InterPro : IPR008294

Name  Meprin alpha/beta subunit Short Name  Meprin
Type  Family Description  This family contains the alpha and beta subunits of meprin. Meprins are metazoan zinc metallopeptidases belonging to MEROPS peptidase family M12 (clan MA(M)), subfamily M12A (astacin family). They are complex and structurally unique homo- or heterotetrameric glycoproteins composed of evolutionarily related alpha and/or beta subunits that contain disulphide-bridged dimers. The two subunits are differentially expressed and processed to yield latent and active proteases as well as membrane-associated and secreted forms. They are excellent models of homo- and hetero-oligomeric enzymes that are regulated at the transcriptional and post translational levels []. Each chain contains an astacin domain, MAM, MATH, and AM (after MATH) domains [], and an EGF-like domain.The astacin domain is a Zn-metalloprotease domain characterised by a unique 18-amino acid signature sequence, HEXXHXXGFXHEXXRXDR [], which begins with the zinc binding motif HEXXH. The MAM domain is necessary for correct folding and transport through the secretory pathway. The MATH domain is required for folding of an activatable zymogen, and the AM domain is important for activity against proteins and efficient secretion of the protein. Meprin is able to cleave a variety of substrates and has a role in matrix remodeling, inflammation, and cell-cell and cell-matrix processes []. Known substrates include FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10 and tenascin-C [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

5 Contains

Id Name Short Name Type
IPR002083 MATH MATH Domain
IPR000742 Epidermal growth factor-like domain EG-like_dom Domain
IPR001506 Peptidase M12A, astacin Peptidase_M12A Domain
IPR000998 MAM domain MAM_dom Domain
IPR006026 Peptidase, metallopeptidase Peptidase_Metallo Domain

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Beckmann G An adhesive domain detected in functionally diverse receptors. 1993 Trends Biochem Sci 18 40-1
Tsukuba T Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase. 1998 J Biol Chem 273 35260-7
Bond JS The astacin family of metalloendopeptidases. 1995 Protein Sci 4 1247-61
Kaushal GP Meprin A metalloproteinase and its role in acute kidney injury. 2013 Am J Physiol Renal Physiol 304 F1150-8
Becker-Pauly C Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates. 2011 Mol Cell Proteomics 10 M111.009233



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)