Molecular cloning and identification of full-length cDNA encoding high affinity Fc receptor for bovine IgG (Fc gamma RI) |
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Authors: | Yan Y Li X Wang A Zhang G |
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Affiliation: | Institute of Animal and Veterinary Sciences, Henan Academy of Agricultural Sciences, 450002, Zhengzhou, China. yanxms@public2.zz.ha.cn |
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Abstract: | The receptor I for the Fc region of immunoglobulin G (Fc gamma RI) is a member of the Ig superfamily with a high affinity, and it mediates antibody-dependent cellular cytotoxicity and immune complex clearance. In this study, a cDNA encoding the bovine Fc gamma RI was cloned. The full-length cDNA sequence is 1050 bp long with a short 5'- and long 3'-untranslated end regions, which codes for 349 amino acids and contains a signal peptide, an extracellular region with three Ig-like domains, and transmembrane and intracytoplasmic domains. Five potential N-linked glycosylation sites are recognized in this sequence. Compared with the sequences of human and mouse Fc gamma RI, the homologies of nucleotide sequences are 80 and 69% and homologies of deduced amino acid sequences are 66 and 55%, respectively. It is shown that the sequences of the monomeric IgG binding domain in these three species of Fc gamma RI are highly conserved. |
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