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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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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skos:exactMatch | |
uniprot:name |
J. Mol. Evol.
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uniprot:author |
Arterburn M.,
Boyle B.,
Bright J.M.,
Emtage P.C.,
Funk W.D.,
Hu T.,
Tang Y.T.
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uniprot:date |
2005
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uniprot:pages |
372-380
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uniprot:title |
PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif.
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uniprot:volume |
61
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dc-term:identifier |
doi:10.1007/s00239-004-0375-2
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