Difference between revisions of "Phosphatase Subfamily MTMR5"
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===Domain Structure=== | ===Domain Structure=== | ||
| − | MTMR5 subfamily has a DENN domain, [http://pfam.xfam.org/family/PF02893.15 PH/GRAM] domain, phosphatase domain, coiled-coil domain and PH domain. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins. | + | MTMR5 subfamily has a [http://www.jbc.org/content/286/16/13791.short DENN domain], [http://pfam.xfam.org/family/PF02893.15 PH/GRAM] domain, phosphatase domain, coiled-coil domain and PH domain. 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 21:33, 30 December 2014
Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: Subfamily MTMR5 (SBF)
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Evolution
MTMR5 subfamily is found throughout metazoan. It consists of two members in human, MTMR5 and MTMR13, also called SBF1 and SBF2, respectively. In fruit fly and C elegans, a single copy is found.
Domain Structure
MTMR5 subfamily has a DENN domain, PH/GRAM domain, phosphatase domain, coiled-coil domain and PH domain. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins.
Catalytic activity and functions
Human MTM1 has phosphatase activity towards the second messenger phosphatidylinositol 3-monophosphate [PI(3)P] in vitro and in human, budding yeast, and fission yeast [1, 2]. Human MTMR1 and MTMR2 have been shown to dephosphorylate PI(3)P ([3] and [4], respectively). Although the enzymatic properties of the three human phosphatases are indistinguishable, their functions are not totally redundant. MTM1 and MTMR2 are differentially regulated in the aspects of developmental expression and subcellular localization, resulting in their use of specific cellular pools of PI(3)P [4].
Related Kinases
See PI3K.
References
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