Molecular cloning and characterization of a novel rat activin receptor.
We report the isolation of a full-length rat cDNA for a new activin receptor. The deduced amino acid sequence of this receptor shows 67 percent overall identity with that of a previously identified mouse activin receptor. As predicted for the mouse activin receptor, the amino acid sequence of the rat receptor is consistent with a polypeptide containing an extracellular ligand binding domain, a hydrophobic transmembrane domain, and a serine/threonine kinase intracellular domain. In an expression assay, this new receptor was found to bind I125 radiolabeled activin.
Legerski
R
R
Department of Molecular Genetics, University of Texas M.D. Anderson Cancer Center, Houston 77030.
Zhou
X
X
Dresback
J
J
Eberspaecher
H
H
McKinney
S
S
Segarini
P
P
de Crombrugghe
B
B
D029404:Activin Receptors; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002478:Cells, Cultured; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D016133:Polymerase Chain Reaction; D011494:Protein Kinases / Q000235:genetics*; D011956:Receptors, Cell Surface / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis*; D012689:Sequence Homology, Nucleic Acid
D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; D011494:Protein Kinases; D029404:Activin Receptors