The MIT domain forms an asymmetric three-helix bundle. It is found in vacuolar sorting proteins, spastin (probable ATPase involved in the assembly or function of nuclear protein complexes), and a sorting nexin, which may play a role in intracellular trafficking.
A 'variant' MIT domain has been described at the N-terminal region of a related AAA-ATPase, mammalian katanin p60 [ (PUBMED:20339000) ].
Family alignment:
There are 5412 MIT domains in 4681 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing MIT domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with MIT domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing MIT domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
Genomics. 2003; 81: 437-41
Display abstract
Multiple sequence alignment has revealed the presence of a sequence domain of approximately 80 amino acids in two molecules, spartin and spastin, mutated in hereditary spastic paraplegia. The domain, which corresponds to a slightly extended version of the recently described ESP domain of unknown function, was also identified in VPS4, SKD1, RPK118, and SNX15, all of which have a well established and consistent role in endosomal trafficking. Recent functional information indicates that spastin is likely to be involved in microtubule interaction. With this new information relating to its likely function, we propose the more descriptive name 'MIT' (contained within microtubule-interacting and trafficking molecules) for the domain and predict endosomal trafficking as the principal functionality of all molecules in which it is present.
SPG20 is mutated in Troyer syndrome, an hereditary spastic paraplegia.
Nat Genet. 2002; 31: 347-8
Display abstract
Troyer syndrome (TRS) is an autosomal recessive complicated hereditary spastic paraplegia (HSP) that occurs with high frequency in the Old Order Amish. We report mapping of the TRS locus to chromosome 13q12.3 and identify a frameshift mutation in SPG20, encoding spartin. Comparative sequence analysis indicates that spartin shares similarity with molecules involved in endosomal trafficking and with spastin, a molecule implicated in microtubule interaction that is commonly mutated in HSP.
Metabolism (metabolic pathways involving proteins which contain this domain)
Click the image to view the interactive version of the map in iPath
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with MIT domain which could be assigned to a KEGG orthologous group, and not all proteins containing MIT domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
