Difference between revisions of "Phosphatase Subfamily PPM1Z"
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=== Evolution === | === Evolution === | ||
| − | The PTC2 subfamily is conserved in opisthokont but lost in human, sponge and monosiga. Its sequence is most similar to PPM1G, but it lacks | + | The PTC2 subfamily is conserved in opisthokont but lost in human, sponge and monosiga. Its sequence is most similar to PPM1G, but it lacks inserted acidic domain of PPM1G. It also has an N-terminal myristoylation site. Notice: Monosiga has [http://phosphatome.net/3.0/database/gene/uid/MbreP135 a unclassified phosphatase] that has a N-terminal myristoylation site but the overall sequence similarity does not well support it is PTC2. |
=== Domain === | === Domain === | ||
| − | The | + | The PTC2 subfamily has a N-terminal myristoylation site and a phosphatase domain. The phosphatase domain is closer to PPM1G than other PPMs in sequence, but it does not have the acidic domain inserted in catalytic domain which is common in PPM1G subfamily. |
=== Functions === | === Functions === | ||
| − | The most studied members of | + | The most studied members of PTC2 subfamily are yeast PTC2, PTC3 and PTC4, whose functions were summarized in Table 1 of <cite>Sharmin14</cite> and reviewed in <cite>Arino11</cite>. |
| + | |||
| + | High osmolarity glycerol (HOG) pathway. All three are involved in HOG pathway, particularly PTC2 and PTC3 can directly dephosphorylate Hog1. | ||
| + | |||
| + | PTC2 and PTC3 also dephosphorylates CDC28 at Thr-169. Interestingly, the substrate protein and the site are also conserved in meta | ||
=== References === | === References === | ||
<biblio> | <biblio> | ||
| + | #Arino11 pmid=21076010 | ||
#Sharmin14 pmid=25088474 | #Sharmin14 pmid=25088474 | ||
</biblio> | </biblio> | ||
Revision as of 18:08, 8 June 2015
Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Family PPM (PP2C): Subfamily PTC2
Evolution
The PTC2 subfamily is conserved in opisthokont but lost in human, sponge and monosiga. Its sequence is most similar to PPM1G, but it lacks inserted acidic domain of PPM1G. It also has an N-terminal myristoylation site. Notice: Monosiga has a unclassified phosphatase that has a N-terminal myristoylation site but the overall sequence similarity does not well support it is PTC2.
Domain
The PTC2 subfamily has a N-terminal myristoylation site and a phosphatase domain. The phosphatase domain is closer to PPM1G than other PPMs in sequence, but it does not have the acidic domain inserted in catalytic domain which is common in PPM1G subfamily.
Functions
The most studied members of PTC2 subfamily are yeast PTC2, PTC3 and PTC4, whose functions were summarized in Table 1 of [1] and reviewed in [2].
High osmolarity glycerol (HOG) pathway. All three are involved in HOG pathway, particularly PTC2 and PTC3 can directly dephosphorylate Hog1.
PTC2 and PTC3 also dephosphorylates CDC28 at Thr-169. Interestingly, the substrate protein and the site are also conserved in meta
References
- Sharmin D, Sasano Y, Sugiyama M, and Harashima S. Effects of deletion of different PP2C protein phosphatase genes on stress responses in Saccharomyces cerevisiae. Yeast. 2014 Oct;31(10):393-409. DOI:10.1002/yea.3032 |
- Ariño J, Casamayor A, and González A. Type 2C protein phosphatases in fungi. Eukaryot Cell. 2011 Jan;10(1):21-33. DOI:10.1128/EC.00249-10 |
