The N-terminal domains of tensin and auxilin are phosphatase homologues

Protein Sci. 1996 Dec;5(12):2643-6. doi: 10.1002/pro.5560051227.


Tensin, an actin filament capping protein, and auxilin, a component of receptor-mediated endocytosis, are known to have 350 residue regions of significant sequence similarity near their N-termini (Schröder et al., 1995, Eur J Biochem 228:297-304). Here we demonstrate that these regions are homologous, not only to each other, but also to the catalytic domain of a putative protein tyrosine phosphatase (PTP) from Saccharomyces cerevisiae and to other PTPs. We propose that the PTP-like portion of the homology region of tensin and auxilin represents a distinct domain. A detailed sequence comparison indicates that the PTP-like domain in tensin is unlikely to exhibit phosphatase activity, whereas in auxilin it may possess a different phosphatase specificity from tyrosine phosphatases. It is probable that the PTP-like domains in tensin and auxilin mediate binding interactions with phosphorylated polypeptides; they may therefore represent members of a distinct class of phosphopeptide recognition domain.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chickens
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / genetics*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / genetics*
  • Phosphoproteins / chemistry
  • Phosphoproteins / genetics*
  • Phosphoric Monoester Hydrolases / genetics*
  • Sequence Alignment
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Tensins


  • Adaptor Proteins, Vesicular Transport
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Tensins
  • Phosphoric Monoester Hydrolases

Associated data

  • GENBANK/H21153
  • GENBANK/H23630
  • GENBANK/H92038
  • GENBANK/M78861
  • GENBANK/N37896
  • GENBANK/N48030