Protein-tyrosine phosphatase-like, PTPLA (IPR007482)

Short name: Tyr_Pase-like_PTPLA

Overlapping homologous superfamilies


Family relationships



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: 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 [PMID: 9818190, PMID: 14625689]. The PTP superfamily can be divided into four subfamilies [PMID: 12678841]:

  • (1) pTyr-specific phosphatases
  • (4) LMW (low molecular weight) phosphatases

Based on their cellular localisation, PTPases are also classified as:

  • Receptor-like, which are transmembrane receptors that contain PTPase domains [PMID: 16672235]
  • Non-receptor (intracellular) PTPases [PMID: 8948575]

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 beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [PMID: 9646865]. Functional diversity between PTPases is endowed by regulatory domains and subunits.

This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types [PMID: 10644438].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.