This domain represents the RNA recognition motif found in Synaptojanin proteins.

Synaptojanins are phosphoinositide phosphatases known to play an important role in vesicle recycling by promoting the uncoating of clathrin following synaptic vesicle uptake [ PUBMED:10931870 PUBMED:27559170 … expand

This domain represents the RNA recognition motif found in Synaptojanin proteins.

Synaptojanins are phosphoinositide phosphatases known to play an important role in vesicle recycling by promoting the uncoating of clathrin following synaptic vesicle uptake [ PUBMED:10931870 PUBMED:27559170 PUBMED:9428629 PUBMED:21932368 PUBMED:21316588 ]. Synaptojanin-1 contains an N-terminal domain homologous to the cytoplasmic portion of the yeast protein Sac1p [ PUBMED:9788876 ], a central inositol 5-phosphatase domain followed by a putative RNA recognition motif (RRM), and a C-terminal proline-rich region mediating the binding of synaptojanin-1 to various SH3 domain-containing proteins including amphiphysin, SH3p4, SH3p8, SH3p13, and Grb2 [ PUBMED:10542231 ]. Synaptojanin-2 is a ubiquitously expressed central regulatory enzyme in the phosphoinositide-signaling cascade [ PUBMED:12699622 ]. As a novel Rac1 effector regulating an early step of clathrin-mediated endocytosis, synaptojanin-2 acts as a polyphosphoinositide phosphatase, directly and specifically interacting with Rac1 in a GTP-dependent manner. Synaptojanin-2 shows high sequence homology to the N-terminal Sac1p homology domain [ PUBMED:9788876 ], the central inositol 5-phosphatase domain, and the putative RNA recognition motif (RRM) of synaptojanin-1, but differs in the proline-rich region.