Molecular characteristics and gene expression of LMIR5. (A) Alignment of amino acid sequences for mLMIR5 and hLMIR5. CBA and B6 indicate CBA/J mice and C57BL/6 mice, respectively. *Identical amino acids in mLMIR5 and hLMIR5. The putative signal sequence is shown in lower case. The variable type Ig-like domain is underlined; the potential N-linked glycosylation site is boxed. The transmembrane domain is marked by an arrow; the positive-charged amino acid residue (lysine) in the transmembrane domain is circled. Y188 in the cytoplasmic tail of hLMIR5 is shaded. (B) The phylogenetic tree of LMIR1/2/3/4/5 is shown based on homology with the Ig-like domain. Percentage of identity in amino acid sequences of the Ig-like domain was indicated. (C) Lysates of Ba/F3 cells transduced with either a Flag-tagged mLMIR5, a Flag-tagged hLMIR5, or mock were immnoprecipitated with anti-Flag mAb. The precipitates treated with or without N-glycosidase F were immunoblotted with anti-Flag mAb. (D-F) RT-PCR analysis on mLMIR5 expression in murine tissues (D), hematopoietic cell lines (E), and primary hematopoietic cells (F). Specific primers were used for mLMIR5 or β-actin as control. Vertical lines have been inserted to indicate a repositioned gel lane.