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Protein

Formyl peptide receptor 2

Gene

Fpr2

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

Functioni

High affinity receptor for N-formyl-methionyl peptides (FMLP), which are powerful neutrophils chemotactic factors. Stimulate chemotaxis in immune cells to site of infection or tissue damage upon recognition of several ligands, such as FMLP, or ligand involved in cell damage, disease or inflammation.3 Publications

GO - Molecular functioni

  • N-formyl peptide receptor activity Source: MGI
  • receptor activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

ReactomeiR-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Names & Taxonomyi

Protein namesi
Recommended name:
Formyl peptide receptor 2
Alternative name(s):
Formylpeptide receptor-related sequence 2
Lipoxin A4 receptor-like protein
N-formylpeptide receptor-like 2
Gene namesi
Name:Fpr2
Synonyms:Fpr-rs2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1278319. Fpr2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929ExtracellularSequence analysisAdd
BLAST
Transmembranei30 – 5021Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini51 – 6111CytoplasmicSequence analysisAdd
BLAST
Transmembranei62 – 8221Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini83 – 9917ExtracellularSequence analysisAdd
BLAST
Transmembranei100 – 12021Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini121 – 14424CytoplasmicSequence analysisAdd
BLAST
Transmembranei145 – 16521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini166 – 20540ExtracellularSequence analysisAdd
BLAST
Transmembranei206 – 22621Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini227 – 24115CytoplasmicSequence analysisAdd
BLAST
Transmembranei242 – 26221Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini263 – 28220ExtracellularSequence analysisAdd
BLAST
Transmembranei283 – 30523Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini306 – 35146CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

GuidetoPHARMACOLOGYi223.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Formyl peptide receptor 2PRO_0000382022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence analysis
Glycosylationi10 – 101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi98 ↔ 176PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO88536.
PaxDbiO88536.
PRIDEiO88536.

PTM databases

PhosphoSiteiO88536.

Expressioni

Tissue specificityi

Primarily expressed in neutrophils. Not detected in vomeronasal neurons.5 Publications

Gene expression databases

BgeeiO88536.
GenevisibleiO88536. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065799.

Structurei

3D structure databases

ProteinModelPortaliO88536.
SMRiO88536. Positions 11-342.
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

eggNOGiENOG410II0H. Eukaryota.
ENOG410YB48. LUCA.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiO88536.
KOiK04173.
OMAiVYCTFNF.
OrthoDBiEOG77DJ6B.
PhylomeDBiO88536.
TreeFamiTF330976.

Family and domain databases

InterProiIPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 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.

O88536-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESNYSIHLN GSEVVVYDST ISRVLWILSM VVVSITFFLG VLGNGLVIWV
60 70 80 90 100
AGFRMPHTVT TIWYLNLALA DFSFTATLPF LLVEMAMKEK WPFGWFLCKL
110 120 130 140 150
VHIVVDVNLF GSVFLIALIA LDRCICVLHP VWAQNHRTVS LARKVVVGPW
160 170 180 190 200
IFALILTLPI FIFLTTVRIP GGDVYCTFNF GSWAQTDEEK LNTAITFVTT
210 220 230 240 250
RGIIRFLIGF SMPMSIVAVC YGLIAVKINR RNLVNSSRPL RVLTAVVASF
260 270 280 290 300
FICWFPFQLV ALLGTVWFKE TLLSGSYKIL DMFVNPTSSL AYFNSCLNPM
310 320 330 340 350
LYVFMGQDFR ERFIHSLPYS LERALSEDSG QTSDSSTSST SPPADIELKA

P
Length:351
Mass (Da):39,422
Last modified:November 1, 1998 - v1
Checksum:iB16BCE7FA9AA8F43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071180 Genomic DNA. Translation: AAC34585.1.
AY138248 Genomic DNA. Translation: AAN06932.1.
CH466642 Genomic DNA. Translation: EDL20513.1.
BC117066 mRNA. Translation: AAI17067.1.
CCDSiCCDS28419.1.
RefSeqiNP_032065.1. NM_008039.2.
UniGeneiMm.378918.

Genome annotation databases

EnsembliENSMUST00000064068; ENSMUSP00000065799; ENSMUSG00000052270.
GeneIDi14289.
KEGGimmu:14289.
UCSCiuc008apu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071180 Genomic DNA. Translation: AAC34585.1.
AY138248 Genomic DNA. Translation: AAN06932.1.
CH466642 Genomic DNA. Translation: EDL20513.1.
BC117066 mRNA. Translation: AAI17067.1.
CCDSiCCDS28419.1.
RefSeqiNP_032065.1. NM_008039.2.
UniGeneiMm.378918.

3D structure databases

ProteinModelPortaliO88536.
SMRiO88536. Positions 11-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065799.

Chemistry

GuidetoPHARMACOLOGYi223.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiO88536.

Proteomic databases

MaxQBiO88536.
PaxDbiO88536.
PRIDEiO88536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064068; ENSMUSP00000065799; ENSMUSG00000052270.
GeneIDi14289.
KEGGimmu:14289.
UCSCiuc008apu.1. mouse.

Organism-specific databases

CTDi2358.
MGIiMGI:1278319. Fpr2.

Phylogenomic databases

eggNOGiENOG410II0H. Eukaryota.
ENOG410YB48. LUCA.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiO88536.
KOiK04173.
OMAiVYCTFNF.
OrthoDBiEOG77DJ6B.
PhylomeDBiO88536.
TreeFamiTF330976.

Enzyme and pathway databases

ReactomeiR-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Miscellaneous databases

PROiO88536.
SOURCEiSearch...

Gene expression databases

BgeeiO88536.
GenevisibleiO88536. MM.

Family and domain databases

InterProiIPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 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. "Differential expansion of the N-formylpeptide receptor gene cluster in human and mouse."
    Gao J.-L., Chen H., Filie J.D., Kozak C.A., Murphy P.M.
    Genomics 51:270-276(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification, cloning, and functional characterization of a murine lipoxin A4 receptor homologue gene."
    Vaughn M.W., Proske R.J., Haviland D.L.
    J. Immunol. 169:3363-3369(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: B10.A.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "N-formylpeptides induce two distinct concentration optima for mouse neutrophil chemotaxis by differential interaction with two N-formylpeptide receptor (FPR) subtypes. Molecular characterization of FPR2, a second mouse neutrophil FPR."
    Hartt J.K., Barish G., Murphy P.M., Gao J.L.
    J. Exp. Med. 190:741-747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  6. "Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant."
    Kurosaka K., Chen Q., Yarovinsky F., Oppenheim J.J., Yang D.
    J. Immunol. 174:6257-6265(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, LIGAND-BINDING.
  7. "F2L, a peptide derived from heme-binding protein, chemoattracts mouse neutrophils by specifically activating Fpr2, the low-affinity N-formylpeptide receptor."
    Gao J.L., Guillabert A., Hu J., Le Y., Urizar E., Seligman E., Fang K.J., Yuan X., Imbault V., Communi D., Wang J.M., Parmentier M., Murphy P.M., Migeotte I.
    J. Immunol. 178:1450-1456(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, LIGAND-BINDING.
  8. "Formyl peptide receptor-like proteins are a novel family of vomeronasal chemosensors."
    Riviere S., Challet L., Fluegge D., Spehr M., Rodriguez I.
    Nature 459:574-577(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  9. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiFPR2_MOUSE
AccessioniPrimary (citable) accession number: O88536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 110 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

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 one 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.