Cloning and sequence analysis of cDNA for diuretic hormone receptor from the Bombyx mori.
The insect diuretic hormone (DH) binds to their receptor in malpighian tubules, and stimulates water secretion and cAMP synthesis. Complementary DNA encoding a diuretic hormone receptor was cloned from the malpighian tubules of Bombyx mori. The cloned cDNA encodes a protein consisting of 391 amino acid residues with the seven transmembrane domains. The receptor protein is homologous with that of other insects, and is structurally related to G-protein coupled receptors such as corticotropin relating factor (CRF), secretin, and vasoactive intestinal peptide.
Ha
S D
SD
Faculty of Food Science and Biotechnology, Pukyong National University, Pusan, Korea.
Kataoka
H
H
Suzuki
A
A
Kim
B J
BJ
Kim
H J
HJ
Hwang
S H
SH
Kong
J Y
JY
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics*; D007301:Insect Hormones / Q000378:metabolism*; D019476:Insect Proteins; D008317:Malpighian Tubules / Q000378:metabolism; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D007301:Insect Hormones; D019476:Insect Proteins; D011956:Receptors, Cell Surface