# MAM domain

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> Source: https://en.wikipedia.org/wiki/MAM_domain
> Source revision: 1288140167
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{{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](/source/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](/source/PTPRM)) 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](/source/signal_peptide), an N-terminal extracellular domain, a single transmembrane domain and an intracellular domain. Such proteins include [meprin](/source/Meprin_A) (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](/source/Neuropilin_1); {{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](/source/cysteine) residues, which probably form [disulphide bridge](/source/disulphide_bridge)s.

==Human proteins containing this domain ==
[ALK](/source/Anaplastic_lymphoma_kinase);       [EGFL6](/source/EGFL6);     [MAMDC2](/source/MAMDC2);    [MAMDC4](/source/MAMDC4);    [MDGA1](/source/MDGA1);     [MDGA2](/source/MDGA2);     [MEP1A](/source/MEP1A);     [MEP1B](/source/MEP1B);     
[NPNT](/source/NPNT);      [NRP1](/source/neuropilin_1);      [NRP2](/source/NRP2);      [PRSS7](/source/PRSS7);     [PTPRK](/source/PTPRK);     [PTPRM](/source/PTPRM);     [PTPRO](/source/PTPRO);     [PTPRT](/source/PTPRT);     
[PTPRU](/source/PTPRU);     [ZAN](/source/zonadhesin)

==References==
{{reflist}}
{{InterPro content|IPR000998}}

Category:Protein domains
Category:Single-pass transmembrane proteins

{{membrane-protein-stub}}

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Adapted from the Wikipedia article [MAM domain](https://en.wikipedia.org/wiki/MAM_domain) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MAM_domain?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.