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- ************************
- * MAM domain signature *
- ************************
-
- 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 that comprises 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 that is 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.
- - A5 antigen. A developmentally regulated cell surface protein from Xenopus
- laevis which is presumed to be involved in the neuronal recognition
- between the optic nerve fibers and the visual centers during nerve
- innervation. In A5 the MAM domain is located near the end of the
- extracellular domain.
- - Receptor-like tyrosine protein phosphatase Mu and Kappa (EC 3.1.3.48).
- These PTPases have an extracellular region which consist of a MAM domain
- followed by an IG-like domain and four fibronectin-type III domains.
-
- 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: G-x(12)-G-x(2)-A-x-L-x(4)-[LIVM]-x(6,7)-C-[LIVM]-x-F
- [C may be involved in a disulfide bond]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Bork P.
- bork@embl-heidelberg.de
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Beckmann G., Bork P.
- Trends Biochem. Sci. 18:40-41(1993).
-