InterPro domain: IPR035542

The name CRIP, for cyclophilin-RNA interacting protein, has been proposed for this family of proteins that comprise a cyclophilin-type peptidyl-prolyl isomerase domain, an RNA recognition motif, followed by a region rich in glutamate and lysine (EK domain) and a C-terminal string of serines [ 1 ]. The family includes among others Paramecium tetraurelia KIN241 [ 2 ], human cyclophilin-like protein PPIL4 [ 2 ], Arabidopsis thaliana AtCYP59 [ 3 ], and Caenorhabditis elegans sig-7 [ 4 ].

1. KIN241: a gene involved in cell morphogenesis in Paramecium tetraurelia reveals a novel protein family of cyclophilin-RNA interacting proteins (CRIPs) conserved from fission yeast to man. Mol. Microbiol. 42, 257-67
2. Molecular cloning, structure and expression of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from human fetal brain. Cytogenet. Cell Genet. 95, 43-7
3. AtCyp59 is a multidomain cyclophilin from Arabidopsis thaliana that interacts with SR proteins and the C-terminal domain of the RNA polymerase II. RNA 12, 631-43
4. A Conserved Nuclear Cyclophilin Is Required for Both RNA Polymerase II Elongation and Co-transcriptional Splicing in Caenorhabditis elegans. PLoS Genet. 12, e1006227