FPR3_GORGO
ID FPR3_GORGO Reviewed; 349 AA.
AC P79178;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 91.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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; X97742; CAA66326.1; -; Genomic_DNA.
DR AlphaFoldDB; P79178; -.
DR SMR; P79178; -.
DR STRING; 9593.ENSGGOP00000008782; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79178; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..>349
FT /note="N-formyl peptide receptor 3"
FT /id="PRO_0000069456"
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 327..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; 39433 MW; C6ED77CFDE023834 CRC64;
METNFSIPLN ETEEVLPEPA GHTVLWIFSL LVHGVTFIFG VLGNGLVIWV AGFLMTRTVN
TICYLNLALA DFSFSAILPF HMVSVAMREK WPFGSFLCKL VHVMIDINLF VSVYLITIIA
LDRCICVLHP AWAQNHRTMS LAKRVMTGLW ILTIVLTLPN FIFWTTISTT NGDTYCIFNF
PFWGDTAVER LNVFITMAKV FLILHFIIGF SMPMSIITVC YGIIAAKIHR NHMIKSSRPL
RVFAAVVASF FICWFPYELI GILMAVWLKE MLLNGKYKII LVLINPTSSL AFFNSCLNPI
LYVFLGSNFQ ERLIRSLPTS LERALTEVPD SAQTSNTHTT SASPPEETE
