A WIDELY EXPRESSED NOVEL C2H2 ZINC-FINGER PROTEIN WITH MULTIPLE CONSENSUS PHOSPHORYLATION SITES IS CONSERVED IN MOUSE AND MAN

We have cloned a murine cDNA whose deduced sequence encodes a 455-amin o-acid (aa) zinc-finger protein (Zfp), PZf (penta Zf protein). Sequenc e analysis shows that PZf has multiple phosphorylation consensus sites for casein kinase II and protein kinase C in its N-terminal portion. This region (aa 1 to 197), which does not share significant homology t o known aa sequences, has a number of charged (39 Glu, 15 Asp, 23 Lys, 22 Arg) and hydroxyl (20 Ser, 12 Thr) aa. This potentially phosphoryl atable region is followed by five C2H2 Zf in the middle of the protein . The Pzf gene is transcribed as a 5-kb mRNA in all murine tissues exa mined. The human genome also seems to contain one or more Pzf-related genes.