PTAFR_RAT
ID PTAFR_RAT Reviewed; 341 AA.
AC P46002;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Platelet-activating factor receptor;
DE Short=PAF-R;
DE Short=PAFr;
GN Name=Ptafr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX PubMed=8168510; DOI=10.1111/j.1432-1033.1994.tb18731.x;
RA Bito H., Honda Z., Nakamura M., Shimizu T.;
RT "Cloning, expression and tissue distribution of rat platelet-activating-
RT factor-receptor cDNA.";
RL Eur. J. Biochem. 221:211-218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Present in almost all organs including spleen,
CC small intestine, kidney, lung, liver and brain.
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; U04740; AAA18422.1; -; mRNA.
DR EMBL; BC072491; AAH72491.1; -; mRNA.
DR PIR; S43252; S43252.
DR RefSeq; NP_445773.1; NM_053321.2.
DR RefSeq; XP_006239125.1; XM_006239063.3.
DR RefSeq; XP_006239126.1; XM_006239064.2.
DR AlphaFoldDB; P46002; -.
DR SMR; P46002; -.
DR STRING; 10116.ENSRNOP00000017687; -.
DR BindingDB; P46002; -.
DR ChEMBL; CHEMBL4127; -.
DR GlyGen; P46002; 2 sites.
DR PhosphoSitePlus; P46002; -.
DR PaxDb; P46002; -.
DR Ensembl; ENSRNOT00000017687; ENSRNOP00000017687; ENSRNOG00000013231.
DR Ensembl; ENSRNOT00000097551; ENSRNOP00000079229; ENSRNOG00000013231.
DR Ensembl; ENSRNOT00000119353; ENSRNOP00000085904; ENSRNOG00000013231.
DR GeneID; 58949; -.
DR KEGG; rno:58949; -.
DR UCSC; RGD:61897; rat.
DR CTD; 5724; -.
DR RGD; 61897; Ptafr.
DR eggNOG; ENOG502QTQI; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P46002; -.
DR OMA; AIHVIIC; -.
DR OrthoDB; 800525at2759; -.
DR PhylomeDB; P46002; -.
DR TreeFam; TF350009; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P46002; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013231; Expressed in spleen and 17 other tissues.
DR Genevisible; P46002; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; ISO:RGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0004992; F:platelet activating factor receptor activity; IDA:RGD.
DR GO; GO:1904317; P:cellular response to 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0071258; P:cellular response to gravity; IEP:RGD.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0007567; P:parturition; IMP:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:RGD.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:RGD.
DR GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; IMP:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; IMP:RGD.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:RGD.
DR GO; GO:1904303; P:positive regulation of maternal process involved in parturition; IMP:RGD.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; IMP:RGD.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:RGD.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:1904300; P:positive regulation of transcytosis; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:1904316; P:response to 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0046683; P:response to organophosphorus; IEP:RGD.
DR GO; GO:0009609; P:response to symbiotic bacterium; IEP:RGD.
DR GO; GO:0045056; P:transcytosis; IMP:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002282; PAF_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01153; PAFRECEPTOR.
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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="Platelet-activating factor receptor"
FT /id="PRO_0000070096"
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..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..295
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..341
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:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 341 AA; 39204 MW; D0AF7290C3D34A5B CRC64;
MEQNGSFRVD SEFRYTLFPI VYSVIFVLGV VANGYVLWVF ATLYPSKKLN EIKIFMVNLT
VADLLFLMTL PLWIVYYSNE GDWIVHKFLC NLAGCLFFIN TYCSVAFLGV ITYNRYQAVA
YPIKTAQATT RKRGITLSLV IWISIAATAS YFLATDSTNV VPKKDGSGNI TRCFEHYEPY
SVPILVVHIF ITSCFFLVFF LIFYCNMVII HTLLTRPVRQ QRKPEVKRRA LWMVCTVLAV
FVICFVPHHV VQLPWTLAEL GYQTNFHQAI NDAHQITLCL LSTNCVLDPV IYCFLTKKFR
KHLSEKFYSM RSSRKCSRAT SDTCTEVMMP ANQTPVLPLK N
