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Platelet-activating factor receptor (PAF-R) (PAFr)

 PTAFR_HUMAN             Reviewed;         342 AA.
P25105; A3KMC8; A8K2H5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=Platelet-activating factor receptor;
Short=PAF-R;
Short=PAFr;
Name=PTAFR; Synonyms=PAFR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Granulocyte;
PubMed=1656963; DOI=10.1016/S0006-291X(05)81261-6;
Ye R.D., Prossnitz E.R., Zou A., Cochrane C.G.;
"Characterization of a human cDNA that encodes a functional receptor
for platelet activating factor.";
Biochem. Biophys. Res. Commun. 180:105-111(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Leukocyte;
PubMed=1657923;
Nakamura M., Honda Z., Izumi T., Sakanaka C., Mutoh H., Minami M.,
Bito H., Seyama Y., Matsumoto T., Noma M., Shimizu T.;
"Molecular cloning and expression of platelet-activating factor
receptor from human leukocytes.";
J. Biol. Chem. 266:20400-20405(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Leukocyte;
PubMed=1374385;
Kunz D., Gerard N.P., Gerard C.;
"The human leukocyte platelet-activating factor receptor. cDNA
cloning, cell surface expression, and construction of a novel epitope-
bearing analog.";
J. Biol. Chem. 267:9101-9106(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Fetal liver;
PubMed=1322356; DOI=10.1016/0888-7543(92)90162-L;
Seyfried C.E., Schweickart V.L., Godiska R., Gray P.W.;
"The human platelet-activating factor receptor gene (PTAFR) contains
no introns and maps to chromosome 1.";
Genomics 13:832-834(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Heart ventricle;
PubMed=1281995; DOI=10.1016/0006-291X(92)92245-S;
Sugimoto T., Tsuchimochi H., McGregor C.G.A., Mutoh H., Shimizu T.,
Kurachi Y.;
"Molecular cloning and characterization of the platelet-activating
factor receptor gene expressed in the human heart.";
Biochem. Biophys. Res. Commun. 189:617-624(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix carcinoma;
Behal R.H., Debuysere M.S., Olson M.S.;
"Nucleotide sequence of platelet-activating-factor receptor derived
from HeLa cell genomic DNA and Rhesus monkey genomic DNA.";
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8383507; DOI=10.1165/ajrcmb/8.3.240;
Chase P.B., Halonen M., Regan J.W.;
"Cloning of a human platelet-activating factor receptor gene: evidence
for an intron in the 5'-untranslated region.";
Am. J. Respir. Cell Mol. Biol. 8:240-244(1993).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
Warren C.N., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
INTERACTION WITH ARRB1.
PubMed=16709866; DOI=10.4049/jimmunol.176.11.7039;
McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F.,
Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C.;
"Platelet-activating factor-induced clathrin-mediated endocytosis
requires beta-arrestin-1 recruitment and activation of the p38 MAPK
signalosome at the plasma membrane for actin bundle formation.";
J. Immunol. 176:7039-7050(2006).
[14]
VARIANTS ASP-224 AND SER-338.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[15]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
-!- FUNCTION: Receptor for platelet activating factor, a chemotactic
phospholipid mediator that possesses potent inflammatory, smooth-
muscle contractile and hypotensive activity. Seems to mediate its
action via a G protein that activates a phosphatidylinositol-
calcium second messenger system. {ECO:0000269|PubMed:1281995,
ECO:0000269|PubMed:1374385, ECO:0000269|PubMed:1656963,
ECO:0000269|PubMed:1657923}.
-!- SUBUNIT: Interacts with ARRB1. {ECO:0000269|PubMed:16709866}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1374385};
Multi-pass membrane protein {ECO:0000269|PubMed:1374385}.
-!- TISSUE SPECIFICITY: Expressed in the placenta, lung, left and
right heart ventricles, heart atrium, leukocytes and
differentiated HL-60 granulocytes. {ECO:0000269|PubMed:1281995,
ECO:0000269|PubMed:1656963, ECO:0000269|PubMed:1657923}.
-!- INDUCTION: By CSF2/GM-CSF, IL5/interleukin-5 and n-butyrate.
{ECO:0000269|PubMed:1657923}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; M80436; AAA60001.1; -; mRNA.
EMBL; D10202; BAA01050.1; -; mRNA.
EMBL; M76674; AAA60002.1; -; mRNA.
EMBL; M88177; AAA60214.1; -; Genomic_DNA.
EMBL; S52624; AAB24695.2; -; mRNA.
EMBL; L07334; AAA60108.1; -; mRNA.
EMBL; S56396; AAB25755.1; -; Genomic_DNA.
EMBL; AY275466; AAP32298.1; -; mRNA.
EMBL; BT009801; AAP88803.1; -; mRNA.
EMBL; AK290240; BAF82929.1; -; mRNA.
EMBL; CH471059; EAX07711.1; -; Genomic_DNA.
EMBL; BC013816; AAH13816.1; -; mRNA.
EMBL; BC063000; AAH63000.1; -; mRNA.
CCDS; CCDS318.1; -.
PIR; A40191; A40191.
RefSeq; NP_000943.1; NM_000952.4.
RefSeq; NP_001158193.1; NM_001164721.1.
RefSeq; NP_001158194.1; NM_001164722.2.
RefSeq; NP_001158195.1; NM_001164723.2.
UniGene; Hs.77542; -.
PDB; 2B0X; Model; -; A=1-342.
PDBsum; 2B0X; -.
ProteinModelPortal; P25105; -.
BioGrid; 111696; 10.
CORUM; P25105; -.
IntAct; P25105; 4.
