Plays a central role in nuclear and mitochondrial anchoring (PubMed:12169658, PubMed:6889924, PubMed:10375507, PubMed:22298703). Probably connects nuclei to the cytoskeleton by interacting with unc-84 at the nuclear envelope and with F-actin in the cytoplasm, creating a bridge across the nuclear envelope between the cytoskeleton and the nucleus (PubMed:15773756). Has a role in positioning of the cell body of the PVQ lumbar interneuron (PubMed:22298703). Interacts with F-actin via its N-terminal domain. Most likely interacts with unc-84; the interaction is probably required to recruit anc-1 to the nuclear envelope. The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, most probably the outer nuclear membrane, or with mitochondrial membrane. Ubiquitously expressed in all postembryonic cells. First expressed in L1 larvae, and thereafter throughout adulthood. The large coiled coil domains are composed of 6 nearly exact repeats of 903 residues. The last repeat is partial. These repeats are conserved in Hawai (CB4856), Australia (AB4) and Germany (RC301) strains. The length of the repeat may be maintained because of a selective advantage to keep the protein large and allow a single molecule to extent more than 0,5 micrometers. The KASH domain, which contains a potential transmembrane domain, is essential for the nuclear envelope targeting. Nuclear anchorage is lost resulting in free-floating nuclei that often cluster as the animal flexes. An increase in PVQ cell bodies mispositioned to the anterior is apparent between three-fold embryos and L1 larvae. Pharyngeal cells show defects including mispositioned organelles. Belongs to the nesprin family.