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PROSITE documentation PDOC51262 [for PROSITE entry PS51262]

COS domain profile





Description

N-terminal RING finger (see <PDOC00449>)/B-box (see <PDOC50119>)/coiled coil (RBCC) or tripartite motif (TRIM) proteins, which are found in metazoan, are involved in a vast array of intracellular functions. They appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. The following RBCC proteins contain an ~60-residue COS (C-terminal subgroup one signature) domain, which is also found in a distantly related non-RBCC microtubule-binding protein, GLFND:

  • Vertebrate MID1 and MID2, which associate with microtubules through homo- and heterodimerization.
  • Animal TRIM9, which plays a regulatory role in synaptic vesicle exocytosis.
  • Mammalian TRIM nine-like (TNL).
  • Mammalian TRIM36, which could play a regulatory role in exocytosis of the sperm vesicle.
  • Mammalian tripartite, fibronectin type III and C-terminal B30.2/SPRY (TRIFIC).
  • Mammalian muscle-specific RING finger (MURF) family. MURF proteins have an ability to form both homo- and heterodimers with each other and to associate with the microtubule cytoskeleton.

In addition to RBCC, the COS domain is also found in association with B30.2/SPRY (see <PDOC50188>) or fibronectin type-III (FN3) (see <PDOC50853>) domains.

The COS domain is predicted to consist of two α-helical coils [1].

The profile we developed covers the entire COS domain.

Last update:

November 2006 / First entry.

Technical section

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

COS, PS51262; COS domain profile  (MATRIX)


Reference

1AuthorsShort K.M. Cox T.C.
TitleSubclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding.
SourceJ. Biol. Chem. 281:8970-8980(2006).
PubMed ID16434393
DOI10.1074/jbc.M512755200



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