Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.

Nuclear pore complexes represent the channels for the the bi-directional movement of macromolecules between the nucleus and cytoplasm, and are thought to contain upwards of 100 different polypeptide subunits. Many of these subunits belong to a growing family of polypeptides termed nucleoporins which are characterized by the presence of O-linked N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). This paper reports the primary structure of hnup153, the human homologue of the rat nucleoporin, nup153, with which it shares 82% amino acid identity. In addition to 33 copies of the XFXFG repeat, hnup153 exhibits four repeats of 37-38 amino acids each containing an apparent 'zinc finger motif'. These zinc fingers are most closely related to those found in the mouse oncoprotein mdm-2 and a product of Drosophila small optic lobes (sol) gene.