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P21462 (FPR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
fMet-Leu-Phe receptor

Short name=fMLP receptor
Alternative name(s):
N-formyl peptide receptor
Short name=FPR
N-formylpeptide chemoattractant receptor
Gene names
Name:FPR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Neutrophils.

Post-translational modification

Phosphorylated; which is necessary for desensitization. Ref.12

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 10823817. Source: ProtInc

activation of MAPK activity

Traceable author statement PubMed 10857861. Source: ProtInc

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 10889468. Source: ProtInc

cellular component movement

Traceable author statement PubMed 10882119. Source: ProtInc

chemotaxis

Traceable author statement PubMed 10857861. Source: ProtInc

nitric oxide mediated signal transduction

Traceable author statement PubMed 10861041. Source: ProtInc

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 22859307. Source: MGI

signal transduction

Traceable author statement PubMed 10820279. Source: ProtInc

   Cellular_componentendosome

Traceable author statement PubMed 10823817. Source: ProtInc

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionN-formyl peptide receptor activity

Inferred from direct assay PubMed 12218158PubMed 22859307. Source: MGI

receptor activity

Traceable author statement PubMed 10857861. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADRBK1P250983EBI-2869495,EBI-3904795
MAPK13O152643EBI-2869495,EBI-2116951

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350fMet-Leu-Phe receptor
PRO_0000069444

Regions

Topological domain1 – 2727Extracellular Potential
Transmembrane28 – 5023Helical; Name=1; Potential
Topological domain51 – 6111Cytoplasmic Potential
Transmembrane62 – 8322Helical; Name=2; Potential
Topological domain84 – 10017Extracellular Potential
Transmembrane101 – 12121Helical; Name=3; Potential
Topological domain122 – 14019Cytoplasmic Potential
Transmembrane141 – 16222Helical; Name=4; Potential
Topological domain163 – 20543Extracellular Potential
Transmembrane206 – 22621Helical; Name=5; Potential
Topological domain227 – 24216Cytoplasmic Potential
Transmembrane243 – 26624Helical; Name=6; Potential
Topological domain267 – 28519Extracellular Potential
Transmembrane286 – 30520Helical; Name=7; Potential
Topological domain306 – 35045Cytoplasmic Potential

Amino acid modifications

Modified residue3281Phosphoserine Potential
Modified residue3291Phosphothreonine Potential
Modified residue3311Phosphothreonine Potential
Modified residue3321Phosphoserine Potential
Modified residue3341Phosphothreonine Potential
Modified residue3361Phosphothreonine Potential
Modified residue3381Phosphoserine Potential
Modified residue3391Phosphothreonine Potential
Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation101N-linked (GlcNAc...) Potential
Disulfide bond98 ↔ 176 Potential

Natural variations

Natural variant111I → T. Ref.7
Corresponds to variant rs5030878 [ dbSNP | Ensembl ].
VAR_055915
Natural variant1011V → L. Ref.1 Ref.2
Corresponds to variant rs2070745 [ dbSNP | Ensembl ].
VAR_003476
Natural variant1901R → W.
Corresponds to variant rs5030880 [ dbSNP | Ensembl ].
VAR_055916
Natural variant1921N → K. Ref.4 Ref.7
Corresponds to variant rs1042229 [ dbSNP | Ensembl ].
VAR_003477
Natural variant3461E → A. Ref.1 Ref.2 Ref.5
Corresponds to variant rs867228 [ dbSNP | Ensembl ].
VAR_003478

Experimental info

Sequence conflict2381R → P in AAA36362. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21462 [UniParc].

Last modified February 9, 2010. Version 3.
Checksum: 06651DF820B1CBD1

FASTA35038,446
        10         20         30         40         50         60 
METNSSLPTN ISGGTPAVSA GYLFLDIITY LVFAVTFVLG VLGNGLVIWV AGFRMTHTVT 

        70         80         90        100        110        120 
TISYLNLAVA DFCFTSTLPF FMVRKAMGGH WPFGWFLCKF VFTIVDINLF GSVFLIALIA 

       130        140        150        160        170        180 
LDRCVCVLHP VWTQNHRTVS LAKKVIIGPW VMALLLTLPV IIRVTTVPGK TGTVACTFNF 

       190        200        210        220        230        240 
SPWTNDPKER INVAVAMLTV RGIIRFIIGF SAPMSIVAVS YGLIATKIHK QGLIKSSRPL 

       250        260        270        280        290        300 
RVLSFVAAAF FLCWSPYQVV ALIATVRIRE LLQGMYKEIG IAVDVTSALA FFNSCLNPML 

       310        320        330        340        350 
YVFMGQDFRE RLIHALPASL ERALTEDSTQ TSDTATNSTL PSAEVELQAK 

« Hide

References

« Hide 'large scale' references
[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], 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], 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].
[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. expand/collapse author list , 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: PHOSPHORYLATION AT SER-328; THR-329; THR-331; SER-332; THR-334; THR-336; SER-338 AND THR-339.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA42009. JC2014.
RefSeqNP_001180235.1. NM_001193306.1.
NP_002020.1. NM_002029.3.
UniGeneHs.753.

3D structure databases

ProteinModelPortalP21462.
SMRP21462. Positions 1-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108640. 1 interaction.
IntActP21462. 4 interactions.
STRING9606.ENSP00000302707.

Chemistry

BindingDBP21462.
ChEMBLCHEMBL3359.
DrugBankDB00716. Nedocromil.
GuidetoPHARMACOLOGY222.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP21462.

Polymorphism databases

DMDM288558848.

Proteomic databases

PaxDbP21462.
PRIDEP21462.

Protocols and materials databases

DNASU2357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304748; ENSP00000302707; ENSG00000171051.
ENST00000595042; ENSP00000471493; ENSG00000171051.
GeneID2357.
KEGGhsa:2357.
UCSCuc002pxq.3. human.

Organism-specific databases

CTD2357.
GeneCardsGC19M052249.
H-InvDBHIX0015389.
HIX0174408.
HGNCHGNC:3826. FPR1.
HPAHPA046550.
MIM136537. gene.
neXtProtNX_P21462.
PharmGKBPA28244.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150376.
HOGENOMHOG000234122.
HOVERGENHBG107927.
InParanoidP21462.
KOK04172.
OMAVIIGPWV.
OrthoDBEOG77DJ6B.
PhylomeDBP21462.
TreeFamTF330976.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP21462.

Gene expression databases

ArrayExpressP21462.
BgeeP21462.
CleanExHS_FPR1.
GenevestigatorP21462.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR027345. Formyl_pep_1_rcpt.
IPR000826. Formyl_pep_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24225. PTHR24225. 1 hit.
PTHR24225:SF15. PTHR24225:SF15. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00526. FMETLEUPHER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFormyl_peptide_receptor_1.
GenomeRNAi2357.
NextBio9561.
PROP21462.
SOURCESearch...

Entry information

Entry nameFPR1_HUMAN
AccessionPrimary (citable) accession number: P21462
Secondary accession number(s): Q14939 expand/collapse secondary AC list , Q7Z6A4, Q86U52, Q9NS48
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries