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Fig. 1. Structural features of human tenomodulin (TeM) and the human chondromodulin-I (ChM-I) precursor proteins deduced from their cDNA sequences. Analysis of primary amino acid sequences reveals several structural features in the putative TeM protein. These include a type II transmembrane domain at the N terminus, a BRICHOS domain and a cysteine-rich domain (Sanchez-Pulido et al., 2002). The TeM protein contains two N-glycosylation sites within the BRICHOS domain. The highest homology with the ChM-I precursor was scored in the cysteine-rich domain at the C terminus (Sachdev et al., 2001; Shukunami et al., 2001).





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