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Protein

fMet-Leu-Phe receptor

Gene

Fpr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system.1 Publication

GO - Molecular functioni

  1. N-formyl peptide receptor activity Source: MGI

GO - Biological processi

  1. chemotaxis Source: MGI
  2. G-protein coupled receptor signaling pathway Source: MGI
  3. phospholipase C-activating G-protein coupled receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

ReactomeiREACT_272716. Formyl peptide receptors bind formyl peptides and many other ligands.
REACT_331048. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
fMet-Leu-Phe receptor
Short name:
fMLP receptor
Alternative name(s):
N-formyl peptide receptor
Short name:
FPR
N-formylpeptide chemoattractant receptor
Gene namesi
Name:Fpr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:107443. Fpr1.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535ExtracellularSequence AnalysisAdd
BLAST
Transmembranei36 – 5823Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini59 – 6911CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei70 – 9122Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini92 – 10817ExtracellularSequence AnalysisAdd
BLAST
Transmembranei109 – 12921Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini130 – 14819CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei149 – 17022Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini171 – 21646ExtracellularSequence AnalysisAdd
BLAST
Transmembranei217 – 23721Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini238 – 25316CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei254 – 27724Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini278 – 29619ExtracellularSequence AnalysisAdd
BLAST
Transmembranei297 – 31620Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini317 – 36448CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364fMet-Leu-Phe receptorPRO_0000069446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
Glycosylationi10 – 101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi18 – 181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi106 ↔ 187PROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated; which is necessary for desensitization.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP33766.

PTM databases

PhosphoSiteiP33766.

Expressioni

Tissue specificityi

Expressed in neutrophils, dendritic cells, microglia, spleen, lung and liver. Low level of expression in the vomeronasal organ.1 Publication

Gene expression databases

BgeeiP33766.
CleanExiMM_FPR1.
GenevestigatoriP33766.

Interactioni

Protein-protein interaction databases

MINTiMINT-127948.
STRINGi10090.ENSMUSP00000052894.

Structurei

3D structure databases

ProteinModelPortaliP33766.
SMRiP33766. Positions 21-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150376.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiP33766.
KOiK04172.
OMAiFTVIDIN.
OrthoDBiEOG77DJ6B.
PhylomeDBiP33766.
TreeFamiTF330976.

Family and domain databases

InterProiIPR027345. Formyl_pep_1_rcpt.
IPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 1 hit.
PTHR24225:SF15. PTHR24225:SF15. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTNMSLLMN KSAVNLMNVS GSTQSVSAGY IVLDVFSYLI FAVTFVLGVL
60 70 80 90 100
GNGLVIWVAG FRMKHTVTTI SYLNLAIADF CFTSTLPFYI ASMVMGGHWP
110 120 130 140 150
FGWFMCKFIY TVIDINLFGS VFLIALIALD RCICVLHPVW AQNHRTVSLA
160 170 180 190 200
KKVIIVPWIC AFLLTLPVII RLTTVPNSRL GPGKTACTFD FSPWTKDPVE
210 220 230 240 250
KRKVAVTMLT VRGIIRFIIG FSTPMSIVAI CYGLITTKIH RQGLIKSSRP
260 270 280 290 300
LRVLSFVVAA FFLCWCPFQV VALISTIQVR ERLKNMTPGI VTALKITSPL
310 320 330 340 350
AFFNSCLNPM LYVFMGQDFR ERLIHSLPAS LERALTEDSA QTSDTGTNLG
360
TNSTSLSENT LNAM
Length:364
Mass (Da):40,327
Last modified:February 1, 1994 - v1
Checksum:i2F59193CF1D74DB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22181 Unassigned DNA. Translation: AAA16110.1.
AK137714 mRNA. Translation: BAE23472.1.
CH466642 Genomic DNA. Translation: EDL20512.1.
CCDSiCCDS28418.1.
PIRiA49542.
RefSeqiNP_038549.1. NM_013521.2.
UniGeneiMm.56951.

Genome annotation databases

EnsembliENSMUST00000061516; ENSMUSP00000052894; ENSMUSG00000045551.
GeneIDi14293.
KEGGimmu:14293.
UCSCiuc008apt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22181 Unassigned DNA. Translation: AAA16110.1.
AK137714 mRNA. Translation: BAE23472.1.
CH466642 Genomic DNA. Translation: EDL20512.1.
CCDSiCCDS28418.1.
PIRiA49542.
RefSeqiNP_038549.1. NM_013521.2.
UniGeneiMm.56951.

3D structure databases

ProteinModelPortaliP33766.
SMRiP33766. Positions 21-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-127948.
STRINGi10090.ENSMUSP00000052894.

Chemistry

BindingDBiP33766.
ChEMBLiCHEMBL1770037.
GuidetoPHARMACOLOGYi222.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP33766.

Proteomic databases

PRIDEiP33766.

Protocols and materials databases

DNASUi14293.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061516; ENSMUSP00000052894; ENSMUSG00000045551.
GeneIDi14293.
KEGGimmu:14293.
UCSCiuc008apt.1. mouse.

Organism-specific databases

CTDi2357.
MGIiMGI:107443. Fpr1.

Phylogenomic databases

eggNOGiNOG150376.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiP33766.
KOiK04172.
OMAiFTVIDIN.
OrthoDBiEOG77DJ6B.
PhylomeDBiP33766.
TreeFamiTF330976.

Enzyme and pathway databases

ReactomeiREACT_272716. Formyl peptide receptors bind formyl peptides and many other ligands.
REACT_331048. G alpha (i) signalling events.

Miscellaneous databases

NextBioi285695.
PROiP33766.
SOURCEiSearch...

Gene expression databases

BgeeiP33766.
CleanExiMM_FPR1.
GenevestigatoriP33766.

Family and domain databases

InterProiIPR027345. Formyl_pep_1_rcpt.
IPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 1 hit.
PTHR24225:SF15. PTHR24225:SF15. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Species and subtype variants of the N-formyl peptide chemotactic receptor reveal multiple important functional domains."
    Gao J.-L., Murphy P.M.
    J. Biol. Chem. 268:25395-25401(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Vagina.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses."
    Migeotte I., Communi D., Parmentier M.
    Cytokine Growth Factor Rev. 17:501-519(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiFPR1_MOUSE
AccessioniPrimary (citable) accession number: P33766
Secondary accession number(s): Q3UV01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 1, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.