Difference between revisions of "Phosphatase Subfamily INPP5F"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_Sac|Family Sac]]: [[Phosphatase_Subfamily_INPP5F|Subfamily INPP5F]] (SAC2) | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_Sac|Family Sac]]: [[Phosphatase_Subfamily_INPP5F|Subfamily INPP5F]] (SAC2) | ||
| + | INPP5F (SAC2) is a phosphoinositide phosphatase in the endocytic pathway. It is conserved in metazoa and fungi and is also found in a few plants and basal eukaryotes. | ||
=== Evolution === | === Evolution === | ||
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=== Domain === | === Domain === | ||
| − | The INPP5F (SAC2) subfamily has | + | The INPP5F (SAC2) subfamily has at least one structural domain, SAC phosphatase domain. It also has a C-terminal proline-rich region. |
=== Function === | === Function === | ||
| − | Human INPP5F (SAC2) is expressed in most tissues and particularly abundant in brain (see [http://www.gtexportal.org/home/gene/INPP5F GTEx]). It has 5-phosphatase activity specific for phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate <cite>Minagawa01</cite>. | + | Human INPP5F (SAC2) is expressed in most tissues and particularly abundant in brain (see [http://www.gtexportal.org/home/gene/INPP5F GTEx]). It has 5-phosphatase activity specific for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)<cite>Minagawa01</cite>. It also has 4-phosphatase activity toward PI(4,5)P2) in the endocytic pathway <cite>Nakatsu15, Hsu15</cite>. It cooperates with OCRL, a 5-phosphatase, in the sequential dephosphorylation of PI(4,5)P2 at the 4 and 5 position of inositol in a partnership that mimics that of the two phosphatase modules of synaptojanin <cite>Nakatsu15</cite>. |
=== References === | === References === | ||
<biblio> | <biblio> | ||
| + | #Hsu15 pmid=25869669 | ||
| + | #Hughes00 pmid=10947947 | ||
| + | #Minagawa01 pmid=11274189 | ||
| + | #Nakatsu15 pmid=25869668 | ||
</biblio> | </biblio> | ||
Latest revision as of 16:56, 29 April 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family Sac: Subfamily INPP5F (SAC2)
INPP5F (SAC2) is a phosphoinositide phosphatase in the endocytic pathway. It is conserved in metazoa and fungi and is also found in a few plants and basal eukaryotes.
Evolution
The INPP5F (SAC2) subfamily is found in most metazoa and fungi. It is also found in a few plants and basal eukaryotes (see gOrtholog database (internal)).
Domain
The INPP5F (SAC2) subfamily has at least one structural domain, SAC phosphatase domain. It also has a C-terminal proline-rich region.
Function
Human INPP5F (SAC2) is expressed in most tissues and particularly abundant in brain (see GTEx). It has 5-phosphatase activity specific for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3)[1]. It also has 4-phosphatase activity toward PI(4,5)P2) in the endocytic pathway [2, 3]. It cooperates with OCRL, a 5-phosphatase, in the sequential dephosphorylation of PI(4,5)P2 at the 4 and 5 position of inositol in a partnership that mimics that of the two phosphatase modules of synaptojanin [2].
References
- Minagawa T, Ijuin T, Mochizuki Y, and Takenawa T. Identification and characterization of a sac domain-containing phosphoinositide 5-phosphatase. J Biol Chem. 2001 Jun 22;276(25):22011-5. DOI:10.1074/jbc.M101579200 |
- Nakatsu F, Messa M, Nández R, Czapla H, Zou Y, Strittmatter SM, and De Camilli P. Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway. J Cell Biol. 2015 Apr 13;209(1):85-95. DOI:10.1083/jcb.201409064 |
- Hsu F, Hu F, and Mao Y. Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2 regulates endocytic recycling. J Cell Biol. 2015 Apr 13;209(1):97-110. DOI:10.1083/jcb.201408027 |
- Hughes WE, Cooke FT, and Parker PJ. Sac phosphatase domain proteins. Biochem J. 2000 Sep 1;350 Pt 2(Pt 2):337-52.
