ID PTAFR_HUMAN Reviewed; 342 AA. AC P25105; A3KMC8; A8K2H5; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 11-NOV-2015, entry version 155. DE RecName: Full=Platelet-activating factor receptor; DE Short=PAF-R; DE Short=PAFr; GN Name=PTAFR; Synonyms=PAFR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Granulocyte; RX PubMed=1656963; DOI=10.1016/S0006-291X(05)81261-6; RA Ye R.D., Prossnitz E.R., Zou A., Cochrane C.G.; RT "Characterization of a human cDNA that encodes a functional receptor RT for platelet activating factor."; RL Biochem. Biophys. Res. Commun. 180:105-111(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND RP INDUCTION. RC TISSUE=Leukocyte; RX PubMed=1657923; RA Nakamura M., Honda Z., Izumi T., Sakanaka C., Mutoh H., Minami M., RA Bito H., Seyama Y., Matsumoto T., Noma M., Shimizu T.; RT "Molecular cloning and expression of platelet-activating factor RT receptor from human leukocytes."; RL J. Biol. Chem. 266:20400-20405(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Leukocyte; RX PubMed=1374385; RA Kunz D., Gerard N.P., Gerard C.; RT "The human leukocyte platelet-activating factor receptor. cDNA RT cloning, cell surface expression, and construction of a novel epitope- RT bearing analog."; RL J. Biol. Chem. 267:9101-9106(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Fetal liver; RX PubMed=1322356; DOI=10.1016/0888-7543(92)90162-L; RA Seyfried C.E., Schweickart V.L., Godiska R., Gray P.W.; RT "The human platelet-activating factor receptor gene (PTAFR) contains RT no introns and maps to chromosome 1."; RL Genomics 13:832-834(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Heart ventricle; RX PubMed=1281995; DOI=10.1016/0006-291X(92)92245-S; RA Sugimoto T., Tsuchimochi H., McGregor C.G.A., Mutoh H., Shimizu T., RA Kurachi Y.; RT "Molecular cloning and characterization of the platelet-activating RT factor receptor gene expressed in the human heart."; RL Biochem. Biophys. Res. Commun. 189:617-624(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cervix carcinoma; RA Behal R.H., Debuysere M.S., Olson M.S.; RT "Nucleotide sequence of platelet-activating-factor receptor derived RT from HeLa cell genomic DNA and Rhesus monkey genomic DNA."; RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8383507; DOI=10.1165/ajrcmb/8.3.240; RA Chase P.B., Halonen M., Regan J.W.; RT "Cloning of a human platelet-activating factor receptor gene: evidence RT for an intron in the 5'-untranslated region."; RL Am. J. Respir. Cell Mol. Biol. 8:240-244(1993). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RA Warren C.N., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Lymph; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] RP INTERACTION WITH ARRB1. RX PubMed=16709866; DOI=10.4049/jimmunol.176.11.7039; RA McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., RA Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C.; RT "Platelet-activating factor-induced clathrin-mediated endocytosis RT requires beta-arrestin-1 recruitment and activation of the p38 MAPK RT signalosome at the plasma membrane for actin bundle formation."; RL J. Immunol. 176:7039-7050(2006). RN [14] RP VARIANTS ASP-224 AND SER-338. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [15] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: Receptor for platelet activating factor, a chemotactic CC phospholipid mediator that possesses potent inflammatory, smooth- CC muscle contractile and hypotensive activity. Seems to mediate its CC action via a G protein that activates a phosphatidylinositol- CC calcium second messenger system. {ECO:0000269|PubMed:1281995, CC ECO:0000269|PubMed:1374385, ECO:0000269|PubMed:1656963, CC ECO:0000269|PubMed:1657923}. CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000269|PubMed:16709866}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1374385}; CC Multi-pass membrane protein {ECO:0000269|PubMed:1374385}. CC -!- TISSUE SPECIFICITY: Expressed in the placenta, lung, left and CC right heart ventricles, heart atrium, leukocytes and CC differentiated HL-60 granulocytes. {ECO:0000269|PubMed:1281995, CC ECO:0000269|PubMed:1656963, ECO:0000269|PubMed:1657923}. CC -!- INDUCTION: By CSF2/GM-CSF, IL5/interleukin-5 and n-butyrate. CC {ECO:0000269|PubMed:1657923}. 