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Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
cDNAs encoding the complement decay-accelerating factor (DAF) were isolated from HeLa and differentiated HL-60 lambdagt cDNA libraries by screening with a codon preference oligonucleotide corresponding to DAF NH/sub 2/-terminal amino acids 3-14. The composite cDNA sequence showed a 347-amino acid protein preceded by an NH/sub 2/-terminal leader peptide sequence. The translated sequence beginning at the DAF NH/sub 2/ terminus encodes four contiguous approx. = 61-amino acid long repetitive units of internal homology. The repetitive regions contain four conserved cysteines, one proline, one glycine, one glycine/alanine, four leucines/isoleucines/valines, one serine, three tyrosines/phenylalanines, and on tryptophan and show striking homology to similar regions previously identified in factor B, C2, C4 binding protein, factor H, C1r, factor XIII, interleukin 2 receptor, and serum ..beta../sub 2/-glycoprotein I. The consensus repeats are attached to a 70-amino acid long segment rich in serine and threonine (potential O-glycosylation sites), which is in turn followed by a stretch of hydrophobic amino acids. RNA blot analysis of HeLa and HL-60 RNA revealed three DAF mRNA species of 3.1, 2.7, and 2.0 kilobases. The results indicate that portions of the DAF gene may have evolved from a DNA element common to the above proteins, that DAF cDNA predicts a COOH-terminal anchoring polypeptide, and that distinct species of DAF message are elaborated in cells.
Research Organization:
Case Western Reserve Univ., Cleveland, OH
OSTI ID:
6027580
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 84:7; ISSN PNASA
Country of Publication:
United States
Language:
English