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11  structures 613  species 0  interactions 21129  sequences 1226  architectures

Family: MAM (PF00629)

Summary: MAM domain, meprin/A5/mu

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This is the Wikipedia entry entitled "MAM domain". More...

MAM domain Edit Wikipedia article

MAM domain

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 (meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu) domain, has been recognised in the extracellular region of functionally diverse proteins.[1] 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);[2] A5 antigen (a developmentally-regulated cell surface protein; Xenopus nrp1; P28824);[3] and receptor-like tyrosine protein phosphatase.[4] 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



  1. ^ Bork P, Beckmann G (1993). "An adhesive domain detected in functionally diverse receptors". Trends Biochem. Sci. 18 (2): 40–41. doi:10.1016/0968-0004(93)90049-s. PMID 8387703.
  2. ^ Grant GA, Jiang W, Gorbea CM, Flannery AV, Beynon RJ, Bond JS (1992). "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". J. Biol. Chem. 267 (13): 9185–9193. PMID 1374387.
  3. ^ Takagi S, Hirata T, Agata K, Eguchi G, Fujisawa H, Mochii M (1991). "The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors". Neuron. 7 (2): 295–307. doi:10.1016/0896-6273(91)90268-5. PMID 1908252. S2CID 11355150.
  4. ^ Gebbink MF, Hateboer G, Suijkerbuijk R, Beijersbergen RL, Moolenaar WH, van Etten I, Geurts van Kessel A (1991). "Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase". FEBS Lett. 290 (1): 123–130. doi:10.1016/0014-5793(91)81241-Y. PMID 1655529. S2CID 7237197.
This article incorporates text from the public domain Pfam and InterPro: IPR000998

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

MAM domain, meprin/A5/mu Provide feedback

An extracellular domain found in many receptors [1]. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerisation of the phosphatase ectoprotein and in cell adhesion [2,3]. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases [4].

Literature references

  1. Beckmann G, Bork P; , Trends Biochem Sci. 1993;18:40-41.: An adhesive domain detected in functionally diverse receptors. PUBMED:8387703 EPMC:8387703

  2. Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY;, Science. 2007;317:1217-1220.: Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism. PUBMED:17761881 EPMC:17761881

  3. Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY;, EMBO J. 2006;25:701-712.: Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion. PUBMED:16456543 EPMC:16456543

  4. Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stocker W, Becker-Pauly C, Gomis-Ruth FX;, Proc Natl Acad Sci U S A. 2012;109:16131-16136.: Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane. PUBMED:22988105 EPMC:22988105

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000998

MAM is an acronym derived from meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu. The MAM domain consists of approximately 170 amino acids. It occurs in several cell surface proteins and is likely to have an adhesive function [ PUBMED:8387703 ]. The domain has been shown to play a role in homodimerization of protein-tyrosine phosphatase mu [ PUBMED:7782276 ] and appears to help determine the specificity of these interactions. It contains four conserved cysteines which probably form two disulfide bridges. It has been reported that certain cysteine mutations in the MAM domain of murine meprin A result in the formation of monomeric meprin, which has altered stability and activity [ PUBMED:8798668 ]. This indicates that these domain-domain interactions are critical for structure and function of the enzyme.

Proteins containing this domain 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. It has also been shown that the MAM domain of meprins is necessary for correct folding and transport through the secretory pathway [ PUBMED:9857066 ].
  • Neuropilin (A5 antigen), a calcium-independent cell adhesion molecule that function during the formation of certain neuronal circuits. The sequence contains 2 CUB domains and a MAM domain.
  • Receptor-like tyrosine protein phosphatases Mu, Kappa and PCP-2 ( EC ) . 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 ), 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, a MAM domain, a SRCR domain and a CUB domain.
  • 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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

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Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 55
Number in full: 21129
Average length of the domain: 152.40 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 24.07 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.4 26.4
Trusted cut-off 26.4 26.4
Noise cut-off 26.3 26.3
Model length: 161
Family (HMM) version: 26
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MAM domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2K9H4 View 3D Structure Click here
A0A0G2KB47 View 3D Structure Click here
A0A0G2KNX7 View 3D Structure Click here
A0A0G2KWA4 View 3D Structure Click here
A0A0G2L8W4 View 3D Structure Click here
A0A0R4IFQ9 View 3D Structure Click here
A0A0R4IG13 View 3D Structure Click here
A0A0R4ITP4 View 3D Structure Click here
A0A286Y7Z0 View 3D Structure Click here
A0A2R8Q7M4 View 3D Structure Click here
A0A2R8QCZ8 View 3D Structure Click here
A0A2R8QQY7 View 3D Structure Click here
A0A2R8RP90 View 3D Structure Click here
A1Z8V0 View 3D Structure Click here
A2AJA7 View 3D Structure Click here
A2AJX4 View 3D Structure Click here
A5I9F0 View 3D Structure Click here
B0S6D0 View 3D Structure Click here
B1AUH1 View 3D Structure Click here
B3DK56 View 3D Structure Click here
B3DKP9 View 3D Structure Click here
D4A911 View 3D Structure Click here
E3W739 View 3D Structure Click here
E7F0Q1 View 3D Structure Click here
E7F1Z9 View 3D Structure Click here
E7FDT4 View 3D Structure Click here
F1LPJ1 View 3D Structure Click here
F1LRZ0 View 3D Structure Click here
F1LXJ9 View 3D Structure Click here
F1M9P7 View 3D Structure Click here
F1MAG7 View 3D Structure Click here
F1QN93 View 3D Structure Click here
F1QVU0 View 3D Structure Click here
F1RDD1 View 3D Structure Click here
F1RER3 View 3D Structure Click here
H2DL88 View 3D Structure Click here
O14522 View 3D Structure Click here
O14786 View 3D Structure Click here
O35276 View 3D Structure Click here
O35375 View 3D Structure Click here