPWTKDPVE KRKVAVTMLT VRGIIRFIIG FSTPMSIVAI CYGLITTKIH
RQGLIKSSRP LRVLSFVVAA FFLCWCPFQV VALISTIQVR ERLKNMTPGI VTALKITSPL
AFFNSCLNPM LYVFMGQDFR ERLIHSLPAS LERALTEDSA QTSDTGTNLG TNSTSLSENT
LNAM
