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Protein

fMet-Leu-Phe receptor

Gene

FPR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:2161213, PubMed:2176894, PubMed:10514456, PubMed:15153520). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:2161213, PubMed:1712023, PubMed:15153520). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:1712023, PubMed:10514456).4 Publications4 Publications

GO - Molecular functioni

  1. N-formyl peptide receptor activity Source: MGI
  2. receptor activity Source: ProtInc

GO - Biological processi

  1. activation of MAPK activity Source: ProtInc
  2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: ProtInc
  3. chemotaxis Source: ProtInc
  4. G-protein coupled receptor signaling pathway Source: ProtInc
  5. movement of cell or subcellular component Source: ProtInc
  6. nitric oxide mediated signal transduction Source: ProtInc
  7. phospholipase C-activating G-protein coupled receptor signaling pathway Source: MGI
  8. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
SignaLinkiP21462.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3826. FPR1.

Subcellular locationi

  1. Cell membrane 1 Publication2 Publications; Multi-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727ExtracellularSequence AnalysisAdd
BLAST
Transmembranei28 – 5023Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini51 – 6111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei62 – 8322Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini84 – 10017ExtracellularSequence AnalysisAdd
BLAST
Transmembranei101 – 12121Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini122 – 14019CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei141 – 16222Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini163 – 20543ExtracellularSequence AnalysisAdd
BLAST
Transmembranei206 – 22621Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini227 – 24216CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei243 – 26624Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini267 – 28519ExtracellularSequence AnalysisAdd
BLAST
Transmembranei286 – 30520Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini306 – 35045CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome Source: ProtInc
  2. integral component of membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28244.

Chemistry

DrugBankiDB00716. Nedocromil.

Polymorphism and mutation databases

BioMutaiFPR1.
DMDMi288558848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350fMet-Leu-Phe receptorPRO_0000069444Add
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
Modified residuei328 – 3281PhosphoserineSequence Analysis
Modified residuei329 – 3291PhosphothreonineSequence Analysis
Modified residuei331 – 3311PhosphothreonineSequence Analysis
Modified residuei332 – 3321PhosphoserineSequence Analysis
Modified residuei334 – 3341PhosphothreonineSequence Analysis
Modified residuei336 – 3361PhosphothreonineSequence Analysis
Modified residuei338 – 3381PhosphoserineSequence Analysis
Modified residuei339 – 3391PhosphothreonineSequence Analysis

Post-translational modificationi

Phosphorylated; which is necessary for desensitization.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP21462.
PRIDEiP21462.

PTM databases

PhosphoSiteiP21462.

Expressioni

Tissue specificityi

Neutrophils.

Gene expression databases

BgeeiP21462.
CleanExiHS_FPR1.
ExpressionAtlasiP21462. baseline and differential.
GenevestigatoriP21462.

Organism-specific databases

HPAiHPA046550.

Interactioni

Subunit structurei

Interacts with S.aureus chemotaxis inhibitory protein (CHIPS); the interaction blocks the receptor and may thus inhibit the immune response.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRBK1P250983EBI-2869495,EBI-3904795
MAPK13O152643EBI-2869495,EBI-2116951

Protein-protein interaction databases

BioGridi108640. 1 interaction.
IntActiP21462. 4 interactions.
STRINGi9606.ENSP00000302707.

Structurei

3D structure databases

ProteinModelPortaliP21462.
SMRiP21462. Positions 14-342.
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

eggNOGiNOG150376.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiP21462.
KOiK04172.
OMAiVIIGPWV.
OrthoDBiEOG77DJ6B.
PhylomeDBiP21462.
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.

P21462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METNSSLPTN ISGGTPAVSA GYLFLDIITY LVFAVTFVLG VLGNGLVIWV
60 70 80 90 100
AGFRMTHTVT TISYLNLAVA DFCFTSTLPF FMVRKAMGGH WPFGWFLCKF
110 120 130 140 150
VFTIVDINLF GSVFLIALIA LDRCVCVLHP VWTQNHRTVS LAKKVIIGPW
160 170 180 190 200
VMALLLTLPV IIRVTTVPGK TGTVACTFNF SPWTNDPKER INVAVAMLTV
210 220 230 240 250
RGIIRFIIGF SAPMSIVAVS YGLIATKIHK QGLIKSSRPL RVLSFVAAAF
260 270 280 290 300
FLCWSPYQVV ALIATVRIRE LLQGMYKEIG IAVDVTSALA FFNSCLNPML
310 320 330 340 350
YVFMGQDFRE RLIHALPASL ERALTEDSTQ TSDTATNSTL PSAEVELQAK
Length:350
Mass (Da):38,446
Last modified:February 9, 2010 - v3
Checksum:i06651DF820B1CBD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381R → P in AAA36362 (PubMed:2161213).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111I → T.1 Publication
Corresponds to variant rs5030878 [ dbSNP | Ensembl ].
VAR_055915
Natural varianti101 – 1011V → L.2 Publications
Corresponds to variant rs2070745 [ dbSNP | Ensembl ].
VAR_003476
Natural varianti190 – 1901R → W.
Corresponds to variant rs5030880 [ dbSNP | Ensembl ].
VAR_055916
Natural varianti192 – 1921N → K.2 Publications
Corresponds to variant rs1042229 [ dbSNP | Ensembl ].
VAR_003477
Natural varianti346 – 3461E → A.3 Publications
Corresponds to variant rs867228 [ dbSNP | Ensembl ].
VAR_003478

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37128 mRNA. Translation: AAA36362.1.
M60626 mRNA. Translation: AAA35846.1.
M60627 mRNA. Translation: AAA35847.1.
L10820 Genomic DNA. Translation: AAA16863.1.
AY301273 Genomic DNA. Translation: AAP58403.1.
BT007429 mRNA. Translation: AAP36097.1.
AC018755 Genomic DNA. Translation: AAF87842.1.
BC005315 mRNA. Translation: AAH05315.1.
S49810 mRNA. Translation: AAD14906.1.
CCDSiCCDS12839.1.
PIRiJC2014. A42009.
RefSeqiNP_001180235.1. NM_001193306.1.
NP_002020.1. NM_002029.3.
UniGeneiHs.753.

