P25105 (PTAFR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet-activating factor receptor
Short name=PAF-R
Short name=PAFr

Gene names

Name:	PTAFR
Synonyms:	PAFR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.3 Ref.5
Subunit structure	Interacts with ARRB1. Ref.13
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.3.
Tissue specificity	Expressed in the placenta, lung, left and right heart ventricles, heart atrium, leukocytes and differentiated HL-60 granulocytes. Ref.1 Ref.2 Ref.5
Induction	By CSF2/GM-CSF, IL5/interleukin-5 and n-butyrate. Ref.2
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Traceable author statement PubMed 10601267. Source: ProtInc cytokine production Inferred from electronic annotation. Source: Compara inflammatory response Traceable author statement PubMed 8978777. Source: ProtInc inositol trisphosphate biosynthetic process Inferred from electronic annotation. Source: Compara interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	integral to plasma membrane Traceable author statement PubMed 8168510. Source: ProtInc nucleus Inferred from direct assay. Source: HPA
Molecular_function	lipopolysaccharide binding Inferred from electronic annotation. Source: Compara lipopolysaccharide receptor activity Inferred from electronic annotation. Source: Compara phospholipid binding Inferred from direct assay Ref.1Ref.2. Source: UniProtKB platelet activating factor receptor activity Inferred from direct assay Ref.5Ref.1Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 342	342	Platelet-activating factor receptor		PRO_0000070092
Regions
	Topological domain	1 – 16	16	Extracellular Potential
	Transmembrane	17 – 38	22	Helical; Name=1; Potential
	Topological domain	39 – 54	16	Cytoplasmic Potential
	Transmembrane	55 – 74	20	Helical; Name=2; Potential
	Topological domain	75 – 91	17	Extracellular Potential
	Transmembrane	92 – 113	22	Helical; Name=3; Potential
	Topological domain	114 – 133	20	Cytoplasmic Potential
	Transmembrane	134 – 155	22	Helical; Name=4; Potential
	Topological domain	156 – 184	29	Extracellular Potential
	Transmembrane	185 – 205	21	Helical; Name=5; Potential
	Topological domain	206 – 233	28	Cytoplasmic Potential
	Transmembrane	234 – 254	21	Helical; Name=6; Potential
	Topological domain	255 – 276	22	Extracellular Potential
	Transmembrane	277 – 296	20	Helical; Name=7; Potential
	Topological domain	297 – 342	46	Cytoplasmic Potential
Amino acid modifications
	Modified residue	310	1	Phosphoserine By similarity
	Glycosylation	169	1	N-linked (GlcNAc...) Potential
	Disulfide bond	90 ↔ 173		By similarity
Natural variations
	Natural variant	224	1	A → D. Ref.14 Corresponds to variant rs5938 [ dbSNP | Ensembl ].		VAR_011851
	Natural variant	338	1	N → S. Ref.14 Corresponds to variant rs5939 [ dbSNP | Ensembl ].		VAR_011852
Experimental info
	Sequence conflict	28	1	L → P in AAA60108. Ref.6
	Sequence conflict	66	1	F → L in AAA60108. Ref.6
	Sequence conflict	95	1	C → R in AAA60108. Ref.6
	Sequence conflict	227 – 228	2	KR → TG in AAA60214. Ref.4
	Sequence conflict	227 – 228	2	KR → TT in AAA60108. Ref.6
	Sequence conflict	247	1	P → A in AAA60108. Ref.6
	Sequence conflict	316	1	K → N in AAB24695. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P25105 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 890073C9EBA79228	FASTA	342	39,203
	10 20 30 40 50 60 MEPHDSSHMD SEFRYTLFPI VYSIIFVLGV IANGYVLWVF ARLYPCKKFN EIKIFMVNLT 70 80 90 100 110 120 MADMLFLITL PLWIVYYQNQ GNWILPKFLC NVAGCLFFIN TYCSVAFLGV ITYNRFQAVT 130 140 150 160 170 180 RPIKTAQANT RKRGISLSLV IWVAIVGAAS YFLILDSTNT VPDSAGSGNV TRCFEHYEKG 190 200 210 220 230 240 SVPVLIIHIF IVFSFFLVFL IILFCNLVII RTLLMQPVQQ QRNAEVKRRA LWMVCTVLAV 250 260 270 280 290 300 FIICFVPHHV VQLPWTLAEL GFQDSKFHQA INDAHQVTLC LLSTNCVLDP VIYCFLTKKF 310 320 330 340 RKHLTEKFYS MRSSRKCSRA TTDTVTEVVV PFNQIPGNSL KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a human cDNA that encodes a functional receptor for platelet activating factor." Ye R.D., Prossnitz E.R., Zou A., Cochrane C.G. Biochem. Biophys. Res. Commun. 180:105-111(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Granulocyte.
[2]	"Molecular cloning and expression of platelet-activating factor receptor from human leukocytes." Nakamura M., Honda Z., Izumi T., Sakanaka C., Mutoh H., Minami M., Bito H., Seyama Y., Matsumoto T., Noma M., Shimizu T. J. Biol. Chem. 266:20400-20405(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Tissue: Leukocyte.
[3]	"The human leukocyte platelet-activating factor receptor. cDNA cloning, cell surface expression, and construction of a novel epitope-bearing analog." Kunz D., Gerard N.P., Gerard C. J. Biol. Chem. 267:9101-9106(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Leukocyte.
[4]	"The human platelet-activating factor receptor gene (PTAFR) contains no introns and maps to chromosome 1." Seyfried C.E., Schweickart V.L., Godiska R., Gray P.W. Genomics 13:832-834(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Fetal liver.
[5]	"Molecular cloning and characterization of the platelet-activating factor receptor gene expressed in the human heart." Sugimoto T., Tsuchimochi H., McGregor C.G.A., Mutoh H., Shimizu T., Kurachi Y. Biochem. Biophys. Res. Commun. 189:617-624(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Heart ventricle.
[6]	"Nucleotide sequence of platelet-activating-factor receptor derived from HeLa cell genomic DNA and Rhesus monkey genomic DNA." Behal R.H., Debuysere M.S., Olson M.S. Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix carcinoma.
[7]	"Cloning of a human platelet-activating factor receptor gene: evidence for an intron in the 5'-untranslated region." Chase P.B., Halonen M., Regan J.W. Am. J. Respir. Cell Mol. Biol. 8:240-244(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Warren C.N., Aronstam R.S., Sharma S.V. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[11]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lymph.
[13]	"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." McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C. J. Immunol. 176:7039-7050(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB1.
[14]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." 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. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-224 AND SER-338.
[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)
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80436 mRNA. Translation: AAA60001.1.
D10202 mRNA. Translation: BAA01050.1.
M76674 mRNA. Translation: AAA60002.1.
M88177 Genomic DNA. Translation: AAA60214.1.
S52624 mRNA. Translation: AAB24695.2.
L07334 mRNA. Translation: AAA60108.1.
S56396 Genomic DNA. Translation: AAB25755.1.
AY275466 mRNA. Translation: AAP32298.1.
BT009801 mRNA. Translation: AAP88803.1.
AK290240 mRNA. Translation: BAF82929.1.
CH471059 Genomic DNA. Translation: EAX07711.1.
BC013816 mRNA. Translation: AAH13816.1.
BC063000 mRNA. Translation: AAH63000.1.

