Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products.
We have cloned and determined the entire nucleotide sequence of cDNAs corresponding to the putative alpha subunits of the human and rat mast cell high-affinity IgE receptors. Both human and rat cDNAs encode an NH2-terminal signal peptide, two immunoglobulin-like extracellular domains (encoded by discrete exons), a hydrophobic transmembrane region, and a positively charged cytoplasmic tail. The human and rat alpha subunits share an overall homology with one another and the immunoglobulin gene family, suggesting that they arose from a common ancestral gene and continue to share structural homology with their ligands. In addition, the rat gene is transcribed into at least three distinct forms, each of which yields a somewhat different coding sequence.
Shimizu
A
A
Department of Genetics, Harvard Medical School, Howard Hughes Medical Institute, Boston, MA 02115.
Tepler
I
I
Benfey
P N
PN
Berenstein
E H
EH
Siraganian
R P
RP
Leder
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D006801:Humans; D008407:Mast Cells / Q000378:metabolism*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D051381:Rats; D011961:Receptors, Fc / Q000378:metabolism*; D017455:Receptors, IgE
D011961:Receptors, Fc; D017455:Receptors, IgE; D004247:DNA