Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins

doi:10.1084/jem.168.1.181

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Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins

DM Lublin, MK Liszewski, TW Post, MA Arce, MM Le Beau, MB Rebentisch, LS Lemons, T Seya and JP Atkinson
Department of Pathology, Washington University, St. Louis, Missouri 63110.

Membrane cofactor protein (MCP), a regulatory molecular of the complement system with cofactor activity for the factor I-mediated inactivation of C3b and C4b, is widely distributed, being present on leukocytes, platelets, endothelial cells, epithelial cells, and fibroblasts. MCP was purified from a human T cell line (HSB2) and the NH2-terminal 24-amino acid sequence obtained by Edman degradation. An oligonucleotide probe based on this sequence was used to identify a clone from a human monocytic (U937) cDNA library. Nucleotide sequencing showed a 43-bp 5'-untranslated region, an open reading frame of 1,152 bp, and a 335-bp 3'-untranslated region followed by a 16-bp poly(A) track. The deduced full-length MCP protein consists of a 34-amino acid signal peptide and a 350-amino acid mature protein. The protein has, beginning at the NH2 terminus, four approximately 60-amino acid repeat units that match the consensus sequence found in a multigene family of complement regulatory proteins (C3b-receptor or CR1, C3d-receptor or CR2, decay-accelerating factor, C4-binding protein, and factor H), as well as several other complement and non-complement proteins. The remainder of the MCP protein consists of 25 amino acids that are rich in serine and threonine (probable site of heavy O-linked glycosylation of MCP), 17 amino acids of unknown significance, and a 23-amino acid transmembrane hydrophobic region followed by a 33-amino acid cytoplasmic tail. The MCP gene was localized to human chromosome 1, bands 1q31-41, by analysis of human x rodent somatic cell hybrid clones and by in situ hybridization. This same genetic region contains the multigene family of complement-regulatory proteins, which is thereby enlarged to include the functionally and structurally related MCP.
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Makar, K. W., Pham, C. T. N., Dehoff, M. H., O'Connor, S. M., Jacobi, S. M., Holers, V. M. (1998). An Intronic Silencer Regulates B Lymphocyte Cell- and Stage-Specific Expression of the Human Complement Receptor Type 2 (CR2, CD21) Gene. J. Immunol. 160: 1268-1278 [Abstract] [Full Text]
Seeber, F, Dubremetz, J., Boothroyd, J. (1998). Analysis of Toxoplasma gondii stably transfected with a transmembrane variant of its major surface protein, SAG1. J. Cell Sci. 111: 23-29 [Abstract]
Iwata, K., Seya, T., Yanagi, Y., Pesando, J. M., Johnson, P. M., Okabe, M., Ueda, S., Ariga, H., Nagasawa, S. (1995). Diversity of Sites for Measles Virus Binding and for Inactivation of Complement C3b and C4b on Membrane Cofactor Protein CD46. J. Biol. Chem. 270: 15148-15152 [Abstract] [Full Text]
Kotwal, G., Isaacs, S., McKenzie, R, Frank, M., Moss, B (1990). Inhibition of the complement cascade by the major secretory protein of vaccinia virus. Science 250: 827-830 [Abstract]
Weisman, H., Bartow, T, Leppo, M., Marsh, H. Jr, Carson, G., Concino, M., Boyle, M., Roux, K., Weisfeldt, M., Fearon, D. (1990). Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis. Science 249: 146-151 [Abstract]
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