Is pantetheinase the actual identity of mouse and human vanin-1 proteins?

Pantetheinase is an amidohydrolase involved in the dissimilative pathway of CoA, allowing the turnover of the pantothenate moiety. We have determined the N-terminal sequence as well as the sequences of a number of tryptic and chymotryptic peptides of the protein isolated from pig kidney. These seque nce stretches were used as probes to search in the SwissProt database and s ignificant similarities were found with a GPI-anchored protein (mouse vanin -1, with a suggested role in lymphocyte migration), with two putative prote ins encoded by human cDNAs (VNN1 and VNN2) and with human biotinidase, On t he basis of sequence similarity we propose that vanin-1 and VNN1 should be identified as pantetheinase. (C) 1999 Federation of European Biochemical So cieties.