UniProt functional annotation for P36022

UniProt code: P36022.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Function: Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle. {ECO:0000269|PubMed:15642746}.
Subunit: The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN3. {ECO:0000269|PubMed:15642746}.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15642746}. Note=Concentrates at motile dots in the cytoplasm corresponding to the plus ends of cytoplasmic microtubules.
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.
Miscellaneous: Present with 195 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
Similarity: Belongs to the dynein heavy chain family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.