FPR2_HUMAN
ID FPR2_HUMAN Reviewed; 351 AA.
AC P25090; A8K3E2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=N-formyl peptide receptor 2;
DE AltName: Full=FMLP-related receptor I;
DE Short=FMLP-R-I;
DE AltName: Full=Formyl peptide receptor-like 1;
DE AltName: Full=HM63;
DE AltName: Full=Lipoxin A4 receptor;
DE Short=LXA4 receptor;
DE AltName: Full=RFP;
GN Name=FPR2; Synonyms=FPRH1, FPRL1, LXA4R;
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 [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=1511907; DOI=10.1016/0378-1119(92)90208-7;
RA Perez H.D., Holmes R., Kelly E., McClary J., Andrews W.H.;
RT "Cloning of a cDNA encoding a receptor related to the formyl peptide
RT receptor of human neutrophils.";
RL Gene 118:303-304(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Granulocyte;
RX PubMed=1374236; DOI=10.1016/0006-291x(92)90629-y;
RA Ye R.D., Cavanagh S.L., Quehenberger O., Prossnitz E.R., Cochrane C.G.;
RT "Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide
RT receptor.";
RL Biochem. Biophys. Res. Commun. 184:582-589(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1373134; DOI=10.1016/s0021-9258(18)42563-x;
RA Murphy P.M., Ozcelik T., Kenney R.T., Tiffany H.L., McDermott D.,
RA Francke U.;
RT "A structural homologue of the N-formyl peptide receptor. Characterization
RT and chromosome mapping of a peptide chemoattractant receptor family.";
RL J. Biol. Chem. 267:7637-7643(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Monocyte;
RX PubMed=7505609; DOI=10.1093/intimm/5.10.1239;
RA Nomura H., Nielsen B.W., Matsushima K.;
RT "Molecular cloning of cDNAs encoding a LD78 receptor and putative leukocyte
RT chemotactic peptide receptors.";
RL Int. Immunol. 5:1239-1249(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Maddox J.F., Hachicha M., Takano T., Petasis N.A., Fokin V.V., Serhan C.N.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9547339; DOI=10.1084/jem.187.8.1285;
RA Gronert K., Gewirtz A., Madara J.L., Serhan C.N.;
RT "Identification of a human enterocyte lipoxin A4 receptor that is regulated
RT by interleukin (IL)-13 and interferon gamma and inhibits tumor necrosis
RT factor alpha-induced IL-8 release.";
RL J. Exp. Med. 187:1285-1294(1998).
RN [8]
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 (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [13]
RP TISSUE SPECIFICITY.
RX PubMed=9151906; DOI=10.1084/jem.185.9.1693;
RA Takano T., Fiore S., Maddox J.F., Brady H.R., Petasis N.A., Serhan C.N.;
RT "Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 stable analogues are
RT potent inhibitors of acute inflammation: evidence for anti-inflammatory
RT receptors.";
RL J. Exp. Med. 185:1693-1704(1997).
RN [14]
RP INTERACTION WITH AMYLOID-BETA PROTEIN 42, AND SUBCELLULAR LOCATION.
RX PubMed=11689470; DOI=10.1096/fj.01-0251com;
RA Yazawa H., Yu Z.-X., Takeda K., Le Y., Gong W., Ferrans V.J.,
RA Oppenheim J.J., Li C.C.H., Wang J.M.;
RT "Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled
RT receptor FPRL1 and forms fibrillar aggregates in macrophages.";
RL FASEB J. 15:2454-2462(2001).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, 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).
RN [16]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SSL13 (MICROBIAL INFECTION).
RX PubMed=30098280; DOI=10.1111/cmi.12941;
RA Zhao Y., van Kessel K.P.M., de Haas C.J.C., Rogers M.R.C.,
RA van Strijp J.A.G., Haas P.A.;
RT "Staphylococcal superantigen-like protein 13 activates neutrophils via
RT formyl peptide receptor 2.";
RL Cell. Microbiol. 20:E12941-E12941(2018).
CC -!- FUNCTION: Low affinity receptor for N-formyl-methionyl peptides, which
CC are powerful neutrophil chemotactic factors (PubMed:1374236). Binding
CC of FMLP to the receptor causes activation of neutrophils
CC (PubMed:1374236). This response is mediated via a G-protein that
CC activates a phosphatidylinositol-calcium second messenger system
CC (PubMed:1374236). The activation of LXA4R could result in an anti-
CC inflammatory outcome counteracting the actions of pro-inflammatory
CC signals such as LTB4 (leukotriene B4) (PubMed:9547339). Receptor for
CC the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated
CC macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-
CC induced osteoclast differentiation (By similarity). Acts as a receptor
CC for humanin (PubMed:15465011). {ECO:0000250|UniProtKB:O88536,
CC ECO:0000269|PubMed:1374236, ECO:0000269|PubMed:15465011,
CC ECO:0000269|PubMed:9547339}.
