Structure of mouse major urinary protein genes: different splicing configurations in the 3′‐non‐coding region

• Published in: The EMBO journal Vol. 3; no. 5; pp. 1045 - 1052
• Main Authors: Clark, A.J., Clissold, P.M., Al Shawi, R., Beattie, P., Bishop, J.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 01.05.1984
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA Restriction Enzymes; Endonucleases; Fundamental and applied biological sciences. Psychology; Genes; Genes. Genome; Mice; Molecular and cellular biology; Molecular genetics; Molecular Weight; Plasmids; Proteins - genetics; RNA, Messenger - genetics; Single-Strand Specific DNA and RNA Endonucleases; Proteins; Urine; Vertebrata; Mammalia; Messenger RNA; Mouse; Splicing; Animal; Biological evolution; Rodentia; Gene organization
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1984.tb01925.x

The multigene family which codes for the mouse major urinary proteins (MUPs) consists of approximately 35 genes. Most of these are members of two different groups, Group 1 and Group 2, which can be distinguished by nucleic acid hybridisation. Here we describe the structure of a Group 1 gene and show that two size classes of MUP mRNA which are found in mouse liver result from different splicing events in the 3′‐non‐coding region and contain different polyadenylation sites. Short mRNA is approximately 750 nucleotides long, contains six exons, and is the main product of the Group 2 genes. Long mRNA is approximately 880 nucleotides long, contains seven exons and is the main product of the Group 1 genes. Five exons and part of the sixth are common to long and short mRNA and contain the coding region. This codes for an acidic protein of 180 amino acids containing an 18 residue signal peptide. A comparison of the mouse sequence with a homologous rat alpha 2u‐globulin sequence shows that the rate of evolutionary divergence of the two proteins has been high. Silent sites have diverged four times more rapidly than replacement sites, showing that there has been selection against change in the protein sequence.