Genome annotation databases

EnsembliENST00000304748; ENSP00000302707; ENSG00000171051.
ENST00000595042; ENSP00000471493; ENSG00000171051.
GeneIDi2357.
KEGGihsa:2357.
UCSCiuc002pxq.3. human.

Polymorphism and mutation databases

BioMutaiFPR1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37128 mRNA. Translation: AAA36362.1.
M60626 mRNA. Translation: AAA35846.1.
M60627 mRNA. Translation: AAA35847.1.
L10820 Genomic DNA. Translation: AAA16863.1.
AY301273 Genomic DNA. Translation: AAP58403.1.
BT007429 mRNA. Translation: AAP36097.1.
AC018755 Genomic DNA. Translation: AAF87842.1.
BC005315 mRNA. Translation: AAH05315.1.
S49810 mRNA. Translation: AAD14906.1.
CCDSiCCDS12839.1.
PIRiJC2014. A42009.
RefSeqiNP_001180235.1. NM_001193306.1.
NP_002020.1. NM_002029.3.
UniGeneiHs.753.

3D structure databases

ProteinModelPortaliP21462.
SMRiP21462. Positions 14-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108640. 1 interaction.
IntActiP21462. 4 interactions.
STRINGi9606.ENSP00000302707.

Chemistry

BindingDBiP21462.
ChEMBLiCHEMBL3359.
DrugBankiDB00716. Nedocromil.
GuidetoPHARMACOLOGYi222.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP21462.

Polymorphism and mutation databases

BioMutaiFPR1.
DMDMi288558848.

Proteomic databases

PaxDbiP21462.
PRIDEiP21462.

Protocols and materials databases

DNASUi2357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304748; ENSP00000302707; ENSG00000171051.
ENST00000595042; ENSP00000471493; ENSG00000171051.
GeneIDi2357.
KEGGihsa:2357.
UCSCiuc002pxq.3. human.

Organism-specific databases

CTDi2357.
GeneCardsiGC19M052249.
H-InvDBHIX0015389.
HIX0174408.
HGNCiHGNC:3826. FPR1.
HPAiHPA046550.
MIMi136537. gene.
neXtProtiNX_P21462.
PharmGKBiPA28244.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG150376.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiP21462.
KOiK04172.
OMAiVIIGPWV.
OrthoDBiEOG77DJ6B.
PhylomeDBiP21462.
TreeFamiTF330976.

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
SignaLinkiP21462.

Miscellaneous databases

GeneWikiiFormyl_peptide_receptor_1.
GenomeRNAii2357.
NextBioi9561.
PROiP21462.
SOURCEiSearch...

Gene expression databases

BgeeiP21462.
CleanExiHS_FPR1.
ExpressionAtlasiP21462. baseline and differential.
GenevestigatoriP21462.

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. "Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA."
    Boulay F., Tardif M., Brouchon L., Vignais P.
    Biochem. Biophys. Res. Commun. 168:1103-1109(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS LEU-101 AND ALA-346.
  2. "The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors."
    Boulay F., Tardif M., Brouchon L., Vignais P.
    Biochemistry 29:11123-11133(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, VARIANTS LEU-101 AND ALA-346.
  3. "Functional expression of the human formyl peptide receptor in Xenopus oocytes requires a complementary human factor."
    Murphy P.M., McDermott D.
    J. Biol. Chem. 266:12560-12567(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  4. "Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19."
    Bao L., Gerard N.P., Eddy R.L. Jr., Shows T.B., Gerard C.
    Genomics 13:437-440(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-192.
  5. Perez H.D.
    Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-346.
  6. "Sequence and organization of the human N-formyl peptide receptor-encoding gene."
    Murphy P.M., Tiffany H.L., McDermott D., Ahuja S.K.
    Gene 133:285-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-11 AND LYS-192.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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: Kidney.
  11. "Cloning of the gene coding for a human receptor for formyl peptides. Characterization of a promoter region and evidence for polymorphic expression."
    Perez H.D., Holmes R., Kelly E., McClary J., Chou Q., Andrews W.H.
    Biochemistry 31:11595-11599(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-5.
    Tissue: Bone marrow.
  12. "Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor."
    Maestes D.C., Potter R.M., Prossnitz E.R.
    J. Biol. Chem. 274:29791-29795(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-328; THR-329; THR-331; SER-332; THR-334; THR-336; SER-338 AND THR-339.
  13. "Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor."
    Postma B., Poppelier M.J.J.G., van Galen J.C., Prossnitz E.R., van Strijp J.A.G., de Haas C.J.C., van Kessel K.P.M.
    J. Immunol. 172:6994-7001(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHIPS, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFPR1_HUMAN
AccessioniPrimary (citable) accession number: P21462
Secondary accession number(s): Q14939
, Q7Z6A4, Q86U52, Q9NS48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 9, 2010
Last modified: April 29, 2015
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. 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.