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 27-MAR-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-20126; -. DR EMDB; EMD-25726; -. DR EMDB; EMD-25728; -. DR EMDB; EMD-25729; -. 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 TCDB; 9.A.14.13.44; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P25090; 1 site, No reported glycans. 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; 9606-ENSP00000468897; -. DR PeptideAtlas; P25090; -. DR ProteomicsDB; 54252; -. DR TopDownProteomics; P25090; -. DR Antibodypedia; 19050; 453 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 AGR; HGNC:3827; -. 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; ENSGT01020000230438; -. DR HOGENOM; CLU_009579_8_0_1; -. DR InParanoid; P25090; -. DR OMA; VYCTFNF; -. DR OrthoDB; 5384006at2759; -. 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; 12 hits in 1147 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 108 other cell types or tissues. DR ExpressionAtlas; P25090; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0016020; C: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; TAS:ProtInc. 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: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 CDD; cd15117; 7tmA_FPR-like; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000826; Formyl_rcpt-rel. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1. DR PANTHER; PTHR24225:SF0; N-FORMYL PEPTIDE RECEPTOR 2; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00526; FMETLEUPHER. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P25090; HS. 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 STRAND 87..89 FT /evidence="ECO:0007829|PDB:7WVX" 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 //