Force generating protein required for cilia beating in respiratory epithelia (PubMed:30471717, PubMed:30471718). 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. Consists of at least two heavy chains and a number of intermediate and light chains. Interacts with ODAD1 (PubMed:30471718). Found in the distal portion of ciliary axoneme. Expressed in upper and lower respiratory airway epithelia (at protein level). Not detected in spermatozoa (at protein level) (PubMed:31178125). 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. The disease is caused by variants affecting the gene represented in this entry. Belongs to the dynein heavy chain family.