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We have isolated additional cDNA clones encoding type II
inositol polyphosphate 5-phosphatase (5-phosphatase II) resulting in a
combined cDNA of 3076 nucleotides encoding a protein of 942 amino
acids. The 5-phosphatase II hydrolyzed both
Ins
(1, 4, 5) P
Volume 270,
Number 16,
Issue of April 21, pp. 9370-9377, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
to
Ins
(1, 4) P
and the phospholipid
PtdIns
(4, 5) Pto PtdIns
(4) P both
in vitro and in vivo. There are two motifs highly
conserved between types I and II 5-phosphatase and several other
proteins presumed to be inositol phosphatases suggesting a possible
role in catalysis. The type II 5-phosphatase also contains homology to
several GTPase activating proteins although no such activity for
5-phosphatase II was found. The predicted protein ends with the
sequence CNPL, suggesting that it is isoprenylated as a mechanism for
membrane attachment. We found evidence for isoprenylation by
demonstrating incorporation of [H]mevalonate into
native but not C939S mutant 5-phosphatase II expressed in Sf9 insect
cells. Furthermore, we showed that membrane localization and the
activity of 5-phosphatase II toward its lipid substrate
PtdIns
(4, 5) Pis reduced by eliminating
5-phosphatase II isoprenylation in the mutant C939S relative to the
native enzyme.
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