MAM domain is an evolutionary conserved protein domain. It is an extracellular domain found in many receptors.
A 170 amino acid domain, the so-called MAM (meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu) domain, has been recognised in the extracellular region of functionally diverse proteins.[1] These proteins have a modular, receptor-like architecture comprising a signal peptide, an N-terminal extracellular domain, a single transmembrane domain and an intracellular domain. Such proteins include meprin (a cell surface glycoprotein);[2] A5 antigen (a developmentally-regulated cell surface protein; Xenopusnrp1; P28824);[3] and receptor-like tyrosine protein phosphatase.[4] The MAM domain is thought to have an adhesive function. It contains 4 conserved cysteine residues, which probably form disulphide bridges.
^Bork P, Beckmann G (1993). "An adhesive domain detected in functionally diverse receptors". Trends Biochem. Sci. 18 (2): 40–41. doi:10.1016/0968-0004(93)90049-s. PMID8387703.
^Grant GA, Jiang W, Gorbea CM, Flannery AV, Beynon RJ, Bond JS (1992). "The alpha subunit of meprin A. Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the alpha and beta subunits". J. Biol. Chem. 267 (13): 9185–9193. PMID1374387.
^Takagi S, Hirata T, Agata K, Eguchi G, Fujisawa H, Mochii M (1991). "The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors". Neuron. 7 (2): 295–307. doi:10.1016/0896-6273(91)90268-5. PMID1908252. S2CID11355150.
