Presenilin sel-12
| Presenilin sel-12 ( Caenorhabditis elegans ) | ||
|---|---|---|
| Mass / length primary structure | 444 amino acids | |
| Secondary to quaternary structure | Homodimer, multipass membrane protein | |
| Identifier | ||
| Gene name (s) | sel-12 (WormBase) | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 3.4.23.- , Aspartylpeptidase | |
| MEROPS | A22.009 | |
Presenilin sel-12 is a protein from the roundworm Caenorhabditis elegans . It is an enzyme that breaks down proteins called aspartyl protease . sel-12 is part of the gamma-secretase - protein complex . Presenilins are found in many multicellular animals . In the nematode it is ubiquitously expressed in neurons, both in the mother and in the zygote throughout development. Presenilin sel-12 is essential for the correct connectivity of the AIY cholinergic interneurons and their function in thermotaxis . It is also indispensable for the mesodermal patterning of muscle function.
Sel-12 is a transmembrane protein and is orthologous to the protein presenilin in humans . In the worm it plays a role in the development of the sexual organs ( vulva ) (the worm is a hermaphrodite). Some mutations in sel-12 can cause the worm to have an egg-laying defect. Sel-12 regulates the proteins lin-12 and glp-1 (defective germ line proliferation) in a notch-analogous signaling pathway . In addition, sel-12 is important for thermotaxis (the worm prefers certain temperatures and seeks out regions with corresponding temperatures).
literature
- Stefan Eimer: Analysis and suppression of mutant sel-12 in C. elegans. Dissertation, LMU Munich, 2003