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Protein

N-formyl peptide receptor 2

Gene

FPR2

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

Functioni

Low 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. The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of proinflammatory signals such as LTB4 (leukotriene B4).

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: ProtInc
  2. N-formyl peptide receptor activity Source: ProtInc

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. chemotaxis Source: ProtInc
  3. G-protein coupled receptor signaling pathway Source: ProtInc
  4. inflammatory response Source: ProtInc
  5. movement of cell or subcellular component Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.

Names & Taxonomyi

Protein namesi
Recommended name:
N-formyl peptide receptor 2
Alternative name(s):
FMLP-related receptor I
Short name:
FMLP-R-I
Formyl peptide receptor-like 1
HM63
Lipoxin A4 receptor
Short name:
LXA4 receptor
RFP
Gene namesi
Name:FPR2
Synonyms:FPRH1, FPRL1, LXA4R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3827. FPR2.

Subcellular locationi

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 – 28620ExtracellularSequence AnalysisAdd
BLAST
Transmembranei287 – 30620Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini307 – 35145CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351N-formyl peptide receptor 2PRO_0000069451Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP25090.
PRIDEiP25090.

PTM databases

PhosphoSiteiP25090.

Expressioni

Tissue specificityi

Expressed abundantly in the lung and neutrophils. Also found in the spleen and testis.1 Publication

Gene expression databases

BgeeiP25090.
CleanExiHS_FPR2.
ExpressionAtlasiP25090. baseline and differential.
GenevestigatoriP25090.

Organism-specific databases

HPAiHPA029154.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000340191.

Structurei

3D structure databases

ProteinModelPortaliP25090.
SMRiP25090. Positions 26-310.
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.
InParanoidiP25090.
KOiK04173.
OMAiYCTFNFA.
PhylomeDBiP25090.
TreeFamiTF330976.

Family and domain databases

InterProiIPR027347. Formyl_pep_2/3_rcpt.
IPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 1 hit.
PTHR24225:SF16. PTHR24225:SF16. 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.

P25090-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METNFSTPLN EYEEVSYESA GYTVLRILPL VVLGVTFVLG VLGNGLVIWV
60 70 80 90 100
AGFRMTRTVT TICYLNLALA DFSFTATLPF LIVSMAMGEK WPFGWFLCKL
110 120 130 140 150
IHIVVDINLF GSVFLIGFIA LDRCICVLHP VWAQNHRTVS LAMKVIVGPW
160 170 180 190 200
ILALVLTLPV FLFLTTVTIP NGDTYCTFNF ASWGGTPEER LKVAITMLTA
210 220 230 240 250
RGIIRFVIGF SLPMSIVAIC YGLIAAKIHK KGMIKSSRPL RVLTAVVASF
260 270 280 290 300
FICWFPFQLV ALLGTVWLKE MLFYGKYKII DILVNPTSSL AFFNSCLNPM
310 320 330 340 350
LYVFVGQDFR ERLIHSLPTS LERALSEDSA PTNDTAANSA SPPAETELQA

M
Length:351
Mass (Da):38,964
Last modified:July 1, 1993 - v2
Checksum:iDC6A1D77AFC0D780
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti339 – 3391S → C in AAA58481 (PubMed:1612600).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76672 mRNA. Translation: AAA58481.1.
X63819 mRNA. Translation: CAA45319.1.
M88107 mRNA. Translation: AAA60070.1.
M84562 mRNA. Translation: AAA52473.1.
D10922 mRNA. Translation: BAA01720.1.
U81501 mRNA. Translation: AAB51133.1.
AF054013 mRNA. Translation: AAC13684.1.
AY225226 Genomic DNA. Translation: AAO67711.1.
AK290557 mRNA. Translation: BAF83246.1.
AC018755 Genomic DNA. Translation: AAF87844.1.
CH471135 Genomic DNA. Translation: EAW72043.1.
BC029125 mRNA. Translation: AAH29125.1.
BC071722 mRNA. Translation: AAH71722.1.
CCDSiCCDS12840.1.
PIRiB42009.
RefSeqiNP_001005738.1. NM_001005738.1.
NP_001453.1. NM_001462.3.
XP_006723183.1. XM_006723120.1.
UniGeneiHs.99855.

Genome annotation databases

EnsembliENST00000340023; ENSP00000340191; ENSG00000171049.
ENST00000598776; ENSP00000468897; ENSG00000171049.
ENST00000598953; ENSP00000468876; ENSG00000171049.
GeneIDi2358.
KEGGihsa:2358.
UCSCiuc002pxr.3. human.