STRING; 9606.ENSP00000301974; -.
BindingDB; P25105; -.
ChEMBL; CHEMBL250; -.
GuidetoPHARMACOLOGY; 334; -.
SwissLipids; SLP:000001565; -.
TCDB; 9.A.14.13.3; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P25105; -.
PhosphoSitePlus; P25105; -.
BioMuta; PTAFR; -.
DMDM; 129557; -.
PaxDb; P25105; -.
PeptideAtlas; P25105; -.
PRIDE; P25105; -.
DNASU; 5724; -.
Ensembl; ENST00000305392; ENSP00000301974; ENSG00000169403.
Ensembl; ENST00000373857; ENSP00000362965; ENSG00000169403.
Ensembl; ENST00000539896; ENSP00000442658; ENSG00000169403.
GeneID; 5724; -.
KEGG; hsa:5724; -.
UCSC; uc001bpl.4; human.
CTD; 5724; -.
DisGeNET; 5724; -.
EuPathDB; HostDB:ENSG00000169403.11; -.
GeneCards; PTAFR; -.
HGNC; HGNC:9582; PTAFR.
HPA; HPA027543; -.
MIM; 173393; gene.
neXtProt; NX_P25105; -.
OpenTargets; ENSG00000169403; -.
PharmGKB; PA33933; -.
eggNOG; ENOG410IIY4; Eukaryota.
eggNOG; ENOG410YB0R; LUCA.
GeneTree; ENSGT00900000140808; -.
HOGENOM; HOG000013041; -.
HOVERGEN; HBG101106; -.
InParanoid; P25105; -.
KO; K04279; -.
OMA; AHQVTLC; -.
OrthoDB; EOG091G0A7Q; -.
PhylomeDB; P25105; -.
TreeFam; TF350009; -.
Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; P25105; -.
GeneWiki; Platelet-activating_factor_receptor; -.
GenomeRNAi; 5724; -.
PRO; PR:P25105; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000169403; -.
CleanEx; HS_PTAFR; -.
Genevisible; P25105; HS.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0045028; F:G-protein coupled purinergic nucleotide receptor activity; IBA:GO_Central.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0001875; F:lipopolysaccharide receptor activity; IEA:Ensembl.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
GO; GO:0004992; F:platelet activating factor receptor activity; IDA:UniProtKB.
GO; GO:1904317; P:cellular response to 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071258; P:cellular response to gravity; IEA:Ensembl.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0001816; P:cytokine production; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007567; P:parturition; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; IEA:Ensembl.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:1904303; P:positive regulation of maternal process involved in parturition; IEA:Ensembl.
GO; GO:0043315; P:positive regulation of neutrophil degranulation; IEA:Ensembl.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IEA:Ensembl.
GO; GO:1904058; P:positive regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:1904300; P:positive regulation of transcytosis; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0009609; P:response to symbiotic bacterium; IEA:Ensembl.
GO; GO:0045056; P:transcytosis; IEA:Ensembl.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR002282; PAF_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01153; PAFRECEPTOR.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Chemotaxis; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 342 Platelet-activating factor receptor.
/FTId=PRO_0000070092.
TOPO_DOM 1 16 Extracellular. {ECO:0000255}.
TRANSMEM 17 38 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 39 54 Cytoplasmic. {ECO:0000255}.
TRANSMEM 55 74 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 75 91 Extracellular. {ECO:0000255}.
TRANSMEM 92 113 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 114 133 Cytoplasmic. {ECO:0000255}.
TRANSMEM 134 155 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 156 184 Extracellular. {ECO:0000255}.
TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 206 233 Cytoplasmic. {ECO:0000255}.
TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 255 276 Extracellular. {ECO:0000255}.
TRANSMEM 277 296 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 297 342 Cytoplasmic. {ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 90 173 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 224 224 A -> D (in dbSNP:rs5938).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011851.
VARIANT 338 338 N -> S (in dbSNP:rs5939).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011852.
CONFLICT 28 28 L -> P (in Ref. 6; AAA60108).
{ECO:0000305}.
CONFLICT 66 66 F -> L (in Ref. 6; AAA60108).
{ECO:0000305}.
CONFLICT 95 95 C -> R (in Ref. 6; AAA60108).
{ECO:0000305}.
CONFLICT 227 228 KR -> TG (in Ref. 4; AAA60214).
{ECO:0000305}.
CONFLICT 227 228 KR -> TT (in Ref. 6; AAA60108).
{ECO:0000305}.
CONFLICT 247 247 P -> A (in Ref. 6; AAA60108).
{ECO:0000305}.
CONFLICT 316 316 K -> N (in Ref. 5; AAB24695).
{ECO:0000305}.
SEQUENCE 342 AA; 39203 MW; 890073C9EBA79228 CRC64;
MEPHDSSHMD SEFRYTLFPI VYSIIFVLGV IANGYVLWVF ARLYPCKKFN EIKIFMVNLT
MADMLFLITL PLWIVYYQNQ GNWILPKFLC NVAGCLFFIN TYCSVAFLGV ITYNRFQAVT
RPIKTAQANT RKRGISLSLV IWVAIVGAAS YFLILDSTNT VPDSAGSGNV TRCFEHYEKG
SVPVLIIHIF IVFSFFLVFL IILFCNLVII RTLLMQPVQQ QRNAEVKRRA LWMVCTVLAV
FIICFVPHHV VQLPWTLAEL GFQDSKFHQA INDAHQVTLC LLSTNCVLDP VIYCFLTKKF
RKHLTEKFYS MRSSRKCSRA TTDTVTEVVV PFNQIPGNSL KN


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