| Primary Identifier | IPR041847 | Type | Domain |
| Short Name | C2_cPLA2 |
| description | This entry represents the C2 domain found in cytosolic phospholipase A2 (cPLA2), which hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. The cooperative binding of two Ca(2+) ions to the C2 domain of cPLA2-alpha induces docking to phosphatidylcholine (PC) membranes []. This domain have a type-II C2 domain topology. C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, ]. |
