{PDOC00604}
{PS00740; MAM_1}
{PS50060; MAM_2}
{BEGIN}
************************************
* MAM domain signature and profile *
************************************

A domain of about 170 amino acids has been recognized [1] 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 (alpha and beta) 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
   domain.
 - 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 3.1.3.48). These PTPases have an extracellular region which consists of
   a MAM  domain  followed  by an Ig-like domain and four fibronectin-type III
   domains.
 - Vertebrate enteropeptidase (EC 3.4.21.9), 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
   MAM domains.
 - 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.

-Consensus pattern: [GE]-x-[LIVMFY](2)-x(3)-[STA]-x(10,11)-[LV]-x(4)-[LIVMF]-
                    x(6,7)-C-[LIVM]-x-F-x-[LIVMFY]-x(3)-[GSC]
                    [C may be involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for apical endosomal glycoprotein from rat.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Bork P.; bork@embl-heidelberg.de

-Last update: December 2004 / Pattern and text revised.

[ 1] Beckmann G., Bork P.
     "An adhesive domain detected in functionally diverse receptors."
     Trends Biochem. Sci. 18:40-41(1993).
     PubMed=8387703
{END}