JAML is related to JAM proteins. (A) cDNA and deduced amino acid sequences of the human JAML. Nucleotide residues are numbered in the 5′ to 3′ orientation, and amino acids in the reading frame are designated by the one-letter code. Asterisk indicates the stop codon. The putative hydrophobic signal peptide (underlined) and transmembrane sequences (dotted underline) are marked. Potential N-linked glycosylation sites are shaded. Cysteines likely to form disulfide bonds in the 2 Ig domains are circled. (B) Dendogram of various IgSF family members containing 2 Ig domains (JAM-1, JAM-2, JAM-3, JAML, Coxsackie and adenovirus receptor (CAR), and endothelial cell-selective adhesion molecule (ESAM)). (C) Alignment of the amino-terminal region of the membrane distal Ig domains of these proteins and their mouse (JAM-1, JAM-2, JAM-3, CAR, ESAM) or bos taurus (JAML) homologs. Shaded regions represent residues identical between at least 4 proteins. The dimerization motif is boxed.