Polymorphism databases

DMDMi399504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76672 mRNA. Translation: AAA58481.1.
X63819 mRNA. Translation: CAA45319.1.
M88107 mRNA. Translation: AAA60070.1.
M84562 mRNA. Translation: AAA52473.1.
D10922 mRNA. Translation: BAA01720.1.
U81501 mRNA. Translation: AAB51133.1.
AF054013 mRNA. Translation: AAC13684.1.
AY225226 Genomic DNA. Translation: AAO67711.1.
AK290557 mRNA. Translation: BAF83246.1.
AC018755 Genomic DNA. Translation: AAF87844.1.
CH471135 Genomic DNA. Translation: EAW72043.1.
BC029125 mRNA. Translation: AAH29125.1.
BC071722 mRNA. Translation: AAH71722.1.
CCDSiCCDS12840.1.
PIRiB42009.
RefSeqiNP_001005738.1. NM_001005738.1.
NP_001453.1. NM_001462.3.
XP_006723183.1. XM_006723120.1.
UniGeneiHs.99855.

3D structure databases

ProteinModelPortaliP25090.
SMRiP25090. Positions 26-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000340191.

Chemistry

BindingDBiP25090.
ChEMBLiCHEMBL3038479.
GuidetoPHARMACOLOGYi223.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP25090.

Polymorphism databases

DMDMi399504.

Proteomic databases

PaxDbiP25090.
PRIDEiP25090.

Protocols and materials databases

DNASUi2358.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340023; ENSP00000340191; ENSG00000171049.
ENST00000598776; ENSP00000468897; ENSG00000171049.
ENST00000598953; ENSP00000468876; ENSG00000171049.
GeneIDi2358.
KEGGihsa:2358.
UCSCiuc002pxr.3. human.

Organism-specific databases

CTDi2358.
GeneCardsiGC19P052264.
HGNCiHGNC:3827. FPR2.
HPAiHPA029154.
MIMi136538. gene.
neXtProtiNX_P25090.
PharmGKBiPA162388901.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG150376.
GeneTreeiENSGT00760000118990.
HOGENOMiHOG000234122.
HOVERGENiHBG107927.
InParanoidiP25090.
KOiK04173.
OMAiYCTFNFA.
PhylomeDBiP25090.
TreeFamiTF330976.

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.

Miscellaneous databases

GeneWikiiFormyl_peptide_receptor_2.
GenomeRNAii2358.
NextBioi9565.
PROiP25090.
SOURCEiSearch...

Gene expression databases

BgeeiP25090.
CleanExiHS_FPR2.
ExpressionAtlasiP25090. baseline and differential.
GenevestigatoriP25090.

Family and domain databases

InterProiIPR027347. Formyl_pep_2/3_rcpt.
IPR000826. Formyl_rcpt-rel.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24225. PTHR24225. 1 hit.
PTHR24225:SF16. PTHR24225:SF16. 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. "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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of a cDNA encoding a receptor related to the formyl peptide receptor of human neutrophils."
    Perez H.D., Holmes R., Kelly E., McClary J., Andrews W.H.
    Gene 118:303-304(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone marrow.
  3. "Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor."
    Ye R.D., Cavanagh S.L., Quehenberger O., Prossnitz E.R., Cochrane C.G.
    Biochem. Biophys. Res. Commun. 184:582-589(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Granulocyte.
  4. "A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family."
    Murphy P.M., Ozcelik T., Kenney R.T., Tiffany H.L., McDermott D., Francke U.
    J. Biol. Chem. 267:7637-7643(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Molecular cloning of cDNAs encoding a LD78 receptor and putative leukocyte chemotactic peptide receptors."
    Nomura H., Nielsen B.W., Matsushima K.
    Int. Immunol. 5:1239-1249(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocyte.
  6. Maddox J.F., Hachicha M., Takano T., Petasis N.A., Fokin V.V., Serhan C.N.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Identification of a human enterocyte lipoxin A4 receptor that is regulated by interleukin (IL)-13 and interferon gamma and inhibits tumor necrosis factor alpha-induced IL-8 release."
    Gronert K., Gewirtz A., Madara J.L., Serhan C.N.
    J. Exp. Med. 187:1285-1294(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "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 (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  10. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Blood.
  13. "Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 stable analogues are potent inhibitors of acute inflammation: evidence for anti-inflammatory receptors."
    Takano T., Fiore S., Maddox J.F., Brady H.R., Petasis N.A., Serhan C.N.
    J. Exp. Med. 185:1693-1704(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiFPR2_HUMAN
AccessioniPrimary (citable) accession number: P25090
Secondary accession number(s): A8K3E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: March 4, 2015
This is version 141 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. 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.