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 Drosphila small optic lobes (sol) gene.