MAMDomain in meprin, A5, receptor protein tyrosine phosphatase mu (and others)
|SMART accession number:||SM00137|
|Description:||Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.|
|Interpro abstract (IPR000998):|
MAM is an acronym derived from meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu. The MAM domain consists of approximately 170 amino acids. It occurs in several cell surface proteins, including Meprins, and is thought to function as an interaction or adhesion domain [(PUBMED:8387703)]. The domain has been shown to play a role in homodimerization of protein-tyrosine phosphatase mu [(PUBMED:7782276)] and appears to help determine the specificity of these interactions. It has been reported that certain cysteine mutations in the MAM domain of murine meprin A result in the formation of monomeric meprin, which has altered stability and activity [(PUBMED:8798668)]. This indicates that these domain-domain interactions are critical for structure and function of the enzyme. It has also been shown that the MAM domain of meprins is necessary for correct folding and transport through the secretory pathway [(PUBMED:9857066)].
|GO component:||membrane (GO:0016020)|
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- Evolution (species in which this domain is found)
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