| Primary Identifier | IPR017903 | Type | Domain |
| Short Name | COS_domain |
| description | N-terminal RING finger/B-box/coiled coil (RBCC) or tripartite motif (TRIM) proteins, which are found in metazoa, 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 heterodimerizationAnimal TRIM9, which plays a regulatory role in synaptic vesicle exocytosisMammalian TRIM nine-like (TNL)Mammalian TRIM36, which could play a regulatory role in exocytosis of the sperm vesicleMammalian 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 cytoskeletonIn addition to RBCC, the COS domain is also found in association with B30.2/SPRY or fibronectin type-III (FN3) domains.The COS domain is predicted to consist of two α-helical coils []. |
