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Nucleic Acids Research, 1984, Vol. 12, No. 22 8685-8697
© 1984

MOLECULAR BIOLOGY

Comparison of the whey acidic protein genra of the rat and mouse

S.M. Campbell1, J.M. Rosen1, L.G. Hennighausen2,+, U. Strech-Jurk2,* and A.E. Sippel2

1Department of Cell Biology, Baylor College of Medicine One Baylor Plaza, Houston, TX 77030, USA 2Institut für Genetik, Universität zu Köln 5000 Köln 41, FRG

Received August 6, 1984. Revised October 22, 1984. Accepted October 22, 1984.

Whey acidic protein (WAP), a hormonally-regulated 14,000 dalton cysteine-rich protein, is the principal whey protein found in rodent milk. Genomic clones encompassing both the 2.8 Kb rat and 3.3 Kb mouse WAP genes have been characterized. The genes consist of four exons and three introns. The middle two exons encode the two cysteine-rich regions which probably form separate protein domains. Homology in the 5' flanking DNA of the mouse and rat extends at least 325 bp upstream of the putative CAP site, including a precisely conserved stretch of 50 bp around the unusual TATA and CAAT sites. The homology previously observed between the 3' noncoding sequences of the rat and mouse mRNAa extends at least 20 bp into the 3' flanking region. Several potential glucocorticoid receptor binding sites have been found in the 5' flanking region of the WAP gene. The conservation of the 5' flanking region of the WAP genes may be related to regulation of expression of WAP by peptide and/or steroid hormones.

+Present address: Department of Genetics, Harvard Medical School, 45 Shattuck Street, Boston, MA 02115, USA

*Present address: Zentrum für Molecular Biologic Heidelberg, Universität Heidelberg, 69 Heidelberg, FRG


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