{PDOC51262}
{PS51262; COS}
{BEGIN}
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* COS domain profile *
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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 alpha-helical coils [1].

The profile we developed covers the entire COS domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2006 / First entry.

[ 1] Short K.M., Cox T.C.
     "Subclassification of the RBCC/TRIM superfamily reveals a novel motif
     necessary for microtubule binding."
     J. Biol. Chem. 281:8970-8980(2006).
     PubMed=16434393; DOI=10.1074/jbc.M512755200

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