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J. Biol. Chem., Vol. 261, Issue 15, 6878-6887, 05, 1986
K Drickamer, MS Dordal and L Reynolds
Preparations of mannose-binding protein isolated from rat liver contain two
distinct but homologous polypeptides. The complete primary structures of
both of these polypeptides have been determined by sequencing of peptides
derived from the proteins, isolation and sequencing of cDNAs for both
proteins, and partial characterization of the gene for one of the proteins.
Each polypeptide consists of three regions: (a) an NH2-terminal segment of
18-19 amino acids which is rich in cysteine and appears to be involved in
the formation of interchain disulfide bonds which stabilize dimeric and
trimeric forms of the protein, (b) a collagen-like domain consisting of
18-20 repeats of the sequence Gly-X-Y and containing 4-hydroxyproline
residues in several of the Y positions, and (c) a COOH-terminal
carbohydrate-binding domain of 148-150 amino acids. The sequences of the
COOH-terminal domains are highly homologous to the sequence of the
COOH-terminal carbohydrate- recognition portion of the chicken liver
receptor for N- acetylglucosamine-terminated glycoproteins and the rat
liver asialoglycoprotein receptor. Each protein is preceded by a cleaved,
NH2- terminal signal sequence, consistent with the finding that this
protein is found in serum as well as in the liver. The entire structure of
the mannose-binding proteins is homologous to dog pulmonary surfactant
apoprotein.
Mannose-binding proteins isolated from rat liver contain carbohydrate- recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
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