Summary for peptidase M10.036: Dm2-matrix metallopeptidase

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Literature Substrates Inhibitors


MEROPS NameDm2-matrix metallopeptidase
Other namesAgMMP2 (Anopheles gambiense), Dm2-MMP (Drosophila melanogaster), CG1794 protein (Drosophila melanogaster), Mmp2 (Drosophila melanogaster)
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(M) >> Family M10 >> Subfamily A >> M10.036
HolotypeDm2-matrix metallopeptidase (Drosophila melanogaster), Uniprot accession Q8MPP3 (peptidase unit: 512-697), MERNUM MER0013586
History Identifier created: MEROPS 6.0 (30 August 2002)
Catalytic typeMetallo
NC-IUBMBNot yet included in IUBMB recommendations.
SpecificityPredicted structural studies of the catalytic domain have suggested an abnormally large S1' pocket, implying a wide substrate specificity (Llano et al., 2002).
Substrate commentsDm2-MMP cleaves the synthetic substrates QF-24,35 and 41 (Llano et al., 2002).
StructureA C-terminal GPI-anchor tethers Dm2-MMP to the membrane (Llano et al., 2002).
LocationDm2-MMP is attached to plasma membrane via a GPI anchor (Llano et al., 2002).
Biological aspectsThe gene for Dm2-MMP is expressed at all developmental stages of Drosophila, although sometimes at very low levels (Llano et al., 2002). Dm2-MMP has been shown to regulate levels of collagen IV and perlecan in the extracellular matrix around disc-associated trachea and the air sac primordium. This function is required to properly bring together tracheal and disc cells, for growth of the air sac primordium (Guha et al., 2009). Mutagenesis studies have shown that Dm2-MMP plays a critical role in dendrite reshaping via degradation of the basement membrane that the dendrites of the sensory neurons innervate (Yasunaga et al., 2010).
Distinguishing featuresDm2-MMP is structurally and functionally similar to Dm1-MMP (M10.031). However, Dm2-MMP contains a characteristic 200-amino acid insert into the hinge region which is not observed in any other MMP.
Contributing authorsKeith Brew, Department of Biomedical Sciences, Charles E. Schmidt College of Medicine, Florida Atlantic University, Boca Raton, Florida 33431, USA