title: EMR1, an unusual member in the family of hormone receptors with seven transmembrane segments.
abstract: Proteins with seven transmembrane segments (7TM) define a superfamily of receptors (7TM receptors) sharing the same topology: an extracellular N-terminus, three extramembranous loops on either side of the plasma membrane, and a cytoplasmic C-terminal tail. Upon ligand binding, cytoplasmic portions of the activated receptor interact with heterotrimeric G-coupled proteins to induce various second messengers. A small group, recently recognized on the basis of homologous primary amino acid sequences, comprises receptors to hormones of the secretin/vasoactive intestinal peptide/glucagon family, parathyroid hormone and parathyroid hormone-related peptides, growth hormone-releasing factor, corticotropin-releasing factor, and calcitonin. A cDNA, extracted from a neuroectodermal cDNA library, was predicted to encode a new 886-amino-acid protein with three distinct domains. The C-terminal third contains the seven hydrophobic segments and characteristic residues that allow the protein to be readily aligned with the various hormone receptors in the family. Six egf-like modules, at the N-terminus of the predicted mature protein, are separated from the transmembrane segments by a serine/threonine-rich domain, a feature reminiscent of mucin-like, single-span, integral membrane glycoproteins with adhesive properties. Because of its unique characteristics, this putative egf module-containing, mucin-like hormone receptor has been named EMR1. Southern analysis of a panel of somatic cell hybrids and fluorescence in situ hybridization have assigned the EMR1 gene to human chromosome 19p13.3.
authors.affiliation: Laboratoire de Biologie des Tumeurs Humaines, CNRS URA 1156, Institut Gustave Roussy, Villejuif, France.
authors.forename: V
authors.initials: V
authors.lastname: Baud
authors.forename: S L
authors.initials: SL
authors.lastname: Chissoe
authors.forename: E
authors.initials: E
authors.lastname: Viegas-Péquignot
authors.forename: S
authors.initials: S
authors.lastname: Diriong
authors.forename: V C
authors.initials: VC
authors.lastname: N'Guyen
authors.forename: B A
authors.initials: BA
authors.lastname: Roe
authors.forename: M
authors.initials: M
authors.lastname: Lipinski
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002135:Calcium-Binding Proteins; D002888:Chromosomes, Human, Pair 19; D016384:Consensus Sequence; D006224:Cricetinae; D018076:DNA, Complementary / Q000235:genetics; D004815:Epidermal Growth Factor / Q000737:chemistry; D005796:Genes; D006801:Humans; D006822:Hybrid Cells; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D009077:Mucins / Q000737:chemistry / Q000235:genetics*; D005810:Multigene Family; D011487:Protein Conformation; D012332:RNA, Heterogeneous Nuclear / Q000235:genetics; D011956:Receptors, Cell Surface / Q000737:chemistry; D043562:Receptors, G-Protein-Coupled; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: C094471:ADGRE1 protein, human; D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D008562:Membrane Glycoproteins; D009077:Mucins; D012332:RNA, Heterogeneous Nuclear; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; D004815:Epidermal Growth Factor