- histone H3T45 kinase activity
Catalysis of the reaction: histone H3-threonine (position 45) + ATP = histone H3-phosphothreonine (position 45) + ADP. This reaction is the addition of a phosphate group to the threonine residue at position 45 of histone H3.
- granular vesicle
A cytoplasmic membrane-bounded vesicle of varying size, but usually larger than 45 nm, with an electron dense granular core, found in noradrenergic and peptidergic cells.
- neuropeptide F receptor activity
Combining with neuropeptide F and transmitting the signal within the cell to initiate a change in cell activity. Neuropeptide F is an arthropod peptide of more than 28 residues (typically 28-45) with a consensus C-terminal RxRFamide (commonly RPRFa, but also RVRFa.
- pattern orientation
The actions or reactions of an individual in response to the orientation of a visual pattern. This is exemplified by some classes of insects which are able to detect and learn the orientation of a set of stripes and subsequently behaviorally discriminate between horizontal, vertical or 45 degree stripes.
- Ecsit-NDUFAF1 complex
Any large protein complex that contains Ecsit and NDUFAF1, is located in the mitochondrion, and is involved in the assembly of complex I of the oxidative phosphorylation system. In mammalian cells, three complexes of approximately 500, 600, and 850 kDa containing the 45 kDa isoform of Ecsit and NDUFAF1 have been observed.
- defecation rhythm
The rhythmic process of defecation that consists of an intestinal oscillator which regulates calcium waves. These waves in turn control a stereotypical, three-part pattern of muscle contractions. In some organisms, defecation can recur with a regularity more frequent than every 24 hours. For example, in a well-fed Caenorhabditis elegans, the defecation motor program occurs approximately every 45 seconds, and is temperature- and touch-compensated.
- LIM domain binding
Binding to a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions.
- nuclear pore central transport channel
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.