DNAH3
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 (By similarity).
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 (By similarity).
Sequence Similarities
Belongs to the dynein heavy chain family.
Tissue Specificity
Expressed primarily in trachea and testis, 2 tissues containing axonemal structures. Also expressed in lung.
Cellular localization
- Cytoplasm
- Cytoskeleton
- Cilium axoneme
Alternative names
DNAHC3B, DNAH3, Dynein axonemal heavy chain 3, Axonemal beta dynein heavy chain 3, Ciliary dynein heavy chain 3, Dnahc3-b, HsADHC3