MAM domain

MAM domain is an evolutionary conserved protein domain. It is an extracellular domain found in many receptors.

MAM domain
Identifiers
SymbolMAM
PfamPF00629
InterProIPR000998
PROSITEPDOC00604
CDDcd06263

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; Xenopus nrp1; 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.

Human proteins containing this domain

ALK; EGFL6; MAMDC2; MAMDC4; MDGA1; MDGA2; MEP1A; MEP1B; NPNT; NRP1; NRP2; PRSS7; PTPRK; PTPRM; PTPRO; PTPRT; PTPRU; ZAN

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References
  1. 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. PMID 8387703.
  2. 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. PMID 1374387.
  3. 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. PMID 1908252.
  4. Gebbink MF, Hateboer G, Suijkerbuijk R, Beijersbergen RL, Moolenaar WH, van Etten I, Geurts van Kessel A (1991). "Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase". FEBS Lett. 290 (1): 123–130. doi:10.1016/0014-5793(91)81241-Y. PMID 1655529.
This article incorporates text from the public domain Pfam and InterPro: IPR000998


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