Primary Information |
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| BoMiProt ID | Bomi307 |
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| Protein Name | Myosin-Id |
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| Organism | Bos taurus |
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| Uniprot ID | Q17R14 |
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| Milk Fraction | Whey, MFGM, Exosome |
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| Ref Sequence ID | NP_001069306.1 |
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| Aminoacid Length | 1006 |
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| Molecular Weight | 115939 |
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| FASTA Sequence |
Download |
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| Gene Name | MYO1D |
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| Gene ID | 522967 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | found in a wide range of tissues, but highly
expressed in the nervous system |
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| Protein Function | plays a role in
membrane trafficking, control of membrane tension and the establishment of left-right asymmetry during Drosophila development; important role in nervous system
tissues; enriched component of the myelin proteome |
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| Biochemical Properties | monomeric actin-based motor; bind directly to acidic
phospholipids via a C-terminal basic domain; presence of two IQ motifs that bind calmodulin in rat myosin 1d; Myo1d ATPase activity is regulated by its light chain binding
domain and the associated light chain CaM; CaM
binds in a cooperative manner to the light chain binding
domain of Myo1d |
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| Significance in milk | Cytoskeletal proteins; found increased during infection |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Köhler, D., Struchholz, S. and Bähler, M. (2005) ‘The two IQ-motifs and Ca2+/calmodulin regulate the rat myosin 1d ATPase activity’, FEBS Journal, 272(9), pp. 2189–2197. doi: 10.1111/j.1742-4658.2005.04642.x.
2. Benesh, A. E. et al. (2012) ‘Expression and localization of myosin-1d in the developing nervous system’, Brain Research, 1440, pp. 9–22. doi: 10.1016/j.brainres.2011.12.054. |
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