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| PROSITE documentation PDOC50919 [for PROSITE entry PS50919] |
MIR domain profile
The protein mannosyltransferase, inositol 1,4,5-trisphosphate receptor (IP3R) and ryanodine receptor (RyR) (MIR) domain is an ~50-residue motif found generally in multiple copies in:
- Eukaryotic protein O-mannosyl-transferases (EC 2.4.1.109).
- Eukaryotic stromal cell-derived factor 2 (SDF-2).
- Animal inositol 1,4,5-trisphosphate receptors.
- Animal ryanodine receptors.
- Chlamydia trachomatis protein CT153.
As single MIR domains are found in the chlamydial proteins and in a splice variant of mouse tape-2 IP3R, it is proposed that MIR domains represent independent structural units, rather than being tandem repeats arranged within a single structural domain. The MIR domain can be found associated with other domains such as MAC/Perforin domain, SPRY, RyR repeated domain, EF-hand domain (see <PDOC00018>) or RIH. The function of the MIR domain is not yet known [1].
The profile we developed covers the entire MIR domain.
Last update:August 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Ponting C.P. |
| Title | Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases. | |
| Source | Trends Biochem. Sci. 25:48-50(2000). | |
| PubMed ID | 10664581 |
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