Human ERMAP: An Erythroid Adhesion/Receptor Transmembrane Protein

Abstract

ABSTRACTA human cDNA and gene encoding for human ERMAP, a putative erythroid transmembrane adhesion/receptor protein, is reported. The predicted protein is made up of 475 amino acids and shares high homology with the murine ERMAP (73% identity and 14% conservative changes). Human Ermap is highly expressed in erythroid tissues and the protein localizes to the plasma membrane, particularly in sites of cell contact, and “cytoplasmic bodies.” The extracellular segment contains one IgV fold that shares high homology with the butyrophilin family of milk proteins, autoantigens, and avian blood group antigens. In the intracellular region, there is a conserved B30.2 domain that is encoded by a single exon and is highly homologous with a similar domain in a diverse group of proteins, including butyrophilin, pyrin, and MID 1. The human Ermap gene is composed of 11 exons spanning 19 kb on chromosome 1p34.