FPR3_HUMAN
ID FPR3_HUMAN Reviewed; 353 AA.
AC P25089;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=N-formyl peptide receptor 3;
DE AltName: Full=FMLP-related receptor II;
DE Short=FMLP-R-II;
DE AltName: Full=Formyl peptide receptor-like 2;
GN Name=FPR3; Synonyms=FPRH1, FPRL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1612600; DOI=10.1016/0888-7543(92)90265-t;
RA Bao L., Gerard N.P., Eddy R.L. Jr., Shows T.B., Gerard C.;
RT "Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor
RT (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to
RT chromosome 19.";
RL Genomics 13:437-440(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8198572; DOI=10.1006/bbrc.1994.1685;
RA Durstin M., Gao J.-L., Tiffany H.L., McDermott D., Murphy P.M.;
RT "Differential expression of members of the N-formylpeptide receptor gene
RT cluster in human phagocytes.";
RL Biochem. Biophys. Res. Commun. 201:174-179(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15465011; DOI=10.1016/j.bbrc.2004.09.046;
RA Harada M., Habata Y., Hosoya M., Nishi K., Fujii R., Kobayashi M.,
RA Hinuma S.;
RT "N-Formylated humanin activates both formyl peptide receptor-like 1 and
RT 2.";
RL Biochem. Biophys. Res. Commun. 324:255-261(2004).
CC -!- FUNCTION: Low affinity receptor for N-formyl-methionyl peptides, which
CC are powerful neutrophils chemotactic factors. Binding of FMLP to the
CC receptor causes activation of neutrophils. This response is mediated
CC via a G-protein that activates a phosphatidylinositol-calcium second
CC messenger system. Acts as a receptor for humanin (PubMed:15465011).
CC {ECO:0000269|PubMed:15465011}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in various tissues with highest expression
CC in lung. {ECO:0000269|PubMed:15465011}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M76673; AAA58482.1; -; mRNA.
DR EMBL; L14061; AAA52474.1; -; Genomic_DNA.
DR EMBL; AY262690; AAP20654.1; -; Genomic_DNA.
DR EMBL; BC059388; AAH59388.1; -; mRNA.
DR EMBL; BC069070; AAH69070.1; -; mRNA.
DR EMBL; BC069593; AAH69593.1; -; mRNA.
DR EMBL; BC069812; AAH69812.1; -; mRNA.
DR CCDS; CCDS12841.1; -.
DR PIR; C42009; C42009.
DR RefSeq; NP_002021.3; NM_002030.4.
DR RefSeq; XP_011524989.1; XM_011526687.2.
DR AlphaFoldDB; P25089; -.
DR SMR; P25089; -.
DR STRING; 9606.ENSP00000341821; -.
DR BindingDB; P25089; -.
DR GuidetoPHARMACOLOGY; 224; -.
DR GlyGen; P25089; 2 sites.
DR iPTMnet; P25089; -.
DR PhosphoSitePlus; P25089; -.
DR BioMuta; FPR3; -.
DR DMDM; 38258904; -.
DR jPOST; P25089; -.
DR MassIVE; P25089; -.
DR PaxDb; P25089; -.
DR PeptideAtlas; P25089; -.
DR PRIDE; P25089; -.
DR ProteomicsDB; 54251; -.
DR TopDownProteomics; P25089; -.
DR Antibodypedia; 19053; 356 antibodies from 30 providers.
DR DNASU; 2359; -.
DR Ensembl; ENST00000339223.5; ENSP00000341821.3; ENSG00000187474.5.
DR Ensembl; ENST00000595991.1; ENSP00000470471.1; ENSG00000187474.5.
DR GeneID; 2359; -.
DR KEGG; hsa:2359; -.
DR MANE-Select; ENST00000339223.5; ENSP00000341821.3; NM_002030.5; NP_002021.3.
DR CTD; 2359; -.
DR DisGeNET; 2359; -.
DR GeneCards; FPR3; -.
DR HGNC; HGNC:3828; FPR3.
DR HPA; ENSG00000187474; Tissue enhanced (lung).
DR MIM; 136539; gene.
DR neXtProt; NX_P25089; -.
DR OpenTargets; ENSG00000187474; -.
DR PharmGKB; PA162388910; -.
DR VEuPathDB; HostDB:ENSG00000187474; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P25089; -.
DR OMA; RVIMGLW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P25089; -.
DR TreeFam; TF330976; -.
DR PathwayCommons; P25089; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR SignaLink; P25089; -.
DR SIGNOR; P25089; -.
DR BioGRID-ORCS; 2359; 10 hits in 1064 CRISPR screens.
DR GeneWiki; Formyl_peptide_receptor_3; -.
DR GenomeRNAi; 2359; -.
DR Pharos; P25089; Tchem.
DR PRO; PR:P25089; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P25089; protein.
DR Bgee; ENSG00000187474; Expressed in gall bladder and 123 other tissues.
DR ExpressionAtlas; P25089; baseline and differential.
DR Genevisible; P25089; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR027347; Formyl_pep_3_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF16; PTHR24225:SF16; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="N-formyl peptide receptor 3"
FT /id="PRO_0000069457"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 327..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 94
FT /note="G -> A (in Ref. 1; AAA58482)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> T (in Ref. 1; AAA58482)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> H (in Ref. 1; AAA58482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39965 MW; FFB7150B6A833F4C CRC64;
METNFSIPLN ETEEVLPEPA GHTVLWIFSL LVHGVTFVFG VLGNGLVIWV AGFRMTRTVN
TICYLNLALA DFSFSAILPF RMVSVAMREK WPFGSFLCKL VHVMIDINLF VSVYLITIIA
LDRCICVLHP AWAQNHRTMS LAKRVMTGLW IFTIVLTLPN FIFWTTISTT NGDTYCIFNF
AFWGDTAVER LNVFITMAKV FLILHFIIGF SVPMSIITVC YGIIAAKIHR NHMIKSSRPL
RVFAAVVASF FICWFPYELI GILMAVWLKE MLLNGKYKII LVLINPTSSL AFFNSCLNPI
LYVFMGRNFQ ERLIRSLPTS LERALTEVPD SAQTSNTDTT SASPPEETEL QAM
