Taxonomic distribution of proteins containing Mob1_phocein domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Mob1_phocein domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Molecular cloning and characterization of phocein, a protein found from the Golgicomplex to dendritic spines.

Baillat G, Moqrich A, Castets F, Baude A, Bailly Y, Benmerah A, Monneron A
Mol Biol Cell. 2001; 12: 663-73

Phocein is a widely expressed, highly conserved intracellular protein of 225amino acids, the sequence of which has limited homology to the sigma subunitsfrom clathrin adaptor complexes and contains an additional stretch bearing aputative SH3-binding domain. This sequence is evolutionarily very conserved (80% identity between Drosophila melanogaster and human). Phocein was discovered by a yeast two-hybrid screen using striatin as a bait. Striatin, SG2NA, and zinedin,the three mammalian members of the striatin family, are multimodular, WD-repeat, and calmodulin-binding proteins. The interaction of phocein with striatin, SG2NA,and zinedin was validated in vitro by coimmunoprecipitation and pull-downexperiments. Fractionation of brain and HeLa cells showed that phocein isassociated with membranes, as well as present in the cytosol where it behaves as a protein complex. The molecular interaction between SG2NA and phocein wasconfirmed by their in vivo colocalization, as observed in HeLa cells whereantibodies directed against either phocein or SG2NA immunostained the Golgicomplex. A 2-min brefeldin A treatment of HeLa cells induced the redistributionof both proteins. Immunocytochemical studies of adult rat brain sections showedthat phocein reactivity, present in many types of neurons, is strictlysomato-dendritic and extends down to spines, just as do striatin and SG2NA.