P79114 · MYO10_BOVIN

  • Protein
    Unconventional myosin-X
  • Gene
    MYO10
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).

Features

Showing features for binding site.

120522004006008001,0001,2001,4001,6001,8002,000
TypeIDPosition(s)Description
Binding site104ATP (UniProtKB | ChEBI)
Binding site113ATP (UniProtKB | ChEBI)
Binding site160-165ATP (UniProtKB | ChEBI)
Binding site215ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell cortex
Cellular Componentcytosol
Cellular Componentfilopodium
Cellular Componentfilopodium membrane
Cellular Componentfilopodium tip
Cellular Componentlamellipodium
Cellular Componentmyosin complex
Cellular Componentruffle
Molecular Functionactin filament binding
Molecular FunctionATP binding
Molecular Functioncalmodulin binding
Molecular Functionmicrofilament motor activity
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate binding
Molecular Functionplus-end directed microfilament motor activity
Biological Processcytoskeleton-dependent intracellular transport
Biological Processregulation of cell shape
Biological Processregulation of filopodium assembly
Biological Processsignal transduction

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Unconventional myosin-X
  • Alternative names
    • Unconventional myosin-10

Gene names

    • Name
      MYO10

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P79114

Proteomes

Subcellular Location

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

Phenotypes & Variants

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00001234721-2052Unconventional myosin-X
Modified residue963Phosphoserine
Modified residue966Phosphoserine
Modified residue1152Phosphothreonine

Keywords

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

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for domain, region, coiled coil, compositional bias.

TypeIDPosition(s)Description
Domain63-739Myosin motor
Region619-641Actin-binding
Domain742-763IQ 1
Domain764-787IQ 2
Domain788-817IQ 3
Region814-884SAH
Region819-843Disordered
Coiled coil885-935
Region964-1093Disordered
Compositional bias1002-1031Basic and acidic residues
Compositional bias1036-1056Polar residues
Domain1206-1304PH 1
Domain1386-1491PH 2
Domain1541-1689MyTH4
Domain1694-2038FERM

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).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,052
  • Mass (Da)
    235,839
  • Last updated
    1997-05-01 v1
  • Checksum
    43DF13424B4B2D28
MDNFFPEGTRVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITHQKVMPMQPTDEEGVDDMATLTELHGGAIMHNLYQRYKRNQIYTYIGSIIASVNPYKTITGLYSRDAVDRYSRCHLGELPPHVFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSAISQQSVDLSSKEKTSSVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIGQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLGHEEREEFYLSVPENYHYLNQSGCVTDRTISDQESFREVIMAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPAQLTDALTQRSMFLRGEEILTPLNVQQAADSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSASNPFFVRCIKPNMQKMPDQFDQAVVVNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNVALPEDIRGKCTALLQLYDASNSEWQLGKTKVFLRESLEQKLEKRQEEEVTRAAMVIRAHVLGYLARKQYKKVLDCVVIIQKNYRAFLLRRRFLHLKKAAVVFQKQLRGQIARRVYRQLLAEKRAEEEKRKREEEEKRKREEEERERERERREAELRAQQEEAARKQRELEALQQESQRAAELSRELEKQKENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSGCTGEQGAGAEKPSFNFSQPYPEEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDESSEEDPYMNDTVVPTSPSADSTVLLAPSEHDSSAGEPTYCLPQTPGALPAPEGDYDYDQDDYEDGAITSGSSVTFSNSCSSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQAKLMYFENDSEEKLKGTVEVRAAKEIIDNTSKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRHTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLCSWQILTCLSCTFLPSRGILKYLKFHLRRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVHCHGGGSCKITVNSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTIVADVLAKFEKLAATSEVGEQPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHYPAPEENLQVLAALRLQYLQGDYAPHAPVPPLEEVYSLQRLKARISQSTKSFTPGERLEKRRTSFLEGTLRRSFRTGSAIRQKAEEEQMVDMWVKEEVCSARASILDKWKKFQGMSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQDLWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTSRSVSSQGSSR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1002-1031Basic and acidic residues
Compositional bias1036-1056Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U55042
EMBL· GenBank· DDBJ
AAB39486.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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