cDNA sequences from the alpha subunit of the fibronectin receptor predict a transmembrane domain and a short cytoplasmic peptide.
The fibronectin receptor is a complex of two cell surface glycopeptides that mediate the binding of cells to fibronectin substrata. To study the structure of this receptor, we have isolated cDNA clones coding for the human fibronectin receptor alpha subunit from a lambda gt11 placental cDNA library. The cDNAs code for 229 amino acids from the COOH terminus of the alpha subunit. The deduced sequence has a hydrophobic region with properties characteristic of a membrane-spanning domain. From the membrane-spanning domain to the COOH terminus are 23-28 amino acids that are likely to constitute the cytoplasmic domain. These results establish the fibronectin receptor alpha subunit as an integral membrane protein.
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000032:analysis*; D004247:DNA / Q000032:analysis*; D006801:Humans; D007163:Immunosorbent Techniques; D046911:Macromolecular Substances; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic / Q000032:analysis / Q000235:genetics*
D046911:Macromolecular Substances; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic; D004247:DNA