High impact information on Cyp1

• The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins [1].
• This involves a cyclophilin-mediated modification of R/G opsin, possibly involving proline isomerization [2].
• In Drosophila, the cyclophilin NinaA is expressed in all photoreceptors and is required for the expression of only a subset of opsins [2].
• Two new retinal cyclophilin isoforms, types I and II, are highly expressed in cone photoreceptors of the vertebrate retina [2].
• The immunophilins cyclophilin and FK506 binding protein (FKBP) are small, predominantly soluble proteins that bind the immunosuppressant drugs cyclosporin A and FK506, respectively, with high affinity, and which seem to mediate their pharmacological actions [3].

Biological context of Cyp1

• The ninaA gene was isolated and found to encode a 237-amino-acid protein that has over 40% amino-acid sequence identity with the vertebrate cyclosporin A-binding protein, cyclophilin, a protein that seems to be involved in T-lymphocyte activation [4].
• The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein [4].
• In Drosophila, biogenesis of the major rhodopsin, Rh1, is dependent on the presence of a photoreceptor cell-specific cyclophilin, NinaA [5].
• Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein) [6].
• Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA [7].

Anatomical context of Cyp1

• The muscle, fat body, and colleterial gland contained the lowest cyclophilin mRNA level (1-5% the content of ovary) [8].
• The highest values for B. germanica cyclophilin mRNA tissue content were found in 6-day-old ovary, followed by brain, testis, and gut (15-30% the content of ovary) [8].

Associations of Cyp1 with chemical compounds

• The availability of mutations in a cyclophilin gene provides a new model system for the study of cyclophilin and cyclosporin action [4].
• Isolation of the ninaA gene by chromosomal walking revealed that it is expressed only in the eye and encodes a 237-amino acid polypeptide that shows strong sequence similarity to cyclophilin, a putative molecular target for cyclosporine A, a potent immunosuppressant used in human organ transplantations [6].
• Compared with cyclophilin 18, the enzymatic activity carried by the PPIase domain of Moca-cyp is low, exhibits characteristic substrate specificity, and shows a reduced sensitivity to the drug cyclosporin A (CsA) [9].

Physical interactions of Cyp1

• The ninaA protein is a membrane bound cyclophilin which acts as a peptidyl-prolyl cis/trans isomerase during the folding process of rhodopsin 1 in D. melanogaster rhabdomere [10].

Other interactions of Cyp1

• Identification and characterization of Moca-cyp. A Drosophila melanogaster nuclear cyclophilin [9].

Analytical, diagnostic and therapeutic context of Cyp1

• These mutations provide a detailed dissection of the structure/function relationships in cyclophilin [7].
• Investigations of cyclophilin interactions with oligopeptides containing proline by affinity capillary electrophoresis [11].

References