Title : The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain
Abstract :
- The complete primary structure of the human type IV collagen alpha 2(IV ) chain has been determined by nucleotide sequencing of cDNA clones
- The overlapping cDNA clones cover 6,257 base pairs with a 5'-untranslated region of 283 base pairs, the 5,136-base pair open reading frame, and the 3'-untranslated region of 838 base pairs
- The predicted amino acid sequence demonstrates that the complete translation product consists of 1,712 residues corresponding in molecular weight to 167,560
- The translated polypeptide has a signal peptide of 36 amino acids, an amino-terminal noncollagenous part of 21 residues , a 1,428-residue collagenous domain with 23 interruptions, and a carboxyl-terminal noncollagenous (NC) domain of 227 residues
- The calculated molecular mass of the mature human alpha 2(IV) chain is 163,774 Da