Extracellular and intracellular functions of coiled-coil domain containing 3

Abstract

Coiled-coil domain containing 3 (CCDC3, also called favine) is a highly conserved protein initially identified as a protein secreted from adipocytes and endothelial cells (ECs) in the vascular system with endocrine-like functions. Recently, CCDC3 was also found to function as a nuclear tumor suppressor in breast cancers (BrCs). Although it is still understudied, CCDC3, since its discovery, has been shown to play multiple roles in lipid metabolism, fatty liver, abdominal obesity, anti-inflammation, atherosclerosis, and cancer. This essay is thus composed to offer an overview of these extracellular endocrine-like and intracellular (nuclear) functions of CCDC3. We will also discuss the possible underlying cellular and molecular mechanisms of CCDC3, their implications for clinical translation, and the remaining puzzles about this special molecule.

Cloning grass carp (Ctenopharyngodon idella) ccdc3 and its expression affected by nutrition state, insulin, and glucagon

“…CCDC3 is a member of the coiled-coil domain containing (CCDC) family. The key region in all CCDC members is the coiled-coil motif (Omari et al, 2023). The grass carp Ccdc3 protein in the present study contained a predicted coiled-coil motif in the C terminal.…”

“…The Ccdc3 protein contained a signal peptide of 16 amino acids and a mature protein of 260 amino acids. The grass carp Ccdc3 protein structure is similar to that of mammals, which contains the N-terminus secretory signal peptide sequence (Omari et al, 2023). As a secretory protein, CCDC3 is secreted from the vascular system and adipose tissue (Kobayashi et al, 2010).…”

“…A previous study showed that the CCDC3 protein contains two predicted N-glycosylation sites (Kobayashi et al, 2010). In addition, CCDC3 protein in mice was experimentally verified to be N-glycosylation through the transfection of CCDC3 gene into COS-7 cells (Kobayashi et al, 2010;Omari et al, 2023). Grass carp Ccdc3 protein has three predicted N-glycosylation sites.…”

“…Grass carp Ccdc3 protein has three predicted N-glycosylation sites. N-glycosylation is associated with proliferative, secretory, and apoptotic functions (Kukuruzinska & Lennon, 1998;Omari et al, 2023). It is suggested that N-glycosylation of grass carp Ccdc3 may play a role in these functions.…”

“…The grass carp Ccdc3 protein in the present study contained a predicted coiled-coil motif in the C terminal. The coiledcoil motif is a ubiquitous biological functional motif in proteins (Li et al, 2023;Omari et al, 2023). It has multiple biological functions in protein refolding, structural integrity, and molecular recognition (Burkhard et al, 2001;Omari et al, 2023).…”