{PDOC50919}
{PS50919; MIR}
{BEGIN}
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* MIR domain profile *
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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 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2003 / First entry.

[ 1] Ponting C.P.
     "Novel repeats in ryanodine and IP3 receptors and protein
     O-mannosyltransferases."
     Trends Biochem. Sci. 25:48-50(2000).
     PubMed=10664581

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{END}