InterPro : IPR016304

Name  Cyclophilin-type peptidyl-prolyl cis-trans isomerase E Short Name  Cyclophilin-type_PPIase_E
Type  Family Description  Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [, ]. They also have protein chaperone-like functions []and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [].Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function []. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation [].This entry represents the peptidyl-prolyl cis-trans isomerase E family of enzymes, which are a type of cyclophilin. In addition to their PPIase activity and role in protein folding, PPIase E family members also possess RNA-binding activity and may be involved in pre-mRNA splicing [, ].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR000504 RNA recognition motif domain RRM_dom Domain
IPR012677 Nucleotide-binding alpha-beta plait domain Nucleotide-bd_a/b_plait Domain
IPR002130 Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain Cyclophilin-type_PPIase_dom Domain
IPR020892 Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site Cyclophilin-type_PPIase_CS Conserved_site

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0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Fischer G The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. 1990 Biochemistry 29 2205-12
Stamnes MA Cyclophilins: a new family of proteins involved in intracellular folding. 1992 Trends Cell Biol 2 272-6
Wang P The cyclophilins. 2005 Genome Biol 6 226
Lee J An overview of cyclophilins in human cancers. 2010 J Int Med Res 38 1561-74
Nagy PD Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. 2011 Virology 411 374-82
Mi H A nuclear RNA-binding cyclophilin in human T cells. 1996 FEBS Lett 398 201-5
Jurica MS Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. 2002 RNA 8 426-39



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)