Lectin mannose-binding 1, also designated vesicular integral-membrane protein (VIP36), and lectin mannose-binding 2, also designated ERGIC-53, comprise a family of membrane bound, ubiquitously expressed proteins involved in the selective transport of newly synthesized glycoproteins from the endoplasmic reticulum to the ER-Golgi intermediate compartment. VIPL (VIP36-like protein), also known as LMAN2L (lectin, mannose-binding 2-like), is a 348 amino acid single-pass type I membrane protein that localizes to the endoplasmic reticulum and Golgi apparatus. Containing one L-type lectin-like domain, VIPL is highly expressed in skeletal muscle and kidney, and is found at intermediate levels in heart, liver and placenta, and low levels in brain, thymus, spleen, small intestine and lung. VIPL is suggested to be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. VIPL may function as a regulator of ERGIC-53. VIPL exists a two alternatively spliced isoforms.