| First Author | Julkunen M | Year | 1988 |
| Journal | Proc Natl Acad Sci U S A | Volume | 85 |
| Issue | 23 | Pages | 8845-9 |
| PubMed ID | 3194393 | Mgi Jnum | J:20467 |
| Mgi Id | MGI:68559 | Doi | 10.1073/pnas.85.23.8845 |
| Citation | Julkunen M, et al. (1988) Complete amino acid sequence of human placental protein 14: a progesterone-regulated uterine protein homologous to beta-lactoglobulins. Proc Natl Acad Sci U S A 85(23):8845-9 |
| abstractText | Placental protein 14 (PP14), also known as progestagen-dependent endometrial protein and pregnancy-associated endometrial alpha 2-globulin, is synthesized by the human secretory endometrium and decidua. We have isolated from a human decidual cDNA library clones corresponding to PP14 and deduced its entire amino acid sequence. PP14 contains 180 amino acids, 18 of which correspond to a putative signal peptide. The predicted molecular weight of the pre-PP14 is 20,555 and that of the mature protein is 18,787. PP14 is encoded by a 1-kilobase-pair mRNA that is expressed in human secretory endometrium and decidua but not in postmenopausal endometrium, placenta, liver, kidney, and adrenals. The 162-residue-long sequence of PP14 is highly homologous to beta-lactoglobulins, with a 53.4% identity with the amino acid sequence of horse beta-lactoglobulin I. The four cysteinyl residues (positions 66, 106, 119, and 160) responsible for intramolecular disulfide bridges in beta-lactoglobulins are all conserved in PP14. Southern blot analysis of human DNA suggested that PP14 gene sequences encompass some 20 kilobase pairs of the human genomic DNA. |
