v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions [ ]. This group is composed of CBY1-interacting BAR domain-containing protein 1/2 (also known as the family with sequence similarity 92 (FAM92)), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, CBAR1 (FAM92A) and CBAR2 (FAM92B), which may exist in many variants. These may be involved in ciliogenesis regulation during limb morphogenesis [, ]. Human CBAR1 plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure []. The Xenopus homologue of CBAR1A (FAM92A1), xVAP019, is essential for embryo survival and cell differentiation. CBAR1A may be involved in regulating cell proliferation and apoptosis [, , ]. |
| Short Name | BAR_CBAR1/2 |