| ID | Sequence | Length | GC content |
|---|---|---|---|
| CUUCGGGCGCUGACAGGGAGAGCCUGGGGCCGGGCCGUGUGGAUGCCAU… | 822 nt | 0.5195 | |
| AGAUGCGCCACGGUUUCGGUAGCGACGGUAUCUCUAGCCGGGCCUGAGC… | 677 nt | 0.4668 | |
| AGAUGCGCCACGGUUUCGGUAGCGACGGUAUCUCUAGCCGGGCCUGAGC… | 663 nt | 0.4630 |
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. [provided by RefSeq, Jul 2008]
A study in mice demonstrated that the DYNLL1 was notably upregulated in excitatory neurons in post-mortem brain tissues stored for 24 to 54 hours, where it is involved in neuronal projection development and synaptic vesicle endocytosis and physically interacts with neuronal nitric oxide synthase [Guo et al. DOI:10.1016/j.ijbiomac.2025.147708]. A study in mice demonstrated that the DYNLL1 is a marker for electrophysiologically associated cardiomyocytes, as it is highly expressed in the ventricular cardiomyocyte cluster vCM5 following myocardial infarction [Bian et al. DOI:10.3892/mmr.2025.13680].