The following text describes a protein:
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 a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Plays a role in formation of the podosome belt in osteoclasts.
Subcellular Localization:
Cytoplasm, cytosol. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein. Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Interacts with microtubules. Undergoes forward and rearward movements within filopodia. Interaction with membranes containing phosphatidylinositol 3,4,5-trisphosphate mediates localization at filopodium membranes.
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; Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains; IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP; The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. An anti-parallel coiled coil is located C-terminal to the SAH domain and mediates dimerization.
Sequence:
MDNFFPEGTRVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITHQKVMPMQPTDEEGVDDMATLTELHGGAIMHNLYQRYKRNQIYTYIGSIIASVNPYKTITGLYSRDAVDRYSRCHLGELPPHVFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSAISQQSVDLSSKEKTSSVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIGQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLGHEEREEFYLSVPENYHYLNQSGCVTDRTISDQESFREVIMAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPAQLTDALTQRSMFLRGEEILTPLNVQQAADSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSASNPFFVRCIKPNMQKMPDQFDQAVVVNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNVALPEDIRGKCTALLQLYDASNSEWQLGKTKVFLRESLEQKLEKRQEEEVTRAAMVIRAHVLGYLARKQYKKVLDCVVIIQKNYRAFLLRRRFLHLKKAAVVFQKQLRGQIARRVYRQLLAEKRAEEEKRKREEEEKRKREEEERERERERREAELRAQQEEAARKQRELEALQQESQRAAELSRELEKQKENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSGCTGEQGAGAEKPSFNFSQPYPEEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDESSEEDPYMNDTVVPTSPSADSTVLLAPSEHDSSAGEPTYCLPQTPGALPAPEGDYDYDQDDYEDGAITSGSSVTFSNSCSSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQAKLMYFENDSEEKLKGTVEVRAAKEIIDNTSKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRHTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLCSWQILTCLSCTFLPSRGILKYLKFHLRRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVHCHGGGSCKITVNSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTIVADVLAKFEKLAATSEVGEQPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHYPAPEENLQVLAALRLQYLQGDYAPHAPVPPLEEVYSLQRLKARISQSTKSFTPGERLEKRRTSFLEGTLRRSFRTGSAIRQKAEEEQMVDMWVKEEVCSARASILDKWKKFQGMSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQDLWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTSRSVSSQGSSR