PROSITE documentation PDOC00660
CAP-Gly domain signature and profile


It has been shown [1] that some cytoskeleton-associated proteins (CAP) share the presence of a conserved, glycine-rich domain of about 42 residues, called here CAP-Gly. Proteins known to contain this domain are listed below.

  • Restin (also known as cytoplasmic linker protein-170 or CLIP-170), a 160 Kd protein associated with intermediate filaments and that links endocytic vesicles to microtubules. Restin contains two copies of the CAP-Gly domain.
  • Vertebrate dynactin (150 Kd dynein-associated polypeptide; DAP) and Drosophila glued, a major component of activator I, a 20S polypeptide complex that stimulates dynein-mediated vesicle transport.
  • Yeast protein BIK1 which seems to be required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.
  • Yeast protein NIP100 (NIP80).
  • Human protein CKAP1/TFCB, Schizosaccharomyces pombe protein alp11 and Caenorhabditis elegans hypothetical protein F53F4.3. These proteins contain a N-terminal ubiquitin domain (see <PDOC00271>) and a C-terminal CAP-Gly domain.
  • Caenorhabditis elegans hypothetical protein M01A8.2.
  • Yeast hypothetical protein YNL148c.

Structurally, these proteins are made of three distinct parts: an N-terminal section that is most probably globular and contains the CAP-Gly domain, a large central region predicted to be in an α-helical coiled-coil conformation and, finally, a short C-terminal globular domain.

The signature for the CAP-Gly domain corresponds to the first 32 residues of the domain and includes five of the six conserved glycines. A profile was also developed that spans the complete CAP-Gly domain.

Last update:

April 2006 / Pattern revised.


Technical section

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

CAP_GLY_2, PS50245; CAP-Gly domain profile  (MATRIX)

CAP_GLY_1, PS00845; CAP-Gly domain signature  (PATTERN)


1AuthorsRiehemann K. Sorg C.
TitleSequence homologies between four cytoskeleton-associated proteins.
SourceTrends Biochem. Sci. 18:82-83(1993).
PubMed ID8480366

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