The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to M-band constituents of apparent molecular masses of 190 kD (myomesin 1) and 165 kD (myomesin 2). This protein, myomesin 1, like myomesin 2, titin, and other myofibrillar proteins contains structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin 1 and myomesin 2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. The integrating structure of the sarcomere arises from muscle-specific members of the superfamily of immunoglobulin-like proteins. Alternatively spliced transcript variants encoding different isoforms have been identified.
MYOM1; myomesin 1, 185kDa; myomesin 1 (skelemin) (185kD) , myomesin 1 (skelemin) 185kDa; myomesin-1; skelemin; EH-myomesin; myomesin family member 1; myomesin 1 (skelemin) 185kDa; myomesin (M-protein) 1 (190kD); 190 kDa titin-associated protein; 190 kDa; 190 kDa connectin-associated protein; MGC134946; MGC134947; myomesin 1