title: Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29.
abstract: Membrane-bound immunoglobulins (Ig) on the surface of murine B cells are noncovalently associated with a heterodimeric protein complex of MB-1 and B29 (also called Ig-alpha and Ig-beta). The Ig-associated proteins are predicted to regulate the assembly and transport of the Ig complex to the cell surface and to couple membrane-bound Ig to intracellular signal transduction pathways. We have isolated and sequenced a full-length cDNA clone encoding the human homologue of the B29 protein. The predicted amino acid sequence was compared to its murine counterpart, to MB-1 and to the human T cell receptor (TcR)-associated CD3 proteins. The alignment of the human B29 protein with its murine counterpart revealed 90% homology in the C-terminal portion comprising the cytoplasmic tails, the transmembrane regions and the adjacent 26 amino acids of the extracellular regions. Only 59% homology was found in the rest of the Ig-like extracellular domains. The high degree of conservation observed for the C-terminal amino acids suggested that these domains of the proteins play important functional roles for the Ig complex. Indicative of this was the conservation of the antigen receptor tail motif D-(X)7-E/D-(X)2-Y-(X)2-L-(X)7-Y-(X)2-L/I which is thought to be a component of signal transduction pathways. This motif is also found in the human and murine MB-1 proteins as well as in the TcR-associated CD3 molecules. Further regions of homology between B29, MB-1 and the CD3 proteins included extracellular residues which were predicted to maintain the Ig-like structure, and hydrophilic residues within the transmembrane regions which may be utilized during the intracellular assembly and transport of the oligomeric Ig/MB-1/B29 or TcR/CD3 complexes. Thus the similarities found between B29, MB-1 and the CD3 proteins suggest conserved functions for both the Ig- and TcR-associated proteins.
authors.affiliation: Division of Immunology, Beth Israel Hospital, Boston, MA 02215.
authors.forename: B
authors.initials: B
authors.lastname: Müller
authors.forename: L
authors.initials: L
authors.lastname: Cooper
authors.forename: C
authors.initials: C
authors.lastname: Terhorst
mesh_terms: D000595:Amino Acid Sequence; D015703:Antigens, CD; D000945:Antigens, Differentiation, T-Lymphocyte / Q000235:genetics; D001402:B-Lymphocytes / Q000378:metabolism; D001483:Base Sequence; D017252:CD3 Complex; D051925:CD79 Antigens; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004247:DNA / Q000302:isolation & purification; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics*; D011947:Receptors, Antigen, B-Cell; D011948:Receptors, Antigen, T-Cell / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
chemical_list: D015703:Antigens, CD; D000945:Antigens, Differentiation, T-Lymphocyte; D017252:CD3 Complex; D051925:CD79 Antigens; C497881:CD79A protein, human; C497883:CD79B protein, human; D008562:Membrane Glycoproteins; D010750:Phosphoproteins; D011947:Receptors, Antigen, B-Cell; D011948:Receptors, Antigen, T-Cell; D004247:DNA