Primary Information |
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| BoMiProt ID | Bomi262 |
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| Protein Name | Dynein assembly factor 1, axonemal |
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| Organism | Bos taurus |
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| Uniprot ID | Q3SYS4 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001030422.2 |
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| Aminoacid Length | 643 |
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| Molecular Weight | 71786 |
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| FASTA Sequence |
Download |
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| Gene Name | DNAAF1 |
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| Gene ID | 523187 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | cytoskeletal motor protein; hexameric rings that unfold proteins, dismantle DNA and RNA duplexes and pry apart
macromolecular complexes and aggregates |
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| Biochemical Properties | dynein belongs to the AAA+ superfamily
(ATPases associated with diverse activities); has a ring of six AAA+ modules at its core but, unusually, these are linked together into one
large polypeptide, along with several unique appendages that enable motor function; operate as protein complexes built around force-generating subunits called heavy
chains; Each
heavy chain contains a motor domain that belongs to the AAA+ superfamily attached to a
divergent amino-terminal tail domain; The tail specifies distinct oligomerization
properties and serves as a platform for the binding of several types of associated subunit, which in turn mediate interactions with cargo either via direct binding or through
the recruitment of adaptor proteins; |
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| Significance in milk | associated
with microtubules and actin and
involved in the binding and movement of
vesicular cargoes, have been found in isolated MFGMs and mammary lipid droplets |
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| PTMs | tubulin glutamylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | 1-85,332-405,537-643 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | tubulin glutamylation is present on microtubles that regulate ciliary motility |
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| Bibliography | 1. Neuwald, A. F., Aravind, L., Spouge, J. L., & Koonin, E. V. (1999). AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Research, 9(1), 27–43. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/9927482.
2. GIBBONS, I. R. (1963). STUDIES ON THE PROTEIN COMPONENTS OF CILIA FROM TETRAHYMENA PYRIFORMIS. Proceedings of the National Academy of Sciences of the United States Of, 50, 1002–1010. https://doi.org/10.1073/pnas.50.5.1002. |
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