The homeostasis of P-i in marine teleosts is maintained by renal P-i s
ecretion as well as by P-i reabsorption. A Na/P-i co-transport system
belonging to the NaPi-II protein family is instrumental in tightly con
trolled renal P-i handling in mammals and fish. We have isolated an Na
Pi-II related cDNA from winter flounder. It was cloned from a female g
onad cDNA library and is 624 bp long. The transcript is expressed in f
emale and male flounder gonads as well as in kidney and intestine, alt
hough at very low levels. RNase H digestion experiments revealed an op
posite orientation of the transcript with regard to NaPi-II-related mR
NA. The anti-sense orientation was confirmed by genomic sequence analy
sis and Southern blotting. Alluding to the sense transcript, the anti-
sense transcript was denoted IPAN. The open reading frame of IPAN enco
des a basic protein of 68 amino acid residues. Immunohistochemistry co
nfined the anti-sense related protein, Ipan, to a submembranous compar
tment of immature oocytes, suggesting a role in oocyte development. In
kidney and intestine Ipan is partly co-localized with the Na/P-i co-t
ransporter, implying a regulatory function for the anti-sense protein.
However, direct protein-protein interaction could not be established.
The existence of a putative open reading frame in other species exten
ds the biological significance of the novel protein.