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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 220.127.116.11).
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 .
The profile we developed covers the entire MIR domain.
August 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases.
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