| First Author | Inglis JD | Year | 1991 |
| Journal | EMBO J | Volume | 10 |
| Issue | 2 | Pages | 255-61 |
| PubMed ID | 1991447 | Mgi Jnum | J:25107 |
| Mgi Id | MGI:72820 | Doi | 10.1002/j.1460-2075.1991.tb07945.x |
| Citation | Inglis JD, et al. (1991) The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J 10(2):255-61 |
| abstractText | We have isolated 10 closely linked members of a proteinase inhibitor multigene family from the inbred mouse strain 129. These sequences, termed the Serine Proteinase Inhibitor 2 (Spi-2) genes, appear to have been derived from a common ancestor represented in man by the single copy alpha 1-antichymotrypsin gene. The genes are clustered on two cloned genomic DNA segments spanning 220 kb, and have at least partially retained the intragenic structure of the ancestral Spi-2 gene. Sequence analysis from the final coding exon indicates that most of the mouse genes may be competent to encode functional proteins, some with a predictable inhibitory spectrum, and several representing novel inhibitor types. An oligonucleotide probe designed to one reactive centre sequence enabled the isolation of the cognate expressed transcript from a liver cDNA library. However, whether expressed or not, the reactive centre regions of all the sequences have diverged at a rapid rate relative to structurally defined flanking sequences. The divergence is also appreciably greater than that occurring in an adjacent non-coding sequence. This phenomenon has established novel potential inhibitory specificities, while maintaining a functional inhibitor structure. |
