The globular domains of type VI collagen are related to the collagen-binding domains of cartilage matrix protein and von Willebrand factor.
Type VI collagen is a transformation-sensitive glycoprotein of the extracellular matrix of fibroblasts. We have isolated and sequenced several overlapping cDNA clones (4153 bp) which encode the entire alpha 2 subunit of chicken type VI collagen. The deduced amino acid sequence predicts that the alpha 2(VI) polypeptide consists of 1015 amino acid residues that are arranged in four domains: a hydrophobic signal peptide of 20 residues, an amino-terminal globular domain of 228 residues, a collagenous segment of 335 residues and a carboxy-terminal globular domain of 432 residues. The collagenous domain contains seven Arg-Gly-Asp tripeptide units, some of which are likely to be used as cell-binding sites. The globular domains contain three homologous repeats with an average length of 180 amino acid residues. These repeats show a striking similarity to the collagen-binding motifs found in von Willebrand factor and cartilage matrix protein. We therefore speculate that the globular domains of the alpha 2(VI) polypeptide may interact with collagenous structures.
Koller
E
E
Laboratorium für Biochemie I, ETH Zentrum, Zürich, Switzerland.
Winterhalter
K H
KH
Trueb
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002645:Chickens / Q000235:genetics; D003094:Collagen / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D004247:DNA / Q000235:genetics; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins / Q000378:metabolism; D064235:Matrilin Proteins; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D014841:von Willebrand Factor / Q000378:metabolism
D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D064235:Matrilin Proteins; D014841:von Willebrand Factor; D003094:Collagen; D004247:DNA