| Primary Identifier | IPR021922 | Type | Domain |
| Short Name | Par3/HAL_N |
| description | This domain is found in eukaryotes and is about 150 amino acids in length. It has a conserved GILD sequence motif. Some proteins containing this domain are essential for cell polarity establishment and maintenance such as Par3 (partitioning defective), and some are involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament []. |
