Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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MIT Microtubule Interacting and Trafficking molecule domain

SMART accession number:	SM00745
Description:
Interpro abstract (IPR007330):	The MIT domain 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.
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 516 MIT domains in 457 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a MIT domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with MIT domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Ciccarelli FD et al.
  • 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.

  • Patel H et al.
  • 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

  % proteins involved KEGG pathway ID Description 36.36 map04140 Regulation of autophagy 36.36 map04150 mTOR signaling pathway 9.09 map00780 Biotin metabolism 9.09 map00310 Lysine degradation 9.09 map00230 Purine metabolism 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%.

• Structure (3D structures containing this domain)

• 3D Structures of MIT domains in PDB

  PDB code	Main view	Title
  1wfd		Solution structure of mouse mit domain
  1wr0		Structural characterization of the mit domain from human vps4b
  1yxr		Nmr structure of vps4a mit domain
  2cpt		Solution structure of mit domain from human skd1
  2dl1		Solution structure of the mit domain from human spartin
  2jq9		Vps4a mit-chmp1a complex
  2jqh		Vps4b mit
  2jqk		Vps4b mit-chmp2b complex
  2k3w		Nmr structure of vps4a-mit-chmp6
  2v6x		Stractural insight into the interaction between escrt-iii and vps4
  2v6y		Structure of the mit domain from a s. solfataricus vps4- like atpase
  2w2u		Structural insight into the interaction between archaeal escrt-iii and aaa-atpase
  2zam		Crystal structure of mouse skd1/vps4b apo-form
  2zan		Crystal structure of mouse skd1/vps4b atp-form
  2zao		Crystal structure of mouse skd1/vps4b adp-form
  3eab		Crystal structure of spastin mit in complex with escrt iii

• Links (links to other resources describing this domain)

• INTERPRO	IPR007330

Send comments to Ivica Letunic