Description

IPR017867 is a Protein-tyrosine phosphatase, low molecular weight.

<p>This entry represents the low molecular weight (LMW) protein-tyrosine phosphatases (or acid phosphatase), which act on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates [[cite:PUB00002706], [cite:PUB00005003]]. The structure of a LMW PTPase has been solved by X-ray crystallography [[cite:PUB00004186]] and is found to form a single structural domain. It belongs to the α/β class, with 6 α-helices and 4 β-strands forming a 3-layer α-β-α sandwich architecture.</p> <p>Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; [ec:3.1.3.48]) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [[cite:PUB00035793], [cite:PUB00035794]]. The PTP superfamily can be divided into four subfamilies [[cite:PUB00035795]]:</p> <ul> <li>(1) pTyr-specific phosphatases</li> <li>(2) dual specificity phosphatases (dTyr and dSer/dThr)</li> <li>(3) Cdc25 phosphatases (dTyr and/or dThr)</li> <li>(4) LMW (low molecular weight) phosphatases</li> </ul> <p>Based on their cellular localisation, PTPases are also classified as:</p> <ul> <li>Receptor-like, which are transmembrane receptors that contain PTPase domains [[cite:PUB00035796]]</li> <li>Non-receptor (intracellular) PTPases [[cite:PUB00035797]]</li> </ul> <p>All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel β-sheet with flanking α-helices containing a β-loop-α-loop that encompasses the PTP signature motif [[cite:PUB00035798]]. Functional diversity between PTPases is endowed by regulatory domains and subunits.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 2

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: