Meprin alpha/beta subunit (IPR008294)

Short name: Meprin

Overlapping homologous superfamilies


Family relationships


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 [PMID: 8387703]. Each chain contains an astacin domain, MAM, MATH, and AM (after MATH) domains [PMID: 9857066], and an EGF-like domain.

The astacin domain is a Zn-metalloprotease domain characterised by a unique 18-amino acid signature sequence, HEXXHXXGFXHEXXRXDR [PMID: 7670368], 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 [PMID: 23427141]. Known substrates include FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10 and tenascin-C [PMID: 21693781].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding

Cellular Component

GO:0016020 membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.