Difference between revisions of "Phosphatase Subfamily MTMR3"
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===Domain Structure=== | ===Domain Structure=== | ||
| − | MTMR3 subfamily has a conserved domain combination: a divergent GRAM/PH domain, phosphatase domain and [http://pfam.xfam.org/family/PF01363.16 FYVE domain], which can bind to the second messenger phosphatidylinositol 3-monophosphate PI3P. | + | MTMR3 subfamily has a conserved domain combination: a divergent GRAM/PH domain, phosphatase domain and [http://pfam.xfam.org/family/PF01363.16 FYVE domain], which can bind to the second messenger phosphatidylinositol 3-monophosphate PI3P. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins. |
===Catalytic activity and functions=== | ===Catalytic activity and functions=== | ||
Revision as of 19:12, 30 December 2014
Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: MTMR3
MTMR1 is a lipid phosphatase that dephosphorylates the second messenger phosphatidylinositol 3-monophosphate [PI(3)P].
Evolution
MTMR1 is in metazoan. It consists of two members in human, MTMR3 and MTMR4. In fruit fly and C elegans, a single copy is found.
Domain Structure
MTMR3 subfamily has a conserved domain combination: a divergent GRAM/PH domain, phosphatase domain and FYVE domain, which can bind to the second messenger phosphatidylinositol 3-monophosphate PI3P. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins.
Catalytic activity and functions
Human MTMR3 is an inositol lipid 3-phosphatase, with a so-far-unique substrate specificity. It is able to hydrolyze PtdIns3P and PtdIns(3,5)P2, both in vitro and when heterologously expressed in S. cerevisiae. Thus, MTMR3 plays critical role in the cellular production of PtdIns5P [1].
Related Kinases
See PI3K.
