Difference between revisions of "Phosphatase Subfamily PPM1Z"

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=== Evolution ===
 
=== Evolution ===
The PTC2 subfamily is conserved in opisthokont but lost in jawed vertebrates, 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. However, the subfamily belongs to the same gene cluster in our [http://resdev.gene.com/gOrtholog/view/cluster/MC0000187/overview internal orthology database] based on [http://genome.cshlp.org/content/13/9/2178.full OrthoMCL algorithm].  
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The PPM1Z subfamily is conserved in metazoa but lost in jawed vertebrates and sponge. Its sequence is most similar to PPM1G, but it lacks the acidic domain inserted into phosphatase domain which is a character of PPM1G.  
  
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.
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The subfamily belongs to the same gene cluster with [[Phosphatase_Subfamily_PPM1A|PPM1A subfamily]] in our [http://resdev.gene.com/gOrtholog/view/cluster/MC0000187/overview internal orthology database] based on [http://genome.cshlp.org/content/13/9/2178.full OrthoMCL algorithm]. Inferring the evolutionary history by comparing the sequences of the gene cluster, the subfamily is mostly like to emerge in metazoa or holozoa through the duplication of the common ancestral gene of this subfamily and [[Phosphatase_Subfamily_PPM1A|PPM1A subfamily]].
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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 PPM1Z.
  
 
=== Domain ===
 
=== 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.
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The PPM1Z 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 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>.
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The function of PPM1Z is unclear.  
 
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High osmolarity glycerol (HOG) pathway. All three are involved in HOG pathway, particularly PTC2 and PTC3 can directly dephosphorylate Hog1.
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PTC2 and PTC3 also dephosphorylates CDC28 at Thr-169.
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=== References ===
 
=== References ===
 
<biblio>
 
<biblio>
#Arino11 pmid=21076010
 
#Sharmin14 pmid=25088474
 
 
</biblio>
 
</biblio>

Revision as of 20:47, 8 June 2015

Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Family PPM (PP2C): Subfamily PPM1Z

Evolution

The PPM1Z subfamily is conserved in metazoa but lost in jawed vertebrates and sponge. Its sequence is most similar to PPM1G, but it lacks the acidic domain inserted into phosphatase domain which is a character of PPM1G.

The subfamily belongs to the same gene cluster with PPM1A subfamily in our internal orthology database based on OrthoMCL algorithm. Inferring the evolutionary history by comparing the sequences of the gene cluster, the subfamily is mostly like to emerge in metazoa or holozoa through the duplication of the common ancestral gene of this subfamily and PPM1A subfamily.

Notice: Monosiga has a unclassified phosphatase that has a N-terminal myristoylation site but the overall sequence similarity does not well support it is PPM1Z.

Domain

The PPM1Z 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 function of PPM1Z is unclear.

References

  1. []