MIRDomain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases
|SMART accession number:||SM00472|
|Interpro abstract (IPR016093):|
The MIR domain is named after three of the proteins in which it occurs: protein Mannosyltransferase (EC 184.108.40.206), Inositol 1,4,5-trisphosphate receptor (IP3R) and Ryanodine receptor (RyR). MIR domains have also been found in eukaryotic stromal cell-derived factor 2 (SDF-2) and in Chlamydia trachomatis protein CT153. The MIR domain may have a ligand transferase function. This domain has a closed beta-barrel structure with a hairpin triplet, and has an internal pseudo-threefold symmetry. The MIR motifs that make up the MIR domain consist of ~50 residues and are often found in multiple copies.
Inositol 1,4,5-trisphosphate (InsP3) is an intracellular second messenger that transduces growth factor and neurotransmitter signals. InsP3 mediates the release of Ca2+ from intracellular stores by binding to specific Ca2+ channel-coupled receptors. Ryanodine receptors are involved in communication between transverse-tubules and the sarcoplamic reticulum of cardiac and skeletal muscle. The proteins function as a Ca2+-release channels following depolarisation of transverse-tubules [(PUBMED:1645727)]. The function is modulated by Ca2+, Mg2+, ATP and calmodulin. Deficiency in the ryanodine receptor may be the cause of malignant hyperthermia (MH) and of central core disease of muscle (CCD) [(PUBMED:7829078)]. protein O-mannosyltransferases transfer mannose from DOL-P-mannose to ser or thr residues on proteins.
|GO component:||membrane (GO:0016020)|
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