FPR2_GORGO
ID FPR2_GORGO Reviewed; 348 AA.
AC P79177;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Flags: Fragment;
GN Name=FPR2; Synonyms=FPRL1;
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 neutrophil chemotactic factors (By similarity). Binding of
CC FMLP to the receptor causes activation of neutrophils (By similarity).
CC This response is mediated via a G-protein that activates a
CC phosphatidylinositol-calcium second messenger system (By similarity).
CC Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-
CC stimulated macrophage chemotaxis and the inhibitory effect on
CC TNFSF11/RANKL-induced osteoclast differentiation (By similarity).
CC {ECO:0000250|UniProtKB:O88536, ECO:0000250|UniProtKB:P25090}.
CC -!- SUBUNIT: Interacts with APP; the interaction takes place at the cell
CC surface and the complex is then rapidly internalized.
CC {ECO:0000250|UniProtKB:P25090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25090};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P25090}.
CC Note=Associates with APP at the cell surface and the complex is then
CC rapidly internalized. {ECO:0000250|UniProtKB:P25090}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X97738; CAA66322.1; -; Genomic_DNA.
DR AlphaFoldDB; P79177; -.
DR SMR; P79177; -.
DR STRING; 9593.ENSGGOP00000005547; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79177; -.
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; 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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..>348
FT /note="N-formyl peptide receptor 2"
FT /id="PRO_0000069450"
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..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1
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 348
SQ SEQUENCE 348 AA; 38581 MW; B1F0B3BDCC76CAA0 CRC64;
NFSTPLNEHE EVSYESAGYT VLRILPLVVL GVTFVLGVLG NGLVIWVAGF RMTRTVTTIC
YLNLALADFS FTATLPFLIV SMAMGEKWPF GWFLCKLIHI VVDINLFGSV FLIGFIALDR
CICVLHPVWA QNHRTVSLAM KVIVGPWILA LVLTLPVFLF LTTVTIPNGD TYCTFNFASW
GGTPEERQKV AITMLTARGI IRFVIGFSLP MSIVAICYGL IAAKIHKKGM IKSSRPLRVL
TAVVASFFIC WFPFQLVALL GTVWLKEMLF YGKYKIIDIL VNPTSSLAFF NSCLNPMLYV
FVGQDFRERL IHSLPTSLER ALSEDSAPTN DTAASCASPP AETELQAM
