MmuEX6077695 @ mm10

Four membrane-bound (HLA-G1 to -G4) and two soluble (HLA-G5, and -G6) proteins are generated by alternative splicing. Only HLA-G1 has been extensively studied in terms of both expression and function. The authors provide evidence here that HLA-G2, -G3, and -G4 truncated isoforms reach the cell surface of transfected cells, as endoglycosidase H-sensitive glycoproteins, after a 2-h chase period. Moreover, cytotoxicity experiments show that these transfected cells are protected from the lytic activity of both innate (NK cells) and acquired (CTL) effectors, although to slightly different levels. The full-length transcript (HLA-G1) encodes three extracellular domains (alpha1, alpha2, and alpha3), a transmembrane region, and a cytoplasmic tail. Three other spliced transcripts encode membrane-bound proteins that lack alpha2 (HLA-G2; skipping exon 3, HsaEX0030116), alpha3 (HLA-G4; skipping of exon 4, HsaEX6046105), or both the alpha2 and alpha3 domains (HLA-G3).