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(Received for publication, May 17, 1996, and in revised form, July 9, 1996)
From the The mineralization process associated with the
conversion of predentin to dentin is believed to be initiated and
controlled by a set of acidic regulatory noncollagenous proteins (NCPs)
which include phosphophoryn, the major NCP in dentin. Phosphophoryn
binds tightly to collagen and is believed to initiate the formation of
apatite crystals which play a central role in the mineralization
process. During the process of analyzing the 3
Volume 271, Number 36,
Issue of September 6, 1996
pp. 21695-21698
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
and
Department of Pediatrics, the University of
Iowa, Iowa City, Iowa 52242 and the ¶ Division of Hematology, the
Department of Internal Medicine, the University of Texas Medical
School, Houston, Texas 77030
end of an
odontoblast-specific cDNA which codes for dentin sialoprotein
(Ritchie, H. H., Hou, H., Veis, A., and Butler, W. T. (1994)
J. Biol. Chem. 269, 3698-3702), we discovered a
801-base pair open reading frame. This downstream open reading frame
encodes a putative leader sequence and a very acidic mature protein
sequence having a deduced amino acid composition containing high
percentages of both Ser (43%) and Asp (31%) residues which closely
coincides with the amino acid composition of phosphophoryns from human,
bovine, rat, and rabbit (i.e. Asp (30-40%) and Ser
(38-50%)). This newly identified cDNA therefore encodes a protein
with characteristics similar to phosphophoryn. Here we present the
cDNA sequence, the deduced amino acid sequence, and the prospective
Ser residue-specific casein kinase I and II phosphorylation sites for
this putative phosphophoryn.
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