P79114 · MYO10_BOVIN
- ProteinUnconventional myosin-X
- GeneMYO10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2052 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
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
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell cortex | |
Cellular Component | cytosol | |
Cellular Component | filopodium | |
Cellular Component | filopodium membrane | |
Cellular Component | filopodium tip | |
Cellular Component | lamellipodium | |
Cellular Component | myosin complex | |
Cellular Component | ruffle | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | microfilament motor activity | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate binding | |
Molecular Function | plus-end directed microfilament motor activity | |
Biological Process | cytoskeleton-dependent intracellular transport | |
Biological Process | regulation of cell shape | |
Biological Process | regulation of filopodium assembly | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-X
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP79114
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000123472 | 1-2052 | Unconventional myosin-X | |||
Sequence: MDNFFPEGTRVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITHQKVMPMQPTDEEGVDDMATLTELHGGAIMHNLYQRYKRNQIYTYIGSIIASVNPYKTITGLYSRDAVDRYSRCHLGELPPHVFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSAISQQSVDLSSKEKTSSVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIGQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLGHEEREEFYLSVPENYHYLNQSGCVTDRTISDQESFREVIMAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPAQLTDALTQRSMFLRGEEILTPLNVQQAADSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSASNPFFVRCIKPNMQKMPDQFDQAVVVNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNVALPEDIRGKCTALLQLYDASNSEWQLGKTKVFLRESLEQKLEKRQEEEVTRAAMVIRAHVLGYLARKQYKKVLDCVVIIQKNYRAFLLRRRFLHLKKAAVVFQKQLRGQIARRVYRQLLAEKRAEEEKRKREEEEKRKREEEERERERERREAELRAQQEEAARKQRELEALQQESQRAAELSRELEKQKENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSGCTGEQGAGAEKPSFNFSQPYPEEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDESSEEDPYMNDTVVPTSPSADSTVLLAPSEHDSSAGEPTYCLPQTPGALPAPEGDYDYDQDDYEDGAITSGSSVTFSNSCSSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQAKLMYFENDSEEKLKGTVEVRAAKEIIDNTSKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRHTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLCSWQILTCLSCTFLPSRGILKYLKFHLRRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVHCHGGGSCKITVNSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTIVADVLAKFEKLAATSEVGEQPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHYPAPEENLQVLAALRLQYLQGDYAPHAPVPPLEEVYSLQRLKARISQSTKSFTPGERLEKRRTSFLEGTLRRSFRTGSAIRQKAEEEQMVDMWVKEEVCSARASILDKWKKFQGMSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQDLWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTSRSVSSQGSSR | ||||||
Modified residue | 963 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 966 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1152 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Detected in kidney, testis, liver, kidney, cerebellum and brain cortex (at protein level).
Interaction
Subunit
Monomer, when in an inactive conformation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts with NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility (By similarity).
Interacts with ITGB1, ITGB3 and ITGB5
Interacts with ITGB1, ITGB3 and ITGB5
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 63-739 | Myosin motor | ||||
Sequence: EGVDDMATLTELHGGAIMHNLYQRYKRNQIYTYIGSIIASVNPYKTITGLYSRDAVDRYSRCHLGELPPHVFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSAISQQSVDLSSKEKTSSVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIGQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLGHEEREEFYLSVPENYHYLNQSGCVTDRTISDQESFREVIMAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPAQLTDALTQRSMFLRGEEILTPLNVQQAADSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSASNPFFVRCIKPNMQKMPDQFDQAVVVNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNVALPEDIRGKCTALLQLYDASNSEWQLGKTKVFLRESLEQKLEKRQE | ||||||
Region | 619-641 | Actin-binding | ||||
Sequence: LHSLMATLSASNPFFVRCIKPNM | ||||||
Domain | 742-763 | IQ 1 | ||||
Sequence: VTRAAMVIRAHVLGYLARKQYK | ||||||
Domain | 764-787 | IQ 2 | ||||
Sequence: KVLDCVVIIQKNYRAFLLRRRFLH | ||||||
Domain | 788-817 | IQ 3 | ||||
Sequence: LKKAAVVFQKQLRGQIARRVYRQLLAEKRA | ||||||
Region | 814-884 | SAH | ||||
Sequence: EKRAEEEKRKREEEEKRKREEEERERERERREAELRAQQEEAARKQRELEALQQESQRAAELSRELEKQKE | ||||||
Region | 819-843 | Disordered | ||||
Sequence: EEKRKREEEEKRKREEEERERERER | ||||||
Coiled coil | 885-935 | |||||
Sequence: NKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEA | ||||||
Region | 964-1093 | Disordered | ||||
Sequence: VGSGCTGEQGAGAEKPSFNFSQPYPEEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDESSEEDPYMNDTVVPTSPSADSTVLLAPSEHDSSAGEPTYCLPQTPGALPAPEGDYDYDQDDYEDG | ||||||
Compositional bias | 1002-1031 | Basic and acidic residues | ||||
Sequence: DAFKDSPNPSEHGHSDQRTSGIRTSDESSE | ||||||
Compositional bias | 1036-1056 | Polar residues | ||||
Sequence: MNDTVVPTSPSADSTVLLAPS | ||||||
Domain | 1206-1304 | PH 1 | ||||
Sequence: EALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQAKLMYFENDSEEKLKGTVEVRAAKEIIDNTSKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHA | ||||||
Domain | 1386-1491 | PH 2 | ||||
Sequence: EFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTD | ||||||
Domain | 1541-1689 | MyTH4 | ||||
Sequence: LPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLCSWQILTCLSCTFLPSRGILKYLKFHLRRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALI | ||||||
Domain | 1694-2038 | FERM | ||||
Sequence: MTSTVHCHGGGSCKITVNSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTIVADVLAKFEKLAATSEVGEQPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHYPAPEENLQVLAALRLQYLQGDYAPHAPVPPLEEVYSLQRLKARISQSTKSFTPGERLEKRRTSFLEGTLRRSFRTGSAIRQKAEEEQMVDMWVKEEVCSARASILDKWKKFQGMSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQDLWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKR |
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 (PubMed:25122759).
It can refold after extension suggesting an in vivo force-dependent function (PubMed:25122759).
An anti-parallel coiled coil is located C-terminal to the SAH domain and mediates dimerization (PubMed:27276269, PubMed:27580874).
It can refold after extension suggesting an in vivo force-dependent function (PubMed:25122759).
An anti-parallel coiled coil is located C-terminal to the SAH domain and mediates dimerization (PubMed:27276269, PubMed:27580874).
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,052
- Mass (Da)235,839
- Last updated1997-05-01 v1
- Checksum43DF13424B4B2D28
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1002-1031 | Basic and acidic residues | ||||
Sequence: DAFKDSPNPSEHGHSDQRTSGIRTSDESSE | ||||||
Compositional bias | 1036-1056 | Polar residues | ||||
Sequence: MNDTVVPTSPSADSTVLLAPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U55042 EMBL· GenBank· DDBJ | AAB39486.1 EMBL· GenBank· DDBJ | mRNA |