PROSITE documentation PDOC00547 [for PROSITE entry PS00630]

Inositol monophosphatase family signatures




Description

It has been shown [1] that several proteins share two sequence motifs. Two of these proteins are enzymes of the inositol phosphate second messenger signalling pathway:

  • Vertebrate, plants and microbial myo-inositol monophosphatase (EC 3.1.3.25).
  • Vertebrate inositol polyphosphate 1-phosphatase (EC 3.1.3.57).

The function of the other proteins is not yet clear:

  • Bacterial protein cysQ. CysQ could help to control the pool of PAPS (3'-phosphoadenoside 5'-phosphosulfate), or be useful in sulfite synthesis.
  • Neurospora crassa protein Qa-X. Probably involved in quinate metabolism.
  • Emericella nidulans protein qutG. Probably involved in quinate metabolism.
  • Yeast protein HAL2/MET22 [2] involved in salt tolerance as well as methionine biosynthesis.
  • Yeast hypothetical hypothetical protein YHR046c.
  • Caenorhabditis elegans hypothetical protein F13G3.5.

It is suggested [1] that these proteins may act by enhancing the synthesis or degradation of phosphorylated messenger molecules. From the X-ray structure of human inositol monophosphatase [3], it seems that some of the conserved residues are involved in binding a metal ion and/or the phosphate group of the substrate.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

IMP_2, PS00630; Inositol monophosphatase family signature 2  (PATTERN)

IMP_1, PS00629; Inositol monophosphatase family signature 1  (PATTERN)


References

1AuthorsNeuwald A.F., York J.D., Majerus P.W.
TitleDiverse proteins homologous to inositol monophosphatase.
SourceFEBS Lett. 294:16-18(1991).
PubMed ID1660408

2AuthorsGlaeser H.-U., Thomas D., Gaxiola R., Montrichard F., Surdin-Kerjan Y., Serrano R.
SourceEMBO J. 12:3105-3110(1993).

3AuthorsBone R., Springer J.P., Atack J.R.
TitleStructure of inositol monophosphatase, the putative target of lithium therapy.
SourceProc. Natl. Acad. Sci. U.S.A. 89:10031-10035(1992).
PubMed ID1332026



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)