{{Pfam_box | Symbol = MAM | Name = MAM domain | image = | width = | caption = | Pfam= PF00629 | InterPro= IPR000998 | SMART= | Prosite = PDOC00604 | SCOP = | TCDB = | OPM family= | OPM protein= | CDD = cd06263 | PDB= {{PDB3|2c9a}}A:27-184 }}
'''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 ('''m'''eprin, '''A'''-5 protein, and receptor protein-tyrosine phosphatase '''m'''u) domain, has been recognised in the extracellular region of functionally diverse proteins.<ref name="PUB00005405">{{cite journal |vauthors=Bork P, Beckmann G |title=An adhesive domain detected in functionally diverse receptors |journal=Trends Biochem. Sci. |volume=18 |issue=2 |pages=40–41 |year=1993 |pmid=8387703 |doi=10.1016/0968-0004(93)90049-s}}</ref> 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);<ref name="PUB00002774">{{cite journal |vauthors=Grant GA, Jiang W, Gorbea CM, Flannery AV, Beynon RJ, Bond JS |title=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 |journal=J. Biol. Chem. |volume=267 |issue=13 |pages=9185–9193 |year=1992 |pmid=1374387}}</ref> A5 antigen (a developmentally-regulated cell surface protein; ''Xenopus'' nrp1; {{UniProt|P28824}});<ref name="PUB00004307">{{cite journal |vauthors=Takagi S, Hirata T, Agata K, Eguchi G, Fujisawa H, Mochii M |title=The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors |journal=Neuron |volume=7 |issue=2 |pages=295–307 |year=1991 |pmid=1908252 |doi=10.1016/0896-6273(91)90268-5|s2cid=11355150 }}</ref> and receptor-like tyrosine protein phosphatase.<ref name="PUB00001624">{{cite journal |vauthors=Gebbink MF, Hateboer G, Suijkerbuijk R, Beijersbergen RL, Moolenaar WH, van Etten I, Geurts van Kessel A |title=Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase |journal=FEBS Lett. |volume=290 |issue=1 |pages=123–130 |year=1991 |pmid=1655529 |doi=10.1016/0014-5793(91)81241-Y|s2cid=7237197 |doi-access=free }}</ref> 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
==References== {{reflist}} {{InterPro content|IPR000998}}
Category:Protein domains Category:Single-pass transmembrane proteins
{{membrane-protein-stub}}