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Primary Structure and Tissue Distribution of Two Novel Proline-Rich γ -carboxyglutamic Acid Proteins
John D. Kulman, Jeff E. Harris, Betty A. Haldeman and Earl W. Davie
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 17 (Aug. 19, 1997), pp. 9058-9062
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/42556
Page Count: 5
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Two human cDNAs that encode novel vitamin K-dependent proteins have been cloned and sequenced. The predicted amino acid sequences suggest that both are single-pass transmembrane proteins with amino-terminal γ -carboxyglutamic acid-containing domains preceded by the typical propeptide sequences required for posttranslational γ -carboxylation of glutamic acid residues. The polypeptides, with deduced molecular masses of 23 and 17 kDa, are proline-rich within their putative cytoplasmic domains and contain several copies of the sequences PPXY and PXXP, motifs found in a variety of signaling and cytoskeletal proteins. Accordingly, these two proteins have been called proline-rich Gla proteins (PRGP1 and PRGP2). Unlike the γ -carboxyglutamic acid domain-containing proteins of the blood coagulation cascade, the two PRGPs are expressed in a variety of extrahepatic tissues, with PRGP1 and PRGP2 most abundantly expressed in the spinal cord and thyroid, respectively, among those tissues tested. Thus, these observations suggest a novel physiological role for these two new members of the vitamin K-dependent family of proteins.
Proceedings of the National Academy of Sciences of the United States of America © 1997 National Academy of Sciences