Cloning and sequence analysis of membrane-bound alkaline phosphatase cDNA of the silkworm, Bombyx mori.
The nucleotide sequence (1974 bp) of cDNA coding for membrane-bound alkaline phosphatases (m-ALP) of Bombyx mori was isolated. The cDNA clone contained an open reading frame encoding a polypeptide (547 amino acids), which contains a hydrophobic signal peptide of 36 amino acids and the mature protein of 511 amino acids (Mr = 56,163). We found a highly hydrophobic domain presumed to be a membrane anchoring region at the C-terminus. Comparing analysis between Bombyx m-ALP and mammalian and Escherichia coli ALPs suggested an evolutionary relationship of sharing a common ancestral gene.
Itoh
M
M
Department of Applied Biology, Kyoto Institute of Technology, Japan.
Takeda
S
S
Yamamoto
H
H
Izumi
S
S
Tomino
S
S
Eguchi
M
M
D000469:Alkaline Phosphatase / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D012831:Bombyx / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D021382:Protein Sorting Signals / Q000235:genetics; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D008565:Membrane Proteins; D021382:Protein Sorting Signals; D000469:Alkaline Phosphatase