PROSITE documentation PDOC50919 [for PROSITE entry PS50919]

MIR domain profile




Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

MIR, PS50919; MIR domain profile  (MATRIX)


Reference

1AuthorsPonting C.P.
TitleNovel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases.
SourceTrends Biochem. Sci. 25:48-50(2000).
PubMed ID10664581



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