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FLASH GENE
Symbol TMOD1 contributors: mct - updated : 21-10-2016
HGNC name tropomodulin 1
HGNC id 11871
Location 9q22.33      Physical location : 100.263.461 - 100.364.023
Synonym name E-tropomodulin
Synonym symbol(s) D9S57E, EMOD, TMOD
DNA
TYPE functioning gene
STRUCTURE 100.56 kb     10 Exon(s)
10 Kb 5' upstream gene genomic sequence study
regulatory sequence Promoter
alternative promoter
Binding site
text structure
  • binding sites for tropomyosin and actin
  • two conserved sequences, one in the 5prime-end of the first exon and the other in the intron next to the first exon, are necessary for the basal promoter activity (
  • MAPPING cloned Y linked N status confirmed
    Map see NBCCS
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    10 - 3275 41 359 - 2006 16434395
    10 - 3352 41 359 - 2006 16434395
    EXPRESSION
    Type
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart     Homo sapiens
    Endocrinepancreas    
    Nervousbrain     Homo sapiens
    Respiratorylung    
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / Hematopoieticbone marrow   
    Muscularstriatumskeletal   Homo sapiens
    Muscularstriatumcardiac   Homo sapiens
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Blood/Hematopoieticerthrocyte Homo sapiens
    Blood/Hematopoieticleukocyte
    Muscularmyocyte Homo sapiens
    Nervousneuron Homo sapiens
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    physiological period pregnancy
    Text placenta
    PROTEIN
    PHYSICAL PROPERTIES globular
    STRUCTURE
    motifs/domains
  • N-terminal region, with three functional sites: two TM-binding sites for both short and long TM isoforms within residues 138 and 109144 and a TM-dependent actin-capping site within residues 4892
  • a LRR domain necessary for pointed end assembly of TMOD1, having roles in the formation of neurite-like processes
  • a folded C-terminal domain (AAs 160-359), which does not bind to TM , and the C-terminal half of tropomodulin consists of one compact domain containing a tropomyosin-independent actin-capping site
  • HOMOLOGY
    interspecies homolog to murine Tmod1
    intraspecies homolog to Graves autoantigene (HGT)
    Homologene
    FAMILY
    CATEGORY motor/contractile , regulatory
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton
    intracellular,nucleus
    text
  • localizes to two narrow bands immediately adjacent to M-lines in myofibrils
  • is enriched along the proximal part of F-actin bundles in lamellipodia of spreading cells and in growth cones of extending neurites
  • TMOD1, TMOD2 and TMOD3 are associated with the cytoskeleton of non-muscle cells and their expression has distinct consequences on cell morphology
  • basic FUNCTION
  • modulating association of tropomyosin with the spectrin-actin complex in the erythrocyte membrane skeleton
  • actin-capping protein that interacts with tropomyosin (TM) at the pointed end of actin filaments
  • novel regulator of skeletal muscle physiology (
  • capping protein that specify thin filament lengths by controlling actin dynamics at pointed ends (
  • TMOD3 and TMOD4 compensate for the absence of TMOD1 structurally but not functionally
  • TMOD1-TMOD3 but not TMOD4 nucleate actin filament assembly
  • also required for proper myofibril formation
  • TMOD1 and TMOD2 have mechanistically distinct inhibitory roles in neurite formation, likely mediated via different effects on F-actin dynamics and via differential localizations during early neuritogenesis
  • is an actin-capping protein that binds to the two tropomyosins (TM) at the pointed end of the actin filament to prevent further actin polymerization and depolymerization
  • TMOD1 is involved in neuronal differentiation for proper neurite formation and outgrowth, and TMOD2 inhibits these processes
  • TMOD1, TMOD3, TMOD4 are novel regulators of actomyosin crossbridge formation and muscle contractility
  • in skeletal muscle TMOD1 is a pointed-end capping and tropomyosin-binding protein that controls thin-filament assembly, stability, and lengths
  • is a protein that binds and caps the pointed ends of actin filaments in erythroid and nonerythoid cell types
  • TMOD1, TMOD2, TMOD3 regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component part of a molecular ruler that plays an important role in generating short actin protofilaments critical for the integrity of the cell membrane
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • binding tropomyosin and actin,then blocking the elongation and depolarization of the actin filaments at the pointed end
  • interacting with LMOD2 (LMOD2 antagonizes the function of TMOD1, and together, these molecules might fine-tune thin filament lengths)
  • TMOD1 and TMOD4 cap thin filament pointed ends and functionally interact with the LMOD isoforms LMOD2 and LMOD3 to control myofibril organization, thin filament lengths, and actomyosin crossbridge formation in skeletal muscle fibers
  • cell & other
    REGULATION
    activated by WNT5A, while gelsolin, known as an actin-severing protein, is down-regulated by WNT5A
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • overexpression of Tmod1 in mice leads to dilated cardiomyopathy
  • Tmod1-null mice display a mild anemia with features resembling hereditary spherocytic elliptocytosis, including decreased red blood cell (RBC) mean corpuscular volume, cellular dehydration, increased osmotic fragility, reduced deformability