Difference between revisions of "Phosphatase Subfamily PAPL"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_MTDP|Fold MTDP]]:[[Phosphatase_Superfamily_MTDP|Superfamily MTDP]]: [[Phosphatase_Family_PAP|Family PAP]]: [[Phosphatase_Subfamily_PAPL|PAPL]]
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__NOTOC__
 
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPPL|Fold PPPL]]: [[Phosphatase_Superfamily_PPPL|Superfamily PPPL]]: [[Phosphatase_Family_PAP|Family PAP]]: [[Phosphatase_Subfamily_PAPL|PAPL]]
 
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=== Evolution ===
 
=== Evolution ===
PAPL subfamily is found in [[Phosphatase_Glossary#Holozoa|holozoan]]. It is absent from most athropoda.
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PAPL is found in [[Phosphatase_Glossary#Holozoa|holozoa]] but lost from most arthropods. Humans have a single member, PAPL (aka ACP7, PAPL1), but many invertebrates have multiple members, including 3 members each in Monosiga, Nematostella, sponge, and sea urchin. These appear to be independent expansions by protein sequence similarity, and in sea urchin, they form a tandem duplication cluster.
  
=== Domain ===
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=== Domain Structure ===
PAPL has a phosphatase domain and a signal peptide cleavage site on N-terminus.
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PAPL has a phosphatase domain and most members have an N-terminal signal peptide cleavage site. Though predicted to be secreted, human PAPL is found mostly in the cytoplasm (http://www.proteinatlas.org/ENSG00000183760-PAPL/tissue).
  
 
=== Function ===
 
=== Function ===
Human ACP5 hydrolyzes a variety of phosphomonoesters at acid pH ''in vitro''. ACP5 also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is a protein that in humans is encoded by the SPP1 gene (secreted phosphoprotein 1). Osteopontin is involved in many biological processes including biomineralization, bone remodeling, immune functions in heart, chemotaxis, cell activation, apoptosis.
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PAPL function is unclear. There may be some confusion in the literature, as PAPL/ACP7 may be confused with another PAP family member, ACP5, both of which are putative secreted proteins. The structural similarity between PAPL and ACP5 has been explored <cite>Flanagan</cite>.
 
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ACP5 also dephosphorylate mannose 6-phosphate modification on lysosomal proteins. Most newly synthesized proteins destined for the lysosome reach this location via a specific intracellular pathway. In the Golgi, a phosphotransferase specifically labels lysosomal proteins with mannose 6-phosphate (Man-6-P). This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the Man-6-P recognition marker is rapidly removed <cite>sun08</cite>.
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=== References ===
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===References===
 
<biblio>
 
<biblio>
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#Flanagan pmid=16793224
 
</biblio>
 
</biblio>

Latest revision as of 01:16, 26 October 2016

Phosphatase Classification: Fold PPPL: Superfamily PPPL: Family PAP: PAPL

Evolution

PAPL is found in holozoa but lost from most arthropods. Humans have a single member, PAPL (aka ACP7, PAPL1), but many invertebrates have multiple members, including 3 members each in Monosiga, Nematostella, sponge, and sea urchin. These appear to be independent expansions by protein sequence similarity, and in sea urchin, they form a tandem duplication cluster.

Domain Structure

PAPL has a phosphatase domain and most members have an N-terminal signal peptide cleavage site. Though predicted to be secreted, human PAPL is found mostly in the cytoplasm (http://www.proteinatlas.org/ENSG00000183760-PAPL/tissue).

Function

PAPL function is unclear. There may be some confusion in the literature, as PAPL/ACP7 may be confused with another PAP family member, ACP5, both of which are putative secreted proteins. The structural similarity between PAPL and ACP5 has been explored [1].

References

  1. Flanagan JU, Cassady AI, Schenk G, Guddat LW, and Hume DA. Identification and molecular modeling of a novel, plant-like, human purple acid phosphatase. Gene. 2006 Aug 1;377:12-20. DOI:10.1016/j.gene.2006.02.031 | PubMed ID:16793224 | HubMed [Flanagan]