Molecular cloning of avian matrix Gla protein.
Matrix Gla protein plays an essential role in preventing the calcification of blood vessel walls, cartilage and other tissues. We report here the primary structure of chicken matrix Gla protein as deduced from the cDNA sequence. The avian protein exhibited the characteristic motifs previously identified in the mammalian proteins, but its amino acid sequence shared only 51-56% identity with the latter proteins. Moreover, a region proposed to function as binding site for gamma-carboxylase in the mammalian proteins was poorly conserved in the chicken protein. Our sequence data should be helpful in the design of mutational analyses which are intended to characterize functional interactions of matrix Gla proteins with other proteins.
Wiedemann
M
M
MEM Institute, Division of Biology, University of Bern, Switzerland.
Trueb
B
B
Belluoccio
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D002642:Chick Embryo; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D016326:Extracellular Matrix Proteins; D018507:Gene Expression Regulation, Developmental; D008969:Molecular Sequence Data; D009928:Organ Specificity; D012333:RNA, Messenger / Q000032:analysis; D017386:Sequence Homology, Amino Acid; D000097568:Matrix Gla Protein
D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D016326:Extracellular Matrix Proteins; D012333:RNA, Messenger; D000097568:Matrix Gla Protein