Despite the cloning of four disease-associated genes for Fanconi anemia (FA), 
the molecular pathogenesis of FA remains largely unknown. To study FA 
complementation group A using the mouse as a model system, we cloned and 
characterized the mouse homolog of the human FANCA cDNA. The mouse cDNA (Fanca) 
encodes a 161-kDa protein that shares 65% amino acid sequence identity with 
human FANCA. Fanca is located at the distal region of mouse chromosome 8 and has 
a ubiquitous pattern of expression in embryonic and adult tissues. Expression of 
the mouse cDNA in human FA-A cells restores the cellular drug sensitivity to 
normal levels. Thus, the expression pattern, protein structure, chromosomal 
location, and function of FANCA are conserved in the mouse. We also isolated a 
novel zinc finger protein, Zfp276, which has five C(2)H(2) domains. 
Interestingly, Zfp276 is situated in the Fanca locus, and the 3'UTR of its cDNA 
overlaps with the last four exons of Fanca in a tail-to-tail manner. Zfp276 is 
expressed in the same tissues as Fanca, but does not complement the mitomycin C 
(MMC)-sensitive phenotype of FA-A cells. The overlapping genomic organization 
between Zfp276 and Fanca may have relevance to the disease phenotype of FA.