P21462 (FPR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

FPR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Chemotaxis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 superoxide anion generation Inferred from electronic annotation. Source: InterPro
Cellular_component	endosome Traceable author statement PubMed 10823817. Source: ProtInc integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome
Molecular_function	N-formyl peptide receptor activity Inferred from direct assay PubMed 12218158. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADRBK1	P25098	3	EBI-2869495,EBI-3904795
MAPK13	O15264	3	EBI-2869495,EBI-2116951

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	fMet-Leu-Phe receptor		PRO_0000069444
Regions
	Topological domain	1 – 27	27	Extracellular Potential
	Transmembrane	28 – 50	23	Helical; Name=1; Potential
	Topological domain	51 – 61	11	Cytoplasmic Potential
	Transmembrane	62 – 83	22	Helical; Name=2; Potential
	Topological domain	84 – 100	17	Extracellular Potential
	Transmembrane	101 – 121	21	Helical; Name=3; Potential
	Topological domain	122 – 140	19	Cytoplasmic Potential
	Transmembrane	141 – 162	22	Helical; Name=4; Potential
	Topological domain	163 – 205	43	Extracellular Potential
	Transmembrane	206 – 226	21	Helical; Name=5; Potential
	Topological domain	227 – 242	16	Cytoplasmic Potential
	Transmembrane	243 – 266	24	Helical; Name=6; Potential
	Topological domain	267 – 285	19	Extracellular Potential
	Transmembrane	286 – 305	20	Helical; Name=7; Potential
	Topological domain	306 – 350	45	Cytoplasmic Potential
Amino acid modifications
	Modified residue	328	1	Phosphoserine Potential
	Modified residue	329	1	Phosphothreonine Potential
	Modified residue	331	1	Phosphothreonine Potential
	Modified residue	332	1	Phosphoserine Potential
	Modified residue	334	1	Phosphothreonine Potential
	Modified residue	336	1	Phosphothreonine Potential
	Modified residue	338	1	Phosphoserine Potential
	Modified residue	339	1	Phosphothreonine Potential
	Glycosylation	4	1	N-linked (GlcNAc...) Potential
	Glycosylation	10	1	N-linked (GlcNAc...) Potential
	Disulfide bond	98 ↔ 176		Potential
Natural variations
	Natural variant	11	1	I → T. Ref.7 Corresponds to variant rs5030878 [ dbSNP | Ensembl ].		VAR_055915
	Natural variant	101	1	V → L. Ref.1 Ref.2 Corresponds to variant rs2070745 [ dbSNP | Ensembl ].		VAR_003476
	Natural variant	190	1	R → W. Corresponds to variant rs5030880 [ dbSNP | Ensembl ].		VAR_055916
	Natural variant	192	1	N → K. Ref.4 Ref.7 Corresponds to variant rs1042229 [ dbSNP | Ensembl ].		VAR_003477
	Natural variant	346	1	E → A. Ref.1 Ref.2 Ref.5 Corresponds to variant rs867228 [ dbSNP | Ensembl ].		VAR_003478
Experimental info
	Sequence conflict	238	1	R → P in AAA36362. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21462 [UniParc]. Last modified February 9, 2010. Version 3. Checksum: 06651DF820B1CBD1	FASTA	350	38,446
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00328644.
PIR	A42009. JC2014.
RefSeq	NP_001180235.1. NM_001193306.1. NP_002020.1. NM_002029.3.
UniGene	Hs.753.
3D structure databases
ProteinModelPortal	P21462.
SMR	P21462. Positions 24-342.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21462. 4 interactions.
STRING	9606.ENSP00000302707.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P21462.
Polymorphism databases
DMDM	288558848.
Proteomic databases
PaxDb	P21462.
PRIDE	P21462.
Protocols and materials databases
DNASU	2357.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304748; ENSP00000302707; ENSG00000171051. ENST00000595042; ENSP00000471493; ENSG00000171051.
GeneID	2357.
KEGG	hsa:2357.
UCSC	uc002pxq.3. human.
Organism-specific databases
CTD	2357.
GeneCards	GC19M052249.
H-InvDB	HIX0015389. HIX0174408.
HGNC	HGNC:3826. FPR1.
MIM	136537. gene.
neXtProt	NX_P21462.
PharmGKB	PA28244.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG150376.
HOGENOM	HOG000234122.
HOVERGEN	HBG107927.
InParanoid	P21462.
KO	K04172.
OMA	VCVLHPV.
OrthoDB	EOG4SQWWZ.
PhylomeDB	P21462.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
SignaLink	P21462.
Gene expression databases
Bgee	P21462.
CleanEx	HS_FPR1.
Genevestigator	P21462.
GermOnline	ENSG00000171051. Homo sapiens.
Family and domain databases
InterPro	IPR027345. Formyl_pep_1_rcpt. IPR000826. Formyl_pep_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
PANTHER	PTHR24225. PTHR24225. 1 hit. PTHR24225:SF15. PTHR24225:SF15. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00526. FMETLEUPHER. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P21462.
ChEMBL	CHEMBL3359.
DrugBank	DB00716. Nedocromil.
GenomeRNAi	2357.
NextBio	9561.
SOURCE	Search...

Entry information

Entry name

FPR1_HUMAN

Accession

Primary (citable) accession number: P21462
Secondary accession number(s): Q14939 , Q7Z6A4, Q86U52, Q9NS48

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.