ID:MYO10_HUMAN DESCRIPTION: RecName: Full=Unconventional myosin-X; AltName: Full=Unconventional myosin-10; FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity). SUBUNIT: Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation. Interacts with CALM. Interacts with ECM29. Interacts with NEO1. Interacts with ITGB1 and ITGB3 (By similarity). Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein (By similarity). Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Undergoes forward and rearward movements within filopodia. Interacts with microtubules. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity (By similarity). DOMAIN: Interacts with membranes containing phosphatidylinositol- 3,4,5-trisphosphate via the PH domains (By similarity). SIMILARITY: Contains 1 FERM domain. SIMILARITY: Contains 3 IQ domains. SIMILARITY: Contains 1 myosin head-like domain. SIMILARITY: Contains 1 MyTH4 domain. SIMILARITY: Contains 2 PH domains. CAUTION: Represents a unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10). SEQUENCE CAUTION: Sequence=BAA34519.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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 Q9HD67
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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.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
