Molecular cloning of a human serum protein structurally related to complement factor H

C Skerka, RD Horstmann, PF Zipfel - Journal of Biological Chemistry, 1991 - Elsevier
C Skerka, RD Horstmann, PF Zipfel
Journal of Biological Chemistry, 1991Elsevier
Two cDNA clones termed H36-1 and H36-2 were isolated from a human liver cDNA library.
Clone H36-1 appears to represent the recently isolated human serum proteins h37 and h42,
which are two differently glycosylated forms of a protein antigenically related to human
complement factor H. The H36-1 deduced protein sequence is 327 amino acid long and
possesses a leader sequence. The secreted part of the protein is comprised of five tandem
repeating units, termed short consensus repeats (SCRs). SCR 1 and 2 display high …
Two cDNA clones termed H36-1 and H36-2 were isolated from a human liver cDNA library. Clone H36-1 appears to represent the recently isolated human serum proteins h37 and h42, which are two differently glycosylated forms of a protein antigenically related to human complement factor H. The H36-1 deduced protein sequence is 327 amino acid long and possesses a leader sequence. The secreted part of the protein is comprised of five tandem repeating units, termed short consensus repeats (SCRs). SCR 1 and 2 display high homology to the corresponding region of the recently isolated murine factor H-related cDNA clone 13G1. In contrast, the 3‘-end of the H36-1 clone shows sequence homology to the 3‘-end of human complement factor H. The second clone, H36-2, is nearly identical to H36-1. Within 1148 base pairs, where the two clones overlap, their nucleotide sequences differed at nine positions. One nucleotide exchange in the sequence of H36-2 which was located within SCR 1 creats a stop codon (TAA). Consequently, the corresponding mRNA cannot code for a functional protein, suggesting that this clone is a transcribed pseudogene. These two clones represent new human members of the family of proteins structurally related to complement factor H.
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