E7F9L8 · MYO1D_DANRE
- ProteinUnconventional myosin-Id
- Genemyo1d
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1004 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity).
Plays a role in the formation of Kupffer's vesicle, an organ that functions as a left-right organizer during embryogenesis (PubMed:29769531, PubMed:30139971).
Plays a role in vesicular trafficking events that are required for normal lumen expansion of Kupffer's vesicle (PubMed:30139971).
Required for normal orientation of cilia in Kupffer's vesicle, and thus for normal, unidirectional circular flow and normal angular flow velocity, which then mediates asymmetric gene expression and left-right asymmetric development (PubMed:29769531).
Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity).
Required for normal planar cell polarity in ciliated cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement (By similarity).
Plays a role in the formation of Kupffer's vesicle, an organ that functions as a left-right organizer during embryogenesis (PubMed:29769531, PubMed:30139971).
Plays a role in vesicular trafficking events that are required for normal lumen expansion of Kupffer's vesicle (PubMed:30139971).
Required for normal orientation of cilia in Kupffer's vesicle, and thus for normal, unidirectional circular flow and normal angular flow velocity, which then mediates asymmetric gene expression and left-right asymmetric development (PubMed:29769531).
Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity).
Required for normal planar cell polarity in ciliated cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement (By similarity).
Miscellaneous
Agents that activate cftr increase the size of Kupffer's vesicle in myo1d mutants (PubMed:29769531, PubMed:30139971).
Expansion of the lumen size is not sufficient to restore the normal spherical shape of Kupffer's vesicle and rescue laterality defects (PubMed:29769531, PubMed:30139971).
Heterologous expression of rat Myo1d can complement the defects in Kupffer's vesicle lumen size and anterior-posterior cell shape changes (PubMed:30139971).
Expansion of the lumen size is not sufficient to restore the normal spherical shape of Kupffer's vesicle and rescue laterality defects (PubMed:29769531, PubMed:30139971).
Heterologous expression of rat Myo1d can complement the defects in Kupffer's vesicle lumen size and anterior-posterior cell shape changes (PubMed:30139971).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cell cortex | |
Cellular Component | cytoplasm | |
Cellular Component | dendrite | |
Cellular Component | early endosome | |
Cellular Component | extracellular region | |
Cellular Component | microvillus | |
Cellular Component | myosin complex | |
Cellular Component | perikaryon | |
Cellular Component | plasma membrane | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | microfilament motor activity | |
Biological Process | actin filament organization | |
Biological Process | actin filament-based movement | |
Biological Process | determination of liver left/right asymmetry | |
Biological Process | determination of pancreatic left/right asymmetry | |
Biological Process | endocytosis | |
Biological Process | epithelial cilium movement involved in determination of left/right asymmetry | |
Biological Process | establishment of left/right asymmetry | |
Biological Process | heart jogging | |
Biological Process | Kupffer's vesicle development | |
Biological Process | protein transport |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-Id
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionE7F9L8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane. Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Morpholino knockdown of the protein causes situs inversus, a left-right asymmetry defect where organs are placed at a position corresponding to the mirror image of the normal body plan. Causes laterality defects at the level of the heart, viscera and brain (PubMed:29769531).
Morpholino knockdown of the protein leads to the formation of a Kupffer's vesicle with reduced volume and dismorphic shape. Morpholino knockdown of the protein interferes with the normal cellular remodeling that gives rise to anterior-posterior asymmetry of Kupffer's vesicle. Cells with a columnar shape persist at the posterior end of the vesicle, contrary to wild-type, where cells display columnar shape at the anterior part of the vesicle, and squamous or cuboidal shape at the posterior end of Kupffer's vesicle. Epithelial cells lining Kupffer's vesicle display an increased number of vacuoles, and disruption of the normal, directed vacuolar trafficking toward the apical cell membrane (PubMed:30139971).
