ID:MYO1C_HUMAN DESCRIPTION: RecName: Full=Unconventional myosin-Ic; AltName: Full=Myosin I beta; Short=MMI-beta; Short=MMIb; FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes (By similarity). FUNCTION: Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation (By similarity). SUBUNIT: Interacts (via its IQ motifs) with calmodulin. Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and calmodulin. Interacts with POLR1A and POLR2A. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity). Interacts with RPS6 and actin. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane (By similarity). Cell projection, stereocilium membrane (By similarity). Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 in actin-based membranes. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm. Nucleus, nucleolus. Nucleus, nuclear pore complex. Note=Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli (By similarity). In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level. DOMAIN: Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to a putative PH domain present in its tail domain (By similarity). PTM: Isoform 2 contains a N-acetylmethionine at position 1. SIMILARITY: Contains 2 IQ domains. SIMILARITY: Contains 1 myosin head-like domain. CAUTION: Represents a unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1). SEQUENCE CAUTION: Sequence=AAH68013.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=BAE06097.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=BAF85599.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O00159
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006605 protein targeting GO:0006612 protein targeting to membrane GO:0007018 microtubule-based movement GO:0015031 protein transport GO:0030050 vesicle transport along actin filament GO:0030335 positive regulation of cell migration GO:0030838 positive regulation of actin filament polymerization GO:0038089 positive regulation of cell migration by vascular endothelial growth factor signaling pathway GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis GO:0045815 positive regulation of gene expression, epigenetic GO:0051028 mRNA transport GO:0071346 cellular response to interferon-gamma GO:0090314 positive regulation of protein targeting to membrane GO:1900078 positive regulation of cellular response to insulin stimulus GO:1900748 positive regulation of vascular endothelial growth factor signaling pathway GO:2000810 regulation of bicellular tight junction assembly