Open AccessSEQUENCES OF INTEREST: Molecular Cloning of the Complementary Deoxyribonucleic Acid for Human Thyroid Peroxidase
Author(s) -
Ronald P. Magnusson,
Gregorio D. Chazenbalk,
Jane Gestautas,
Pui Seto,
S. Filetti,
Leslie J. DeGroot,
Basil Rapoport
Publication year - 1987
Publication title -
molecular endocrinology
Language(s) - English
Resource type - Journals
eISSN - 1944-9917
pISSN - 0888-8809
DOI - 10.1210/mend-1-11-856
Subject(s) - complementary dna , biology , peptide sequence , amino acid , signal peptide , cdna library , microbiology and biotechnology , biochemistry , transmembrane domain , nucleic acid sequence , thyroid peroxidase , gene , hormone
Five overlapping cDNA clones representing the entire mRNA for human thyroid peroxidase (TPO) have been isolated from a human Graves' thyroid cDNA library. The cDNA sequence has been determined. Human TPO cDNA contains 3060 bases from the start of transcription to the beginning of the poly (A) tail at the 3'-end. The derived amino acid sequence of human TPO consists of 933 amino acids with a mol wt of 102,937. The derived amino acid sequence contains five potential glycosylation sites (Asn-X-Ser/Thr), a probable transmembrane signal peptide sequence at the amino terminus, and a hydrophobic putative membrane-spanning region beginning 85 amino acid residues from the carboxyl terminal end. Comparison of the human TPO amino acid sequence to that of pig TPO shows strong homology extending from the amino terminus to within 44 amino acid residues of the carboxyl-terminus.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom