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J. Biol. Chem., Vol. 266, Issue 5, 2818-2823, 02, 1991
DE Nies, TJ Hemesath, JH Kim, JR Gulcher and K Stefansson
Hexabrachion (Tenascin) is a large glycoprotein that appears in
extracellular matrices as a disulfide-linked multimer. It is synthesized in
an ordered fashion at particular sites during development, is made in large
amounts by certain tumors, and is found in restricted tissue locations in
the adult. In this report, we describe the sequence of a full length cDNA
of human hexabrachion. The encoded protein contains a total of 2203 amino
acids and is a linear array of discrete reiterated domains. At the 5' end
are encoded hydrophobic residues and 8 flanking cysteines predicted to be
responsible for assembly of hexabrachion polypeptides into a radially
arranged, six-armed complex. Following this region are 14 1/2 contiguous
31-amino acid epidermal growth factor-like repeats that have a unique
structure with respect to the known examples of this type of domain.
Immediately adjacent to these repeats lie 15 uninterrupted segments of
approximately 90 amino acids which are similar to the Type III units found
in fibronectin. At the carboxyl terminus of the protein is a 210-amino acid
domain that is similar to fibrinogen. The domain structure of this protein
is consistent with the potential for interaction with multiple ligands and
for roles in cell adhesion and/or signaling.
The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain protein containing unique epidermal growth factor repeats
Department of Neurology, University of Chicago, Illinois 60637.
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