A domain of about 170 amino acids has been recognized  in the extracellular
region of functionally diverse proteins. All these proteins have a modular,
receptor-like architecture consisting of a signal peptide, followed by a large
N-terminal extracellular domain, a single transmembrane region and a
intracellular domain. These proteins are listed below.
Meprin. This cell surface glycoprotein contains a zinc-metalloprotease
domain capable of degrading a variety of polypeptides. Meprin is composed
of two structurally related subunits (α and β) that form homo- or
heterotetramers by the non-covalent association of two disulfide-linked
dimers. In both subunits, the MAM domain is located after the catalytic
Neuropilin (A5 antigen), a calcium-independent cell adhesion molecule that
function during the formation of certain neuronal circuits. The sequence
contains 2 CUB domains (see <PDOC00908>, 2 FA58C domains (see <PDOC00988>)
and a MAM domain.
Receptor-like tyrosine protein phosphatases Mu, Kappa and PCP-2
(EC 18.104.22.168). These PTPases have an extracellular region which consists of
a MAM domain followed by an Ig-like domain and four fibronectin-type III
Vertebrate enteropeptidase (EC 22.214.171.124), a type II membrane protein of the
intestinal brush border, which activates trypsinogen. It consists at least
of a catalytic light chain and a multidomain heavy chain which has 2 LDL
receptor class A domains (see <PDOC00929>), a MAM domain, a SRCR domain
(see <PDOC00348>) and a CUB domain (see <PDOC00604>).
Apical endosomal glycoprotein from rat, a protein probably involved in the
sorting and selective transport of receptors and ligands across polarized
epithelia. This protein contains 6 MAM domains.
Xenopus laevis thyroid hormone induced protein B. This protein contains 4
Pig zonadhesin, a protein that binds in a species-specific manner to the
zona pellucida of the egg.
The MAM domain is likely to have an adhesive function. It contains four
conserved cysteines which probably form two disulfide bridges. The pattern for
MAM contains the third conserved cysteine which is located in the central part
of the domain.
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