A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S.
Affinity purified antibodies to human sex hormone binding globulin (SHBG) were used in screening a human liver cDNA library, constructed in the expression vector lambda gt11. One clone, identified as producing recombinant SHBG, carried a cDNA insert of 1.1 kb. The nucleotide sequence of the insert had an open reading frame coding for 356 amino acid residues. The coding sequence was followed by a short 3'-region of 19 non-translated nucleotides and a poly(A) tail. Confirmation that the cDNA clone represented human SHBG was obtained by the finding of a complete agreement in amino acid sequence with several peptide fragments generated from purified SHBG by proteolytic cleavage. The primary structure of SHBG shows a considerable homology to that of protein S, a vitamin K-dependent protein with functions in the coagulation system.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D004247:DNA / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D017293:Protein S; D012689:Sequence Homology, Nucleic Acid; D012738:Sex Hormone-Binding Globulin / Q000032:analysis / Q000235:genetics*
D006023:Glycoproteins; D010446:Peptide Fragments; D017293:Protein S; D012738:Sex Hormone-Binding Globulin; D004247:DNA