Difference between revisions of "Phosphatase Subfamily PGP"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_PGP|Subfamily PGP]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_PGP|Subfamily PGP]] | ||
| − | PGP is | + | PGP is ubiquitous in eukaryotes. The two members in human have distinct functions: PDXP (aka chronophin) dephosphorylates protein cofilin on serine residue, as well as pyridoxal 5'-phosphate; PGP is a putative tyrosine-specific protein phosphatase. PDXP is mainly expressed in brain; PGP is widely expressed in different tissues. |
=== Evolution === | === Evolution === | ||
| − | The PGP subfamily is extremely conserved in eukaryotes, rarely absent from | + | The PGP subfamily is extremely conserved in eukaryotes, rarely absent from eukaryotic genomes. Human has two members of this subfamily: PGP and PDXP. PGP has obvious orthologs in vertebrate, but PDXP has obvious orthologs in coelacanth, birds, eutheria, rodents and primates. Thus, human PGP and PDXP has a deep root in eukaryotes but probably diverged from ancestral gene in function in early vertebrates. |
=== Domain === | === Domain === | ||
| − | PGP subfamily has a single domain: HAD domain. | + | The PGP subfamily has a single domain: HAD domain. |
=== Function === | === Function === | ||
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* Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis <cite>Gao94, Jang03, Kim05</cite>. | * Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis <cite>Gao94, Jang03, Kim05</cite>. | ||
| − | * Protein cofilin. PDXP dephosphorylates cofilin at serine, therefore regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>. Slingshot also | + | * Protein cofilin. PDXP dephosphorylates cofilin at serine, therefore regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>. [[Phosphatase_Subfamily_Slingshot|Slingshot]] also dephosphorylates cofilin. |
In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological substrate needs to be elicited. | In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological substrate needs to be elicited. | ||
Revision as of 01:15, 22 March 2015
Phosphatase Classification: Fold HAD: Superfamily HAD: Family NagD: Subfamily PGP
PGP is ubiquitous in eukaryotes. The two members in human have distinct functions: PDXP (aka chronophin) dephosphorylates protein cofilin on serine residue, as well as pyridoxal 5'-phosphate; PGP is a putative tyrosine-specific protein phosphatase. PDXP is mainly expressed in brain; PGP is widely expressed in different tissues.
Evolution
The PGP subfamily is extremely conserved in eukaryotes, rarely absent from eukaryotic genomes. Human has two members of this subfamily: PGP and PDXP. PGP has obvious orthologs in vertebrate, but PDXP has obvious orthologs in coelacanth, birds, eutheria, rodents and primates. Thus, human PGP and PDXP has a deep root in eukaryotes but probably diverged from ancestral gene in function in early vertebrates.
Domain
The PGP subfamily has a single domain: HAD domain.
Function
PDXP (Chronophin) is abundantly expressed in brain [1] (see also GTEx RNA-seq data). PDXP has two distinct substrates.
- Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis [1, 2, 3].
- Protein cofilin. PDXP dephosphorylates cofilin at serine, therefore regulating assembly and disassembly of actin filaments [4, 5, 6]. Slingshot also dephosphorylates cofilin.
In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also GTEx RNA-seq data). PGP is a putative tyrosine-specific phosphatase [7], but its physiological substrate needs to be elicited.
References
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Error fetching PMID 15580268:
Error fetching PMID 19000834:
Error fetching PMID 14522954:
Error fetching PMID 24338687:
Error fetching PMID 16336786:
Error fetching PMID 24338473:
- Error fetching PMID 14522954:
- Error fetching PMID 8132548:
- Error fetching PMID 16336786:
- Error fetching PMID 15580268:
- Error fetching PMID 19000834:
- Error fetching PMID 24338687:
- Error fetching PMID 24338473:
