Search by BoMiProt ID - Bomi262


Primary Information

BoMiProt ID Bomi262
Protein Name Dynein assembly factor 1, axonemal
Organism Bos taurus
Uniprot IdQ3SYS4
Milk FractionExosome
Ref Sequence Id NP_001030422.2
Amino Acid Lenth 643
Molecular Weight 71786
Fasta Sequence https://www.uniprot.org/uniprot/Q3SYS4.fasta
Gene Name DNAAF1
Gene Id 523187
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Protein Function cytoskeletal motor protein; hexameric rings that unfold proteins, dismantle DNA and RNA duplexes and pry apart macromolecular complexes and aggregates
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;
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
PTMs tubulin glutamylation
Significance of PTMs tubulin glutamylation is present on microtubles that regulate ciliary motility
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.