CC -!- SUBUNIT: Interacts with Amyloid-beta protein 42, product of APP; the
CC interaction takes place at the cell surface and the complex is then
CC rapidly internalized. {ECO:0000269|PubMed:11689470}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein SSL13; this interaction leads to the activation of neutrophils.
CC {ECO:0000269|PubMed:30098280}.
CC -!- INTERACTION:
CC P25090; P05090: APOD; NbExp=3; IntAct=EBI-17291771, EBI-715495;
CC P25090; P05067: APP; NbExp=3; IntAct=EBI-17291771, EBI-77613;
CC P25090; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-17291771, EBI-713304;
CC P25090; Q8N386: LRRC25; NbExp=3; IntAct=EBI-17291771, EBI-11304917;
CC P25090; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-17291771, EBI-17280858;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11689470,
CC ECO:0000269|PubMed:15465011}; Multi-pass membrane protein.
CC Note=Associates with Amyloid-beta protein 42, product of APP, at the
CC cell surface and the complex is then rapidly internalized
CC (PubMed:11689470). Also internalized in the presence of humanin
CC (PubMed:15465011). {ECO:0000269|PubMed:11689470,
CC ECO:0000269|PubMed:15465011}.
CC -!- TISSUE SPECIFICITY: Detected in lung, bone marrow, neutrophils, spleen
CC and testis. {ECO:0000269|PubMed:15465011, ECO:0000269|PubMed:9151906}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M76672; AAA58481.1; -; mRNA.
DR EMBL; X63819; CAA45319.1; -; mRNA.
DR EMBL; M88107; AAA60070.1; -; mRNA.
DR EMBL; M84562; AAA52473.1; -; mRNA.
DR EMBL; D10922; BAA01720.1; -; mRNA.
DR EMBL; U81501; AAB51133.1; -; mRNA.
DR EMBL; AF054013; AAC13684.1; -; mRNA.
DR EMBL; AY225226; AAO67711.1; -; Genomic_DNA.
DR EMBL; AK290557; BAF83246.1; -; mRNA.
DR EMBL; AC018755; AAF87844.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72043.1; -; Genomic_DNA.
DR EMBL; BC029125; AAH29125.1; -; mRNA.
DR EMBL; BC071722; AAH71722.1; -; mRNA.
DR CCDS; CCDS12840.1; -.
DR PIR; B42009; B42009.
DR RefSeq; NP_001005738.1; NM_001005738.1.
DR RefSeq; NP_001453.1; NM_001462.3.
DR RefSeq; XP_006723183.1; XM_006723120.3.
DR RefSeq; XP_016882031.1; XM_017026542.1.
DR PDB; 6LW5; X-ray; 2.80 A; A=3-322.
DR PDB; 6OMM; EM; 3.17 A; R=1-342.
DR PDB; 7T6S; EM; 3.00 A; R=1-342.
DR PDB; 7T6U; EM; 2.90 A; R=1-342.
DR PDB; 7T6V; EM; 3.10 A; R=1-342.
DR PDB; 7WVV; EM; 2.90 A; R=2-347.
DR PDB; 7WVW; EM; 3.10 A; R=2-347.
DR PDB; 7WVX; EM; 2.80 A; R=2-347.
DR PDB; 7WVY; EM; 3.00 A; R=2-347.
DR PDBsum; 6LW5; -.
DR PDBsum; 6OMM; -.
DR PDBsum; 7T6S; -.
DR PDBsum; 7T6U; -.
DR PDBsum; 7T6V; -.
DR PDBsum; 7WVV; -.
DR PDBsum; 7WVW; -.
DR PDBsum; 7WVX; -.
DR PDBsum; 7WVY; -.
DR AlphaFoldDB; P25090; -.
DR SMR; P25090; -.
DR BioGRID; 108641; 150.
DR IntAct; P25090; 76.
DR STRING; 9606.ENSP00000468897; -.
DR BindingDB; P25090; -.
DR ChEMBL; CHEMBL4227; -.
DR GuidetoPHARMACOLOGY; 223; -.
