The domain within your query sequence starts at position 161 and ends at position 206; the E-value for the MIR domain shown below is 1.11e-6.
GEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPI
MIRDomain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases |
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SMART accession number: | SM00472 |
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Description: | - |
Interpro abstract (IPR016093): | The MIR domain is named after three of the proteins in which it occurs: protein Mannosyltransferase ( EC 2.4.1.109 ), 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 Ca 2+ from intracellular stores by binding to specific Ca 2+ 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 Ca 2+ -release channels following depolarisation of transverse-tubules [ (PUBMED:1645727) ]. The function is modulated by Ca 2+ 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) |
Family alignment: |
There are 28318 MIR domains in 8773 proteins in SMART's nrdb database.
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