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; M80436; AAA60001.1; -; mRNA. DR EMBL; D10202; BAA01050.1; -; mRNA. DR EMBL; M76674; AAA60002.1; -; mRNA. DR EMBL; M88177; AAA60214.1; -; Genomic_DNA. DR EMBL; S52624; AAB24695.2; -; mRNA. DR EMBL; L07334; AAA60108.1; -; mRNA. DR EMBL; S56396; AAB25755.1; -; Genomic_DNA. DR EMBL; AY275466; AAP32298.1; -; mRNA. DR EMBL; BT009801; AAP88803.1; -; mRNA. DR EMBL; AK290240; BAF82929.1; -; mRNA. DR EMBL; CH471059; EAX07711.1; -; Genomic_DNA. DR EMBL; BC013816; AAH13816.1; -; mRNA. DR EMBL; BC063000; AAH63000.1; -; mRNA. DR CCDS; CCDS318.1; -. DR PIR; A40191; A40191. DR RefSeq; NP_000943.1; NM_000952.4. DR RefSeq; NP_001158193.1; NM_001164721.1. DR RefSeq; NP_001158194.1; NM_001164722.2. DR RefSeq; NP_001158195.1; NM_001164723.2. DR UniGene; Hs.77542; -. DR PDB; 2B0X; Model; -; A=1-342. DR PDBsum; 2B0X; -. DR ProteinModelPortal; P25105; -. DR SMR; P25105; 6-304. DR BioGrid; 111696; 11. DR IntAct; P25105; 4. DR STRING; 9606.ENSP00000301974; -. DR BindingDB; P25105; -. DR ChEMBL; CHEMBL250; -. DR GuidetoPHARMACOLOGY; 334; -. DR TCDB; 9.A.14.13.3; the g-protein-coupled receptor (gpcr) family. DR PhosphoSite; P25105; -. DR BioMuta; PTAFR; -. DR DMDM; 129557; -. DR PaxDb; P25105; -. DR PRIDE; P25105; -. DR DNASU; 5724; -. DR Ensembl; ENST00000305392; ENSP00000301974; ENSG00000169403. DR Ensembl; ENST00000373857; ENSP00000362965; ENSG00000169403. DR Ensembl; ENST00000539896; ENSP00000442658; ENSG00000169403. DR GeneID; 5724; -. DR KEGG; hsa:5724; -. DR UCSC; uc001bpl.3; human. DR CTD; 5724; -. DR GeneCards; PTAFR; -. DR HGNC; HGNC:9582; PTAFR. DR HPA; HPA027543; -. DR MIM; 173393; gene. DR neXtProt; NX_P25105; -. DR PharmGKB; PA33933; -. DR eggNOG; ENOG410IIY4; Eukaryota. DR eggNOG; ENOG410YB0R; LUCA. DR GeneTree; ENSGT00760000118784; -. DR HOGENOM; HOG000013041; -. DR HOVERGEN; HBG101106; -. DR InParanoid; P25105; -. DR KO; K04279; -. DR OMA; FLCNLAG; -. DR OrthoDB; EOG7QVM3C; -. DR PhylomeDB; P25105; -. DR TreeFam; TF350009; -. DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors). DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR GeneWiki; Platelet-activating_factor_receptor; -. DR GenomeRNAi; 5724; -. DR NextBio; 22248; -. DR PRO; PR:P25105; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P25105; -. DR CleanEx; HS_PTAFR; -. DR Genevisible; P25105; HS. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0045028; F:G-protein coupled purinergic nucleotide receptor activity; IBA:GO_Central. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc. DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl. DR GO; GO:0001875; F:lipopolysaccharide receptor activity; IEA:Ensembl. DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB. DR GO; GO:0004992; F:platelet activating factor receptor activity; IDA:UniProtKB. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0001816; P:cytokine production; IEA:Ensembl. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0035589; P:G-protein coupled purinergic nucleotide receptor signaling pathway; IBA:GOC. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Cell membrane; Chemotaxis; Complete proteome; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; KW Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 342 Platelet-activating factor receptor. FT /FTId=PRO_0000070092. FT TOPO_DOM 1 16 Extracellular. {ECO:0000255}. FT TRANSMEM 17 38 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 39 54 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 55 74 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 75 91 Extracellular. {ECO:0000255}. FT TRANSMEM 92 113 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 114 133 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 134 155 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 156 184 Extracellular. {ECO:0000255}. FT TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 206 233 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 255 276 Extracellular. {ECO:0000255}. FT TRANSMEM 277 296 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 297 342 Cytoplasmic. {ECO:0000255}. FT CARBOHYD 169 169 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 90 173 {ECO:0000255|PROSITE-ProRule:PRU00521}. FT VARIANT 224 224 A -> D (in dbSNP:rs5938). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_011851. FT VARIANT 338 338 N -> S (in dbSNP:rs5939). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_011852. FT CONFLICT 28 28 L -> P (in Ref. 6; AAA60108). FT {ECO:0000305}. FT CONFLICT 66 66 F -> L (in Ref. 6; AAA60108). FT {ECO:0000305}. FT CONFLICT 95 95 C -> R (in Ref. 6; AAA60108). FT {ECO:0000305}. FT CONFLICT 227 228 KR -> TG (in Ref. 4; AAA60214). FT {ECO:0000305}. FT CONFLICT 227 228 KR -> TT (in Ref. 6; AAA60108). FT {ECO:0000305}. FT CONFLICT 247 247 P -> A (in Ref. 6; AAA60108). FT {ECO:0000305}. FT CONFLICT 316 316 K -> N (in Ref. 5; AAB24695). FT {ECO:0000305}. SQ 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 //