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P33766 (FPR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in neutrophils, dendritic cells, microglia, spleen, lung and liver. Low level of expression in the vomeronasal organ. Ref.5

Post-translational modification

Phosphorylated; which is necessary for desensitization By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364fMet-Leu-Phe receptor
PRO_0000069446

Regions

Topological domain1 – 3535Extracellular Potential
Transmembrane36 – 5823Helical; Name=1; Potential
Topological domain59 – 6911Cytoplasmic Potential
Transmembrane70 – 9122Helical; Name=2; Potential
Topological domain92 – 10817Extracellular Potential
Transmembrane109 – 12921Helical; Name=3; Potential
Topological domain130 – 14819Cytoplasmic Potential
Transmembrane149 – 17022Helical; Name=4; Potential
Topological domain171 – 21646Extracellular Potential
Transmembrane217 – 23721Helical; Name=5; Potential
Topological domain238 – 25316Cytoplasmic Potential
Transmembrane254 – 27724Helical; Name=6; Potential
Topological domain278 – 29619Extracellular Potential
Transmembrane297 – 31620Helical; Name=7; Potential
Topological domain317 – 36448Cytoplasmic Potential

Amino acid modifications

Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation101N-linked (GlcNAc...) Potential
Glycosylation181N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 187 Potential

Sequences

Sequence LengthMass (Da)Tools
P33766 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 2F59193CF1D74DB2

FASTA36440,327
        10         20         30         40         50         60 
MDTNMSLLMN KSAVNLMNVS GSTQSVSAGY IVLDVFSYLI FAVTFVLGVL GNGLVIWVAG 

        70         80         90        100        110        120 
FRMKHTVTTI SYLNLAIADF CFTSTLPFYI ASMVMGGHWP FGWFMCKFIY TVIDINLFGS 

       130        140        150        160        170        180 
VFLIALIALD RCICVLHPVW AQNHRTVSLA KKVIIVPWIC AFLLTLPVII RLTTVPNSRL 

       190        200        210        220        230        240 
GPGKTACTFD FSPWTKDPVE KRKVAVTMLT VRGIIRFIIG FSTPMSIVAI CYGLITTKIH 

       250        260        270        280        290        300 
RQGLIKSSRP LRVLSFVVAA FFLCWCPFQV VALISTIQVR ERLKNMTPGI VTALKITSPL 

       310        320        330        340        350        360 
AFFNSCLNPM LYVFMGQDFR ERLIHSLPAS LERALTEDSA QTSDTGTNLG TNSTSLSENT 


LNAM 

« Hide

References

« Hide 'large scale' references
[1]"Species and subtype variants of the N-formyl peptide chemotactic receptor reveal multiple important functional domains."
Gao J.-L., Murphy P.M.
J. Biol. Chem. 268:25395-25401(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Vagina.
[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]"Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses."
Migeotte I., Communi D., Parmentier M.
Cytokine Growth Factor Rev. 17:501-519(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Formyl peptide receptors are candidate chemosensory receptors in the vomeronasal organ."
Liberles S.D., Horowitz L.F., Kuang D., Contos J.J., Wilson K.L., Siltberg-Liberles J., Liberles D.A., Buck L.B.
Proc. Natl. Acad. Sci. U.S.A. 106:9842-9847(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22181 Unassigned DNA. Translation: AAA16110.1.
AK137714 mRNA. Translation: BAE23472.1.
CH466642 Genomic DNA. Translation: EDL20512.1.
CCDSCCDS28418.1.
PIRA49542.
RefSeqNP_038549.1. NM_013521.2.
UniGeneMm.56951.

3D structure databases

ProteinModelPortalP33766.
SMRP33766. Positions 21-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-127948.
STRING10090.ENSMUSP00000052894.

Chemistry

ChEMBLCHEMBL1770037.
GuidetoPHARMACOLOGY222.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP33766.

Proteomic databases

PRIDEP33766.

Protocols and materials databases

DNASU14293.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061516; ENSMUSP00000052894; ENSMUSG00000045551.
GeneID14293.
KEGGmmu:14293.
UCSCuc008apt.1. mouse.

Organism-specific databases

CTD2357.
MGIMGI:107443. Fpr1.

Phylogenomic databases

eggNOGNOG150376.
GeneTreeENSGT00730000110302.
HOGENOMHOG000234122.
HOVERGENHBG107927.
InParanoidQ3UV01.
KOK04172.
OMAVIIGPWV.
OrthoDBEOG77DJ6B.
PhylomeDBP33766.
TreeFamTF330976.

Gene expression databases

BgeeP33766.
CleanExMM_FPR1.
GenevestigatorP33766.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR027345. Formyl_pep_1_rcpt.
IPR000826. Formyl_rcpt-rel.
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]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285695.
PROP33766.
SOURCESearch...

Entry information

Entry nameFPR1_MOUSE
AccessionPrimary (citable) accession number: P33766
Secondary accession number(s): Q3UV01
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries