Neural cell recognition molecule F11: homology with fibronectin type III and immunoglobulin type C domains

Neuron. 1989 Apr;2(4):1351-61. doi: 10.1016/0896-6273(89)90073-1.

Abstract

We report here the complete cDNA sequence of F11 130 kd polypeptide, a chick neural cell surface-associated glycoprotein implicated in neurite fasciculation and elongation. The predicted protein sequence of 1010 amino acids includes an amino-terminal signal peptide and a carboxy-terminal hydrophobic stretch, which is compatible with the consensus motif for covalent attachment of glycosyl-phosphatidylinositol. Accordingly, F11 lacks an intracellular domain, which is consistent with evidence obtained from protease protection experiments on isolated microsomes. In addition, the molecule comprises six domains related to the immunoglobulin domain type C and four resembling fibronectin repeat type III. Both types of repeats resemble those present in neural cell adhesion molecules L1 and N-CAM. The possible identity of F11 with the chick neural glycoprotein contactin is discussed.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology
  • Antigens, Surface / genetics*
  • Antigens, Surface / immunology
  • Axons / analysis*
  • Base Sequence
  • Cell Adhesion Molecules, Neuronal / genetics
  • Chick Embryo
  • DNA / genetics
  • Fibronectins / genetics
  • Genes
  • Immunoglobulins / genetics
  • Leukocyte L1 Antigen Complex
  • Molecular Sequence Data
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Nucleic Acid

Substances

  • Antibodies, Monoclonal
  • Antigens, Surface
  • Cell Adhesion Molecules, Neuronal
  • Fibronectins
  • Immunoglobulins
  • Leukocyte L1 Antigen Complex
  • DNA