cDNA cloning and primary structure of yellow tail (Seriola quinqueradiata) pregrowth hormone

Full-length cDNA of yellow tail (Seriola quinqueradiata) growth hormone (GH) was cloned from the pituitary gland and nucleotide sequence was analyzed. The cDNA clone contained one open reading frame to encode a preprotein consisting of 204 amino acids. The deduced amino acid sequence shows two possible sites for signal peptide cleavage, suggesting that the mature forms of yellow tail growth hormone consist of 185 or 187 amino acids. Yellow tail growth hormone exhibits a typical structural feature as growth hormone, including four cysteine residues to form two disulfide bonds and other identical amino acids with other vertebrate GHs. Amino acid sequence of yellow tail growth hormone shows homology of approximately 66, 42, 37, and 34% with those of salmon, eel, bovine, and human GHs, respectively. Nucleotide sequence of the coding region of yellow tail growth hormone cDNA shows approximately 58 and 40% homology with those of salmon and human growth hormone cDNAs, respectively.