Abstract
Drosophila projectin is an extremely large protein found within the muscle sarcomeric unit, parallel with the actin and myosin filaments. Projectin has been suggested as the elastic component of C-filaments in insect indirect flight muscles, which is consistent with its localization from the Z band to the tip of the A band in these muscles. Here, we describe the completion of the projectin sequence analysis, which defines projectin as a 1 MDa protein, composed of 39 immunoglobulin and 39 fibronectin III domains. This analysis led also to the identification of a domain rich in the amino acids P, E, V and K within the NH(2) terminus of projectin. The length of the projectin PEVK-like region varies from 100 to 624 amino acid residues, following a complex pattern of alternative splicing events. PEVK domains were first identified in vertebrate titin and they have been associated with the elasticity of the protein. The PEVK-like domain of the projectin isoforms in indirect flight muscles may contribute to the elastic function of the C-filaments. The synchronous projectin isoforms contain a PEVK-like region, and the possible non-elastic function(s) of this domain in synchronous muscles are discussed.
