LASP1 encompasses 51.65 kb on the genomic level and consists of 7 exons

3845 bp mRNA, 783 bp coding sequence

261 amino acids; 29 kDa. LASP1 encodes a member of a LIM (Lin-11, Isl-1 and Mec-3) protein subfamily and is characterized by a LIM motif (cysteine-rich LIM/double zinc finger motif) at the N-terminus, an SH3 domain (Src homology region 3) at the C-terminus, and two actin-binding domains in the core of the protein

ubiquitous

intracellular, cytoplasmic; associated with the F-actin rich cortical cytoskeleton

LASP1 plays an important role in the regulation of dynamic actin-based, cytoskeletal activities and cell motility. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types. Together, (LIM-) nebulette, Lasp-1, and zyxin may play an important role in the organization of focal adhesions.

LASP family of proteins: actin-binding repeats similar to those in LASP1 are also present in other nebulin-related proteins such as NEBL (nebulette, 107 kD actin-binding Z-disk protein) and NRAP (nebulin-related anchoring protein); NRAP also contains an N-terminal LIM domain and NEB (nebulin) a C-terminal SH3 domain, both of which are highly homologous to the respective domains of LASP1.