InterPro domain: IPR044834

This is a family of proteins widely distributed across the plant kingdom. Patellin (PATL) proteins are yeast Sec14 protein (Sec14p)-like phosphatidylinositol transfer proteins (PITPs) involved in several biological processes such as plant development and stress tolerance regulation, playing a role in membrane-trafficking events [ 1 , 2 ]. In Arabidopsis, this family consists of six members, PATL1-6, and are characterised by the presence of two conserved domains observed in other membrane trafficking-related proteins: a Sec14p-like lipid-binding domain and a GOLD following the N-terminal variable domain. The GOLD domain is found in proteins related to Golgi function, membrane homeostasis and vesicle trafficking [ 3 ]. PATL1 is the defining member of this family, associated to the cell-plate, and has a regulatory role during cytokinesis, which is thought to be involved in clathrin-dependent endocytosis that aids cell plate remodeling and completion [ 3 ]. These proteins are able to interact with phosphoinositides, varying their affinity among them which results their involvement in different processes and signalling pathways. PATLs also respond to auxin and play a role in the regulation of PIN1, which suggests that they play a redundant and crucial role in polarity and patterning in Arabidopsis [ 3 , 3 ].

This entry also includes some CRAL-TRIO domain-containing proteins from fungi.

1. Patellin protein family functions in plant development and stress response. J Plant Physiol 234-235, 94-97
2. Patellin1, a novel Sec14-like protein, localizes to the cell plate and binds phosphoinositides. Plant Physiol 136, 3080-94; discussion 3001-2
3. PATELLINS are regulators of auxin-mediated PIN1 relocation and plant development in Arabidopsis thaliana. J Cell Sci 131