ID PTAFR_CAPHI Reviewed; 342 AA.
AC Q9GK76;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Platelet-activating factor receptor;
DE Short=PAF-R;
DE Short=PAFr;
GN Name=PTAFR {ECO:0000250|UniProtKB:P25105}; Synonyms=PAFR;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1] {ECO:0000312|EMBL:AAG39982.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11916258; DOI=10.3109/10425170109024998;
RA Yang W., Diehl J.R., Roudebush W.E.;
RT "Comparison of the coding sequence of the platelet-activating factor
RT receptor gene in three species.";
RL DNA Seq. 12:239-251(2001).
CC -!- FUNCTION: Receptor for platelet activating factor, a chemotactic
CC phospholipid mediator that possesses potent inflammatory, smooth-muscle
CC contractile and hypotensive activity. Seems to mediate its action via a
CC G protein that activates a phosphatidylinositol-calcium second
CC messenger system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
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}.
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; AF302764; AAG39982.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GK76; -.
DR SMR; Q9GK76; -.
DR STRING; 9925.ENSCHIP00000009023; -.
DR GlyCosmos; Q9GK76; 2 sites, No reported glycans.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Proteomes; UP000694566; Unplaced.
DR Proteomes; UP000694900; Genome assembly.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004992; F:platelet activating factor receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd15147; 7tmA_PAFR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002282; PAF_rcpt.
DR PANTHER; PTHR24233; P2Y PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24233:SF6; PLATELET-ACTIVATING FACTOR RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01153; PAFRECEPTOR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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..342
FT /note="Platelet-activating factor receptor"
FT /id="PRO_0000070090"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..173
FT /evidence="ECO:0000250|UniProtKB:P25105,
FT ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 342 AA; 39612 MW; 39D9379AED60FD4E CRC64;
MEPNNSFRVD SEFRYTLFPI FYSIVFVLGV IANSYVLWVF ARLYPSKKFN EIKIFMVNLT
MADLLFLVTL PLWIVYYYNQ GDWILPKFLC NLAGCFFFIN TYCSVAFLAV ITYNRFQAVT
RPIKTAQATT RKRGFLLSLI IWVSIVGAAS YFFVLDSTNS EPKKTGSGNI TRCFEHYEKG
SIPVLIIHIF LVFSFFLVFL IILFCNLVII RTLLTQQVQM QRNAEVKRRA LWMVCTVLAV
FVICFVPHHL VQLPWTLAEL GFQDTDFHQG INDAHQVTLC LLSTNCVLDP IIYCFLTKKF
RKHLTEKLYS MRESRKCSRA TSETGTEVVV QLKDAPIKSL KY
//