DR GlyGen; P25090; 1 site.
DR iPTMnet; P25090; -.
DR PhosphoSitePlus; P25090; -.
DR BioMuta; FPR2; -.
DR DMDM; 399504; -.
DR jPOST; P25090; -.
DR MassIVE; P25090; -.
DR PaxDb; P25090; -.
DR PeptideAtlas; P25090; -.
DR PRIDE; P25090; -.
DR ProteomicsDB; 54252; -.
DR TopDownProteomics; P25090; -.
DR Antibodypedia; 19050; 413 antibodies from 35 providers.
DR DNASU; 2358; -.
DR Ensembl; ENST00000340023.7; ENSP00000340191.4; ENSG00000171049.9.
DR Ensembl; ENST00000598776.1; ENSP00000468897.1; ENSG00000171049.9.
DR Ensembl; ENST00000598953.1; ENSP00000468876.1; ENSG00000171049.9.
DR GeneID; 2358; -.
DR KEGG; hsa:2358; -.
DR MANE-Select; ENST00000340023.7; ENSP00000340191.4; NM_001005738.2; NP_001005738.1.
DR UCSC; uc002pxr.4; human.
DR CTD; 2358; -.
DR DisGeNET; 2358; -.
DR GeneCards; FPR2; -.
DR HGNC; HGNC:3827; FPR2.
DR HPA; ENSG00000171049; Tissue enhanced (lymphoid).
DR MIM; 136538; gene.
DR neXtProt; NX_P25090; -.
DR OpenTargets; ENSG00000171049; -.
DR PharmGKB; PA162388901; -.
DR VEuPathDB; HostDB:ENSG00000171049; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P25090; -.
DR OMA; CKLIHII; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P25090; -.
DR TreeFam; TF330976; -.
DR PathwayCommons; P25090; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
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 Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P25090; -.
DR SIGNOR; P25090; -.
DR BioGRID-ORCS; 2358; 9 hits in 1066 CRISPR screens.
DR GeneWiki; Formyl_peptide_receptor_2; -.
DR GenomeRNAi; 2358; -.
DR Pharos; P25090; Tchem.
DR PRO; PR:P25090; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P25090; protein.
DR Bgee; ENSG00000171049; Expressed in blood and 106 other tissues.
DR ExpressionAtlas; P25090; baseline and differential.
DR Genevisible; P25090; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; ISS:ARUK-UCL.
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:0005124; F:scavenger receptor binding; IPI:ARUK-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IDA:ARUK-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0048143; P:astrocyte activation; ISS:ARUK-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IGI:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:ARUK-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IDA:ARUK-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0001774; P:microglial cell activation; ISS:ARUK-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:ARUK-UCL.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050918; P:positive chemotaxis; ISS:ARUK-UCL.
DR GO; GO:0061903; P:positive regulation of 1-phosphatidylinositol-3-kinase activity; ISS:ARUK-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:ARUK-UCL.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IGI:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
DR InterPro; IPR027345; Formyl_pep_1/2_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:SF15; PTHR24225:SF15; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="N-formyl peptide receptor 2"
FT /id="PRO_0000069451"
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..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 325..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 339
FT /note="S -> C (in Ref. 1; AAA58481)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:6LW5"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 20..53
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 95..128
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:6LW5"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:6LW5"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6LW5"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 187..207
FT /evidence="ECO:0007829|PDB:6LW5"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 211..230
FT /evidence="ECO:0007829|PDB:6LW5"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 240..266
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:6LW5"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:6LW5"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:6LW5"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6LW5"
SQ SEQUENCE 351 AA; 38964 MW; DC6A1D77AFC0D780 CRC64;
METNFSTPLN EYEEVSYESA GYTVLRILPL VVLGVTFVLG VLGNGLVIWV AGFRMTRTVT
TICYLNLALA DFSFTATLPF LIVSMAMGEK WPFGWFLCKL IHIVVDINLF GSVFLIGFIA
LDRCICVLHP VWAQNHRTVS LAMKVIVGPW ILALVLTLPV FLFLTTVTIP NGDTYCTFNF
ASWGGTPEER LKVAITMLTA RGIIRFVIGF SLPMSIVAIC YGLIAAKIHK KGMIKSSRPL
RVLTAVVASF FICWFPFQLV ALLGTVWLKE MLFYGKYKII DILVNPTSSL AFFNSCLNPM
LYVFVGQDFR ERLIHSLPTS LERALSEDSA PTNDTAANSA SPPAETELQA M
