This entry represents a domain found in nuclear migration protein nudC, which is implicated in cell division through the regulation of cytoplasmic dynein [, ]. NudC may play a role not only in mitosis and cytokinesis [], but also in interkinetic nuclear migration and neuronal migration during neocortical development [].
This family includes NudC (nuclear distribution gene C), NudC-like (NudCL) [], NudC-like 2/NudC domain-containing protein 2 (NudCL2/NUDCD2)[], NudC domain-containing protein 3, and NudC domain protein BOBBER from plants []. All members of the NudC family share a conserved p23 domain, which possesses chaperone activity both in conjunction with and independently of heat shock protein 90 (Hsp90) []. NudC proteins play multiple roles in cell cycle progression, cell migration, inflammatory response, platelet production, carcinogenesis [, ].
This entry represents NAD-capped RNA hydrolase NudC from bacteria. NudC is a mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolysing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. This enzyme has preference for mRNAs with a 5'-end purine and catalyses the hydrolysis of a broad range of dinucleotide pyrophosphates. NudC assemblies into a homodimer with the appearance of a butterfly. Each monomer shows two tandem Nudix-fold domains, a N-terminal and a C-terminal, and an extended zinc-binding motif in-between. As a subgroup of the Nudix hydrolase family, NudC has a conserved Nudix motif [, ].
Proteins in this family contain the NudC domain. They share protein sequence similarity with Aspergillus NudC, which is required for nuclear movement [].
Nuclear distribution gene C homologue (nudC) proteins form complexes with other nud proteins and are involved in several cellular division activities. Recently it was shown that nudC regulates platelet-activating factor (PAF) acetylhydrolase with PAF being a pro-inflammatory secondary lipidic messenger []. The N terminus of nudC proteins contain a highly conserved region consisting of a predicted three helix bundle. This entry represents the N-terminal conserved domain.
NudC domain-containing protein 3 (NUDCD3) has not been characterised. It is a member of the NudC family. All members of the NudC family share a conserved p23 domain, which possesses chaperone activity both in conjunction with and independently of heat shock protein 90 (Hsp90) []. NudC proteins play multiple roles in cell cycle progression, cell migration, inflammatory response, platelet production, carcinogenesis [].
NudCD1, also known as CML66 or OVA66, belongs to the NudC family, whose members share a conserved p23 domain. It is the more distant and less characterised family member. NudCD1 is a tumour associated antigen highly expressed in human leukaemia, some solid tumours and tumour cell lines []. Its expression in normal tissues is restricted to testis [, ]. Different NudCD1 isoforms have unique interacting partners, with the first isoform binding to a putative RNA helicase named DHX15 involved in mRNA splicing [].
NudC-like 2/NudC domain-containing protein 2 (NudCL2/NUDCD2) regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. LIS1 is a key regulator of cytoplasmic dynein, and is critical for cell proliferation, survival, and neuronal migration []. Like other members of the NudC family, NUDCD2 has a conserved p23 domain, which possesses chaperone activity both in conjunction with and independently of Hsp90 [, ]. This entry represents the p23 domain of NUDCD2.
