| First Author | Shamir A | Year | 2001 |
| Journal | Gene | Volume | 271 |
| Issue | 2 | Pages | 285-91 |
| PubMed ID | 11418250 | Mgi Jnum | J:70791 |
| Mgi Id | MGI:2148328 | Doi | 10.1016/s0378-1119(01)00502-9 |
| Citation | Shamir A, et al. (2001) Characterization of two genes, Impa1 and Impa2 encoding mouse myo-inositol monophosphatases. Gene 271(2):285-91 |
| abstractText | The enzyme myo-inositol monophosphatase (Impa) catalyzes the synthesis of free myo-inositol from various myo-inositol monophosphates in the phosphatidylinositol signaling system. Impa is a lithium-blockable enzyme that has been hypothesized to be the biological target for lithium-salts used as mood-stabilizing drugs in the treatment of manic-depressive (bipolar) illness. As an initial step to explore the functional consequences of reduced or absent Impa activity in an animal model we here report the isolation of two Impa-encoding mouse genes, Impa1 and Impa2. Impa1 spans approximately 17.5 kb and contains nine exons of 46--1354 bp encoding a protein of 277 amino acids. Impa2 spans at least 19.5 kb and contains eight exons of 46--444 bp size encoding a protein of 290 amino acids. The genomic structure including the positions of the exon-intron splice sites seems to be conserved among myo-inositol monophosphatase genes in mammalian species. One or more Impa-like genes do also exist in evolutionary more distant species like invertebrates, plants and bacteria. The proteins encoded by the non-vertebrate genes seem to be equally related to Impa1 and Impa2. We therefore suggest that the Impa1 and Impa2 genes duplicated from a common ancestral gene after the evolutionary divergence of vertebrates. |
