Dyneins are microtubule-associated motor protein complexes composed of several heavy, light, and intermediate chains. The axonemal dyneins, found in cilia and flagella, are components of the outer and inner dynein arms attached to the peripheral microtubule doublets. DNAH2 is an axonemal inner arm dynein heavy chain (Chapelin et al., 1997 [PubMed 9256245]).[supplied by OMIM, Mar 2008],
show all
Function:
Domain:Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.,Function:Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly.,similarity:Belongs to the dynein heavy chain family.,similarity:Contains 5 LRR (leucine-rich) repeats.,similarity:Contains 5 TPR repeats.,subunit:Consists of at least two heavy chains and a number of intermediate and light chains.,tissue specificity:Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in lung.,
Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in lung. Expressed in spermatozoa (at protein level) (PubMed:31178125).