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FLASH GENE
Symbol MAL contributors: mct - updated : 08-06-2017
HGNC name mal, T-cell differentiation protein
HGNC id 6817
PROTEIN
PHYSICAL PROPERTIES Hydrophobic
STRUCTURE
motifs/domains
  • four transmembrane segments (4TM)
  • short hydrophilic segments
  • a MARVEL domain
  • HOMOLOGY
    Homologene
    FAMILY
  • MAL proteolipid family
  • CATEGORY tumor suppressor , transport
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,organelle,endosome
    basic FUNCTION
  • involved in formation, stabilization and maintenance of glycosphingolipid and cholesterol-enriched membrane microdomains (raft5)
  • 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
  • required in T cells for efficient expression of LCK at the plasma membrane and activation of IL2 transcription
  • required for recruitment of LCK to specialized membranes and formation of specific transport carriers for LCK targeting
  • potentially having a functional role in peripheral myelination by influencing the expression of membrane components that mediate axon-glia interaction during ensheathment and myelin wrapping
  • may be playing an important role in apical sorting or in maintaining the stability of the apical membrane
  • involvement of MAL in the activation and surface expression of SLC12A1 could play an important role in the regulated absorption of Na+ and Cl- in the kidney
  • MAL, but not MAL2, self-associates, forms higher-order cholesterol-dependent complexes with apical proteins and promotes the formation of detergent-resistant membranes that recruit apical prote
  • role for MAL in raft coalescence and stabilization
  • is involved in apical vesicle transport
  • in epithelial cells, the MAL family members MAL, MAL2, and MYADM regulate the function and dynamics of ordered membrane domains
  • is a component of lipid rafts that is important for targeting proteins and lipids to distinct domains
  • CELLULAR PROCESS cell organization/biogenesis
    PHYSIOLOGICAL PROCESS cellular trafficking transport
    text
  • biogenesis myelin
  • transport between Golgi and apical membrane
  • PATHWAY
    metabolism
    signaling signal transduction
    signal transduction in T cells
    a component
  • essential component of the specialized machinery for apical targeting in epithelial cells
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with SLC12A1 (MAL increases the cell surface retention of SLC12A1 by attenuating its internalization, and this coincides with an increase in cotransporter phosphorylation)
  • BTK was involved in close contact with Tyr86 and Tyr106 of MAL whereas PKRKCD may phosphorylate Tyr106 only
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --low  
    in esophageal cancer
    tumoral     --low  
    in head and neck squamous cell carcinoma
    tumoral     --low  
    most down-regulated gene in cervical cancer, by promoter methylation (by promoter methylation)
    constitutional     --over  
    is also associated with shortened or absent cilia, and cyst development
    constitutional     --over  
    leads to disturbed expression of genes that influence cytoskeletal organization and differentiation of Schwann cells
    Susceptibility
    Variant & Polymorphism SNP
    Candidate gene
    Marker
  • inactivation of MAL, as a candidate tumor suppressor gene, can contribute to human epithelial cell carcinoma and may be served as a biomarker in head and neck squamous cell carcinoma
  • Therapy target
    ANIMAL & CELL MODELS
  • overexpression of MAL/VIP17 in the kidney of transgenic mice results in cysts formation in distal nephron structures