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. 1998 Jul 13;142(1):117–127. doi: 10.1083/jcb.142.1.117

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(A) Nucleotide and deduced amino acid sequence of murine BV11 antigen (JAM) cDNA. The putative hydrophobic signal peptide (dotted underlined) and transmembrane sequences (underlined) are marked. Potential N-linked glycosylation sites are marked in bold and underlined at positions 42 and 185. Putative phosphorylation sites are marked in bold. Cysteines likely to form disulfide bonds in the two Ig domains (V-type) are boxed. These sequence data are available from GenBank, European Molecular Biology Laboratory, and DNA Data Base of Japan under the accession code U89915. (B) Structural model for murine JAM. The extracellular portion contains two domains with intrachain disulfide bonds typical of immunoglobulin-like loops of the V-type. Two putative N-linked glycosylation sites (—•) are shown.

(A) Nucleotide and deduced amino acid sequence of murine BV11 antigen (JAM) cDNA. The putative hydrophobic signal peptide (dotted underlined) and transmembrane sequences (underlined) are marked. Potential N-linked glycosylation sites are marked in bold and underlined at positions 42 and 185. Putative phosphorylation sites are marked in bold. Cysteines likely to form disulfide bonds in the two Ig domains (V-type) are boxed. These sequence data are available from GenBank, European Molecular Biology Laboratory, and DNA Data Base of Japan under the accession code U89915. (B) Structural model for murine JAM. The extracellular portion contains two domains with intrachain disulfide bonds typical of immunoglobulin-like loops of the V-type. Two putative N-linked glycosylation sites (—•) are shown.