Alternative titles; symbols
HGNC Approved Gene Symbol: RANGRF
Cytogenetic location: 17p13.1 Genomic coordinates (GRCh38) : 17:8,288,670-8,290,087 (from NCBI)
Steggerda and Paschal (2000) cloned mouse Mog1. The deduced protein contains 185 amino acids. Epitope-tagged Mog1 localized to nuclei of transfected baby hamster kidney cells, but it was excluded from nucleoli.
By screening an EST database for homologs of S. cerevisiae Mog1, Marfatia et al. (2001) identified 2 alternately spliced variants of MOG1. One variant, which they designated MOG1a, contains 187 amino acids and has a calculated molecular mass of about 20 kD. The other variant, MOG1b, contains 146 amino acids and has a calculated molecular mass of about 16 kD. MOG1a and MOG1b share 29% and 30% amino acid identity with S. cerevisiae Mog1, respectively. Northern blot analysis detected a 0.85-kb MOG1a transcript and a 1.1-kb MOG1b transcript in all tissues examined, with MOG1a being the predominant transcript. PCR of a breast cancer cell line showed multiple products, suggesting the presence of additional splice variants. SDS-PAGE of in vitro translated MOG1a indicated that the protein migrates with an apparent molecular mass of about 28 kD. Transfection of fluorescence-labeled MOG1 into HEK293 cells resulted in overall staining with a nuclear concentration.
Using chromatography and both solution- and solid-phase binding assays, Steggerda and Paschal (2000) determined that mouse Mog1 formed a complex with Ran (601179) and Ranbp1 (601180). Mog1 stably bound to nucleotide-free Ran in the absence of Ranbp1, and it bound to RanGTP in the presence of Ranbp1. Mog1 and Ranbp1 did not interact directly, indicating that RanGTP acted as a bridge. Steggerda and Paschal (2000) showed that Mog1 stimulated the release of GTP from Ran, and following GTP release, Mog1 remained bound to nucleotide-free Ran in a conformation that prevented rebinding of the guanine nucleotide.
By yeast 2-hybrid analysis and in vitro binding assays, Marfatia et al. (2001) confirmed that MOG1 interacts with both human and S. cerevisiae Ran. The interaction was independent of guanine nucleotides, as MOG1 interacted with Ran-GTP, Ran-GDT, nucleotide-free Ran, and Ran preincubated with nonhydrolyzable guanine nucleotide analogs. Human MOG1 partially complemented the growth defect of a Mog1 null yeast cell line.
The International Radiation Hybrid Mapping Consortium mapped the RANGNRF gene to chromosome 17 (A006E21).
Marfatia, K. A., Harreman, M. T., Fanara, P., Vertino, P. M., Corbett, A. H. Identification and characterization of the human MOG1 gene. Gene 266: 45-56, 2001. [PubMed: 11290418] [Full Text: https://doi.org/10.1016/s0378-1119(01)00364-x]
Steggerda, S. M., Paschal, B. M. The mammalian Mog1 protein is a guanine nucleotide release factor for Ran. J. Biol. Chem. 275: 23175-23180, 2000. [PubMed: 10811801] [Full Text: https://doi.org/10.1074/jbc.C000252200]