Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
2  structures 158  species 1  interaction 3415  sequences 308  architectures

Family: MAM (PF00629)

Summary: MAM domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

MAM domain Edit Wikipedia article

MAM domain
Identifiers
Symbol MAM
Pfam PF00629
InterPro IPR000998
PROSITE PDOC00604
CDD cd06263

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 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);[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

ALK; EGFL6; MAMDC2; MAMDC4; MDGA1; MDGA2; MEP1A; MEP1B; NPNT; NRP1; NRP2; PRSS7; PTPRK; PTPRM; PTPRO; PTPRT; PTPRU; ZAN

References

  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. 
  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. 

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 Provide feedback

An extracellular domain found in many receptors.

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


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, including Meprins, and is thought to function as an interaction or adhesion domain [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 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. It has also been shown that the MAM domain of meprins is necessary for correct folding and transport through the secretory pathway [PUBMED:9857066].

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...

Loading domain graphics...

Pfam Clan

This family is a member of clan GBD (CL0202), which has the following description:

This large superfamily contains beta sandwich domains with a jelly roll topology. Many of these families are involved in carbohydrate recognition. Despite sharing little sequence similarity they do share a weak sequence motif, with a conserved bulge in the C-terminal beta sheet. The probable role of this bulge is in bending of the beta sheet that contains the bulge. This enables the curvature of the sheet forming the sugar binding site [1].

The clan contains the following 27 members:

Allantoicase APC10 Bac_rhamnosid_N BetaGal_dom4_5 CBM_11 CBM_15 CBM_17_28 CBM_4_9 CBM_6 CIA30 Cleaved_Adhesin DUF642 Endotoxin_C Ephrin_lbd F5_F8_type_C FBA Glyco_hydro_2_N Laminin_N Lyase_N MAM Muskelin_N P_proprotein PA-IL PepX_C PITH Sad1_UNC XRCC1_N

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

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.

  Seed
(92)
Full
(3415)
Representative proteomes NCBI
(3145)
Meta
(308)
RP15
(938)
RP35
(1052)
RP55
(1428)
RP75
(1950)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(92)
Full
(3415)
Representative proteomes NCBI
(3145)
Meta
(308)
RP15
(938)
RP35
(1052)
RP55
(1428)
RP75
(1950)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(92)
Full
(3415)
Representative proteomes NCBI
(3145)
Meta
(308)
RP15
(938)
RP35
(1052)
RP55
(1428)
RP75
(1950)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

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...

Trees

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.

Note: You can also download the data file for the tree.

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.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 92
Number in full: 3415
Average length of the domain: 149.40 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 28.95 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.2 21.2
Trusted cut-off 21.2 21.2
Noise cut-off 21.0 21.1
Model length: 160
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Interactions

There is 1 interaction for this family. More...

ig

Structures

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 2 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 seqence.

Loading structure mapping...