| First Author | Yan Y | Year | 2000 |
| Journal | Vet Immunol Immunopathol | Volume | 75 |
| Issue | 1-2 | Pages | 151-9 |
| PubMed ID | 10889306 | Mgi Jnum | J:63556 |
| Mgi Id | MGI:1861176 | Doi | 10.1016/s0165-2427(00)00197-5 |
| Citation | Yan Y, et al. (2000) Molecular cloning and identification of full-length cDNA encoding high affinity Fc receptor for bovine IgG (FcgammaRI). Vet Immunol Immunopathol 75(1-2):151-9 |
| abstractText | The receptor I for the Fc region of immunoglobulin G (FcgammaRI) 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 FcgammaRI was cloned. The full-length cDNA sequence is 1050bp 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 FcgammaRI, 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 FcgammaRI are highly conserved. |
