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P21462

- FPR1_HUMAN

UniProt

P21462 - FPR1_HUMAN

Protein

fMet-Leu-Phe receptor

Gene

FPR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. N-formyl peptide receptor activity Source: MGI
    2. protein binding Source: IntAct
    3. 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. cellular component movement Source: ProtInc
    4. chemotaxis Source: ProtInc
    5. G-protein coupled receptor signaling pathway 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

    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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3826. FPR1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28244.

    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

    ArrayExpressiP21462.
    BgeeiP21462.
    CleanExiHS_FPR1.
    GenevestigatoriP21462.

    Organism-specific databases

    HPAiHPA046550.

    Interactioni

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini51 – 6111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini84 – 10017ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini122 – 14019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini163 – 20543ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini227 – 24216CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini267 – 28519ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini306 – 35045CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 5023Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei62 – 8322Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei101 – 12121Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei141 – 16222Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei206 – 22621Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei243 – 26624Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei286 – 30520Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    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

    METNSSLPTN ISGGTPAVSA GYLFLDIITY LVFAVTFVLG VLGNGLVIWV    50
    AGFRMTHTVT TISYLNLAVA DFCFTSTLPF FMVRKAMGGH WPFGWFLCKF 100
    VFTIVDINLF GSVFLIALIA LDRCVCVLHP VWTQNHRTVS LAKKVIIGPW 150
    VMALLLTLPV IIRVTTVPGK TGTVACTFNF SPWTNDPKER INVAVAMLTV 200
    RGIIRFIIGF SAPMSIVAVS YGLIATKIHK QGLIKSSRPL RVLSFVAAAF 250
    FLCWSPYQVV ALIATVRIRE LLQGMYKEIG IAVDVTSALA FFNSCLNPML 300
    YVFMGQDFRE RLIHALPASL ERALTEDSTQ TSDTATNSTL PSAEVELQAK 350
    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:
    EMBL
    GenBank
    DDBJ
    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 databases

    DMDMi288558848.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12839.1.
    PIRi JC2014. A42009.
    RefSeqi NP_001180235.1. NM_001193306.1.
    NP_002020.1. NM_002029.3.
    UniGenei Hs.753.

    3D structure databases

    ProteinModelPortali P21462.
    SMRi P21462. Positions 14-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108640. 1 interaction.
    IntActi P21462. 4 interactions.
    STRINGi 9606.ENSP00000302707.

    Chemistry

    BindingDBi P21462.
    ChEMBLi CHEMBL3038479.
    DrugBanki DB00716. Nedocromil.
    GuidetoPHARMACOLOGYi 222.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P21462.

    Polymorphism databases

    DMDMi 288558848.

    Proteomic databases

    PaxDbi P21462.
    PRIDEi P21462.

    Protocols and materials databases

    DNASUi 2357.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304748 ; ENSP00000302707 ; ENSG00000171051 .
    ENST00000595042 ; ENSP00000471493 ; ENSG00000171051 .
    GeneIDi 2357.
    KEGGi hsa:2357.
    UCSCi uc002pxq.3. human.

    Organism-specific databases

    CTDi 2357.
    GeneCardsi GC19M052249.
    H-InvDB HIX0015389.
    HIX0174408.
    HGNCi HGNC:3826. FPR1.
    HPAi HPA046550.
    MIMi 136537. gene.
    neXtProti NX_P21462.
    PharmGKBi PA28244.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150376.
    HOGENOMi HOG000234122.
    HOVERGENi HBG107927.
    InParanoidi P21462.
    KOi K04172.
    OMAi VIIGPWV.
    OrthoDBi EOG77DJ6B.
    PhylomeDBi P21462.
    TreeFami TF330976.

    Enzyme and pathway databases

    Reactomei REACT_19231. G alpha (i) signalling events.
    REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
    SignaLinki P21462.

    Miscellaneous databases

    GeneWikii Formyl_peptide_receptor_1.
    GenomeRNAii 2357.
    NextBioi 9561.
    PROi P21462.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21462.
    Bgeei P21462.
    CleanExi HS_FPR1.
    Genevestigatori P21462.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR027345. Formyl_pep_1_rcpt.
    IPR000826. Formyl_rcpt-rel.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24225. PTHR24225. 1 hit.
    PTHR24225:SF15. PTHR24225:SF15. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 152 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