IPI

IPI00012730.

PIR

A40191.

RefSeq

NP_000943.1. NM_000952.4.
NP_001158193.1. NM_001164721.1.
NP_001158194.1. NM_001164722.2.
NP_001158195.1. NM_001164723.2.

UniGene

Hs.77542.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B0X	model	-	A	1-342	[»]

ProteinModelPortal

P25105.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25105. 4 interactions.

STRING

9606.ENSP00000301974.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P25105.

Polymorphism databases

DMDM

129557.

Proteomic databases

PRIDE

P25105.

Protocols and materials databases

DNASU

5724.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305392; ENSP00000301974; ENSG00000169403.
ENST00000373857; ENSP00000362965; ENSG00000169403.
ENST00000539896; ENSP00000442658; ENSG00000169403.

GeneID

5724.

KEGG

hsa:5724.

UCSC

uc001bpl.3. human.

Organism-specific databases

CTD

5724.

GeneCards

GC01M028473.

HGNC

HGNC:9582. PTAFR.

HPA

HPA027543.

MIM

173393. gene.

neXtProt

NX_P25105.

PharmGKB

PA33933.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG149133.

HOGENOM

HOG000013041.

HOVERGEN

HBG101106.

InParanoid

P25105.

KO

K04279.

OMA

YVLWVFA.

OrthoDB

EOG4GHZPH.

PhylomeDB

P25105.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

Bgee

P25105.

CleanEx

HS_PTAFR.

Genevestigator

P25105.

GermOnline

ENSG00000169403. Homo sapiens.

Family and domain databases

InterPro

IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002282. PAF_rcpt.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR01153. PAFRECEPTOR.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P25105.

ChEMBL

CHEMBL250.

GenomeRNAi

5724.

NextBio

22248.

SOURCE

Search...

Entry information

Entry name

PTAFR_HUMAN

Accession

Primary (citable) accession number: P25105
Secondary accession number(s): A3KMC8, A8K2H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.