It has been shown  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
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.
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