Myelin and lymphocyte protein (MAL)
The protein contains 153 amino acids for an estimated molecular weight of 16714 Da.
Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Apical protein localization
Apoptotic process
Cell differentiation
Central nervous system development
Membrane raft polarization
Myelination
Positive regulation of extrinsic apoptotic signaling pathway via death domain receptors
Protein insertion into plasma membrane
Protein localization to paranode region of axon
The reference OMIM entry for this protein is 188860
Myelin and lymphocyte protein; mal
T-lymphocyte maturation-associated protein
T-cell differentiation protein
CLONING
As many as 200 mRNA species are expressed in T cells but not in B cells. A third of these encode membrane-associated proteins. Monoclonal antibodies against T cells have identified many surface molecules expressed during intrathymic ontogeny. The approach has permitted delineation of 3 discrete stages of T-cell differentiation. The earliest identified T-lineage cells express the sheep erythrocyte receptor T11 (stage I). Thymocytes then express T6, T4, and T8 antigens (stage II). Later, T6 disappears, thymocytes acquire the T3/T-cell receptor structure and ultimately they appear in the periphery as either T4+T8- or T4-T8+ cells (stage III). Alonso and Weissman (1987) characterized a cDNA clone present in mature T cells and not expressed earlier. This cDNA encodes a 16.7-kD protein that the authors termed MAL. Rancano et al. (1994) determined that MAL contains 4 hydrophobic, presumably membrane-associated, segments and each with an adjacent hydrophilic sequence. Amplification by PCR of cDNA from different T-cell samples indicated the existence of 4 different isoforms of MAL mRNA, termed MAL-a, -b, -c, and -d, that arise through differential usage of exons 2 and/or 3. As the 3 introns are located between complete codons, the reading frame was maintained in all the transcripts. Rancano et al. (1994) noted that model structures for each form of MAL mRNA demonstrated that MAL encodes proteolipid proteins, which, as Millan et al. (1997) stated, are proteins that are soluble in the organic solvents used to extract cell lipids. Sanchez-Pulido et al. (2002) stated that MAL has a 4 transmembrane-helix architecture with cytoplasmic N- and C-terminal regions. They called the 4 transmembrane-helix region the Marvel domain (Mal and related proteins for vesicle trafficking and membrane link) and showed that the Marvel domain is shared by members of the MAL family (see MAL2, 609684), as well as by members of the physin, gyrin, and occludin families. Sanchez-Pulido et al. (2002) suggested that the Marvel domain has functional importance in proteins involved in epithelial membrane appositionGENE STRUCTURE
Rancano et al. (1994) determined that the MAL gene comprises 4 exons.MAPPING
By study of somatic cell hybrid cells, including some with rearrangements of chromosome 2, Alonso et al. (1987, 1988) assigned the MAL locus to chromosome 2cen-q13.GENE FUNCTION
Millan et al. (1997) found that epitope-tagged MAL in epithelial cells was localized mainly in glycolipid- and cholesterol-enriched membrane microdomains belonging to the trans-Golgi network, and at low levels in early endosomes. MAL is also a component of the detergent-resistant membrane microdomains in T-lymphocytes, and the authors suggest that MAL plays a role in modulating the function of these microdomains during T-cell differentiation. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 188860 was added.
Dec. 10, 2018: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).