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*Now available with Java™ 1.5!*
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| Family: |
INOSITOL MONOPHOSPHATASE (PTHR20854)
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| Subfamilies: |
8
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| PANTHER Links: |
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| Abstract: |
It has been shown that several proteins share two sequence motifs [PMID:1660408]. Two of these
proteins, vertebrate and plant inositol monophosphatase (EC: 3.1.3.25), and vertebrate inositol
polyphosphate 1-phosphatase (EC: 3.1.3.57), are enzymes of the inositol phosphate second messenger
signalling pathway, and share similar enzyme activity. Both enzymes exhibit an absolute requirement
for metal ions (Mg2+ is preferred), and their amino acid sequences contain a number of conserved
motifs, which are also shared by several other proteins related to MPTASE (including products of fungal QaX and qutG, bacterial suhB and cysQ, and yeast hal2) [PMID:7761465]. The function of the
other proteins is not yet clear, but it is suggested that they may act by enhancing the synthesis
or degradation of phosphorylated messenger molecules [PMID:1660408]. Structural analysis of these
proteins has revealed a common core of 155 residues, which includes residues essential for metal
binding and catalysis. An interesting property of the enzymes of this family is their sensitivity
to Li+. The targets and mechanism of action of Li+ are unknown, but overactive inositol phosphate
signalling may account for symptoms of manic depression [PMID:2553271].
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| InterPro Accession: |
IPR000760
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| PANTHER Molecular Function: |
Phosphatase Other phosphatase
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| PANTHER Biological Process: |
Biological process unclassified
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| Pathway Categories: |
No pathway information available
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| Training Sequences: |
107
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| HMM Length |
242
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| Downloads: |
HMM (HMMER format) |
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Total |
Celera |
FlyBase |
NCBI |
| H. sapiens |
11
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6
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0 |
5
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| M. musculus |
11
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6
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0 |
5
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| R. norvegicus |
10
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5
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0 |
5
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| D. melanogaster |
9
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0 |
9
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0 |
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