LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | The AP180 N-terminal homology (ANTH) domain is a membrane binding domain found in endocytotic accessory proteins, such as AP180. The ANTH domain is involved in phosphatidylinositol 4,5-bisphosphate (also known as PIP2) binding and is also responsible for membrane localisation of AP180. The ANTH domain containing proteins appear to be universal elements in nucleation of clathrin coats [ , ]. The N-terminal phosphoinositide-binding domain of CALM and AP180 consist of nine alpha helices forming a solenoid structure. This is most similar to the ENTH domain of epsin, with the first seven helices of epsin superimposing well on those of CALM. However, in epsin the final alpha8 helix folds back across the others, whereas in CALM and AP180 the final three long helices continue the solenoidal pattern [ ]. |
| Short Name | ANTH_dom_sf |
