ID   FPR3_PONPY              Reviewed;         349 AA.
AC   P79237;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 94.
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;
DE   Flags: Fragment;
GN   Name=FPR3; Synonyms=FPRL2;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8824156; DOI=10.1007/bf02602806;
RA   Alvarez V., Coto E., Sehen F., Gouzalek-Koces S., Lopez-Larrea C.;
RT   "Molecular evolution of the N-formyl peptide and C5a receptors in non-human
RT   primates.";
RL   Immunogenetics 44:446-452(1996).
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X97741; CAA66325.1; -; Genomic_DNA.
DR   AlphaFoldDB; P79237; -.
DR   SMR; P79237; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004982; F:N-formyl peptide receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..>349
FT                   /note="N-formyl peptide receptor 3"
FT                   /id="PRO_0000069460"
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..>349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          328..349
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   NON_TER         349
SQ   SEQUENCE   349 AA;  39424 MW;  C8298D223395EECB CRC64;
     METNFSIPLN ESEEVLPEPA GHTVLWIFSL LVHGVTFIFG VLGNGLVIWV AGFRMTRTVN
     TICYLNLALA DFSFSAILPF RMVSVAMREK WPFGTFLCKL VHVMIDINLF VSVYLITIIA
     LDRCICVLHP AWAQNHRTMS LAKRVMMGLW ILAIVLTLPN FIFWTTISTK NGDTYCIFNF
     PFWGDTAVER LNAFITMGKV FLILHFIIGF SMPMSIITVC YGIIAAKIHR NHMIKSSSPL
     RVFAAVVASF FICWFPYELI GILMAVWLKE MLLNGKYKII LVLLNPTSSL AFFNSCLNPI
     LYVFLGSNFQ ERLIRSLPTS LERALTEVPD SAQTSNTHTN SASPPEETE