Morpholino knockdown of the protein leads to the formation of a Kupffer's vesicle with reduced volume and dismorphic shape. Morpholino knockdown of the protein interferes with the normal cellular remodeling that gives rise to anterior-posterior asymmetry of Kupffer's vesicle. Cells with a columnar shape persist at the posterior end of the vesicle, contrary to wild-type, where cells display columnar shape at the anterior part of the vesicle, and squamous or cuboidal shape at the posterior end of Kupffer's vesicle. Epithelial cells lining Kupffer's vesicle display an increased number of vacuoles, and disruption of the normal, directed vacuolar trafficking toward the apical cell membrane (PubMed:30139971).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446322 | 1-1004 | Unconventional myosin-Id | |||
Sequence: MAEHESLEFGKADFVLLDNVSLEEFMANLKLRFEKGRIYSYIGEVVVSVNPYRAMNIYGRDVIEQYKGRELYERPPHLFAIADAAYKAMKRRNKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIFQQEGERSFHSFYQLVKGAPDAQLRSLHIQRDPTAYNYIKVGGQLKSSINDSAEFKAVADAMKVIGFTTEEIQTVYKILATILHLGNLKFGTDGDVTLIENSKLVSVLGDLLSTKEENVEKAMLYRTVATGRDVIDKQHTHQEASYGRDALAKAIYERLFCWIVGRINDIIEVKNYDARVHGKNTVIGVLDIYGFEIFQNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIFAVLDEACMNVGKVTDEMFLQALNGKLAKHAHYTSRKLSPTDKNLEFERDFRIRHYAGDVTYSVVGFIDKNKDTLFQDFKRLLYNSSNPVLKAMWPEGKLSITEVTKRPLTAATLFKNSMISLVEKLASKEPYYVRCIKPNDVKSPLLFEHERCKHQVEYLGLLENVRVRRAGFANRQTYPRFLQRYKMISEFTWPNHDLSSDKEAVKRLLQGCGFEHDVAYGKTKVFIRTPRTIFSLEEQRAEMVKRIVLFLQKVWRGTLARMRYRRMRAALIIIRAYRRYKVKSYIREVIRRFKNVRDMKDHGKHVKWPTPPKVLRKFEEALRSIYNRWWAWTLIKPLSPEKTVQIRAKVATLECLKGQRADLGLQRAWEGNYLKKDSPGTASSFTLVSSDLQRKDKFMRVLFSSNVRKINRFNKAEDRALLITDRHLYKMDPLKQYKPMKSIPLYNVTGVSISPGKDQLVVFHTKDNRDLIVCLQGMVPAGDSRIGELVGTLLSHFKSEKRKLQVNTVSPIHCSMNGRKCTVVVETKISQSQPDFTKSRSGYILSVPGN |
Proteomic databases
Expression
Developmental stage
Expressed both maternally and zygotically (PubMed:29769531).
Ubiquitous in embryos at the four cell stage (PubMed:30139971).
Detected at the eight cell stage. Detected at low levels throughout the embryo at the six somite stage, with higher levels in the developing notochord (PubMed:29769531).
Ubiquitous in embryos at the four cell stage (PubMed:30139971).
Detected at the eight cell stage. Detected at low levels throughout the embryo at the six somite stage, with higher levels in the developing notochord (PubMed:29769531).
Gene expression databases
Interaction
Subunit
Interacts (via the two IQ motifs) with calmodulin. Interacts with F-actin.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-695 | Myosin motor | ||||
Sequence: FGKADFVLLDNVSLEEFMANLKLRFEKGRIYSYIGEVVVSVNPYRAMNIYGRDVIEQYKGRELYERPPHLFAIADAAYKAMKRRNKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIFQQEGERSFHSFYQLVKGAPDAQLRSLHIQRDPTAYNYIKVGGQLKSSINDSAEFKAVADAMKVIGFTTEEIQTVYKILATILHLGNLKFGTDGDVTLIENSKLVSVLGDLLSTKEENVEKAMLYRTVATGRDVIDKQHTHQEASYGRDALAKAIYERLFCWIVGRINDIIEVKNYDARVHGKNTVIGVLDIYGFEIFQNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIFAVLDEACMNVGKVTDEMFLQALNGKLAKHAHYTSRKLSPTDKNLEFERDFRIRHYAGDVTYSVVGFIDKNKDTLFQDFKRLLYNSSNPVLKAMWPEGKLSITEVTKRPLTAATLFKNSMISLVEKLASKEPYYVRCIKPNDVKSPLLFEHERCKHQVEYLGLLENVRVRRAGFANRQTYPRFLQRYKMISEFTWPNHDLSSDKEAVKRLLQGCGFEHDVAYGKTKVFIRTPRTIFSLEEQRA | ||||||
Region | 572-594 | Actin-binding | ||||
Sequence: MISLVEKLASKEPYYVRCIKPND | ||||||
Domain | 699-719 | IQ 1 | ||||
Sequence: KRIVLFLQKVWRGTLARMRYR | ||||||
Domain | 721-741 | IQ 2 | ||||
Sequence: MRAALIIIRAYRRYKVKSYIR | ||||||
Domain | 812-1003 | TH1 | ||||
Sequence: GQRADLGLQRAWEGNYLKKDSPGTASSFTLVSSDLQRKDKFMRVLFSSNVRKINRFNKAEDRALLITDRHLYKMDPLKQYKPMKSIPLYNVTGVSISPGKDQLVVFHTKDNRDLIVCLQGMVPAGDSRIGELVGTLLSHFKSEKRKLQVNTVSPIHCSMNGRKCTVVVETKISQSQPDFTKSRSGYILSVPG |
Domain
Binds a calmodulin chain via each of the two IQ domains. IQ domain 1 mediates interaction with calmodulin both in the presence and in the absence of Ca2+. IQ domain 2 mediates interaction with calmodulin in the presence of Ca2+.
The TH1 domain is required for activity in complementing zebrafish defects in Kupffer's vesicle lumen size.
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,004
- Mass (Da)115,885
- Last updated2011-03-08 v1
- Checksum77990A4B7D4C2754
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR391936 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT033798 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT033800 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |