FPR1_RABIT
ID FPR1_RABIT Reviewed; 352 AA.
AC Q05394;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 107.
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;
GN Name=FPR1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Neutrophil;
RX PubMed=8432984;
RA Ye R.D., Quehenberger O., Thomas K.M., Navarro J., Cavanagh S.L.,
RA Prossnitz E.R., Cochrane C.G.;
RT "The rabbit neutrophil N-formyl peptide receptor. cDNA cloning, expression,
RT and structure/function implications.";
RL J. Immunol. 150:1383-1394(1993).
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 Receptor for TAFA4, mediates its effects on chemoattracting
CC macrophages, promoting phagocytosis and increasing ROS release (By
CC similarity). Receptor for cathepsin CTSG, leading to increased
CC phagocyte chemotaxis (By similarity). {ECO:0000250|UniProtKB:P21462,
CC ECO:0000269|PubMed:8432984, ECO:0000303|PubMed:8432984}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8432984};
CC Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in
CC presence of its ligand, TAFA4. {ECO:0000250|UniProtKB:P21462}.
CC -!- TISSUE SPECIFICITY: Neutrophils. {ECO:0000269|PubMed:8432984}.
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}.
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DR EMBL; M94549; AAA31254.1; -; mRNA.
DR PIR; A46520; A46520.
DR RefSeq; NP_001075783.1; NM_001082314.1.
DR AlphaFoldDB; Q05394; -.
DR SMR; Q05394; -.
DR STRING; 9986.ENSOCUP00000007429; -.
DR GeneID; 100009153; -.
DR KEGG; ocu:100009153; -.
DR CTD; 2357; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q05394; -.
DR OrthoDB; 910274at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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..352
FT /note="fMet-Leu-Phe receptor"
FT /id="PRO_0000069449"
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..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 38675 MW; 51DA550DAB13A091 CRC64;
MDSNASLPLN VSGGTQATPA GLVVLDVFSY LILVVTFVLG VLGNGLVIWV TGFRMTHTVT
TISYLNLALA DFSFTSTLPF FIVTKALGGH WPFGWFLCKF VFTIVDINLF GSVFLIALIA
LDRCICVLHP VWAQNHRNVS LAKKVIVGPW ICALLLTLPV IIRVTTLSHP RAPGKMACTF
DWSPWTEDPA EKLKVAISMF MVRGIIRFII GFSTPMSIVA VCYGLIATKI HRQGLIKSSR
PLRVLSFVVA SFLLCWSPYQ IAALIATVRI RELLLGMGKD LRIVLDVTSF VAFFNSCLNP
MLYVFMGQDF RERLIHSLPA SLERALSEDS AQTSDTGTNS TSAPAEAELQ AI
