Abstract
An emerging series of papers has identified new receptor proteins that predict seven-transmembrane pass topologies. We have consolidated this family to 11 human genes and have named the family PAQR, after two of the initially described ligands (progestin and adipoQ receptors). This protein family has ancient evolutionary roots, with identified homologs found in eubacteria. To date, published data indicate that the prokaryotic members of this family appear to encode hemolysin-type proteins, while in eukaryotes, PAQR proteins encode functional receptors with a broad range of apparent ligand specificities. We provide the complete human and mouse complement of this family, suggest a conserved structure/topology with invariant intracellular amino acid residues, and have measured mRNA expression levels for these genes across a range of human tissues.
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Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402
Baida GE, Kuzmin NP (1995) Cloning and primary structure of a new hemolysin gene from Bacillus cereus. Biochim Biophys Acta 1264:151–154
Baida GE, Kuzmin NP (1996) Mechanism of action of hemolysin III from Bacillus cereus. Biochim Biophys Acta 1284:122–124
Durbin R (1998) Biological sequence analysis probabilistic models of proteins and nucleic acids. Cambridge University Press, Cambridge, UK
Ewing B, Green P (1998) Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res 8:186–194
Ewing B, Hillier L, Wendl MC, Green P (1998) Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res 8:175–185
Florea L, Hartzell G, Zhang Z, Rubin GM, Miller W (1998) A computer program for aligning a cDNA sequence with a genomic DNA sequence. Genome Res 8:967–974
Ganfomina MD, Sanchez D (1999) Generation of evolutionary novelty by functional shift. Bioessays 21:432–439
Gether U (2000) Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 21(1):90–113, 2000
Huang X (1996) An improved sequence assembly program. Genomics 33:21–31
Hughey R, Krogh A (1996) Hidden Markov models for sequence analysis: extension and analysis of the basic method. Comput Appl Biosci 12:95–107
Karpichev IV, Cornivelli L, Small GM (2002) Multiple regulatory roles of a novel Saccharomyces cerevisiae protein, encoded by YOL002C, in lipid and phosphate metabolism. J Biol Chem 277:19609–19617
Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673–4680
Tillinghast J, Sinku A, Tang Y (2000) Clustering and assembly of a large number of EST and cDNA sequences using Hyseq’s proprietary software. In: M Satoru R Shamir T Takagi (eds). Currents in computational molecular biology. Universal Academy Press, Tokyo, 74–75
Vassilatis DK, Hohmann JG, Zeng H, Li F, Ranchalis JE, Mortrud MT, Brown A, Rodriguez SS, Weller JR, Wright AC, Bergmann JE, Gaitanaris GA (2003) The G protein-coupled receptor repertoires of human and mouse. Proc Natl Acad Sci USA 100:4903–4908
Yamauchi T, Kamon J, Minokoshi Y, Ito Y, Waki H, Uchida S, Yamashita S, Noda M, Kita S, Ueki K, Eto K, Akanuma Y, Froguel P, Foufelle F, Ferre P, Carling D, Kimura S, Nagai R, Kahn BB, Kadowaki T (2002) Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat Med 8:1288–1295
Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Kara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T (2003) Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423:762–769
Zhu Y, Rice CD, Pang Y, Pace M, Thomas P (2003) Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes. Proc Natl Acad Sci USA 100:2231–2236
Zhu Y, Bond J, Thomas P (2003) Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor. Proc Natl Acad Sci USA 100:2237–2242
Acknowledgments
The authors thank S. Palencia for advocating the study of the adipoR family, S. Andarmani and Matthew Mueller for scientific discussions and bioinformatics assistance, and Lynne Nguyen for technical assistance.
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[Reviewing Editor: Martin Kreitman]
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Tang, Y.T., Hu, T., Arterburn, M. et al. PAQR Proteins: A Novel Membrane Receptor Family Defined by an Ancient7-Transmembrane Pass Motif. J Mol Evol 61, 372–380 (2005). https://doi.org/10.1007/s00239-004-0375-2
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DOI: https://doi.org/10.1007/s00239-004-0375-2