The primary structure of a cell-binding bone sialoprotein.
We have determined the amino acid sequence of rat bone sialoprotein (BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).
Oldberg
A
A
Department of Physiological Chemistry, University of Lund, Sweden.
Franzén
A
A
Heinegård
D
D
D000595:Amino Acid Sequence; D000818:Animals; D000831:Animals, Newborn; D001483:Base Sequence; D001842:Bone and Bones / Q000378:metabolism*; D004247:DNA / Q000235:genetics; D058574:Integrin-Binding Sialoprotein; D008969:Molecular Sequence Data; D011485:Protein Binding; D012333:RNA, Messenger / Q000235:genetics / Q000302:isolation & purification; D051381:Rats; D012795:Sialoglycoproteins / Q000235:genetics*
C546873:Ibsp protein, rat; D058574:Integrin-Binding Sialoprotein; D012333:RNA, Messenger; D012795:Sialoglycoproteins; D004247:DNA