FPR1_GORGO
ID FPR1_GORGO Reviewed; 346 AA.
AC P79176;
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=fMet-Leu-Phe receptor;
DE Short=fMLP receptor;
DE AltName: Full=N-formyl peptide receptor;
DE Short=FPR;
DE AltName: Full=N-formylpeptide chemoattractant receptor;
DE Flags: Fragment;
GN Name=FPR1;
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: High affinity receptor for N-formyl-methionyl peptides
CC (fMLP), which are powerful neutrophil chemotactic factors. Binding of
CC fMLP to the receptor stimulates intracellular calcium mobilization and
CC superoxide anion release. This response is mediated via a G-protein
CC that activates a phosphatidylinositol-calcium second messenger system
CC (By similarity). Receptor for TAFA4, mediates its effects on
CC chemoattracting macrophages, promoting phagocytosis and increasing ROS
CC release (By similarity). Receptor for cathepsin CTSG, leading to
CC increased phagocyte chemotaxis (By similarity).
CC {ECO:0000250|UniProtKB:P21462, ECO:0000250|UniProtKB:P33766}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21462,
CC ECO:0000250|UniProtKB:P33766}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Internalizes in presence of its ligand, TAFA4.
CC {ECO:0000250|UniProtKB:P21462}.
CC -!- PTM: Phosphorylated; which is necessary for desensitization.
CC {ECO:0000250|UniProtKB:P21462}.
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; X97736; CAA66320.1; -; Genomic_DNA.
DR AlphaFoldDB; P79176; -.
DR SMR; P79176; -.
DR STRING; 9593.ENSGGOP00000005146; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79176; -.
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; ISS:UniProtKB.
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; 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 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN <1..>346
FT /note="fMet-Leu-Phe receptor"
FT /id="PRO_0000069443"
FT TOPO_DOM <1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..>346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 346
SQ SEQUENCE 346 AA; 37880 MW; B7FF017586F2D173 CRC64;
NSSLPTNISG GTPAVSAGYL FLDIVTYLVF AVTFVLGVLG NGLVIWVAGF RMTHTVTTIS
YLNLAVADFC FTSTLPFFMV KKAMGGHWPF GWFLCKFIFT IVDINLFGSV FLIALIALDR
CVCVLHPVWT QNHRTVSLAK KVIIGPWVMA LLLTLPVIIR VTTVPGKMGT VACTFNFSPW
TNDPKERIKV AVAMLTVRGI IRFIIGFSAP MSIVAVSYGL IATKIDKQGL IKSSRTLRVL
SFVAAAFFLS WSPYQVVALI ATVRIRELLQ GMYKEIGIAV DVTSALAFFN SCLNPMLYVF
MGQDFRERLI HALPASLERA LTEDSTQTSD TATNSTLPSA EVALQA
